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Database: PDB
Entry: 4OR5
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Original site: 4OR5 
HEADER    TRANSFERASE/TRANSCRIPTION               10-FEB-14   4OR5              
TITLE     CRYSTAL STRUCTURE OF HIV-1 TAT COMPLEXED WITH HUMAN P-TEFB AND AFF4   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 9;                                 
COMPND   3 CHAIN: A, F;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 7-332;                                        
COMPND   5 SYNONYM: C-2K, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4, CELL     
COMPND   6 DIVISION PROTEIN KINASE 9, SERINE/THREONINE-PROTEIN KINASE PITALRE,  
COMPND   7 TAT-ASSOCIATED KINASE COMPLEX CATALYTIC SUBUNIT;                     
COMPND   8 EC: 2.7.11.22, 2.7.11.23;                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: CYCLIN-T1;                                                 
COMPND  12 CHAIN: B, G;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 1-226;                                        
COMPND  14 SYNONYM: CYCT1, CYCLIN-T;                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: PROTEIN TAT;                                               
COMPND  18 CHAIN: C, H;                                                         
COMPND  19 FRAGMENT: UNP RESIDUES 1-48;                                         
COMPND  20 SYNONYM: TRANSACTIVATING REGULATORY PROTEIN;                         
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: AF4/FMR2 FAMILY MEMBER 4;                                  
COMPND  24 CHAIN: E, J;                                                         
COMPND  25 FRAGMENT: UNP RESIDUES 32-69;                                        
COMPND  26 SYNONYM: ALL1-FUSED GENE FROM CHROMOSOME 5Q31 PROTEIN, PROTEIN AF-   
COMPND  27 5Q31, MAJOR CDK9 ELONGATION FACTOR-ASSOCIATED PROTEIN;               
COMPND  28 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK9, CDC2L4, TAK;                                             
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 GENE: CCNT1;                                                         
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HIV-1;                                          
SOURCE  13 ORGANISM_TAXID: 11706;                                               
SOURCE  14 STRAIN: ISOLATE HXB2;                                                
SOURCE  15 GENE: TAT;                                                           
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 GENE: AFF4, AF5Q31, MCEF, HSPC092                                    
KEYWDS    CDK9, TAT, AFF4, ZINC FINGER, TRANSCRIPTION, RNA BINDING,             
KEYWDS   2 PHOSPHORYLATION, TRANSFERASE-TRANSCRIPTION COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GU,N.D.BABAYEVA,Y.SUWA,A.G.BARANOVSKIY,D.H.PRICE,T.H.TAHIROV        
REVDAT   2   11-JUN-14 4OR5    1       JRNL                                     
REVDAT   1   16-APR-14 4OR5    0                                                
JRNL        AUTH   J.GU,N.D.BABAYEVA,Y.SUWA,A.G.BARANOVSKIY,D.H.PRICE,          
JRNL        AUTH 2 T.H.TAHIROV                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF HIV-1 TAT COMPLEXED WITH HUMAN P-TEFB   
JRNL        TITL 2 AND AFF4.                                                    
JRNL        REF    CELL CYCLE                    V.  13  1788 2014              
JRNL        REFN                   ISSN 1538-4101                               
JRNL        PMID   24727379                                                     
JRNL        DOI    10.4161/CC.28756                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 5136435.760                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 60890                          
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) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3092                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8981                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4220                       
REMARK   3   BIN FREE R VALUE                    : 0.4560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 478                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10755                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 100                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.59000                                              
REMARK   3    B22 (A**2) : -1.23000                                             
REMARK   3    B33 (A**2) : -0.36000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 12.99000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.41                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.80                            
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) : 0.50                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.92                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.900                          
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.910                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.740 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.020 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 5.010 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 7.310 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 25.65                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NONE                                                    
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4OR5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-FEB-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB084846.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.08300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH6.5, 3.7-3.75% W/V PEG       
REMARK 280  20000, 5 MM YCL3, 200 MM NDSB 211, 2 MM TCEP PH7.5, VAPOR           
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 295K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       83.43100            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       93.36950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       83.43100            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       93.36950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 30940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12680 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -199.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G, H, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH F 519  LIES ON A SPECIAL POSITION.                          
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     SER A     7                                                      
REMARK 465     TYR A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     CYS A    95                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     ALA B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     LYS B   266                                                      
REMARK 465     GLU E    27                                                      
REMARK 465     GLN E    28                                                      
REMARK 465     ILE E    29                                                      
REMARK 465     GLY E    30                                                      
REMARK 465     GLY E    31                                                      
REMARK 465     SER F     7                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLU G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     GLU G     4                                                      
REMARK 465     ARG G     5                                                      
REMARK 465     LYS G     6                                                      
REMARK 465     GLU G   262                                                      
REMARK 465     ALA G   263                                                      
REMARK 465     ALA G   264                                                      
REMARK 465     LYS G   265                                                      
REMARK 465     LYS G   266                                                      
REMARK 465     GLU J    27                                                      
REMARK 465     GLN J    28                                                      
REMARK 465     ILE J    29                                                      
REMARK 465     GLY J    30                                                      
REMARK 465     GLY J    31                                                      
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   OD2  ASP F   305     Y    YT3 F   401              1.89            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   263     Y    YT3 E   101     2556     1.60            
REMARK 500   OE2  GLU B    17     Y    YT3 B   303     2555     1.70            
REMARK 500   OE2  GLU G    17     Y    YT3 G   301     2555     1.80            
REMARK 500   OE1  GLU B   124     Y    YT3 F   403     2555     1.95            
REMARK 500   Y    YT3 A   403     Y    YT3 B   302     2556     1.95            
REMARK 500   OE1  GLU B    20     Y    YT3 B   303     2555     2.02            
REMARK 500   OD1  ASN A   311     Y    YT3 F   401     3445     2.03            
REMARK 500   OE1  GLU A   266     Y    YT3 E   101     2556     2.09            
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    CYS A  10       50.35   -158.04                                   
REMARK 500    LYS A  18      -13.41    -47.82                                   
REMARK 500    GLN A  27       76.45   -107.61                                   
REMARK 500    PHE A  30      -71.23    -44.71                                   
REMARK 500    GLU A  32      -87.99    -88.53                                   
REMARK 500    ASN A  54       44.22    -82.08                                   
REMARK 500    GLU A  55        7.81    -60.18                                   
REMARK 500    LYS A  56      -85.88    -70.89                                   
REMARK 500    GLU A  57       22.15    -76.58                                   
REMARK 500    LYS A 151      149.60    176.10                                   
REMARK 500    ASP A 167       76.04     69.01                                   
REMARK 500    ALA A 177       67.20   -104.50                                   
REMARK 500    ASN A 179     -115.81    -63.62                                   
REMARK 500    SER A 180     -140.75    -69.80                                   
REMARK 500    ARG A 184       72.46   -112.12                                   
REMARK 500    VAL A 190      129.47     76.25                                   
REMARK 500    PRO A 209      -16.68    -43.88                                   
REMARK 500    SER A 226      141.95   -178.72                                   
REMARK 500    PRO A 227      117.56    -37.85                                   
REMARK 500    GLU A 263        6.33    -50.74                                   
REMARK 500    GLU A 266      -43.46    -28.15                                   
REMARK 500    VAL A 268       71.50   -104.08                                   
REMARK 500    VAL A 275      -71.67    -41.21                                   
REMARK 500    ARG A 284      -68.28     74.06                                   
REMARK 500    LEU A 296       55.17    -91.90                                   
REMARK 500    TRP A 316       65.19   -161.85                                   
REMARK 500    SER A 317      137.52   -174.99                                   
REMARK 500    ASP A 323     -173.32    -60.12                                   
REMARK 500    SER A 329      107.76    -29.02                                   
REMARK 500    THR A 330      128.98     -0.69                                   
REMARK 500    ILE B  72      -61.39   -103.23                                   
REMARK 500    GLN B  97       55.02   -143.86                                   
REMARK 500    GLU B 116      172.27    -45.50                                   
REMARK 500    LEU B 118      101.97    -55.27                                   
REMARK 500    THR B 121       14.67    -57.97                                   
REMARK 500    PRO B 249       33.27    -70.74                                   
REMARK 500    ASN B 250      109.90    -21.18                                   
REMARK 500    LYS B 253      -10.28    -38.26                                   
REMARK 500    TRP B 256      -32.95    -39.62                                   
REMARK 500    TRP B 258      -70.86    -35.89                                   
REMARK 500    ALA B 260     -148.87   -116.09                                   
REMARK 500    CYS B 261     -177.17   -174.53                                   
REMARK 500    GLU E  45       51.26   -140.89                                   
REMARK 500    LYS E  63      -46.28    -19.39                                   
REMARK 500    PHE F  30      -72.33    -52.14                                   
REMARK 500    LYS F  56      -62.89   -157.40                                   
REMARK 500    GLU F  57       23.28    -79.46                                   
REMARK 500    VAL F  79      154.70    -49.99                                   
REMARK 500    THR F  87      -74.70   -112.16                                   
REMARK 500    LYS F  88     -149.21    -98.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 RAMACHANDRAN OUTLIERS.                        
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    TYR F  19         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    TRP B 258        21.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 G 301   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 240   OE2                                                    
REMARK 620 2 GLU G 240   OE1  63.2                                              
REMARK 620 3 GLN G 243   OE1 124.9  65.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 B 303   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 240   OE1                                                    
REMARK 620 2 GLN B 243   OE1  78.9                                              
REMARK 620 3 GLU B 240   OE2  50.9  76.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 E 102   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  37   OE1                                                    
REMARK 620 2 GLU E  37   OE2  50.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 B 301   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 169   OD2                                                    
REMARK 620 2 ARG E  69   OXT 162.3                                              
REMARK 620 3 ARG E  69   O   140.6  51.0                                        
REMARK 620 4 GLN B 172   OE1  74.1 123.5  80.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  33   ND1                                                    
REMARK 620 2 CYS H  37   SG  104.2                                              
REMARK 620 3 CYS H  22   SG   90.0 106.6                                        
REMARK 620 4 CYS H  34   SG  115.6 133.9  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 101  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  33   ND1                                                    
REMARK 620 2 CYS C  37   SG  118.7                                              
REMARK 620 3 CYS C  22   SG   82.2 118.5                                        
REMARK 620 4 CYS C  34   SG  102.8 124.9 100.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  27   SG                                                     
REMARK 620 2 CYS C  25   SG   90.6                                              
REMARK 620 3 CYS B 261   SG  113.0 128.4                                        
REMARK 620 4 CYS C  30   SG   99.8 113.7 106.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 102  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H  27   SG                                                     
REMARK 620 2 CYS H  25   SG   91.2                                              
REMARK 620 3 CYS H  30   SG  142.4 107.8                                        
REMARK 620 4 CYS G 261   SG  138.2  91.4  75.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 G 302   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G 169   OD1                                                    
REMARK 620 2 GLN G 172   OE1  78.0                                              
REMARK 620 3 ARG J  69   O   155.8  78.3                                        
REMARK 620 4 ARG J  69   OXT 158.5 123.3  45.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 F 402   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 167   OD2                                                    
REMARK 620 2 ASP F 149   OD2  88.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 J 101   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG J  69   OXT                                                    
REMARK 620 2 ARG J  69   NH1  81.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 401   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 167   OD2                                                    
REMARK 620 2 ASP A 149   OD2  57.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 B 302   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 169   OD1                                                    
REMARK 620 2 ASP E  64   OD1 143.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 F 403   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F  15   OE2                                                    
REMARK 620 2 GLU F  15   OE1  48.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 G 303   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  64   OD1                                                    
REMARK 620 2 ASP G 169   OD2 105.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 F 401   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 308   OD2                                                    
REMARK 620 2 ASP F 305   OD1  53.9                                              
REMARK 620 3 ASP F 308   OD1  41.8  71.6                                        
REMARK 620 4 ASP F 307   OD1 124.0  93.9  88.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 402   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 305   OD2                                                    
REMARK 620 2 ASP A 308   OD2  62.8                                              
REMARK 620 3 ASP A 305   OD1  45.2  79.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 F 404   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 266   OE2                                                    
REMARK 620 2 GLU F 266   OE1  43.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             YT3 A 403   Y                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 266   OE1                                                    
REMARK 620 2 GLU A 266   OE2  38.9                                              
REMARK 620 3 LYS A 269   NZ   81.1  52.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 F 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 F 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 F 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 G 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 G 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 G 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YT3 J 101                 
DBREF  4OR5 A    7   332  UNP    P50750   CDK9_HUMAN       7    332             
DBREF  4OR5 B    1   266  UNP    O60563   CCNT1_HUMAN      1    266             
DBREF  4OR5 C    1    48  UNP    P04608   TAT_HV1H2        1     48             
DBREF  4OR5 E   32    69  UNP    Q9UHB7   AFF4_HUMAN      32     69             
DBREF  4OR5 F    7   332  UNP    P50750   CDK9_HUMAN       7    332             
DBREF  4OR5 G    1   266  UNP    O60563   CCNT1_HUMAN      1    266             
DBREF  4OR5 H    1    48  UNP    P04608   TAT_HV1H2        1     48             
DBREF  4OR5 J   32    69  UNP    Q9UHB7   AFF4_HUMAN      32     69             
SEQADV 4OR5 GLU E   27  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLN E   28  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 ILE E   29  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLY E   30  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLY E   31  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLU J   27  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLN J   28  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 ILE J   29  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLY J   30  UNP  Q9UHB7              EXPRESSION TAG                 
SEQADV 4OR5 GLY J   31  UNP  Q9UHB7              EXPRESSION TAG                 
SEQRES   1 A  326  SER VAL GLU CYS PRO PHE CYS ASP GLU VAL SER LYS TYR          
SEQRES   2 A  326  GLU LYS LEU ALA LYS ILE GLY GLN GLY THR PHE GLY GLU          
SEQRES   3 A  326  VAL PHE LYS ALA ARG HIS ARG LYS THR GLY GLN LYS VAL          
SEQRES   4 A  326  ALA LEU LYS LYS VAL LEU MET GLU ASN GLU LYS GLU GLY          
SEQRES   5 A  326  PHE PRO ILE THR ALA LEU ARG GLU ILE LYS ILE LEU GLN          
SEQRES   6 A  326  LEU LEU LYS HIS GLU ASN VAL VAL ASN LEU ILE GLU ILE          
SEQRES   7 A  326  CYS ARG THR LYS ALA SER PRO TYR ASN ARG CYS LYS GLY          
SEQRES   8 A  326  SER ILE TYR LEU VAL PHE ASP PHE CYS GLU HIS ASP LEU          
SEQRES   9 A  326  ALA GLY LEU LEU SER ASN VAL LEU VAL LYS PHE THR LEU          
SEQRES  10 A  326  SER GLU ILE LYS ARG VAL MET GLN MET LEU LEU ASN GLY          
SEQRES  11 A  326  LEU TYR TYR ILE HIS ARG ASN LYS ILE LEU HIS ARG ASP          
SEQRES  12 A  326  MET LYS ALA ALA ASN VAL LEU ILE THR ARG ASP GLY VAL          
SEQRES  13 A  326  LEU LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE SER          
SEQRES  14 A  326  LEU ALA LYS ASN SER GLN PRO ASN ARG TYR TPO ASN ARG          
SEQRES  15 A  326  VAL VAL THR LEU TRP TYR ARG PRO PRO GLU LEU LEU LEU          
SEQRES  16 A  326  GLY GLU ARG ASP TYR GLY PRO PRO ILE ASP LEU TRP GLY          
SEQRES  17 A  326  ALA GLY CYS ILE MET ALA GLU MET TRP THR ARG SER PRO          
SEQRES  18 A  326  ILE MET GLN GLY ASN THR GLU GLN HIS GLN LEU ALA LEU          
SEQRES  19 A  326  ILE SER GLN LEU CYS GLY SER ILE THR PRO GLU VAL TRP          
SEQRES  20 A  326  PRO ASN VAL ASP ASN TYR GLU LEU TYR GLU LYS LEU GLU          
SEQRES  21 A  326  LEU VAL LYS GLY GLN LYS ARG LYS VAL LYS ASP ARG LEU          
SEQRES  22 A  326  LYS ALA TYR VAL ARG ASP PRO TYR ALA LEU ASP LEU ILE          
SEQRES  23 A  326  ASP LYS LEU LEU VAL LEU ASP PRO ALA GLN ARG ILE ASP          
SEQRES  24 A  326  SER ASP ASP ALA LEU ASN HIS ASP PHE PHE TRP SER ASP          
SEQRES  25 A  326  PRO MET PRO SER ASP LEU LYS GLY MET LEU SER THR HIS          
SEQRES  26 A  326  LEU                                                          
SEQRES   1 B  266  MET GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP TYR          
SEQRES   2 B  266  PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG ARG          
SEQRES   3 B  266  PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG GLN          
SEQRES   4 B  266  GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG LEU          
SEQRES   5 B  266  ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL TYR          
SEQRES   6 B  266  MET HIS ARG PHE TYR MET ILE GLN SER PHE THR GLN PHE          
SEQRES   7 B  266  PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU ALA          
SEQRES   8 B  266  ALA LYS VAL GLU GLU GLN PRO LYS LYS LEU GLU HIS VAL          
SEQRES   9 B  266  ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU SER          
SEQRES  10 B  266  LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN VAL          
SEQRES  11 B  266  GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN THR          
SEQRES  12 B  266  LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR HIS          
SEQRES  13 B  266  VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS ASP          
SEQRES  14 B  266  LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER LEU          
SEQRES  15 B  266  HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO VAL          
SEQRES  16 B  266  VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP SER          
SEQRES  17 B  266  ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS TRP          
SEQRES  18 B  266  TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU LEU          
SEQRES  19 B  266  ASP GLU LEU THR HIS GLU PHE LEU GLN ILE LEU GLU LYS          
SEQRES  20 B  266  THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG ALA          
SEQRES  21 B  266  CYS GLU ALA ALA LYS LYS                                      
SEQRES   1 C   48  MET GLU PRO VAL ASP PRO ARG LEU GLU PRO TRP LYS HIS          
SEQRES   2 C   48  PRO GLY SER GLN PRO LYS THR ALA CYS THR ASN CYS TYR          
SEQRES   3 C   48  CYS LYS LYS CYS CYS PHE HIS CYS GLN VAL CYS PHE ILE          
SEQRES   4 C   48  THR LYS ALA LEU GLY ILE SER TYR GLY                          
SEQRES   1 E   43  GLU GLN ILE GLY GLY SER PRO LEU PHE ALA GLU PRO TYR          
SEQRES   2 E   43  LYS VAL THR SER LYS GLU ASP LYS LEU SER SER ARG ILE          
SEQRES   3 E   43  GLN SER MET LEU GLY ASN TYR ASP GLU MET LYS ASP PHE          
SEQRES   4 E   43  ILE GLY ASP ARG                                              
SEQRES   1 F  326  SER VAL GLU CYS PRO PHE CYS ASP GLU VAL SER LYS TYR          
SEQRES   2 F  326  GLU LYS LEU ALA LYS ILE GLY GLN GLY THR PHE GLY GLU          
SEQRES   3 F  326  VAL PHE LYS ALA ARG HIS ARG LYS THR GLY GLN LYS VAL          
SEQRES   4 F  326  ALA LEU LYS LYS VAL LEU MET GLU ASN GLU LYS GLU GLY          
SEQRES   5 F  326  PHE PRO ILE THR ALA LEU ARG GLU ILE LYS ILE LEU GLN          
SEQRES   6 F  326  LEU LEU LYS HIS GLU ASN VAL VAL ASN LEU ILE GLU ILE          
SEQRES   7 F  326  CYS ARG THR LYS ALA SER PRO TYR ASN ARG CYS LYS GLY          
SEQRES   8 F  326  SER ILE TYR LEU VAL PHE ASP PHE CYS GLU HIS ASP LEU          
SEQRES   9 F  326  ALA GLY LEU LEU SER ASN VAL LEU VAL LYS PHE THR LEU          
SEQRES  10 F  326  SER GLU ILE LYS ARG VAL MET GLN MET LEU LEU ASN GLY          
SEQRES  11 F  326  LEU TYR TYR ILE HIS ARG ASN LYS ILE LEU HIS ARG ASP          
SEQRES  12 F  326  MET LYS ALA ALA ASN VAL LEU ILE THR ARG ASP GLY VAL          
SEQRES  13 F  326  LEU LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE SER          
SEQRES  14 F  326  LEU ALA LYS ASN SER GLN PRO ASN ARG TYR TPO ASN ARG          
SEQRES  15 F  326  VAL VAL THR LEU TRP TYR ARG PRO PRO GLU LEU LEU LEU          
SEQRES  16 F  326  GLY GLU ARG ASP TYR GLY PRO PRO ILE ASP LEU TRP GLY          
SEQRES  17 F  326  ALA GLY CYS ILE MET ALA GLU MET TRP THR ARG SER PRO          
SEQRES  18 F  326  ILE MET GLN GLY ASN THR GLU GLN HIS GLN LEU ALA LEU          
SEQRES  19 F  326  ILE SER GLN LEU CYS GLY SER ILE THR PRO GLU VAL TRP          
SEQRES  20 F  326  PRO ASN VAL ASP ASN TYR GLU LEU TYR GLU LYS LEU GLU          
SEQRES  21 F  326  LEU VAL LYS GLY GLN LYS ARG LYS VAL LYS ASP ARG LEU          
SEQRES  22 F  326  LYS ALA TYR VAL ARG ASP PRO TYR ALA LEU ASP LEU ILE          
SEQRES  23 F  326  ASP LYS LEU LEU VAL LEU ASP PRO ALA GLN ARG ILE ASP          
SEQRES  24 F  326  SER ASP ASP ALA LEU ASN HIS ASP PHE PHE TRP SER ASP          
SEQRES  25 F  326  PRO MET PRO SER ASP LEU LYS GLY MET LEU SER THR HIS          
SEQRES  26 F  326  LEU                                                          
SEQRES   1 G  266  MET GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP TYR          
SEQRES   2 G  266  PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG ARG          
SEQRES   3 G  266  PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG GLN          
SEQRES   4 G  266  GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG LEU          
SEQRES   5 G  266  ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL TYR          
SEQRES   6 G  266  MET HIS ARG PHE TYR MET ILE GLN SER PHE THR GLN PHE          
SEQRES   7 G  266  PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU ALA          
SEQRES   8 G  266  ALA LYS VAL GLU GLU GLN PRO LYS LYS LEU GLU HIS VAL          
SEQRES   9 G  266  ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU SER          
SEQRES  10 G  266  LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN VAL          
SEQRES  11 G  266  GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN THR          
SEQRES  12 G  266  LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR HIS          
SEQRES  13 G  266  VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS ASP          
SEQRES  14 G  266  LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER LEU          
SEQRES  15 G  266  HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO VAL          
SEQRES  16 G  266  VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP SER          
SEQRES  17 G  266  ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS TRP          
SEQRES  18 G  266  TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU LEU          
SEQRES  19 G  266  ASP GLU LEU THR HIS GLU PHE LEU GLN ILE LEU GLU LYS          
SEQRES  20 G  266  THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG ALA          
SEQRES  21 G  266  CYS GLU ALA ALA LYS LYS                                      
SEQRES   1 H   48  MET GLU PRO VAL ASP PRO ARG LEU GLU PRO TRP LYS HIS          
SEQRES   2 H   48  PRO GLY SER GLN PRO LYS THR ALA CYS THR ASN CYS TYR          
SEQRES   3 H   48  CYS LYS LYS CYS CYS PHE HIS CYS GLN VAL CYS PHE ILE          
SEQRES   4 H   48  THR LYS ALA LEU GLY ILE SER TYR GLY                          
SEQRES   1 J   43  GLU GLN ILE GLY GLY SER PRO LEU PHE ALA GLU PRO TYR          
SEQRES   2 J   43  LYS VAL THR SER LYS GLU ASP LYS LEU SER SER ARG ILE          
SEQRES   3 J   43  GLN SER MET LEU GLY ASN TYR ASP GLU MET LYS ASP PHE          
SEQRES   4 J   43  ILE GLY ASP ARG                                              
MODRES 4OR5 TPO A  186  THR  PHOSPHOTHREONINE                                   
MODRES 4OR5 TPO F  186  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 186      11                                                       
HET    TPO  F 186      11                                                       
HET    YT3  A 401       1                                                       
HET    YT3  A 402       1                                                       
HET    YT3  A 403       1                                                       
HET    SO4  A 404       5                                                       
HET    YT3  B 301       1                                                       
HET    YT3  B 302       1                                                       
HET    YT3  B 303       1                                                       
HET    SO4  B 304       5                                                       
HET     ZN  C 101       1                                                       
HET     ZN  C 102       1                                                       
HET    YT3  E 101       1                                                       
HET    YT3  E 102       1                                                       
HET    YT3  F 401       1                                                       
HET    YT3  F 402       1                                                       
HET    YT3  F 403       1                                                       
HET    YT3  F 404       1                                                       
HET    SO4  F 405       5                                                       
HET    YT3  G 301       1                                                       
HET    YT3  G 302       1                                                       
HET    YT3  G 303       1                                                       
HET    SO4  G 304       5                                                       
HET     ZN  H 101       1                                                       
HET     ZN  H 102       1                                                       
HET    YT3  J 101       1                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     YT3 YTTRIUM (III) ION                                                
HETNAM     SO4 SULFATE ION                                                      
HETNAM      ZN ZINC ION                                                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   9  YT3    16(Y 3+)                                                     
FORMUL  12  SO4    4(O4 S 2-)                                                   
FORMUL  17   ZN    4(ZN 2+)                                                     
FORMUL  33  HOH   *100(H2 O)                                                    
HELIX    1   1 GLU A   15  SER A   17  5                                   3    
HELIX    2   2 PRO A   60  GLN A   71  1                                  12    
HELIX    3   3 LEU A  110  ASN A  116  1                                   7    
HELIX    4   4 THR A  122  ASN A  143  1                                  22    
HELIX    5   5 LYS A  151  ALA A  153  5                                   3    
HELIX    6   6 THR A  191  ARG A  195  5                                   5    
HELIX    7   7 PRO A  196  LEU A  201  1                                   6    
HELIX    8   8 PRO A  208  ARG A  225  1                                  18    
HELIX    9   9 THR A  233  GLY A  246  1                                  14    
HELIX   10  10 ASN A  255  TYR A  259  5                                   5    
HELIX   11  11 LEU A  261  LEU A  265  5                                   5    
HELIX   12  12 LYS A  274  ARG A  284  1                                  11    
HELIX   13  13 ASP A  285  LEU A  296  1                                  12    
HELIX   14  14 ASP A  305  LEU A  310  1                                   6    
HELIX   15  15 ASN A  311  TRP A  316  5                                   6    
HELIX   16  16 THR B   15  GLU B   20  1                                   6    
HELIX   17  17 SER B   22  PHE B   27  1                                   6    
HELIX   18  18 ASP B   30  ASN B   53  1                                  24    
HELIX   19  19 SER B   55  GLN B   73  1                                  19    
HELIX   20  20 PRO B   79  GLU B   95  1                                  17    
HELIX   21  21 LYS B  100  HIS B  113  1                                  14    
HELIX   22  22 SER B  123  LEU B  144  1                                  22    
HELIX   23  23 HIS B  152  VAL B  164  1                                  13    
HELIX   24  24 SER B  167  THR B  185  1                                  19    
HELIX   25  25 THR B  186  GLN B  190  5                                   5    
HELIX   26  26 THR B  192  SER B  208  1                                  17    
HELIX   27  27 HIS B  220  VAL B  225  5                                   6    
HELIX   28  28 THR B  230  THR B  248  1                                  19    
HELIX   29  29 ARG B  251  ILE B  255  5                                   5    
HELIX   30  30 GLU C    9  HIS C   13  5                                   5    
HELIX   31  31 CYS C   27  PHE C   32  1                                   6    
HELIX   32  32 CYS C   34  ALA C   42  1                                   9    
HELIX   33  33 ASP E   46  GLY E   57  1                                  12    
HELIX   34  34 ASN E   58  LYS E   63  1                                   6    
HELIX   35  35 GLU F   15  SER F   17  5                                   3    
HELIX   36  36 PRO F   60  LEU F   73  1                                  14    
HELIX   37  37 LEU F  110  ASN F  116  1                                   7    
HELIX   38  38 THR F  122  ASN F  143  1                                  22    
HELIX   39  39 LYS F  151  ALA F  153  5                                   3    
HELIX   40  40 THR F  191  ARG F  195  5                                   5    
HELIX   41  41 PRO F  196  LEU F  201  1                                   6    
HELIX   42  42 PRO F  208  ARG F  225  1                                  18    
HELIX   43  43 THR F  233  GLY F  246  1                                  14    
HELIX   44  44 ASN F  255  ASN F  258  5                                   4    
HELIX   45  45 TYR F  259  LEU F  265  1                                   7    
HELIX   46  46 LYS F  274  ARG F  284  1                                  11    
HELIX   47  47 ASP F  285  LEU F  296  1                                  12    
HELIX   48  48 ASP F  299  ARG F  303  5                                   5    
HELIX   49  49 ASP F  305  ASN F  311  1                                   7    
HELIX   50  50 HIS F  312  SER F  317  5                                   6    
HELIX   51  51 GLU G   17  ASN G   21  5                                   5    
HELIX   52  52 SER G   24  GLY G   28  5                                   5    
HELIX   53  53 ASP G   30  LEU G   52  1                                  23    
HELIX   54  54 SER G   55  TYR G   70  1                                  16    
HELIX   55  55 PRO G   79  GLU G   95  1                                  17    
HELIX   56  56 LYS G  100  HIS G  113  1                                  14    
HELIX   57  57 SER G  123  LEU G  144  1                                  22    
HELIX   58  58 HIS G  152  VAL G  164  1                                  13    
HELIX   59  59 SER G  167  THR G  185  1                                  19    
HELIX   60  60 THR G  186  TYR G  191  1                                   6    
HELIX   61  61 THR G  192  SER G  208  1                                  17    
HELIX   62  62 HIS G  220  VAL G  225  5                                   6    
HELIX   63  63 THR G  230  LYS G  247  1                                  18    
HELIX   64  64 ARG G  251  ILE G  255  5                                   5    
HELIX   65  65 CYS H   27  HIS H   33  1                                   7    
HELIX   66  66 CYS H   34  ALA H   42  1                                   9    
HELIX   67  67 ASP J   46  GLY J   57  1                                  12    
HELIX   68  68 ASN J   58  LYS J   63  1                                   6    
HELIX   69  69 ASP J   64  ILE J   66  5                                   3    
SHEET    1   A 5 TYR A  19  LYS A  24  0                                        
SHEET    2   A 5 VAL A  33  HIS A  38 -1  O  LYS A  35   N  ALA A  23           
SHEET    3   A 5 LYS A  44  LYS A  49 -1  O  LEU A  47   N  PHE A  34           
SHEET    4   A 5 SER A  98  ASP A 104 -1  O  LEU A 101   N  LYS A  48           
SHEET    5   A 5 LEU A  81  THR A  87 -1  N  CYS A  85   O  TYR A 100           
SHEET    1   B 3 HIS A 108  ASP A 109  0                                        
SHEET    2   B 3 VAL A 155  ILE A 157 -1  O  ILE A 157   N  HIS A 108           
SHEET    3   B 3 LEU A 163  LEU A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   C 2 ILE A 145  LEU A 146  0                                        
SHEET    2   C 2 ARG A 172  ALA A 173 -1  O  ARG A 172   N  LEU A 146           
SHEET    1   D 2 TRP B 210  GLU B 211  0                                        
SHEET    2   D 2 TYR E  39  LYS E  40 -1  O  TYR E  39   N  GLU B 211           
SHEET    1   E 5 TYR F  19  LYS F  24  0                                        
SHEET    2   E 5 VAL F  33  HIS F  38 -1  O  LYS F  35   N  LEU F  22           
SHEET    3   E 5 LYS F  44  LYS F  49 -1  O  LEU F  47   N  PHE F  34           
SHEET    4   E 5 ILE F  99  ASP F 104 -1  O  PHE F 103   N  ALA F  46           
SHEET    5   E 5 LEU F  81  ARG F  86 -1  N  ILE F  82   O  VAL F 102           
SHEET    1   F 3 HIS F 108  ASP F 109  0                                        
SHEET    2   F 3 VAL F 155  ILE F 157 -1  O  ILE F 157   N  HIS F 108           
SHEET    3   F 3 LEU F 163  LEU F 165 -1  O  LYS F 164   N  LEU F 156           
SHEET    1   G 2 ILE F 145  LEU F 146  0                                        
SHEET    2   G 2 ARG F 172  ALA F 173 -1  O  ARG F 172   N  LEU F 146           
SHEET    1   H 2 TRP G 210  GLU G 211  0                                        
SHEET    2   H 2 TYR J  39  LYS J  40 -1  O  TYR J  39   N  GLU G 211           
SSBOND   1 CYS G  261    CYS H   30                          1555   1555  2.81  
LINK         C   TYR A 185                 N   TPO A 186     1555   1555  1.33  
LINK         C   TPO A 186                 N   ASN A 187     1555   1555  1.33  
LINK         C   TYR F 185                 N   TPO F 186     1555   1555  1.32  
LINK         C   TPO F 186                 N   ASN F 187     1555   1555  1.32  
LINK         Y   YT3 G 301                 O   HOH G 412     1555   1555  2.06  
LINK         OE2 GLU G 240                 Y   YT3 G 301     1555   1555  2.06  
LINK         OE1 GLU B 240                 Y   YT3 B 303     1555   1555  2.12  
LINK         OE1 GLU G 240                 Y   YT3 G 301     1555   1555  2.14  
LINK         OE1 GLU E  37                 Y   YT3 E 102     1555   1555  2.14  
LINK         Y   YT3 B 301                 O   HOH B 410     1555   1555  2.14  
LINK         OD2 ASP B 169                 Y   YT3 B 301     1555   1555  2.17  
LINK         OE1 GLN B 243                 Y   YT3 B 303     1555   1555  2.24  
LINK         ND1 HIS H  33                ZN    ZN H 101     1555   1555  2.26  
LINK         ND1 HIS C  33                ZN    ZN C 101     1555   1555  2.28  
LINK         SG  CYS C  37                ZN    ZN C 101     1555   1555  2.28  
LINK         SG  CYS C  27                ZN    ZN C 102     1555   1555  2.28  
LINK         SG  CYS H  27                ZN    ZN H 102     1555   1555  2.29  
LINK         SG  CYS H  25                ZN    ZN H 102     1555   1555  2.29  
LINK         SG  CYS C  25                ZN    ZN C 102     1555   1555  2.30  
LINK         SG  CYS C  22                ZN    ZN C 101     1555   1555  2.30  
LINK         SG  CYS B 261                ZN    ZN C 102     1555   1555  2.30  
LINK         SG  CYS C  34                ZN    ZN C 101     1555   1555  2.30  
LINK         SG  CYS H  30                ZN    ZN H 102     1555   1555  2.30  
LINK         SG  CYS H  37                ZN    ZN H 101     1555   1555  2.30  
LINK         SG  CYS G 261                ZN    ZN H 102     1555   1555  2.31  
LINK         SG  CYS H  22                ZN    ZN H 101     1555   1555  2.31  
LINK         Y   YT3 F 402                 O   HOH F 501     1555   1555  2.31  
LINK         SG  CYS H  34                ZN    ZN H 101     1555   1555  2.31  
LINK         SG  CYS C  30                ZN    ZN C 102     1555   1555  2.31  
LINK         Y   YT3 A 401                 O   HOH A 521     1555   1555  2.36  
LINK         OD1 ASP G 169                 Y   YT3 G 302     1555   1555  2.36  
LINK         OD2 ASP F 167                 Y   YT3 F 402     1555   1555  2.37  
LINK         Y   YT3 F 402                 O   HOH F 502     1555   1555  2.37  
LINK         OXT ARG E  69                 Y   YT3 B 301     1555   1555  2.40  
LINK         OXT ARG J  69                 Y   YT3 J 101     1555   1555  2.43  
LINK         OD2 ASP A 167                 Y   YT3 A 401     1555   1555  2.43  
LINK         OE1 GLN G 172                 Y   YT3 G 302     1555   1555  2.45  
LINK         OD2 ASP F 149                 Y   YT3 F 402     1555   1555  2.45  
LINK         OE1 GLN G 243                 Y   YT3 G 301     1555   1555  2.46  
LINK         Y   YT3 A 403                 O   HOH A 505     1555   1555  2.48  
LINK         Y   YT3 A 401                 O   HOH A 527     1555   1555  2.49  
LINK         OD2 ASP A 149                 Y   YT3 A 401     1555   1555  2.50  
LINK         OD1 ASP B 169                 Y   YT3 B 302     1555   1555  2.52  
LINK         OE2 GLU F  15                 Y   YT3 F 403     1555   1555  2.53  
LINK         Y   YT3 G 303                 O   HOH J 202     1555   1555  2.54  
LINK         OD1 ASP J  64                 Y   YT3 G 303     1555   1555  2.55  
LINK         O   ARG J  69                 Y   YT3 G 302     1555   1555  2.59  
LINK         Y   YT3 G 302                 O   HOH J 201     1555   1555  2.64  
LINK         O   ARG E  69                 Y   YT3 B 301     1555   1555  2.64  
LINK         OD2 ASP G 169                 Y   YT3 G 303     1555   1555  2.68  
LINK         OD2 ASP F 308                 Y   YT3 F 401     1555   1555  2.70  
LINK         OD1 ASP F 305                 Y   YT3 F 401     1555   1555  2.73  
LINK         OD2 ASP A 305                 Y   YT3 A 402     1555   1555  2.73  
LINK         OE1 GLN B 172                 Y   YT3 B 301     1555   1555  2.74  
LINK         OD1 ASP E  64                 Y   YT3 B 302     1555   1555  2.76  
LINK         OE1 GLU F  15                 Y   YT3 F 403     1555   1555  2.79  
LINK         OE2 GLU E  37                 Y   YT3 E 102     1555   1555  2.80  
LINK         Y   YT3 A 402                 O   HOH A 514     1555   1555  2.81  
LINK         OE2 GLU B 240                 Y   YT3 B 303     1555   1555  2.82  
LINK         OXT ARG E  69                 Y   YT3 E 101     1555   1555  2.84  
LINK         OD2 ASP A 308                 Y   YT3 A 402     1555   1555  2.86  
LINK         OE2 GLU F 266                 Y   YT3 F 404     1555   1555  2.87  
LINK         OD1 ASP A 305                 Y   YT3 A 402     1555   1555  2.96  
LINK         OXT ARG J  69                 Y   YT3 G 302     1555   1555  3.00  
LINK         NH1 ARG J  69                 Y   YT3 J 101     1555   1555  3.07  
LINK         OE1 GLU F 266                 Y   YT3 F 404     1555   1555  3.08  
LINK         Y   YT3 A 403                 O   HOH A 502     1555   1555  3.17  
LINK         OE1 GLU A 266                 Y   YT3 A 403     1555   1555  3.22  
LINK         OD1 ASP F 308                 Y   YT3 F 401     1555   1555  3.24  
LINK         OD1 ASP F 307                 Y   YT3 F 401     1555   1555  3.37  
LINK         OE2 GLU A 266                 Y   YT3 A 403     1555   1555  3.37  
LINK         NZ  LYS A 269                 Y   YT3 A 403     1555   1555  3.50  
LINK         Y   YT3 F 401                 O   HOH F 511     1555   1555  3.50  
CISPEP   1 ASP A  318    PRO A  319          0        -0.52                     
CISPEP   2 ASP F  318    PRO F  319          0        -0.27                     
SITE     1 AC1  4 ASP A 149  ASP A 167  HOH A 521  HOH A 527                    
SITE     1 AC2  3 ASP A 305  ASP A 308  HOH A 514                               
SITE     1 AC3  6 GLU A 266  LYS A 269  HOH A 505  ASP B 169                    
SITE     2 AC3  6 YT3 B 302  YT3 E 101                                          
SITE     1 AC4  5 LYS A  48  GLU A  66  PHE A 103  ALA A 166                    
SITE     2 AC4  5 ASP A 167                                                     
SITE     1 AC5  5 ASP B 169  GLN B 172  HOH B 410  ARG E  69                    
SITE     2 AC5  5 YT3 E 101                                                     
SITE     1 AC6  5 GLU A 266  YT3 A 403  ASP B 169  ASP E  64                    
SITE     2 AC6  5 YT3 E 101                                                     
SITE     1 AC7  4 GLU B  17  GLU B  20  GLU B 240  GLN B 243                    
SITE     1 AC8  5 SER B 167  LEU B 170  TRP B 210  TYR E  59                    
SITE     2 AC8  5 LYS E  63                                                     
SITE     1 AC9  4 CYS C  22  HIS C  33  CYS C  34  CYS C  37                    
SITE     1 BC1  4 CYS B 261  CYS C  25  CYS C  27  CYS C  30                    
SITE     1 BC2  7 GLU A 263  GLU A 266  YT3 A 403  HOH A 502                    
SITE     2 BC2  7 YT3 B 301  YT3 B 302  ARG E  69                               
SITE     1 BC3  2 GLU A 251  GLU E  37                                          
SITE     1 BC4  5 ASN A 311  HOH A 501  ASP F 305  ASP F 307                    
SITE     2 BC4  5 ASP F 308                                                     
SITE     1 BC5  4 ASP F 149  ASP F 167  HOH F 501  HOH F 502                    
SITE     1 BC6  2 GLU B 124  GLU F  15                                          
SITE     1 BC7  2 GLU F 263  GLU F 266                                          
SITE     1 BC8  4 LYS F  48  PHE F 103  ALA F 166  ASP F 167                    
SITE     1 BC9  5 GLU G  17  GLU G  20  GLU G 240  GLN G 243                    
SITE     2 BC9  5 HOH G 412                                                     
SITE     1 CC1  5 ASP G 169  GLN G 172  ARG J  69  YT3 J 101                    
SITE     2 CC1  5 HOH J 201                                                     
SITE     1 CC2  4 ASP G 169  ASP J  64  YT3 J 101  HOH J 202                    
SITE     1 CC3  6 SER G 167  ASP G 169  LEU G 170  TRP G 210                    
SITE     2 CC3  6 TYR J  59  LYS J  63                                          
SITE     1 CC4  4 CYS H  22  HIS H  33  CYS H  34  CYS H  37                    
SITE     1 CC5  4 CYS G 261  CYS H  25  CYS H  27  CYS H  30                    
SITE     1 CC6  3 YT3 G 302  YT3 G 303  ARG J  69                               
CRYST1  166.862  186.739  108.661  90.00 120.24  90.00 C 1 2 1       8          
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      0.005993  0.000000  0.003494        0.00000                         
SCALE2      0.000000  0.005355  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010653        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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