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Database: PDB
Entry: 1T2V
LinkDB: 1T2V
Original site: 1T2V 
HEADER    ANTITUMOR PROTEIN                       22-APR-04   1T2V              
TITLE     STRUCTURAL BASIS OF PHOSPHO-PEPTIDE RECOGNITION BY THE BRCT DOMAIN OF 
TITLE    2 BRCA1, STRUCTURE WITH PHOSPHOPEPTIDE                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A, B, C, D, E;                                                
COMPND   4 FRAGMENT: BRCT DOMAIN 1646-1859;                                     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: BRCTIDE-7PS;                                               
COMPND   8 CHAIN: F, G, H, I, J;                                                
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: IN VITRO OPTIMIZED PHOSPHOPEPTIDE                     
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRCA1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 OTHER_DETAILS: IN VITRO OPTIMIZED PHOSPHOPEPTIDE                     
KEYWDS    BRCT, BRCA1, BREAST CANCER, CELL SIGNALING, MISSENSE MUTATION,        
KEYWDS   2 PHOSPHOPEPTIDE, ANTITUMOR PROTEIN                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.S.WILLIAMS,M.S.LEE,D.D.HAU,J.N.M.GLOVER                             
REVDAT   4   13-JUL-11 1T2V    1       VERSN                                    
REVDAT   3   24-FEB-09 1T2V    1       VERSN                                    
REVDAT   2   18-MAY-04 1T2V    1       JRNL                                     
REVDAT   1   11-MAY-04 1T2V    0                                                
JRNL        AUTH   R.S.WILLIAMS,M.S.LEE,D.D.HAU,J.N.M.GLOVER                    
JRNL        TITL   STRUCTURAL BASIS OF PHOSPHOPEPTIDE RECOGNITION BY THE BRCT   
JRNL        TITL 2 DOMAIN OF BRCA1                                              
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  11   519 2004              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   15133503                                                     
JRNL        DOI    10.1038/NSMB776                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 19273                          
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) : 0.261                           
REMARK   3   R VALUE            (WORKING SET) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.301                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1016                            
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) : 3.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.39                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1397                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8380                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
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) : 66.91                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.46000                                              
REMARK   3    B22 (A**2) : -0.51000                                             
REMARK   3    B33 (A**2) : -1.96000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.669         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.541         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.291        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.849                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.814                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8583 ; 0.008 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11716 ; 1.252 ; 1.930       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1085 ; 5.934 ; 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):  1352 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6464 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3680 ; 0.144 ; 0.300       
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):   443 ; 0.164 ; 0.500       
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):    85 ; 0.118 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.195 ; 0.500       
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):  5470 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8778 ; 0.000 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3113 ; 0.000 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2938 ; 0.000 ; 4.500       
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                       
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A   1649       A    1859      4                      
REMARK   3           1     B   1649       B    1859      4                      
REMARK   3           1     C   1649       C    1859      4                      
REMARK   3           1     D   1649       D    1856      4                      
REMARK   3           1     E   1649       E    1859      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1398 ;  0.30 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1398 ;  0.33 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1398 ;  0.27 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1398 ;  0.34 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   1398 ;  0.29 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1398 ;  0.00 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1398 ;  0.00 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1398 ;  0.00 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1398 ;  0.00 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   1398 ;  0.00 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1649        A  1859                          
REMARK   3    RESIDUE RANGE :   F     1        F    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  74.9865  50.6412  38.5340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5115 T22:   0.0967                                     
REMARK   3      T33:   0.1184 T12:  -0.2221                                     
REMARK   3      T13:  -0.0253 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4652 L22:   5.7819                                     
REMARK   3      L33:   4.6762 L12:  -2.3594                                     
REMARK   3      L13:  -1.3743 L23:   0.4638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1380 S12:  -0.3032 S13:   0.2508                       
REMARK   3      S21:   0.1454 S22:  -0.0516 S23:   0.0135                       
REMARK   3      S31:  -0.9217 S32:   0.1366 S33:  -0.0864                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1646        B  1859                          
REMARK   3    RESIDUE RANGE :   G     1        G    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0251  29.6948  -2.2879              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1249 T22:   0.3943                                     
REMARK   3      T33:   0.1693 T12:   0.1210                                     
REMARK   3      T13:  -0.0277 T23:  -0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6775 L22:   8.3934                                     
REMARK   3      L33:   4.5337 L12:   3.0280                                     
REMARK   3      L13:   1.9175 L23:   3.1709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0730 S12:   0.0327 S13:  -0.1228                       
REMARK   3      S21:  -0.1052 S22:  -0.0440 S23:   0.5677                       
REMARK   3      S31:   0.0772 S32:   0.1026 S33:   0.1170                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  1649        C  1859                          
REMARK   3    RESIDUE RANGE :   H     1        H    14                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.9236   8.4195 -16.8480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2162 T22:   0.2732                                     
REMARK   3      T33:   0.1365 T12:   0.1855                                     
REMARK   3      T13:   0.0145 T23:  -0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0789 L22:   9.7286                                     
REMARK   3      L33:   5.2028 L12:   1.4762                                     
REMARK   3      L13:  -0.2384 L23:   0.7183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2909 S12:   0.1844 S13:  -0.1827                       
REMARK   3      S21:  -0.3313 S22:   0.1168 S23:  -0.2367                       
REMARK   3      S31:  -0.2519 S32:   0.6618 S33:  -0.4077                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  1647        D  1856                          
REMARK   3    RESIDUE RANGE :   I     1        I    11                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2580  18.8564  39.9385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4092 T22:   0.3167                                     
REMARK   3      T33:   0.4793 T12:   0.1469                                     
REMARK   3      T13:  -0.0216 T23:  -0.2114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0825 L22:   3.6867                                     
REMARK   3      L33:   7.1142 L12:   2.0082                                     
REMARK   3      L13:   5.1632 L23:   1.1551                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3045 S12:   0.6778 S13:  -0.4083                       
REMARK   3      S21:  -0.1921 S22:   0.2325 S23:   0.0288                       
REMARK   3      S31:  -0.0145 S32:   0.2921 S33:  -0.5370                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E  1649        E  1859                          
REMARK   3    RESIDUE RANGE :   J     2        J    13                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.5649  31.8796  29.9912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1743 T22:   0.1694                                     
REMARK   3      T33:   0.0897 T12:  -0.0612                                     
REMARK   3      T13:  -0.0373 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7214 L22:   3.8173                                     
REMARK   3      L33:   5.1116 L12:  -2.4776                                     
REMARK   3      L13:  -2.8911 L23:   2.3380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1113 S12:   0.0640 S13:  -0.0617                       
REMARK   3      S21:  -0.0355 S22:   0.0692 S23:   0.0090                       
REMARK   3      S31:  -0.1747 S32:  -0.2072 S33:   0.0421                       
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 1T2V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022242.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JAN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11                               
REMARK 200  MONOCHROMATOR                  : NULL                               
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   : 20289                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.303                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000 AMMONIUM ACETATE, TRI-SODIUM    
REMARK 280  CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K,   
REMARK 280  PH 5.60                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       99.13300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       99.13300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       48.55850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.17850            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.55850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.17850            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       99.13300            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       48.55850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       69.17850            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       99.13300            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       48.55850            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       69.17850            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7                                     
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 910 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 970 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J                                  
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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       97.11700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       99.13300            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J                                  
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   BIOMT1   2 -1.000000  0.000000  0.000000       97.11700            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       99.13300            
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     VAL A  1646                                                      
REMARK 465     ASN A  1647                                                      
REMARK 465     LYS A  1648                                                      
REMARK 465     LEU A  1800                                                      
REMARK 465     GLY A  1801                                                      
REMARK 465     THR A  1802                                                      
REMARK 465     GLU B  1817                                                      
REMARK 465     ASP B  1818                                                      
REMARK 465     ASN B  1819                                                      
REMARK 465     GLY B  1820                                                      
REMARK 465     VAL C  1646                                                      
REMARK 465     ASN C  1647                                                      
REMARK 465     LYS C  1648                                                      
REMARK 465     LEU C  1800                                                      
REMARK 465     GLY C  1801                                                      
REMARK 465     THR C  1802                                                      
REMARK 465     GLY C  1803                                                      
REMARK 465     VAL C  1804                                                      
REMARK 465     GLU C  1817                                                      
REMARK 465     ASP C  1818                                                      
REMARK 465     ASN C  1819                                                      
REMARK 465     GLY C  1820                                                      
REMARK 465     VAL D  1646                                                      
REMARK 465     GLU D  1817                                                      
REMARK 465     ASP D  1818                                                      
REMARK 465     ASN D  1819                                                      
REMARK 465     GLY D  1820                                                      
REMARK 465     GLU D  1829                                                      
REMARK 465     GLN D  1857                                                      
REMARK 465     ILE D  1858                                                      
REMARK 465     PRO D  1859                                                      
REMARK 465     VAL E  1646                                                      
REMARK 465     ASN E  1647                                                      
REMARK 465     LYS E  1648                                                      
REMARK 465     LYS F    15                                                      
REMARK 465     LYS F    16                                                      
REMARK 465     LYS G    15                                                      
REMARK 465     LYS G    16                                                      
REMARK 465     LYS H    15                                                      
REMARK 465     LYS H    16                                                      
REMARK 465     PHE I    12                                                      
REMARK 465     ALA I    13                                                      
REMARK 465     LYS I    14                                                      
REMARK 465     LYS I    15                                                      
REMARK 465     LYS I    16                                                      
REMARK 465     GLY J     1                                                      
REMARK 465     LYS J    14                                                      
REMARK 465     LYS J    15                                                      
REMARK 465     LYS J    16                                                      
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 A1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1671    CG   CD   CE   NZ                                   
REMARK 470     GLU A1682    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1724    CG   CD   CE   NZ                                   
REMARK 470     ARG A1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1727    CG   CD   CE   NZ                                   
REMARK 470     ASP A1733    CG   OD1  OD2                                       
REMARK 470     LYS A1750    CG   CD   CE   NZ                                   
REMARK 470     ARG A1751    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1754    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1757    CG   OD1  OD2                                       
REMARK 470     ARG A1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A1816    OG1  CG2                                            
REMARK 470     GLU A1829    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1851    CG   OD1  OD2                                       
REMARK 470     VAL B1646    CG1  CG2                                            
REMARK 470     LYS B1648    CG   CD   CE   NZ                                   
REMARK 470     MET B1663    CG   SD   CE                                        
REMARK 470     ARG B1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1671    CG   CD   CE   NZ                                   
REMARK 470     GLU B1683    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1694    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1724    CG   CD   CE   NZ                                   
REMARK 470     ARG B1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1727    CG   CD   CE   NZ                                   
REMARK 470     ASP B1733    CG   OD1  OD2                                       
REMARK 470     LYS B1750    CG   CD   CE   NZ                                   
REMARK 470     ASP B1757    CG   OD1  OD2                                       
REMARK 470     ARG B1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1800    CG   CD1  CD2                                       
REMARK 470     THR B1802    OG1  CG2                                            
REMARK 470     TRP B1815    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B1815    CZ3  CH2                                            
REMARK 470     THR B1816    OG1  CG2                                            
REMARK 470     PHE B1821    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG C1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1671    CG   CD   CE   NZ                                   
REMARK 470     GLU C1682    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1724    CG   CD   CE   NZ                                   
REMARK 470     ARG C1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1727    CG   CD   CE   NZ                                   
REMARK 470     ARG C1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1750    CG   CD   CE   NZ                                   
REMARK 470     ARG C1751    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C1756    CG   CD   OE1  NE2                                  
REMARK 470     ASP C1757    CG   OD1  OD2                                       
REMARK 470     ARG C1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1793    CG   CD   CE   NZ                                   
REMARK 470     HIS C1805    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR C1816    OG1  CG2                                            
REMARK 470     PHE C1821    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET C1827    CG   SD   CE                                        
REMARK 470     GLU C1829    CG   CD   OE1  OE2                                  
REMARK 470     GLN C1846    CG   CD   OE1  NE2                                  
REMARK 470     GLU C1849    CG   CD   OE1  OE2                                  
REMARK 470     ASP C1851    CG   OD1  OD2                                       
REMARK 470     ASN D1647    CG   OD1                                            
REMARK 470     LYS D1648    CG   CD   CE   NZ                                   
REMARK 470     ARG D1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1671    CG   CD   CE   NZ                                   
REMARK 470     GLU D1682    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1694    CG   CD   OE1  OE2                                  
REMARK 470     ARG D1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D1733    CG   OD1  OD2                                       
REMARK 470     ARG D1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1744    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN D1747    CG   CD   OE1  NE2                                  
REMARK 470     LYS D1750    CG   CD   CE   NZ                                   
REMARK 470     GLU D1754    CG   CD   OE1  OE2                                  
REMARK 470     GLN D1756    CG   CD   OE1  NE2                                  
REMARK 470     ASP D1757    CG   OD1  OD2                                       
REMARK 470     ARG D1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1793    CG   CD   CE   NZ                                   
REMARK 470     LEU D1800    CG   CD1  CD2                                       
REMARK 470     THR D1802    OG1  CG2                                            
REMARK 470     TRP D1815    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D1815    CZ3  CH2                                            
REMARK 470     THR D1816    OG1  CG2                                            
REMARK 470     PHE D1821    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN D1826    CG   CD   OE1  NE2                                  
REMARK 470     MET D1827    CG   SD   CE                                        
REMARK 470     GLN D1846    CG   CD   OE1  NE2                                  
REMARK 470     GLU D1849    CG   CD   OE1  OE2                                  
REMARK 470     ASP D1851    CG   OD1  OD2                                       
REMARK 470     ARG E1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E1667    CG   CD   CE   NZ                                   
REMARK 470     ARG E1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E1682    CG   CD   OE1  OE2                                  
REMARK 470     GLU E1694    CG   CD   OE1  OE2                                  
REMARK 470     ARG E1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E1727    CG   CD   CE   NZ                                   
REMARK 470     ARG E1744    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E1793    CG   CD   CE   NZ                                   
REMARK 470     LEU E1800    CG   CD1  CD2                                       
REMARK 470     THR E1816    OG1  CG2                                            
REMARK 470     GLU E1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP E1818    CG   OD1  OD2                                       
REMARK 470     ASN E1819    CG   OD1                                            
REMARK 470     GLU E1829    CG   CD   OE1  OE2                                  
REMARK 470     LYS F  14    CG   CD   CE   NZ                                   
REMARK 470     PHE G  12    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS G  14    CG   CD   CE   NZ                                   
REMARK 470     LYS H  14    CG   CD   CE   NZ                                   
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    PHE J  10   CA  -  C   -  N   ANGL. DEV. =  18.4 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    ARG A1726      -22.29     68.15                                   
REMARK 500    GLN A1747       40.06    -85.74                                   
REMARK 500    THR A1773      -85.23    -99.43                                   
REMARK 500    CYS B1697     -167.76   -114.97                                   
REMARK 500    ARG B1726      -10.15     60.05                                   
REMARK 500    PHE B1761       41.04   -107.40                                   
REMARK 500    THR B1773      -66.92    -96.30                                   
REMARK 500    LEU B1800       44.42    -87.26                                   
REMARK 500    MET C1650      105.51    -59.78                                   
REMARK 500    ARG C1726       13.42     59.47                                   
REMARK 500    GLN C1747       35.00    -92.56                                   
REMARK 500    ARG C1762      -60.20    -24.85                                   
REMARK 500    THR C1773      -72.73   -105.48                                   
REMARK 500    ASP C1851      -63.02    -16.34                                   
REMARK 500    LYS D1648       66.70   -152.96                                   
REMARK 500    PHE D1734       12.17   -145.35                                   
REMARK 500    PHE D1761       31.79    -97.50                                   
REMARK 500    THR D1773      -74.91    -96.12                                   
REMARK 500    THR D1802       95.03    -60.62                                   
REMARK 500    ASP E1692     -168.41   -102.29                                   
REMARK 500    ARG E1726        3.00     58.80                                   
REMARK 500    THR E1773      -63.82   -103.95                                   
REMARK 500    ALA F   2     -164.30    -64.42                                   
REMARK 500    ALA G  13     -168.46   -115.34                                   
REMARK 500    PRO H  11     -168.72    -78.44                                   
REMARK 500    PRO J  11      170.05    -54.93                                   
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 GLU E 1817     ASP E 1818                 -143.66                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JNX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1N5O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T2U   RELATED DB: PDB                                   
DBREF  1T2V A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  1T2V B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  1T2V C 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  1T2V D 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  1T2V E 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  1T2V F    1    16  PDB    1T2V     1T2V             1     16             
DBREF  1T2V G    1    16  PDB    1T2V     1T2V             1     16             
DBREF  1T2V H    1    16  PDB    1T2V     1T2V             1     16             
DBREF  1T2V I    1    16  PDB    1T2V     1T2V             1     16             
DBREF  1T2V J    1    16  PDB    1T2V     1T2V             1     16             
SEQRES   1 A  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 A  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 A  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 A  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 A  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 A  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 A  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 A  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 A  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 A  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 A  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 A  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 A  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 A  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 A  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 A  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 A  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 B  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 B  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 B  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 B  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 B  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 B  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 B  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 B  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 B  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 B  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 B  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 B  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 B  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 B  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 B  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 B  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 B  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 C  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 C  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 C  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 C  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 C  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 C  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 C  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 C  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 C  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 C  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 C  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 C  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 C  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 C  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 C  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 C  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 C  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 D  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 D  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 D  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 D  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 D  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 D  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 D  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 D  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 D  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 D  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 D  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 D  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 D  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 D  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 D  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 D  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 D  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 E  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 E  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 E  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 E  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 E  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 E  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 E  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 E  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 E  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 E  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 E  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 E  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 E  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 E  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 E  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 E  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 E  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 F   16  GLY ALA ALA TYR ASP ILE SEP GLN VAL PHE PRO PHE ALA          
SEQRES   2 F   16  LYS LYS LYS                                                  
SEQRES   1 G   16  GLY ALA ALA TYR ASP ILE SEP GLN VAL PHE PRO PHE ALA          
SEQRES   2 G   16  LYS LYS LYS                                                  
SEQRES   1 H   16  GLY ALA ALA TYR ASP ILE SEP GLN VAL PHE PRO PHE ALA          
SEQRES   2 H   16  LYS LYS LYS                                                  
SEQRES   1 I   16  GLY ALA ALA TYR ASP ILE SEP GLN VAL PHE PRO PHE ALA          
SEQRES   2 I   16  LYS LYS LYS                                                  
SEQRES   1 J   16  GLY ALA ALA TYR ASP ILE SEP GLN VAL PHE PRO PHE ALA          
SEQRES   2 J   16  LYS LYS LYS                                                  
MODRES 1T2V SEP F    7  SER  PHOSPHOSERINE                                      
MODRES 1T2V SEP G    7  SER  PHOSPHOSERINE                                      
MODRES 1T2V SEP H    7  SER  PHOSPHOSERINE                                      
MODRES 1T2V SEP I    7  SER  PHOSPHOSERINE                                      
MODRES 1T2V SEP J    7  SER  PHOSPHOSERINE                                      
HET    SEP  F   7      10                                                       
HET    SEP  G   7      10                                                       
HET    SEP  H   7      10                                                       
HET    SEP  I   7      10                                                       
HET    SEP  J   7      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   6  SEP    5(C3 H8 N O6 P)                                              
HELIX    1   1 THR A 1658  HIS A 1673  1                                  16    
HELIX    2   2 THR A 1700  GLY A 1709  1                                  10    
HELIX    3   3 TYR A 1716  GLU A 1725  1                                  10    
HELIX    4   4 GLU A 1731  GLU A 1735  5                                   5    
HELIX    5   5 GLN A 1747  SER A 1755  1                                   9    
HELIX    6   6 PRO A 1776  CYS A 1787  1                                  12    
HELIX    7   7 GLU A 1794  PHE A 1798  5                                   5    
HELIX    8   8 GLN A 1811  TRP A 1815  5                                   5    
HELIX    9   9 ASN A 1819  HIS A 1822  5                                   4    
HELIX   10  10 ALA A 1823  CYS A 1828  1                                   6    
HELIX   11  11 ARG A 1835  TYR A 1845  1                                  11    
HELIX   12  12 GLU A 1849  TYR A 1853  5                                   5    
HELIX   13  13 THR B 1658  HIS B 1672  1                                  15    
HELIX   14  14 THR B 1700  GLY B 1709  1                                  10    
HELIX   15  15 TYR B 1716  GLU B 1725  1                                  10    
HELIX   16  16 ASN B 1730  GLU B 1735  5                                   6    
HELIX   17  17 GLN B 1747  SER B 1755  1                                   9    
HELIX   18  18 PRO B 1776  CYS B 1787  1                                  12    
HELIX   19  19 GLU B 1794  PHE B 1798  5                                   5    
HELIX   20  20 ALA B 1823  MET B 1827  5                                   5    
HELIX   21  21 ARG B 1835  TYR B 1845  1                                  11    
HELIX   22  22 THR C 1658  HIS C 1672  1                                  15    
HELIX   23  23 THR C 1700  GLY C 1709  1                                  10    
HELIX   24  24 TYR C 1716  GLU C 1725  1                                  10    
HELIX   25  25 ASN C 1730  PHE C 1734  5                                   5    
HELIX   26  26 GLN C 1747  SER C 1755  1                                   9    
HELIX   27  27 PRO C 1776  CYS C 1787  1                                  12    
HELIX   28  28 GLU C 1794  PHE C 1798  5                                   5    
HELIX   29  29 GLN C 1811  TRP C 1815  5                                   5    
HELIX   30  30 ARG C 1835  TYR C 1845  1                                  11    
HELIX   31  31 GLU C 1849  TYR C 1853  5                                   5    
HELIX   32  32 THR D 1658  HIS D 1673  1                                  16    
HELIX   33  33 THR D 1700  GLY D 1710  1                                  11    
HELIX   34  34 TYR D 1716  ARG D 1726  1                                  11    
HELIX   35  35 ASN D 1730  GLU D 1735  5                                   6    
HELIX   36  36 GLN D 1747  SER D 1755  1                                   9    
HELIX   37  37 PRO D 1776  CYS D 1787  1                                  12    
HELIX   38  38 GLU D 1794  PHE D 1798  5                                   5    
HELIX   39  39 GLN D 1811  TRP D 1815  5                                   5    
HELIX   40  40 ALA D 1823  CYS D 1828  1                                   6    
HELIX   41  41 ARG D 1835  LEU D 1844  1                                  10    
HELIX   42  42 GLU D 1849  TYR D 1853  5                                   5    
HELIX   43  43 THR E 1658  HIS E 1673  1                                  16    
HELIX   44  44 THR E 1700  GLY E 1710  1                                  11    
HELIX   45  45 TYR E 1716  GLU E 1725  1                                  10    
HELIX   46  46 ASN E 1730  PHE E 1734  5                                   5    
HELIX   47  47 GLN E 1747  SER E 1755  1                                   9    
HELIX   48  48 PRO E 1776  CYS E 1787  1                                  12    
HELIX   49  49 GLU E 1794  PHE E 1798  5                                   5    
HELIX   50  50 GLN E 1811  TRP E 1815  5                                   5    
HELIX   51  51 ALA E 1823  CYS E 1828  1                                   6    
HELIX   52  52 ARG E 1835  TYR E 1845  1                                  11    
HELIX   53  53 GLU E 1849  LEU E 1854  5                                   6    
SHEET    1   A 4 THR A1675  LEU A1676  0                                        
SHEET    2   A 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3   A 4 HIS A1686  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    4   A 4 TRP A1712  SER A1715  1  O  VAL A1714   N  MET A1689           
SHEET    1   B 2 VAL A1696  CYS A1697  0                                        
SHEET    2   B 2 GLY A1738  ASP A1739  1  O  GLY A1738   N  CYS A1697           
SHEET    1   C 4 SER A1790  VAL A1792  0                                        
SHEET    2   C 4 LEU A1764  CYS A1768  1  N  ILE A1766   O  SER A1790           
SHEET    3   C 4 HIS A1805  VAL A1810  1  O  HIS A1805   N  GLU A1765           
SHEET    4   C 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1808           
SHEET    1   D 2 GLY A1770  PHE A1772  0                                        
SHEET    2   D 2 ALA J   3  ASP J   5  1  O  TYR J   4   N  PHE A1772           
SHEET    1   E 4 THR B1675  LEU B1676  0                                        
SHEET    2   E 4 SER B1651  SER B1655  1  N  MET B1652   O  THR B1675           
SHEET    3   E 4 HIS B1686  MET B1689  1  O  VAL B1688   N  VAL B1653           
SHEET    4   E 4 TRP B1712  SER B1715  1  O  VAL B1714   N  MET B1689           
SHEET    1   F 2 VAL B1696  CYS B1697  0                                        
SHEET    2   F 2 GLY B1738  ASP B1739  1  O  GLY B1738   N  CYS B1697           
SHEET    1   G 4 SER B1790  VAL B1792  0                                        
SHEET    2   G 4 LEU B1764  TYR B1769  1  N  ILE B1766   O  SER B1790           
SHEET    3   G 4 HIS B1805  VAL B1810  1  O  ILE B1807   N  GLU B1765           
SHEET    4   G 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SHEET    1   H 2 PRO B1771  PHE B1772  0                                        
SHEET    2   H 2 TYR H   4  ASP H   5  1  O  TYR H   4   N  PHE B1772           
SHEET    1   I 4 THR C1675  LEU C1676  0                                        
SHEET    2   I 4 SER C1651  SER C1655  1  N  MET C1652   O  THR C1675           
SHEET    3   I 4 HIS C1686  MET C1689  1  O  VAL C1688   N  VAL C1653           
SHEET    4   I 4 TRP C1712  SER C1715  1  O  TRP C1712   N  VAL C1687           
SHEET    1   J 2 VAL C1696  CYS C1697  0                                        
SHEET    2   J 2 GLY C1738  ASP C1739  1  O  GLY C1738   N  CYS C1697           
SHEET    1   K 4 SER C1790  VAL C1792  0                                        
SHEET    2   K 4 GLU C1765  CYS C1768  1  N  ILE C1766   O  SER C1790           
SHEET    3   K 4 PRO C1806  VAL C1810  1  O  ILE C1807   N  GLU C1765           
SHEET    4   K 4 VAL C1832  THR C1834  1  O  VAL C1833   N  VAL C1808           
SHEET    1   L 2 GLY C1770  PHE C1772  0                                        
SHEET    2   L 2 ALA G   3  ASP G   5  1  O  TYR G   4   N  GLY C1770           
SHEET    1   M 4 THR D1675  LEU D1676  0                                        
SHEET    2   M 4 SER D1651  SER D1655  1  N  MET D1652   O  THR D1675           
SHEET    3   M 4 HIS D1686  MET D1689  1  O  VAL D1688   N  VAL D1653           
SHEET    4   M 4 TRP D1712  SER D1715  1  O  TRP D1712   N  VAL D1687           
SHEET    1   N 2 VAL D1696  CYS D1697  0                                        
SHEET    2   N 2 GLY D1738  ASP D1739  1  O  GLY D1738   N  CYS D1697           
SHEET    1   O 4 SER D1790  VAL D1791  0                                        
SHEET    2   O 4 LEU D1764  CYS D1768  1  N  ILE D1766   O  SER D1790           
SHEET    3   O 4 HIS D1805  VAL D1810  1  O  ILE D1807   N  GLU D1765           
SHEET    4   O 4 VAL D1832  THR D1834  1  O  VAL D1833   N  VAL D1808           
SHEET    1   P 4 THR E1675  LEU E1676  0                                        
SHEET    2   P 4 SER E1651  SER E1655  1  N  MET E1652   O  THR E1675           
SHEET    3   P 4 HIS E1686  MET E1689  1  O  VAL E1688   N  VAL E1653           
SHEET    4   P 4 TRP E1712  SER E1715  1  O  TRP E1712   N  VAL E1687           
SHEET    1   Q 2 VAL E1696  CYS E1697  0                                        
SHEET    2   Q 2 GLY E1738  ASP E1739  1  O  GLY E1738   N  CYS E1697           
SHEET    1   R 4 SER E1790  VAL E1791  0                                        
SHEET    2   R 4 LEU E1764  CYS E1768  1  N  ILE E1766   O  SER E1790           
SHEET    3   R 4 HIS E1805  VAL E1810  1  O  HIS E1805   N  GLU E1765           
SHEET    4   R 4 VAL E1832  THR E1834  1  O  VAL E1833   N  VAL E1808           
SHEET    1   S 2 PRO E1771  PHE E1772  0                                        
SHEET    2   S 2 TYR F   4  ASP F   5  1  O  TYR F   4   N  PHE E1772           
LINK         C   ILE F   6                 N   SEP F   7     1555   1555  1.33  
LINK         C   SEP F   7                 N   GLN F   8     1555   1555  1.33  
LINK         C   ILE G   6                 N   SEP G   7     1555   1555  1.34  
LINK         C   SEP G   7                 N   GLN G   8     1555   1555  1.33  
LINK         C   ILE H   6                 N   SEP H   7     1555   1555  1.33  
LINK         C   SEP H   7                 N   GLN H   8     1555   1555  1.32  
LINK         C   ILE I   6                 N   SEP I   7     1555   1555  1.33  
LINK         C   SEP I   7                 N   GLN I   8     1555   1555  1.33  
LINK         C   ILE J   6                 N   SEP J   7     1555   1555  1.33  
LINK         C   SEP J   7                 N   GLN J   8     1555   1555  1.35  
CISPEP   1 PHE J   10    PRO J   11          0         0.79                     
CRYST1   97.117  138.357  198.266  90.00  90.00  90.00 C 2 2 21     40          
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      0.010297  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007228  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005044        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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