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Database: PDB
Entry: 3FK2
LinkDB: 3FK2
Original site: 3FK2 
HEADER    SIGNALING PROTEIN, HYDROLASE ACTIVATOR  15-DEC-08   3FK2              
TITLE     CRYSTAL STRUCTURE OF THE RHOGAP DOMAIN OF HUMAN                       
TITLE    2 GLUCOCORTICOID RECEPTOR DNA-BINDING FACTOR 1                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCOCORTICOID RECEPTOR DNA-BINDING FACTOR 1;              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES  1212-1439;                                   
COMPND   5 SYNONYM: GLUCOCORTICOID RECEPTOR REPRESSION FACTOR 1, GRF-           
COMPND   6 1, RHO GAP P190A, P190-A;                                            
COMPND   7 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: GRLF1, GRF1, KIAA1722;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRARE2;                      
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;                                
SOURCE  10 OTHER_DETAILS: THE AUTHORS SUSPECT THAT THE SAMPLE WAS               
SOURCE  11 TRUNCATED BY IN-SITU PROTEOLYSIS.                                    
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, GTPASE-ACTIVATING PROTEIN,            
KEYWDS   2 SGC, ALTERNATIVE SPLICING, ANTI-ONCOGENE, CELL CYCLE,                
KEYWDS   3 CYTOPLASM, DNA-BINDING, GTPASE ACTIVATION, NUCLEUS,                  
KEYWDS   4 PHOSPHOPROTEIN, REPRESSOR, TRANSCRIPTION, TRANSCRIPTION              
KEYWDS   5 REGULATION, SIGNALING PROTEIN, HYDROLASE ACTIVATOR                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.NEDYALKOVA,Y.TONG,W.TEMPEL,P.LOPPNAU,C.H.ARROWSMITH,                
AUTHOR   2 A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.PARK,                  
AUTHOR   3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                                 
REVDAT   1   23-DEC-08 3FK2    0                                                
JRNL        AUTH   L.NEDYALKOVA,Y.TONG,W.TEMPEL,P.LOPPNAU,                      
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,J.WEIGELT,              
JRNL        AUTH 3 A.BOCHKAREV,H.PARK                                           
JRNL        TITL   CRYSTAL STRUCTURE OF THE RHOGAP DOMAIN OF HUMAN              
JRNL        TITL 2 GLUCOCORTICOID RECEPTOR DNA-BINDING FACTOR 1                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 21824                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1878                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.4346 -  6.5721    0.99     3011   152  0.2256 0.2737        
REMARK   3     2  6.5721 -  5.2214    1.00     3049   133  0.2275 0.2698        
REMARK   3     3  5.2214 -  4.5628    1.00     2988   195  0.1612 0.2229        
REMARK   3     4  4.5628 -  4.1463    0.99     3052   130  0.1641 0.1809        
REMARK   3     5  4.1463 -  3.8495    0.99     3026   138  0.1671 0.2652        
REMARK   3     6  3.8495 -  3.6227    1.00     2959   202  0.1959 0.2211        
REMARK   3     7  3.6227 -  3.4414    0.99     2986   178  0.2144 0.2510        
REMARK   3     8  3.4414 -  3.2917    0.99     3073    65  0.2220 0.3097        
REMARK   3     9  3.2917 -  3.1651    0.99     2984   181  0.2347 0.2997        
REMARK   3    10  3.1651 -  3.0559    0.97     2874   252  0.2799 0.3541        
REMARK   3    11  3.0559 -  2.9604    0.94     3024     0  0.2805 0.0000        
REMARK   3    12  2.9604 -  2.8758    0.87     2528   252  0.3117 0.3821        
REMARK   3    13  2.8758 -  2.8000    0.79     2499     0  0.3075 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.77500                                              
REMARK   3    B22 (A**2) : -0.52600                                             
REMARK   3    B33 (A**2) : -6.28400                                             
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6315                                  
REMARK   3   ANGLE     :  1.005           8597                                  
REMARK   3   CHIRALITY :  0.074            973                                  
REMARK   3   PLANARITY :  0.003           1111                                  
REMARK   3   DIHEDRAL  : 18.871           2230                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 1244:1437 )             
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 1244:1437 )             
REMARK   3     ATOM PAIRS NUMBER  : 1504                                        
REMARK   3     RMSD               : 0.030                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN C AND (RESSEQ 1244:1437 )             
REMARK   3     SELECTION          : CHAIN A AND (RESSEQ 1244:1437 )             
REMARK   3     ATOM PAIRS NUMBER  : 1515                                        
REMARK   3     RMSD               : 0.033                                       
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1244:1407 )             
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 1244:1407 )             
REMARK   3     ATOM PAIRS NUMBER  : 1297                                        
REMARK   3     RMSD               : 0.035                                       
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 1418:1437 )             
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 1418:1437 )             
REMARK   3     ATOM PAIRS NUMBER  : 175                                         
REMARK   3     RMSD               : 0.038                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3FK2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050685.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
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) : 0.97883                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC Q315                          
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21961                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : 0.15700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
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) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2OSA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 3350, 0.1M BIS-TRIS, 0.2M        
REMARK 280  LITHIUM SULFATE, 0.001M DTT, 1:100 (W/W) TRYPSIN, PH 6.0,           
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       82.51250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.20400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       82.51250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.20400            
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A  1194                                                      
REMARK 465     HIS A  1195                                                      
REMARK 465     HIS A  1196                                                      
REMARK 465     HIS A  1197                                                      
REMARK 465     HIS A  1198                                                      
REMARK 465     HIS A  1199                                                      
REMARK 465     HIS A  1200                                                      
REMARK 465     SER A  1201                                                      
REMARK 465     SER A  1202                                                      
REMARK 465     GLY A  1203                                                      
REMARK 465     ARG A  1204                                                      
REMARK 465     GLU A  1205                                                      
REMARK 465     ASN A  1206                                                      
REMARK 465     LEU A  1207                                                      
REMARK 465     TYR A  1208                                                      
REMARK 465     PHE A  1209                                                      
REMARK 465     GLN A  1210                                                      
REMARK 465     GLY A  1211                                                      
REMARK 465     ASP A  1212                                                      
REMARK 465     PRO A  1213                                                      
REMARK 465     ARG A  1214                                                      
REMARK 465     ARG A  1215                                                      
REMARK 465     ARG A  1216                                                      
REMARK 465     ASN A  1217                                                      
REMARK 465     ILE A  1218                                                      
REMARK 465     LEU A  1219                                                      
REMARK 465     ARG A  1220                                                      
REMARK 465     SER A  1221                                                      
REMARK 465     LEU A  1222                                                      
REMARK 465     ARG A  1223                                                      
REMARK 465     ARG A  1224                                                      
REMARK 465     ASN A  1225                                                      
REMARK 465     THR A  1226                                                      
REMARK 465     LYS A  1227                                                      
REMARK 465     LYS A  1228                                                      
REMARK 465     PRO A  1229                                                      
REMARK 465     LYS A  1230                                                      
REMARK 465     PRO A  1231                                                      
REMARK 465     LYS A  1232                                                      
REMARK 465     PRO A  1233                                                      
REMARK 465     ARG A  1234                                                      
REMARK 465     PRO A  1235                                                      
REMARK 465     SER A  1236                                                      
REMARK 465     ILE A  1237                                                      
REMARK 465     THR A  1238                                                      
REMARK 465     LYS A  1239                                                      
REMARK 465     ALA A  1240                                                      
REMARK 465     THR A  1241                                                      
REMARK 465     ASN A  1438                                                      
REMARK 465     ARG A  1439                                                      
REMARK 465     MET B  1194                                                      
REMARK 465     HIS B  1195                                                      
REMARK 465     HIS B  1196                                                      
REMARK 465     HIS B  1197                                                      
REMARK 465     HIS B  1198                                                      
REMARK 465     HIS B  1199                                                      
REMARK 465     HIS B  1200                                                      
REMARK 465     SER B  1201                                                      
REMARK 465     SER B  1202                                                      
REMARK 465     GLY B  1203                                                      
REMARK 465     ARG B  1204                                                      
REMARK 465     GLU B  1205                                                      
REMARK 465     ASN B  1206                                                      
REMARK 465     LEU B  1207                                                      
REMARK 465     TYR B  1208                                                      
REMARK 465     PHE B  1209                                                      
REMARK 465     GLN B  1210                                                      
REMARK 465     GLY B  1211                                                      
REMARK 465     ASP B  1212                                                      
REMARK 465     PRO B  1213                                                      
REMARK 465     ARG B  1214                                                      
REMARK 465     ARG B  1215                                                      
REMARK 465     ARG B  1216                                                      
REMARK 465     ASN B  1217                                                      
REMARK 465     ILE B  1218                                                      
REMARK 465     LEU B  1219                                                      
REMARK 465     ARG B  1220                                                      
REMARK 465     SER B  1221                                                      
REMARK 465     LEU B  1222                                                      
REMARK 465     ARG B  1223                                                      
REMARK 465     ARG B  1224                                                      
REMARK 465     ASN B  1225                                                      
REMARK 465     THR B  1226                                                      
REMARK 465     LYS B  1227                                                      
REMARK 465     LYS B  1228                                                      
REMARK 465     PRO B  1229                                                      
REMARK 465     LYS B  1230                                                      
REMARK 465     PRO B  1231                                                      
REMARK 465     LYS B  1232                                                      
REMARK 465     PRO B  1233                                                      
REMARK 465     ARG B  1234                                                      
REMARK 465     PRO B  1235                                                      
REMARK 465     SER B  1236                                                      
REMARK 465     ILE B  1237                                                      
REMARK 465     THR B  1238                                                      
REMARK 465     LYS B  1239                                                      
REMARK 465     ALA B  1240                                                      
REMARK 465     THR B  1241                                                      
REMARK 465     PHE B  1409                                                      
REMARK 465     SER B  1410                                                      
REMARK 465     THR B  1411                                                      
REMARK 465     ASN B  1438                                                      
REMARK 465     ARG B  1439                                                      
REMARK 465     MET C  1194                                                      
REMARK 465     HIS C  1195                                                      
REMARK 465     HIS C  1196                                                      
REMARK 465     HIS C  1197                                                      
REMARK 465     HIS C  1198                                                      
REMARK 465     HIS C  1199                                                      
REMARK 465     HIS C  1200                                                      
REMARK 465     SER C  1201                                                      
REMARK 465     SER C  1202                                                      
REMARK 465     GLY C  1203                                                      
REMARK 465     ARG C  1204                                                      
REMARK 465     GLU C  1205                                                      
REMARK 465     ASN C  1206                                                      
REMARK 465     LEU C  1207                                                      
REMARK 465     TYR C  1208                                                      
REMARK 465     PHE C  1209                                                      
REMARK 465     GLN C  1210                                                      
REMARK 465     GLY C  1211                                                      
REMARK 465     ASP C  1212                                                      
REMARK 465     PRO C  1213                                                      
REMARK 465     ARG C  1214                                                      
REMARK 465     ARG C  1215                                                      
REMARK 465     ARG C  1216                                                      
REMARK 465     ASN C  1217                                                      
REMARK 465     ILE C  1218                                                      
REMARK 465     LEU C  1219                                                      
REMARK 465     ARG C  1220                                                      
REMARK 465     SER C  1221                                                      
REMARK 465     LEU C  1222                                                      
REMARK 465     ARG C  1223                                                      
REMARK 465     ARG C  1224                                                      
REMARK 465     ASN C  1225                                                      
REMARK 465     THR C  1226                                                      
REMARK 465     LYS C  1227                                                      
REMARK 465     LYS C  1228                                                      
REMARK 465     PRO C  1229                                                      
REMARK 465     LYS C  1230                                                      
REMARK 465     PRO C  1231                                                      
REMARK 465     LYS C  1232                                                      
REMARK 465     PRO C  1233                                                      
REMARK 465     ARG C  1234                                                      
REMARK 465     PRO C  1235                                                      
REMARK 465     SER C  1236                                                      
REMARK 465     ILE C  1237                                                      
REMARK 465     THR C  1238                                                      
REMARK 465     LYS C  1239                                                      
REMARK 465     ALA C  1240                                                      
REMARK 465     THR C  1241                                                      
REMARK 465     TRP C  1242                                                      
REMARK 465     GLU C  1243                                                      
REMARK 465     ARG C  1439                                                      
REMARK 465     MET D  1194                                                      
REMARK 465     HIS D  1195                                                      
REMARK 465     HIS D  1196                                                      
REMARK 465     HIS D  1197                                                      
REMARK 465     HIS D  1198                                                      
REMARK 465     HIS D  1199                                                      
REMARK 465     HIS D  1200                                                      
REMARK 465     SER D  1201                                                      
REMARK 465     SER D  1202                                                      
REMARK 465     GLY D  1203                                                      
REMARK 465     ARG D  1204                                                      
REMARK 465     GLU D  1205                                                      
REMARK 465     ASN D  1206                                                      
REMARK 465     LEU D  1207                                                      
REMARK 465     TYR D  1208                                                      
REMARK 465     PHE D  1209                                                      
REMARK 465     GLN D  1210                                                      
REMARK 465     GLY D  1211                                                      
REMARK 465     ASP D  1212                                                      
REMARK 465     PRO D  1213                                                      
REMARK 465     ARG D  1214                                                      
REMARK 465     ARG D  1215                                                      
REMARK 465     ARG D  1216                                                      
REMARK 465     ASN D  1217                                                      
REMARK 465     ILE D  1218                                                      
REMARK 465     LEU D  1219                                                      
REMARK 465     ARG D  1220                                                      
REMARK 465     SER D  1221                                                      
REMARK 465     LEU D  1222                                                      
REMARK 465     ARG D  1223                                                      
REMARK 465     ARG D  1224                                                      
REMARK 465     ASN D  1225                                                      
REMARK 465     THR D  1226                                                      
REMARK 465     LYS D  1227                                                      
REMARK 465     LYS D  1228                                                      
REMARK 465     PRO D  1229                                                      
REMARK 465     LYS D  1230                                                      
REMARK 465     PRO D  1231                                                      
REMARK 465     LYS D  1232                                                      
REMARK 465     PRO D  1233                                                      
REMARK 465     ARG D  1234                                                      
REMARK 465     PRO D  1235                                                      
REMARK 465     SER D  1236                                                      
REMARK 465     ILE D  1237                                                      
REMARK 465     THR D  1238                                                      
REMARK 465     LYS D  1239                                                      
REMARK 465     ALA D  1240                                                      
REMARK 465     THR D  1241                                                      
REMARK 465     ASN D  1438                                                      
REMARK 465     ARG D  1439                                                      
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     GLU A1243    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1259    CG   CD   CE   NZ                                   
REMARK 470     THR A1275    OG1  CG2                                            
REMARK 470     LYS A1289    CG   CD   CE   NZ                                   
REMARK 470     SER A1290    OG                                                  
REMARK 470     GLU A1309    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1310    CG   CD   CE   NZ                                   
REMARK 470     ASP A1311    CG   OD1  OD2                                       
REMARK 470     LYS A1363    CE   NZ                                             
REMARK 470     SER A1410    OG                                                  
REMARK 470     THR A1411    OG1  CG2                                            
REMARK 470     LEU A1415    CG   CD1  CD2                                       
REMARK 470     THR A1416    OG1  CG2                                            
REMARK 470     ARG A1419    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1243    OE1  OE2                                            
REMARK 470     SER B1244    OG                                                  
REMARK 470     ASN B1245    CG   OD1  ND2                                       
REMARK 470     LYS B1259    CD   CE   NZ                                        
REMARK 470     THR B1275    OG1  CG2                                            
REMARK 470     LYS B1289    CG   CD   CE   NZ                                   
REMARK 470     SER B1290    OG                                                  
REMARK 470     GLU B1293    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1309    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1310    CG   CD   CE   NZ                                   
REMARK 470     ASP B1311    CG   OD1  OD2                                       
REMARK 470     LYS B1363    CE   NZ                                             
REMARK 470     LEU B1415    CG   CD1  CD2                                       
REMARK 470     THR B1416    OG1  CG2                                            
REMARK 470     ARG B1419    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C1258    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1259    CG   CD   CE   NZ                                   
REMARK 470     THR C1275    OG1  CG2                                            
REMARK 470     LYS C1289    CG   CD   CE   NZ                                   
REMARK 470     SER C1290    OG                                                  
REMARK 470     GLU C1291    CD   OE1  OE2                                       
REMARK 470     GLU C1293    CG   CD   OE1  OE2                                  
REMARK 470     GLN C1296    CG   CD   OE1  NE2                                  
REMARK 470     ARG C1297    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C1306    CG   OD1  OD2                                       
REMARK 470     LEU C1307    CG   CD1  CD2                                       
REMARK 470     GLU C1309    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1310    CG   CD   CE   NZ                                   
REMARK 470     ASP C1311    CG   OD1  OD2                                       
REMARK 470     ASN C1348    CG   OD1  ND2                                       
REMARK 470     LYS C1363    CE   NZ                                             
REMARK 470     SER C1410    OG                                                  
REMARK 470     THR C1411    OG1  CG2                                            
REMARK 470     ARG C1419    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C1438    CG   OD1  ND2                                       
REMARK 470     TRP D1242    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP D1242    CZ3  CH2                                            
REMARK 470     GLU D1243    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1258    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1259    CG   CD   CE   NZ                                   
REMARK 470     THR D1275    OG1  CG2                                            
REMARK 470     SER D1286    OG                                                  
REMARK 470     LYS D1289    CG   CD   CE   NZ                                   
REMARK 470     SER D1290    OG                                                  
REMARK 470     GLU D1293    CG   CD   OE1  OE2                                  
REMARK 470     ARG D1297    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D1304    CG   OD1  ND2                                       
REMARK 470     GLU D1309    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1310    CG   CD   CE   NZ                                   
REMARK 470     ASP D1311    CG   OD1  OD2                                       
REMARK 470     LYS D1346    CD   CE   NZ                                        
REMARK 470     LYS D1362    CG   CD   CE   NZ                                   
REMARK 470     LYS D1363    CE   NZ                                             
REMARK 470     SER D1410    OG                                                  
REMARK 470     THR D1411    OG1  CG2                                            
REMARK 470     LEU D1415    CG   CD1  CD2                                       
REMARK 470     THR D1416    OG1  CG2                                            
REMARK 470     ARG D1419    CG   CD   NE   CZ   NH1  NH2                        
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    TYR A1283      -25.58     79.21                                   
REMARK 500    SER A1410       42.77   -108.65                                   
REMARK 500    THR A1411       -1.61   -151.91                                   
REMARK 500    TYR B1283      -25.35     79.52                                   
REMARK 500    TYR C1283      -25.45     79.14                                   
REMARK 500    SER C1410       42.01   -107.88                                   
REMARK 500    THR C1411       -2.27   -151.74                                   
REMARK 500    PRO D1250      150.46    -45.11                                   
REMARK 500    TYR D1283      -26.65     79.12                                   
REMARK 500    SER D1410       42.79   -107.89                                   
REMARK 500    THR D1411       -1.39   -151.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 2                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX C 3                   
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX D 4                   
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 5                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 6                   
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX C 7                   
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX D 8                   
DBREF  3FK2 A 1212  1439  UNP    Q9NRY4   GRLF1_HUMAN   1212   1439             
DBREF  3FK2 B 1212  1439  UNP    Q9NRY4   GRLF1_HUMAN   1212   1439             
DBREF  3FK2 C 1212  1439  UNP    Q9NRY4   GRLF1_HUMAN   1212   1439             
DBREF  3FK2 D 1212  1439  UNP    Q9NRY4   GRLF1_HUMAN   1212   1439             
SEQADV 3FK2 MET A 1194  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1195  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1196  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1197  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1198  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1199  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS A 1200  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER A 1201  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER A 1202  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY A 1203  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ARG A 1204  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLU A 1205  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ASN A 1206  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 LEU A 1207  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 TYR A 1208  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 PHE A 1209  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLN A 1210  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY A 1211  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 MET B 1194  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1195  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1196  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1197  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1198  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1199  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS B 1200  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER B 1201  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER B 1202  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY B 1203  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ARG B 1204  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLU B 1205  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ASN B 1206  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 LEU B 1207  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 TYR B 1208  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 PHE B 1209  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLN B 1210  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY B 1211  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 MET C 1194  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1195  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1196  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1197  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1198  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1199  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS C 1200  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER C 1201  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER C 1202  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY C 1203  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ARG C 1204  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLU C 1205  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ASN C 1206  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 LEU C 1207  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 TYR C 1208  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 PHE C 1209  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLN C 1210  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY C 1211  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 MET D 1194  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1195  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1196  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1197  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1198  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1199  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 HIS D 1200  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER D 1201  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 SER D 1202  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY D 1203  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ARG D 1204  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLU D 1205  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 ASN D 1206  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 LEU D 1207  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 TYR D 1208  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 PHE D 1209  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLN D 1210  UNP  Q9NRY4              EXPRESSION TAG                 
SEQADV 3FK2 GLY D 1211  UNP  Q9NRY4              EXPRESSION TAG                 
SEQRES   1 A  246  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 A  246  LEU TYR PHE GLN GLY ASP PRO ARG ARG ARG ASN ILE LEU          
SEQRES   3 A  246  ARG SER LEU ARG ARG ASN THR LYS LYS PRO LYS PRO LYS          
SEQRES   4 A  246  PRO ARG PRO SER ILE THR LYS ALA THR TRP GLU SER ASN          
SEQRES   5 A  246  TYR PHE GLY VAL PRO LEU THR THR VAL VAL THR PRO GLU          
SEQRES   6 A  246  LYS PRO ILE PRO ILE PHE ILE GLU ARG CYS ILE GLU TYR          
SEQRES   7 A  246  ILE GLU ALA THR GLY LEU SER THR GLU GLY ILE TYR ARG          
SEQRES   8 A  246  VAL SER GLY ASN LYS SER GLU MET GLU SER LEU GLN ARG          
SEQRES   9 A  246  GLN PHE ASP GLN ASP HIS ASN LEU ASP LEU ALA GLU LYS          
SEQRES  10 A  246  ASP PHE THR VAL ASN THR VAL ALA GLY ALA MET LYS SER          
SEQRES  11 A  246  PHE PHE SER GLU LEU PRO ASP PRO LEU VAL PRO TYR ASN          
SEQRES  12 A  246  MET GLN ILE ASP LEU VAL GLU ALA HIS LYS ILE ASN ASP          
SEQRES  13 A  246  ARG GLU GLN LYS LEU HIS ALA LEU LYS GLU VAL LEU LYS          
SEQRES  14 A  246  LYS PHE PRO LYS GLU ASN HIS GLU VAL PHE LYS TYR VAL          
SEQRES  15 A  246  ILE SER HIS LEU ASN LYS VAL SER HIS ASN ASN LYS VAL          
SEQRES  16 A  246  ASN LEU MET THR SER GLU ASN LEU SER ILE CYS PHE TRP          
SEQRES  17 A  246  PRO THR LEU MET ARG PRO ASP PHE SER THR MET ASP ALA          
SEQRES  18 A  246  LEU THR ALA THR ARG THR TYR GLN THR ILE ILE GLU LEU          
SEQRES  19 A  246  PHE ILE GLN GLN CYS PRO PHE PHE PHE TYR ASN ARG              
SEQRES   1 B  246  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 B  246  LEU TYR PHE GLN GLY ASP PRO ARG ARG ARG ASN ILE LEU          
SEQRES   3 B  246  ARG SER LEU ARG ARG ASN THR LYS LYS PRO LYS PRO LYS          
SEQRES   4 B  246  PRO ARG PRO SER ILE THR LYS ALA THR TRP GLU SER ASN          
SEQRES   5 B  246  TYR PHE GLY VAL PRO LEU THR THR VAL VAL THR PRO GLU          
SEQRES   6 B  246  LYS PRO ILE PRO ILE PHE ILE GLU ARG CYS ILE GLU TYR          
SEQRES   7 B  246  ILE GLU ALA THR GLY LEU SER THR GLU GLY ILE TYR ARG          
SEQRES   8 B  246  VAL SER GLY ASN LYS SER GLU MET GLU SER LEU GLN ARG          
SEQRES   9 B  246  GLN PHE ASP GLN ASP HIS ASN LEU ASP LEU ALA GLU LYS          
SEQRES  10 B  246  ASP PHE THR VAL ASN THR VAL ALA GLY ALA MET LYS SER          
SEQRES  11 B  246  PHE PHE SER GLU LEU PRO ASP PRO LEU VAL PRO TYR ASN          
SEQRES  12 B  246  MET GLN ILE ASP LEU VAL GLU ALA HIS LYS ILE ASN ASP          
SEQRES  13 B  246  ARG GLU GLN LYS LEU HIS ALA LEU LYS GLU VAL LEU LYS          
SEQRES  14 B  246  LYS PHE PRO LYS GLU ASN HIS GLU VAL PHE LYS TYR VAL          
SEQRES  15 B  246  ILE SER HIS LEU ASN LYS VAL SER HIS ASN ASN LYS VAL          
SEQRES  16 B  246  ASN LEU MET THR SER GLU ASN LEU SER ILE CYS PHE TRP          
SEQRES  17 B  246  PRO THR LEU MET ARG PRO ASP PHE SER THR MET ASP ALA          
SEQRES  18 B  246  LEU THR ALA THR ARG THR TYR GLN THR ILE ILE GLU LEU          
SEQRES  19 B  246  PHE ILE GLN GLN CYS PRO PHE PHE PHE TYR ASN ARG              
SEQRES   1 C  246  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 C  246  LEU TYR PHE GLN GLY ASP PRO ARG ARG ARG ASN ILE LEU          
SEQRES   3 C  246  ARG SER LEU ARG ARG ASN THR LYS LYS PRO LYS PRO LYS          
SEQRES   4 C  246  PRO ARG PRO SER ILE THR LYS ALA THR TRP GLU SER ASN          
SEQRES   5 C  246  TYR PHE GLY VAL PRO LEU THR THR VAL VAL THR PRO GLU          
SEQRES   6 C  246  LYS PRO ILE PRO ILE PHE ILE GLU ARG CYS ILE GLU TYR          
SEQRES   7 C  246  ILE GLU ALA THR GLY LEU SER THR GLU GLY ILE TYR ARG          
SEQRES   8 C  246  VAL SER GLY ASN LYS SER GLU MET GLU SER LEU GLN ARG          
SEQRES   9 C  246  GLN PHE ASP GLN ASP HIS ASN LEU ASP LEU ALA GLU LYS          
SEQRES  10 C  246  ASP PHE THR VAL ASN THR VAL ALA GLY ALA MET LYS SER          
SEQRES  11 C  246  PHE PHE SER GLU LEU PRO ASP PRO LEU VAL PRO TYR ASN          
SEQRES  12 C  246  MET GLN ILE ASP LEU VAL GLU ALA HIS LYS ILE ASN ASP          
SEQRES  13 C  246  ARG GLU GLN LYS LEU HIS ALA LEU LYS GLU VAL LEU LYS          
SEQRES  14 C  246  LYS PHE PRO LYS GLU ASN HIS GLU VAL PHE LYS TYR VAL          
SEQRES  15 C  246  ILE SER HIS LEU ASN LYS VAL SER HIS ASN ASN LYS VAL          
SEQRES  16 C  246  ASN LEU MET THR SER GLU ASN LEU SER ILE CYS PHE TRP          
SEQRES  17 C  246  PRO THR LEU MET ARG PRO ASP PHE SER THR MET ASP ALA          
SEQRES  18 C  246  LEU THR ALA THR ARG THR TYR GLN THR ILE ILE GLU LEU          
SEQRES  19 C  246  PHE ILE GLN GLN CYS PRO PHE PHE PHE TYR ASN ARG              
SEQRES   1 D  246  MET HIS HIS HIS HIS HIS HIS SER SER GLY ARG GLU ASN          
SEQRES   2 D  246  LEU TYR PHE GLN GLY ASP PRO ARG ARG ARG ASN ILE LEU          
SEQRES   3 D  246  ARG SER LEU ARG ARG ASN THR LYS LYS PRO LYS PRO LYS          
SEQRES   4 D  246  PRO ARG PRO SER ILE THR LYS ALA THR TRP GLU SER ASN          
SEQRES   5 D  246  TYR PHE GLY VAL PRO LEU THR THR VAL VAL THR PRO GLU          
SEQRES   6 D  246  LYS PRO ILE PRO ILE PHE ILE GLU ARG CYS ILE GLU TYR          
SEQRES   7 D  246  ILE GLU ALA THR GLY LEU SER THR GLU GLY ILE TYR ARG          
SEQRES   8 D  246  VAL SER GLY ASN LYS SER GLU MET GLU SER LEU GLN ARG          
SEQRES   9 D  246  GLN PHE ASP GLN ASP HIS ASN LEU ASP LEU ALA GLU LYS          
SEQRES  10 D  246  ASP PHE THR VAL ASN THR VAL ALA GLY ALA MET LYS SER          
SEQRES  11 D  246  PHE PHE SER GLU LEU PRO ASP PRO LEU VAL PRO TYR ASN          
SEQRES  12 D  246  MET GLN ILE ASP LEU VAL GLU ALA HIS LYS ILE ASN ASP          
SEQRES  13 D  246  ARG GLU GLN LYS LEU HIS ALA LEU LYS GLU VAL LEU LYS          
SEQRES  14 D  246  LYS PHE PRO LYS GLU ASN HIS GLU VAL PHE LYS TYR VAL          
SEQRES  15 D  246  ILE SER HIS LEU ASN LYS VAL SER HIS ASN ASN LYS VAL          
SEQRES  16 D  246  ASN LEU MET THR SER GLU ASN LEU SER ILE CYS PHE TRP          
SEQRES  17 D  246  PRO THR LEU MET ARG PRO ASP PHE SER THR MET ASP ALA          
SEQRES  18 D  246  LEU THR ALA THR ARG THR TYR GLN THR ILE ILE GLU LEU          
SEQRES  19 D  246  PHE ILE GLN GLN CYS PRO PHE PHE PHE TYR ASN ARG              
HET    UNX  A   1       1                                                       
HET    UNX  B   2       1                                                       
HET    UNX  C   3       1                                                       
HET    UNX  D   4       1                                                       
HET    UNX  A   5       1                                                       
HET    UNX  B   6       1                                                       
HET    UNX  C   7       1                                                       
HET    UNX  D   8       1                                                       
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   5  UNX    8(X)                                                         
HELIX    1   1 PRO A 1250  VAL A 1255  5                                   6    
HELIX    2   2 PRO A 1262  GLY A 1276  1                                  15    
HELIX    3   3 ASN A 1288  ASP A 1302  1                                  15    
HELIX    4   4 LEU A 1307  ASP A 1311  5                                   5    
HELIX    5   5 THR A 1313  LEU A 1328  1                                  16    
HELIX    6   6 PRO A 1334  HIS A 1345  1                                  12    
HELIX    7   7 ASP A 1349  LYS A 1363  1                                  15    
HELIX    8   8 PRO A 1365  HIS A 1384  1                                  20    
HELIX    9   9 ASN A 1385  LEU A 1390  1                                   6    
HELIX   10  10 THR A 1392  ARG A 1406  1                                  15    
HELIX   11  11 ASP A 1413  GLN A 1431  1                                  19    
HELIX   12  12 GLN A 1431  TYR A 1437  1                                   7    
HELIX   13  13 PRO B 1250  VAL B 1255  5                                   6    
HELIX   14  14 PRO B 1262  GLY B 1276  1                                  15    
HELIX   15  15 ASN B 1288  ASP B 1302  1                                  15    
HELIX   16  16 LEU B 1307  ASP B 1311  5                                   5    
HELIX   17  17 THR B 1313  LEU B 1328  1                                  16    
HELIX   18  18 PRO B 1334  HIS B 1345  1                                  12    
HELIX   19  19 ASP B 1349  LYS B 1363  1                                  15    
HELIX   20  20 PRO B 1365  HIS B 1384  1                                  20    
HELIX   21  21 ASN B 1385  LEU B 1390  1                                   6    
HELIX   22  22 THR B 1392  ARG B 1406  1                                  15    
HELIX   23  23 ASP B 1413  GLN B 1431  1                                  19    
HELIX   24  24 GLN B 1431  TYR B 1437  1                                   7    
HELIX   25  25 PRO C 1250  VAL C 1255  5                                   6    
HELIX   26  26 PRO C 1262  GLY C 1276  1                                  15    
HELIX   27  27 ASN C 1288  ASP C 1302  1                                  15    
HELIX   28  28 LEU C 1307  ASP C 1311  5                                   5    
HELIX   29  29 THR C 1313  LEU C 1328  1                                  16    
HELIX   30  30 PRO C 1334  HIS C 1345  1                                  12    
HELIX   31  31 ASP C 1349  LYS C 1363  1                                  15    
HELIX   32  32 PRO C 1365  ASN C 1385  1                                  21    
HELIX   33  33 ASN C 1385  LEU C 1390  1                                   6    
HELIX   34  34 THR C 1392  ARG C 1406  1                                  15    
HELIX   35  35 ASP C 1413  GLN C 1431  1                                  19    
HELIX   36  36 GLN C 1431  TYR C 1437  1                                   7    
HELIX   37  37 PRO D 1250  VAL D 1255  5                                   6    
HELIX   38  38 PRO D 1262  GLY D 1276  1                                  15    
HELIX   39  39 ASN D 1288  ASP D 1302  1                                  15    
HELIX   40  40 LEU D 1307  ASP D 1311  5                                   5    
HELIX   41  41 THR D 1313  LEU D 1328  1                                  16    
HELIX   42  42 PRO D 1334  HIS D 1345  1                                  12    
HELIX   43  43 ASP D 1349  LYS D 1363  1                                  15    
HELIX   44  44 PRO D 1365  ASN D 1385  1                                  21    
HELIX   45  45 ASN D 1385  LEU D 1390  1                                   6    
HELIX   46  46 THR D 1392  ARG D 1406  1                                  15    
HELIX   47  47 ASP D 1413  GLN D 1431  1                                  19    
HELIX   48  48 GLN D 1431  TYR D 1437  1                                   7    
SITE     1 AC1  1 THR A1313                                                     
SITE     1 AC2  1 THR B1313                                                     
SITE     1 AC3  1 THR C1313                                                     
SITE     1 AC4  1 THR D1313                                                     
SITE     1 AC5  6 GLN A1431  UNX C   7  GLN C1430  GLN C1431                    
SITE     2 AC5  6 PRO C1433  PHE C1434                                          
SITE     1 AC6  5 GLN B1431  UNX D   8  GLN D1431  PRO D1433                    
SITE     2 AC6  5 PHE D1434                                                     
SITE     1 AC7  6 UNX A   5  GLN A1431  PRO A1433  PHE A1434                    
SITE     2 AC7  6 GLN C1431  PHE C1434                                          
SITE     1 AC8  5 UNX B   6  GLN B1431  PRO B1433  PHE B1434                    
SITE     2 AC8  5 GLN D1431                                                     
CRYST1  165.025   72.408   72.863  90.00  90.00  90.00 P 21 21 2    16          
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      0.006060  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013811  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013724        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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