GenomeNet

Database: PDB
Entry: 2F8X
LinkDB: 2F8X
Original site: 2F8X 
HEADER    TRANSCRIPTION/DNA                       04-DEC-05   2F8X              
TITLE     CRYSTAL STRUCTURE OF ACTIVATED NOTCH, CSL AND MAML ON HES-1           
TITLE    2 PROMOTER DNA SEQUENCE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-                                                        
COMPND   3 D(*GP*TP*TP*AP*CP*TP*GP*TP*GP*GP*GP*AP*AP*AP*GP*AP*AP*A)-            
COMPND   4 3';                                                                  
COMPND   5 CHAIN: X;                                                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 5'-                                                        
COMPND   9 D(*TP*TP*TP*CP*TP*TP*TP*CP*CP*CP*AP*CP*AP*GP*TP*AP*AP*C)-            
COMPND  10 3';                                                                  
COMPND  11 CHAIN: Y;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: RECOMBINING BINDING PROTEIN SUPPRESSOR OF                  
COMPND  15 HAIRLESS, ISOFORM 4;                                                 
COMPND  16 CHAIN: C;                                                            
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1;                  
COMPND  20 CHAIN: K;                                                            
COMPND  21 FRAGMENT: [CONTAINS: NOTCH 1 EXTRACELLULAR TRUNCATION;               
COMPND  22 NOTCH 1 INTRACELLULAR DOMAIN];                                       
COMPND  23 SYNONYM: (NOTCH 1) (HN1) (TRANSLOCATION-ASSOCIATED NOTCH             
COMPND  24 PROTEIN TAN-1);                                                      
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MOL_ID: 5;                                                           
COMPND  27 MOLECULE: MASTERMIND-LIKE PROTEIN 1;                                 
COMPND  28 CHAIN: M;                                                            
COMPND  29 SYNONYM: MAM-1;                                                      
COMPND  30 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 MOL_ID: 2;                                                           
SOURCE   4 SYNTHETIC: YES;                                                      
SOURCE   5 MOL_ID: 3;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  11 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PRSETA;                                   
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: NOTCH1, TAN1;                                                  
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  21 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  22 MOL_ID: 5;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: MAML1, KIAA0200;                                               
SOURCE  27 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  29 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;                            
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PDEST15                                   
KEYWDS    NOTCH, CSL, MASTERMIND, HES-1, ANKYRIN REPEATS, REL-                  
KEYWDS   2 HOMOLOGY REGION, TRANSCRIPTION/DNA COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.NAM,P.SLIZ,S.C.BLACKLOW                                             
REVDAT   2   24-FEB-09 2F8X    1       VERSN                                    
REVDAT   1   04-APR-06 2F8X    0                                                
JRNL        AUTH   Y.NAM,P.SLIZ,L.SONG,J.C.ASTER,S.C.BLACKLOW                   
JRNL        TITL   STRUCTURAL BASIS FOR COOPERATIVITY IN RECRUITMENT            
JRNL        TITL 2 OF MAML COACTIVATORS TO NOTCH TRANSCRIPTION                  
JRNL        TITL 3 COMPLEXES.                                                   
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 124   973 2006              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   16530044                                                     
JRNL        DOI    10.1016/J.CELL.2005.12.037                                   
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 72848                          
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 SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3688                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.45                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3570                       
REMARK   3   BIN FREE R VALUE                    : 0.3740                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 590                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5497                                    
REMARK   3   NUCLEIC ACID ATOMS       : 732                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 12.48100                                             
REMARK   3    B22 (A**2) : 12.48100                                             
REMARK   3    B33 (A**2) : -24.96300                                            
REMARK   3    B12 (A**2) : 4.19400                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.38                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.65                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.44                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.68                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 38.83                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : CNS_TOPPAR:PROTEIN_REP.PARAM                   
REMARK   3  PARAMETER FILE  2  : CNS_TOPPAR:DNA-RNA_REP.PARAM                   
REMARK   3  PARAMETER FILE  3  : CNS_TOPPAR:WATER_REP.PARAM                     
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2F8X COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB035598.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-05                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72848                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.820                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
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: PDB ENTRIES: 1TTU AND 2F8Y                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES, 6% PEG 3350, AND 5%          
REMARK 280  ETHYLENE GLYCOL, PH 7.9, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-Y,X,Z+1/2                                             
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z                                              
REMARK 290      10555   -Y,-X,-Z+1/2                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/2                                            
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        0.00000            
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        0.00000            
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       60.50800            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       60.50800            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       60.50800            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       60.50800            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       60.50800            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       60.50800            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y, C, K, M                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     GLY C   435                                                      
REMARK 465     HIS C   436                                                      
REMARK 465     HIS C   437                                                      
REMARK 465     HIS C   438                                                      
REMARK 465     HIS C   439                                                      
REMARK 465     HIS C   440                                                      
REMARK 465     HIS C   441                                                      
REMARK 465     GLY K  1872                                                      
REMARK 465     MET K  1873                                                      
REMARK 465     ASP K  1874                                                      
REMARK 465     VAL K  1875                                                      
REMARK 465     ASN K  1876                                                      
REMARK 465     VAL K  1877                                                      
REMARK 465     ARG K  1878                                                      
REMARK 465     GLY K  1879                                                      
REMARK 465     PRO K  1880                                                      
REMARK 465     ASP K  1881                                                      
REMARK 465     GLY K  1882                                                      
REMARK 465     PHE K  1883                                                      
REMARK 465     GLY K  1893                                                      
REMARK 465     GLY K  1894                                                      
REMARK 465     GLY K  1895                                                      
REMARK 465     LEU K  1896                                                      
REMARK 465     GLU K  1897                                                      
REMARK 465     THR K  1898                                                      
REMARK 465     GLY K  1899                                                      
REMARK 465     ASN K  1900                                                      
REMARK 465     SER K  1901                                                      
REMARK 465     GLU K  1902                                                      
REMARK 465     GLU K  1903                                                      
REMARK 465     GLU K  1904                                                      
REMARK 465     GLU K  1905                                                      
REMARK 465     ASP K  1906                                                      
REMARK 465     ALA K  1907                                                      
REMARK 465     PRO K  1908                                                      
REMARK 465     GLN K  1917                                                      
REMARK 465     GLY K  1918                                                      
REMARK 465     ALA K  1919                                                      
REMARK 465     ARG K  2121                                                      
REMARK 465     SER K  2122                                                      
REMARK 465     PRO K  2123                                                      
REMARK 465     GLN K  2124                                                      
REMARK 465     LEU K  2125                                                      
REMARK 465     HIS K  2126                                                      
REMARK 465     GLY K  2127                                                      
REMARK 465     GLY M    12                                                      
REMARK 465     LEU M    13                                                      
REMARK 465     PRO M    14                                                      
REMARK 465     ARG M    15                                                      
REMARK 465     ALA M    71                                                      
REMARK 465     GLY M    72                                                      
REMARK 465     LYS M    73                                                      
REMARK 465     HIS M    74                                                      
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     VAL K1910    CG1  CG2                                            
REMARK 470     ILE K1911    CG1  CG2  CD1                                       
REMARK 470     SER K1912    OG                                                  
REMARK 470     ASP K1913    CG   OD1  OD2                                       
REMARK 470     PHE K1914    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ILE K1915    CG1  CG2  CD1                                       
REMARK 470     TYR K1916    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   O    PRO C   392     OH   TYR C   430              2.19            
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     DT X   1   N1  -  C1' -  C2' ANGL. DEV. =   8.4 DEGREES          
REMARK 500     DG X  10   O4' -  C1' -  N9  ANGL. DEV. =   3.2 DEGREES          
REMARK 500     DA Y 117   O4' -  C1' -  N9  ANGL. DEV. =   2.5 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 C  28      -76.70    -73.25                                   
REMARK 500    ARG C  29       60.16     79.27                                   
REMARK 500    LEU C  35      128.79    175.48                                   
REMARK 500    GLU C  49     -160.66    -61.14                                   
REMARK 500    LYS C  50       87.63   -178.25                                   
REMARK 500    PRO C  57      108.48    -50.36                                   
REMARK 500    ARG C  75       20.97    -59.43                                   
REMARK 500    ASP C  76       17.40   -143.35                                   
REMARK 500    SER C  83       41.92   -109.10                                   
REMARK 500    ALA C  87      133.12    177.52                                   
REMARK 500    GLN C  96     -138.75   -121.53                                   
REMARK 500    CYS C 109      130.48   -178.26                                   
REMARK 500    ALA C 111       73.26   -111.22                                   
REMARK 500    ASN C 135       38.84    -81.54                                   
REMARK 500    SER C 136       16.37     50.36                                   
REMARK 500    LYS C 152      141.88    162.54                                   
REMARK 500    LYS C 156     -154.07    -73.32                                   
REMARK 500    ASN C 162       64.87   -100.67                                   
REMARK 500    ALA C 163     -150.52    -67.06                                   
REMARK 500    ASP C 164      -14.25     71.39                                   
REMARK 500    THR C 171     -176.74    -60.78                                   
REMARK 500    ARG C 180       17.27     52.32                                   
REMARK 500    SER C 181       29.62     83.63                                   
REMARK 500    THR C 186      119.16    -21.66                                   
REMARK 500    ALA C 198       32.73   -154.43                                   
REMARK 500    ASP C 213      -36.98    -31.61                                   
REMARK 500    ASP C 214       49.11    -82.22                                   
REMARK 500    SER C 216     -140.09    -76.69                                   
REMARK 500    GLU C 217      -95.78    -91.81                                   
REMARK 500    GLU C 219      179.50    -48.77                                   
REMARK 500    ASP C 225      173.88    -45.67                                   
REMARK 500    VAL C 240      -66.67   -104.66                                   
REMARK 500    ARG C 247      144.95    -21.45                                   
REMARK 500    ASP C 254      144.28    176.51                                   
REMARK 500    ASP C 264      141.39    -36.31                                   
REMARK 500    GLU C 280      -82.76   -174.60                                   
REMARK 500    ARG C 281       20.98   -155.46                                   
REMARK 500    TYR C 283     -169.35   -115.45                                   
REMARK 500    SER C 287       63.97   -103.34                                   
REMARK 500    GLN C 288       24.20     38.18                                   
REMARK 500    GLU C 289      -88.59   -150.30                                   
REMARK 500    GLN C 293      174.07    -49.17                                   
REMARK 500    GLN C 295      -27.29   -142.02                                   
REMARK 500    ALA C 296       75.27     61.56                                   
REMARK 500    CYS C 299      -41.47   -154.27                                   
REMARK 500    PRO C 300       70.62    -59.93                                   
REMARK 500    GLU C 302      157.94    171.97                                   
REMARK 500    LYS C 305       56.47   -166.11                                   
REMARK 500    ASP C 310      104.40    -46.91                                   
REMARK 500    GLU C 328       38.62    -82.17                                   
REMARK 500    PRO C 332      150.23    -41.74                                   
REMARK 500    ALA C 355      136.74    -32.55                                   
REMARK 500    PRO C 366      -17.36    -41.02                                   
REMARK 500    ASN C 367       41.04   -102.08                                   
REMARK 500    ARG C 382      -60.36    -95.33                                   
REMARK 500    ALA C 396        2.83    -61.34                                   
REMARK 500    GLU C 399      -69.01    -25.39                                   
REMARK 500    TRP C 401      115.01     -4.76                                   
REMARK 500    THR C 424      -94.22   -114.25                                   
REMARK 500    SER C 425      -23.37    156.30                                   
REMARK 500    LEU K1921      -68.47   -171.11                                   
REMARK 500    HIS K1922       45.25    -81.35                                   
REMARK 500    SER K1952       70.51     25.80                                   
REMARK 500    SER K2018       25.73    -78.86                                   
REMARK 500    ASN K2051       39.47    -89.29                                   
REMARK 500    MET K2094       41.54   -109.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DG X   0         0.06    SIDE_CHAIN                              
REMARK 500     DT X   1         0.08    SIDE_CHAIN                              
REMARK 500     DA X  12         0.06    SIDE_CHAIN                              
REMARK 500     DA X  13         0.05    SIDE_CHAIN                              
REMARK 500     DG Y 114         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2F8X C    9   435  UNP    Q06330   SUH_HUMAN       23    449             
DBREF  2F8X K 1873  2127  UNP    P46531   NOTC1_HUMAN   1873   2127             
DBREF  2F8X M   13    74  UNP    Q92585   MAML1_HUMAN     13     74             
DBREF  2F8X X    0    17  PDB    2F8X     2F8X             0     17             
DBREF  2F8X Y  101   118  PDB    2F8X     2F8X           101    118             
SEQADV 2F8X MET C    8  UNP  Q06330              INITIATING METHIONINE          
SEQADV 2F8X HIS C  436  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X HIS C  437  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X HIS C  438  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X HIS C  439  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X HIS C  440  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X HIS C  441  UNP  Q06330              EXPRESSION TAG                 
SEQADV 2F8X GLY K 1872  UNP  P46531              CLONING ARTIFACT               
SEQADV 2F8X GLY M   12  UNP  Q92585              CLONING ARTIFACT               
SEQRES   1 X   18   DG  DT  DT  DA  DC  DT  DG  DT  DG  DG  DG  DA  DA          
SEQRES   2 X   18   DA  DG  DA  DA  DA                                          
SEQRES   1 Y   18   DT  DT  DT  DC  DT  DT  DT  DC  DC  DC  DA  DC  DA          
SEQRES   2 Y   18   DG  DT  DA  DA  DC                                          
SEQRES   1 C  434  MET GLY GLU ARG PRO PRO PRO LYS ARG LEU THR ARG GLU          
SEQRES   2 C  434  ALA MET ARG ASN TYR LEU LYS GLU ARG GLY ASP GLN THR          
SEQRES   3 C  434  VAL LEU ILE LEU HIS ALA LYS VAL ALA GLN LYS SER TYR          
SEQRES   4 C  434  GLY ASN GLU LYS ARG PHE PHE CYS PRO PRO PRO CYS VAL          
SEQRES   5 C  434  TYR LEU MET GLY SER GLY TRP LYS LYS LYS LYS GLU GLN          
SEQRES   6 C  434  MET GLU ARG ASP GLY CYS SER GLU GLN GLU SER GLN PRO          
SEQRES   7 C  434  CYS ALA PHE ILE GLY ILE GLY ASN SER ASP GLN GLU MET          
SEQRES   8 C  434  GLN GLN LEU ASN LEU GLU GLY LYS ASN TYR CYS THR ALA          
SEQRES   9 C  434  LYS THR LEU TYR ILE SER ASP SER ASP LYS ARG LYS HIS          
SEQRES  10 C  434  PHE MET LEU SER VAL LYS MET PHE TYR GLY ASN SER ASP          
SEQRES  11 C  434  ASP ILE GLY VAL PHE LEU SER LYS ARG ILE LYS VAL ILE          
SEQRES  12 C  434  SER LYS PRO SER LYS LYS LYS GLN SER LEU LYS ASN ALA          
SEQRES  13 C  434  ASP LEU CYS ILE ALA SER GLY THR LYS VAL ALA LEU PHE          
SEQRES  14 C  434  ASN ARG LEU ARG SER GLN THR VAL SER THR ARG TYR LEU          
SEQRES  15 C  434  HIS VAL GLU GLY GLY ASN PHE HIS ALA SER SER GLN GLN          
SEQRES  16 C  434  TRP GLY ALA PHE PHE ILE HIS LEU LEU ASP ASP ASP GLU          
SEQRES  17 C  434  SER GLU GLY GLU GLU PHE THR VAL ARG ASP GLY TYR ILE          
SEQRES  18 C  434  HIS TYR GLY GLN THR VAL LYS LEU VAL CYS SER VAL THR          
SEQRES  19 C  434  GLY MET ALA LEU PRO ARG LEU ILE ILE ARG LYS VAL ASP          
SEQRES  20 C  434  LYS GLN THR ALA LEU LEU ASP ALA ASP ASP PRO VAL SER          
SEQRES  21 C  434  GLN LEU HIS LYS CYS ALA PHE TYR LEU LYS ASP THR GLU          
SEQRES  22 C  434  ARG MET TYR LEU CYS LEU SER GLN GLU ARG ILE ILE GLN          
SEQRES  23 C  434  PHE GLN ALA THR PRO CYS PRO LYS GLU PRO ASN LYS GLU          
SEQRES  24 C  434  MET ILE ASN ASP GLY ALA SER TRP THR ILE ILE SER THR          
SEQRES  25 C  434  ASP LYS ALA GLU TYR THR PHE TYR GLU GLY MET GLY PRO          
SEQRES  26 C  434  VAL LEU ALA PRO VAL THR PRO VAL PRO VAL VAL GLU SER          
SEQRES  27 C  434  LEU GLN LEU ASN GLY GLY GLY ASP VAL ALA MET LEU GLU          
SEQRES  28 C  434  LEU THR GLY GLN ASN PHE THR PRO ASN LEU ARG VAL TRP          
SEQRES  29 C  434  PHE GLY ASP VAL GLU ALA GLU THR MET TYR ARG CYS GLY          
SEQRES  30 C  434  GLU SER MET LEU CYS VAL VAL PRO ASP ILE SER ALA PHE          
SEQRES  31 C  434  ARG GLU GLY TRP ARG TRP VAL ARG GLN PRO VAL GLN VAL          
SEQRES  32 C  434  PRO VAL THR LEU VAL ARG ASN ASP GLY ILE ILE TYR SER          
SEQRES  33 C  434  THR SER LEU THR PHE THR TYR THR PRO GLU PRO GLY HIS          
SEQRES  34 C  434  HIS HIS HIS HIS HIS                                          
SEQRES   1 K  256  GLY MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR          
SEQRES   2 K  256  PRO LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU          
SEQRES   3 K  256  THR GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL          
SEQRES   4 K  256  ILE SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN          
SEQRES   5 K  256  GLN THR ASP ARG THR GLY GLU THR ALA LEU HIS LEU ALA          
SEQRES   6 K  256  ALA ARG TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU          
SEQRES   7 K  256  GLU ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY          
SEQRES   8 K  256  ARG THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN          
SEQRES   9 K  256  GLY VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP          
SEQRES  10 K  256  LEU ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE          
SEQRES  11 K  256  LEU ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP          
SEQRES  12 K  256  LEU ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP          
SEQRES  13 K  256  LEU GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN          
SEQRES  14 K  256  ASN VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA          
SEQRES  15 K  256  ASN LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU          
SEQRES  16 K  256  PHE LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS          
SEQRES  17 K  256  VAL LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP          
SEQRES  18 K  256  HIS MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG          
SEQRES  19 K  256  MET HIS HIS ASP ILE VAL ARG LEU LEU ASP GLU TYR ASN          
SEQRES  20 K  256  LEU VAL ARG SER PRO GLN LEU HIS GLY                          
SEQRES   1 M   63  GLY LEU PRO ARG HIS SER ALA VAL MET GLU ARG LEU ARG          
SEQRES   2 M   63  ARG ARG ILE GLU LEU CYS ARG ARG HIS HIS SER THR CYS          
SEQRES   3 M   63  GLU ALA ARG TYR GLU ALA VAL SER PRO GLU ARG LEU GLU          
SEQRES   4 M   63  LEU GLU ARG GLN HIS THR PHE ALA LEU HIS GLN ARG CYS          
SEQRES   5 M   63  ILE GLN ALA LYS ALA LYS ARG ALA GLY LYS HIS                  
FORMUL   6  HOH   *10(H2 O)                                                     
HELIX    1   1 THR C   18  GLU C   28  1                                  11    
HELIX    2   2 SER C   64  ARG C   75  1                                  12    
HELIX    3   3 ARG C  178  GLN C  182  5                                   5    
HELIX    4   4 GLY C  351  VAL C  354  5                                   4    
HELIX    5   5 ASP C  393  ARG C  398  5                                   6    
HELIX    6   6 THR K 1884  SER K 1892  1                                   9    
HELIX    7   7 ALA K 1909  TYR K 1916  1                                   8    
HELIX    8   8 THR K 1931  TYR K 1939  1                                   9    
HELIX    9   9 ARG K 1941  ALA K 1951  1                                  11    
HELIX   10  10 THR K 1964  ALA K 1972  1                                   9    
HELIX   11  11 ALA K 1974  ASN K 1984  1                                  11    
HELIX   12  12 THR K 1998  LEU K 2006  1                                   9    
HELIX   13  13 GLY K 2010  SER K 2018  1                                   9    
HELIX   14  14 SER K 2031  VAL K 2039  1                                   9    
HELIX   15  15 ASN K 2041  ASN K 2051  1                                  11    
HELIX   16  16 THR K 2064  GLY K 2073  1                                  10    
HELIX   17  17 SER K 2074  HIS K 2084  1                                  11    
HELIX   18  18 LEU K 2097  ARG K 2105  1                                   9    
HELIX   19  19 HIS K 2107  TYR K 2117  1                                  11    
HELIX   20  20 HIS M   16  ARG M   70  1                                  55    
SHEET    1   A 2 GLN C  32  THR C  33  0                                        
SHEET    2   A 2 THR C 325  PHE C 326 -1  O  PHE C 326   N  GLN C  32           
SHEET    1   B 2 ILE C  36  ALA C  39  0                                        
SHEET    2   B 2 CYS C  58  VAL C  59 -1  O  CYS C  58   N  LEU C  37           
SHEET    1   C 4 ILE C  36  ALA C  39  0                                        
SHEET    2   C 4 TRP C 314  ALA C 322 -1  O  ALA C 322   N  ILE C  36           
SHEET    3   C 4 LYS C 172  ASN C 177 -1  N  ALA C 174   O  ILE C 317           
SHEET    4   C 4 ARG C 187  TYR C 188 -1  O  ARG C 187   N  ASN C 177           
SHEET    1   D 8 ILE C  36  ALA C  39  0                                        
SHEET    2   D 8 TRP C 314  ALA C 322 -1  O  ALA C 322   N  ILE C  36           
SHEET    3   D 8 LYS C 172  ASN C 177 -1  N  ALA C 174   O  ILE C 317           
SHEET    4   D 8 PHE C 206  LEU C 211 -1  O  PHE C 206   N  VAL C 173           
SHEET    5   D 8 THR C 233  CYS C 238 -1  O  VAL C 237   N  PHE C 207           
SHEET    6   D 8 LEU C 248  ASP C 254 -1  O  LEU C 248   N  VAL C 234           
SHEET    7   D 8 THR C 257  LEU C 259 -1  O  THR C 257   N  ASP C 254           
SHEET    8   D 8 LYS C 305  MET C 307 -1  O  GLU C 306   N  ALA C 258           
SHEET    1   E 7 ILE C  36  ALA C  39  0                                        
SHEET    2   E 7 TRP C 314  ALA C 322 -1  O  ALA C 322   N  ILE C  36           
SHEET    3   E 7 LYS C 172  ASN C 177 -1  N  ALA C 174   O  ILE C 317           
SHEET    4   E 7 PHE C 206  LEU C 211 -1  O  PHE C 206   N  VAL C 173           
SHEET    5   E 7 THR C 233  CYS C 238 -1  O  VAL C 237   N  PHE C 207           
SHEET    6   E 7 LEU C 248  ASP C 254 -1  O  LEU C 248   N  VAL C 234           
SHEET    7   E 7 HIS C 270  TYR C 275 -1  O  ALA C 273   N  ARG C 251           
SHEET    1   F 3 VAL C  41  GLN C  43  0                                        
SHEET    2   F 3 ILE C 147  ILE C 150  1  O  ILE C 150   N  ALA C  42           
SHEET    3   F 3 HIS C 124  PHE C 125 -1  N  PHE C 125   O  ILE C 147           
SHEET    1   G 4 GLN C  99  GLN C 100  0                                        
SHEET    2   G 4 PHE C  88  ILE C  91 -1  N  ILE C  89   O  GLN C  99           
SHEET    3   G 4 LEU C 127  PHE C 132 -1  O  SER C 128   N  GLY C  90           
SHEET    4   G 4 ASP C 138  LEU C 143 -1  O  PHE C 142   N  VAL C 129           
SHEET    1   H 2 HIS C 190  GLU C 192  0                                        
SHEET    2   H 2 ASN C 195  HIS C 197 -1  O  ASN C 195   N  GLU C 192           
SHEET    1   I 2 CYS C 285  LEU C 286  0                                        
SHEET    2   I 2 ILE C 291  ILE C 292 -1  O  ILE C 292   N  CYS C 285           
SHEET    1   J 4 VAL C 342  LEU C 348  0                                        
SHEET    2   J 4 MET C 356  GLN C 362 -1  O  THR C 360   N  SER C 345           
SHEET    3   J 4 SER C 386  VAL C 390 -1  O  MET C 387   N  LEU C 359           
SHEET    4   J 4 THR C 379  CYS C 383 -1  N  MET C 380   O  LEU C 388           
SHEET    1   K 4 VAL C 375  ALA C 377  0                                        
SHEET    2   K 4 LEU C 368  PHE C 372 -1  N  PHE C 372   O  VAL C 375           
SHEET    3   K 4 VAL C 412  ARG C 416 -1  O  THR C 413   N  TRP C 371           
SHEET    4   K 4 ILE C 421  SER C 423 -1  O  TYR C 422   N  LEU C 414           
SHEET    1   L 2 VAL C 408  GLN C 409  0                                        
SHEET    2   L 2 THR C 429  TYR C 430 -1  O  TYR C 430   N  VAL C 408           
CISPEP   1 CYS C   54    PRO C   55          0        -0.09                     
CISPEP   2 THR C  338    PRO C  339          0         0.02                     
CRYST1  273.866  273.866  121.016  90.00  90.00 120.00 P 63 2 2     12          
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      0.003651  0.002108  0.000000        0.00000                         
SCALE2      0.000000  0.004216  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008263        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system