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Database: PDB
Entry: 4PKY
LinkDB: 4PKY
Original site: 4PKY 
HEADER    TRANSCRIPTION/CELL CYCLE                15-MAY-14   4PKY              
TITLE     ARNT/HIF TRANSCRIPTION FACTOR/COACTIVATOR COMPLEX                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;            
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: C-TERMINAL PAS 2 DOMAIN RESIDUES 342-456;                  
COMPND   5 SYNONYM: ARNT PROTEIN,CLASS E BASIC HELIX-LOOP-HELIX PROTEIN 2,      
COMPND   6 BHLHE2,DIOXIN RECEPTOR,NUCLEAR TRANSLOCATOR,HYPOXIA-INDUCIBLE FACTOR 
COMPND   7 1-BETA,HIF1-BETA;                                                    
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: THE FIRST SIX RESIDUES OF THE SEQUENCE (GEFKGL) ARE N-
COMPND  10 TERMINAL CLONING ARTIFACTS.;                                         
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: TRANSFORMING ACIDIC COILED-COIL-CONTAINING PROTEIN 3;      
COMPND  13 CHAIN: B, C, E, F;                                                   
COMPND  14 FRAGMENT: C-TERMINAL DOMAIN COILED COIL RESIDUES 496-542;            
COMPND  15 SYNONYM: ARNT-INTERACTING PROTEIN;                                   
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: THE FIRST THREE RESIDUES OF THE SEQUENCE (GEF) ARE N- 
COMPND  18 TERMINAL CLONING ARTIFACTS.;                                         
COMPND  19 MOL_ID: 3;                                                           
COMPND  20 MOLECULE: ENDOTHELIAL PAS DOMAIN-CONTAINING PROTEIN 1;               
COMPND  21 CHAIN: G;                                                            
COMPND  22 FRAGMENT: C-TERMINAL PAS 2 AND PAC DOMAIN RESIDUES 239-350;          
COMPND  23 SYNONYM: EPAS-1,BASIC-HELIX-LOOP-HELIX-PAS PROTEIN MOP2,CLASS E BASIC
COMPND  24 HELIX-LOOP-HELIX PROTEIN 73,BHLHE73,HIF-1-ALPHA-LIKE FACTOR,HLF,     
COMPND  25 HYPOXIA-INDUCIBLE FACTOR 2-ALPHA,HIF2-ALPHA,MEMBER OF PAS PROTEIN 2, 
COMPND  26 PAS DOMAIN-CONTAINING PROTEIN 2;                                     
COMPND  27 ENGINEERED: YES;                                                     
COMPND  28 OTHER_DETAILS: THE FIRST SIX RESIDUES OF THE SEQUENCE (GEFKGL) ARE N-
COMPND  29 TERMINAL CLONING ARTIFACTS.                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ARNT, BHLHE2;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PHIS-GBETA1-PARALLEL;                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 GENE: TACC3, AINT;                                                   
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PHIS-GBETA1-PARALLEL;                     
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: EPAS1, BHLHE73, HIF2A, MOP2, PASD2;                            
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PHIS-GBETA1-PARALLEL                      
KEYWDS    PAS DOMAIN, ARNT-HIF TRANSCRIPTION FACTOR-COACTIVATOR COMPLEX,        
KEYWDS   2 TRANSCRIPTION-CELL CYCLE COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.R.TOMCHICK,C.L.PARTCH,K.H.GARDNER                                   
REVDAT   3   22-NOV-17 4PKY    1       SOURCE JRNL   REMARK                     
REVDAT   2   01-APR-15 4PKY    1       JRNL                                     
REVDAT   1   11-FEB-15 4PKY    0                                                
JRNL        AUTH   Y.GUO,T.H.SCHEUERMANN,C.L.PARTCH,D.R.TOMCHICK,K.H.GARDNER    
JRNL        TITL   COILED-COIL COACTIVATORS PLAY A STRUCTURAL ROLE MEDIATING    
JRNL        TITL 2 INTERACTIONS IN HYPOXIA-INDUCIBLE FACTOR HETERODIMERIZATION. 
JRNL        REF    J.BIOL.CHEM.                  V. 290  7707 2015              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   25627682                                                     
JRNL        DOI    10.1074/JBC.M114.632786                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1690)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 12842                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 626                             
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 48.0734 -  5.0789    1.00     3670   195  0.2339 0.2698        
REMARK   3     2  5.0789 -  4.0319    1.00     3504   172  0.1946 0.2267        
REMARK   3     3  4.0319 -  3.5225    0.97     3373   170  0.2469 0.2993        
REMARK   3     4  3.5225 -  3.2000    0.49     1669    89  0.3234 0.3403        
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)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.78                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.07                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.008           4149                                  
REMARK   3   ANGLE     :  0.926           5566                                  
REMARK   3   CHIRALITY :  0.035            627                                  
REMARK   3   PLANARITY :  0.004            707                                  
REMARK   3   DIHEDRAL  : 12.753           1575                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 361 THROUGH 367 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.7394 120.2080 382.6709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2053 T22:   0.3688                                     
REMARK   3      T33:   0.3937 T12:   0.1979                                     
REMARK   3      T13:   0.0496 T23:  -0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9026 L22:   2.6041                                     
REMARK   3      L33:   8.0541 L12:   2.1452                                     
REMARK   3      L13:   2.3067 L23:  -0.7543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2603 S12:   0.1436 S13:  -0.2777                       
REMARK   3      S21:   0.0527 S22:  -0.0949 S23:  -0.7469                       
REMARK   3      S31:   0.1575 S32:  -0.1360 S33:   0.0368                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 368 THROUGH 372 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8455 117.7002 381.3818              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2649 T22:   0.5936                                     
REMARK   3      T33:   0.6129 T12:  -0.0644                                     
REMARK   3      T13:   0.1064 T23:  -0.0526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4576 L22:   4.8974                                     
REMARK   3      L33:   3.2100 L12:   0.7204                                     
REMARK   3      L13:   1.8965 L23:  -2.6792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2266 S12:   0.1810 S13:  -0.8650                       
REMARK   3      S21:   0.3215 S22:   0.3520 S23:   2.0845                       
REMARK   3      S31:   0.4329 S32:  -2.3345 S33:  -0.0965                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 373 THROUGH 391 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0669 120.7553 374.6327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1496 T22:   0.4050                                     
REMARK   3      T33:   0.4638 T12:   0.0657                                     
REMARK   3      T13:  -0.1259 T23:  -0.0942                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6962 L22:   7.4462                                     
REMARK   3      L33:   2.0724 L12:  -1.6179                                     
REMARK   3      L13:  -3.0049 L23:   2.6541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0514 S12:   0.3828 S13:   0.1741                       
REMARK   3      S21:  -0.5576 S22:   0.4865 S23:  -1.5342                       
REMARK   3      S31:  -0.4212 S32:  -0.6074 S33:  -0.1994                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 392 THROUGH 401 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.8821 111.9744 375.3324              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.9323 T22:   0.4551                                     
REMARK   3      T33:   0.6176 T12:   0.3757                                     
REMARK   3      T13:  -0.5939 T23:   0.0559                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9915 L22:   1.0404                                     
REMARK   3      L33:   0.7867 L12:   0.9582                                     
REMARK   3      L13:  -0.1935 L23:  -0.4694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0932 S12:   0.4275 S13:  -0.6263                       
REMARK   3      S21:  -0.1480 S22:   0.1148 S23:   0.6689                       
REMARK   3      S31:   0.0100 S32:  -0.8077 S33:  -0.1553                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 402 THROUGH 418 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.0507 107.7876 386.7143              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6365 T22:   0.2494                                     
REMARK   3      T33:   0.8479 T12:  -0.1835                                     
REMARK   3      T13:  -0.1100 T23:   0.1332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5811 L22:   6.7042                                     
REMARK   3      L33:   6.3371 L12:  -4.4195                                     
REMARK   3      L13:   0.3337 L23:   3.5578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4712 S12:  -0.7585 S13:  -2.0057                       
REMARK   3      S21:   1.3825 S22:  -0.0418 S23:   1.3012                       
REMARK   3      S31:   0.5557 S32:  -0.8124 S33:   0.5082                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 419 THROUGH 435 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7590 110.2474 381.4329              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0649 T22:   0.3258                                     
REMARK   3      T33:   0.6792 T12:  -0.0855                                     
REMARK   3      T13:  -0.0808 T23:   0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8676 L22:   6.5138                                     
REMARK   3      L33:   5.1839 L12:   0.9074                                     
REMARK   3      L13:   2.1752 L23:  -0.9726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2821 S12:  -0.5196 S13:  -1.0322                       
REMARK   3      S21:   0.2728 S22:  -0.3611 S23:  -0.6361                       
REMARK   3      S31:  -0.2697 S32:   0.3617 S33:  -0.3692                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 446 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6525 112.7470 385.4434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0423 T22:   0.3803                                     
REMARK   3      T33:   0.9723 T12:  -0.0741                                     
REMARK   3      T13:  -0.5766 T23:   0.0675                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8386 L22:   3.5816                                     
REMARK   3      L33:   3.3713 L12:  -1.4998                                     
REMARK   3      L13:  -2.4834 L23:   2.5386                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7251 S12:  -0.5123 S13:  -0.9115                       
REMARK   3      S21:   0.7921 S22:  -0.0996 S23:  -0.2730                       
REMARK   3      S31:   0.0534 S32:   0.0712 S33:   0.0757                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 447 THROUGH 455 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.3372 126.3980 392.8214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9436 T22:   1.2079                                     
REMARK   3      T33:   0.9135 T12:   0.2974                                     
REMARK   3      T13:   0.3171 T23:   0.0084                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8386 L22:   2.2307                                     
REMARK   3      L33:   2.7232 L12:  -1.7335                                     
REMARK   3      L13:  -2.7514 L23:   1.9317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4063 S12:  -1.0158 S13:   0.4385                       
REMARK   3      S21:   0.6306 S22:  -0.4703 S23:   0.3341                       
REMARK   3      S31:  -0.2480 S32:  -0.0874 S33:   0.4253                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 456 THROUGH 464 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7676 117.4175 385.4854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2956 T22:   0.5098                                     
REMARK   3      T33:   0.3040 T12:   0.0272                                     
REMARK   3      T13:  -0.1025 T23:   0.1233                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3363 L22:   2.9437                                     
REMARK   3      L33:   1.0739 L12:   0.0536                                     
REMARK   3      L13:   0.2320 L23:  -0.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2961 S12:  -0.2497 S13:   0.0452                       
REMARK   3      S21:   0.5181 S22:  -0.1332 S23:  -0.6417                       
REMARK   3      S31:  -0.7043 S32:   0.3294 S33:   0.1890                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 583 THROUGH 631 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3752 137.4810 370.0196              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4700 T22:   0.1639                                     
REMARK   3      T33:   0.2714 T12:   0.0334                                     
REMARK   3      T13:   0.0197 T23:  -0.0597                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9127 L22:   3.7073                                     
REMARK   3      L33:   9.3557 L12:   1.2521                                     
REMARK   3      L13:  -2.6488 L23:  -3.5522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2752 S12:  -0.0250 S13:  -0.4419                       
REMARK   3      S21:   0.4446 S22:  -0.1275 S23:  -0.2392                       
REMARK   3      S31:  -0.5149 S32:  -0.4956 S33:   0.0476                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 583 THROUGH 629 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9435 140.2498 371.9804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5176 T22:   0.3524                                     
REMARK   3      T33:   0.2180 T12:  -0.0975                                     
REMARK   3      T13:  -0.0077 T23:  -0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7276 L22:   4.2188                                     
REMARK   3      L33:   6.5042 L12:   2.0335                                     
REMARK   3      L13:  -2.9891 L23:  -3.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1850 S12:  -0.1653 S13:  -0.2744                       
REMARK   3      S21:   0.9664 S22:  -0.8489 S23:  -1.7214                       
REMARK   3      S31:  -1.3203 S32:   0.5161 S33:   0.0678                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 361 THROUGH 418 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1470 176.3669 368.6760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5570 T22:   0.3395                                     
REMARK   3      T33:   0.6020 T12:   0.0448                                     
REMARK   3      T13:   0.1721 T23:   0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4184 L22:   4.6582                                     
REMARK   3      L33:   4.0350 L12:   2.7213                                     
REMARK   3      L13:   1.1025 L23:   1.9697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0250 S12:  -0.3913 S13:   0.6456                       
REMARK   3      S21:   0.6556 S22:   0.1009 S23:   0.8733                       
REMARK   3      S31:  -0.2976 S32:  -0.5244 S33:  -0.0573                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 419 THROUGH 447 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1226 178.5669 365.7745              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4391 T22:   0.1875                                     
REMARK   3      T33:   0.5430 T12:   0.1239                                     
REMARK   3      T13:   0.1133 T23:   0.0932                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7460 L22:   9.8791                                     
REMARK   3      L33:   6.2006 L12:   5.2420                                     
REMARK   3      L13:   0.7844 L23:   3.0930                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3227 S12:  -0.0912 S13:   0.5167                       
REMARK   3      S21:  -0.2665 S22:  -0.1104 S23:   0.0474                       
REMARK   3      S31:  -0.3925 S32:  -0.0339 S33:  -0.1115                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 448 THROUGH 464 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.3063 170.4429 360.7096              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4568 T22:   0.4361                                     
REMARK   3      T33:   0.4270 T12:  -0.0971                                     
REMARK   3      T13:   0.1544 T23:   0.0992                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8139 L22:   4.9688                                     
REMARK   3      L33:   6.6951 L12:  -2.5269                                     
REMARK   3      L13:   0.7121 L23:   0.1606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4402 S12:   0.1982 S13:   0.1157                       
REMARK   3      S21:  -0.4321 S22:   0.5307 S23:   0.4639                       
REMARK   3      S31:  -0.6426 S32:  -0.3725 S33:  -0.5050                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 582 THROUGH 631 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2593 152.4652 380.1102              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3429 T22:   0.2077                                     
REMARK   3      T33:   0.3084 T12:  -0.1550                                     
REMARK   3      T13:   0.0212 T23:   0.0532                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4524 L22:   3.9786                                     
REMARK   3      L33:   3.1629 L12:   0.4420                                     
REMARK   3      L13:   0.1935 L23:  -2.0649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5439 S12:  -0.0332 S13:   0.4799                       
REMARK   3      S21:  -0.2112 S22:   0.7634 S23:   0.0240                       
REMARK   3      S31:  -0.3266 S32:  -1.2969 S33:  -0.5562                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 583 THROUGH 631 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5476 149.1496 377.8251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7521 T22:   0.3653                                     
REMARK   3      T33:   0.3790 T12:  -0.0249                                     
REMARK   3      T13:   0.0354 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4656 L22:   3.2403                                     
REMARK   3      L33:   4.9916 L12:   2.1670                                     
REMARK   3      L13:  -2.7604 L23:  -2.5653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5353 S12:   0.0804 S13:  -0.3165                       
REMARK   3      S21:  -0.4059 S22:  -0.6012 S23:  -1.3731                       
REMARK   3      S31:   0.9229 S32:   0.2692 S33:   0.5152                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 239 THROUGH 248 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1384 129.5765 358.3010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7476 T22:   0.6607                                     
REMARK   3      T33:   0.3784 T12:   0.3499                                     
REMARK   3      T13:   0.0223 T23:  -0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5632 L22:   8.8975                                     
REMARK   3      L33:   9.5955 L12:  -3.1998                                     
REMARK   3      L13:  -0.2261 L23:  -0.1143                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3692 S12:   0.1127 S13:   0.2714                       
REMARK   3      S21:   0.5161 S22:  -0.5184 S23:   0.1446                       
REMARK   3      S31:   0.6787 S32:  -0.1422 S33:   0.5142                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 249 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9532 130.5732 355.8154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6750 T22:   1.0201                                     
REMARK   3      T33:   0.7627 T12:   0.0453                                     
REMARK   3      T13:   0.2326 T23:  -0.0626                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5745 L22:   8.9872                                     
REMARK   3      L33:   8.2578 L12:   0.8390                                     
REMARK   3      L13:   5.4998 L23:  -1.8048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5256 S12:   0.2147 S13:   0.0928                       
REMARK   3      S21:  -1.4059 S22:  -0.4704 S23:  -0.5185                       
REMARK   3      S31:   0.6228 S32:   0.6766 S33:  -0.2023                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 259 THROUGH 264 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4949 126.9445 366.1775              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0167 T22:   0.6814                                     
REMARK   3      T33:   0.6101 T12:   0.1213                                     
REMARK   3      T13:  -0.0922 T23:   0.1344                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0003 L22:   4.8710                                     
REMARK   3      L33:   8.8393 L12:  -5.8688                                     
REMARK   3      L13:   8.3695 L23:  -6.5263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0038 S12:  -1.7597 S13:   0.0534                       
REMARK   3      S21:   1.1680 S22:   0.4033 S23:   1.3602                       
REMARK   3      S31:  -0.5817 S32:  -0.0105 S33:  -0.0716                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 265 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0874 121.2443 359.1930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8627 T22:   0.8792                                     
REMARK   3      T33:   0.8182 T12:   0.3797                                     
REMARK   3      T13:  -0.0227 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1217 L22:   6.6903                                     
REMARK   3      L33:   3.7501 L12:  -0.8406                                     
REMARK   3      L13:  -0.7475 L23:  -3.7200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4849 S12:  -0.6769 S13:  -0.5250                       
REMARK   3      S21:   0.2970 S22:   0.4375 S23:  -0.7409                       
REMARK   3      S31:   0.9556 S32:   1.1085 S33:   0.1824                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 286 THROUGH 299 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5569 122.7553 342.6551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2101 T22:   0.7275                                     
REMARK   3      T33:   1.4319 T12:   0.5245                                     
REMARK   3      T13:   0.1918 T23:   0.1570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6476 L22:   0.6685                                     
REMARK   3      L33:   1.8747 L12:   0.5551                                     
REMARK   3      L13:   0.2839 L23:   0.8012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1621 S12:   0.1474 S13:  -1.1950                       
REMARK   3      S21:  -1.1845 S22:   0.4984 S23:   0.0797                       
REMARK   3      S31:   0.2214 S32:   0.0170 S33:  -0.2076                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 300 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8860 119.5891 354.8626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4230 T22:   0.6427                                     
REMARK   3      T33:   0.9418 T12:   0.3028                                     
REMARK   3      T13:   0.1362 T23:  -0.0458                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8301 L22:   5.7394                                     
REMARK   3      L33:   7.8550 L12:   0.2653                                     
REMARK   3      L13:   0.4170 L23:  -3.6855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3600 S12:  -0.1078 S13:  -1.5419                       
REMARK   3      S21:   0.4440 S22:   0.1333 S23:  -0.2297                       
REMARK   3      S31:   0.4102 S32:   0.5787 S33:   0.5680                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 316 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0228 121.3621 353.5653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1356 T22:   0.5663                                     
REMARK   3      T33:   1.0263 T12:   0.2734                                     
REMARK   3      T13:  -0.1443 T23:  -0.3404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0899 L22:   3.9781                                     
REMARK   3      L33:   5.2148 L12:   1.0209                                     
REMARK   3      L13:  -1.0133 L23:  -4.5315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1788 S12:   0.1477 S13:  -1.2713                       
REMARK   3      S21:  -0.3318 S22:   0.3973 S23:   0.1342                       
REMARK   3      S31:   0.4711 S32:   0.0193 S33:  -0.2959                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 325 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9270 132.6958 351.1032              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2341 T22:   0.4132                                     
REMARK   3      T33:   0.7994 T12:   0.1080                                     
REMARK   3      T13:  -0.1659 T23:  -0.0359                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2799 L22:   3.6154                                     
REMARK   3      L33:   3.3463 L12:   3.1741                                     
REMARK   3      L13:  -2.4470 L23:  -3.2372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5897 S12:  -0.0388 S13:   0.1642                       
REMARK   3      S21:  -0.8453 S22:   0.2231 S23:  -0.7543                       
REMARK   3      S31:   0.5517 S32:   0.4051 S33:   0.0866                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4PKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201580.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-09                          
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                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97951                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 705A                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14853                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: 3F1O, 4LPZ                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M MAGNESIUM SULFATE, 0.1 M MES PH    
REMARK 280  6.5, 20% (W/V) ETHYLENE GLYCOL, PH 6.0, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -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       91.42050            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       48.06800            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       48.06800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       45.71025            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       48.06800            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       48.06800            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      137.13075            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       48.06800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.06800            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       45.71025            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       48.06800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.06800            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      137.13075            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       91.42050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 300 REMARK: THE BIOLOGICAL UNIT IS A HETEROTRIMER CONSISTING OF ONE      
REMARK 300 COPY OF MOLECULE 1 AND TWO COPIES OF MOLECULE 2. THERE ARE TWO       
REMARK 300 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT (CHAINS A, B & C AND CHAINS  
REMARK 300 D, E & F). THERE IS AN ADDITIONAL MOLECULE 3 THAT IS NOT PART OF     
REMARK 300 THE BIOLOGICAL UNIT, BUT IS PART OF THE CRYSTALLINE LATTICE (CHAIN   
REMARK 300 G).                                                                  
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 5630 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   350                                                      
REMARK 465     GLU A   351                                                      
REMARK 465     PHE A   352                                                      
REMARK 465     LYS A   353                                                      
REMARK 465     GLY A   354                                                      
REMARK 465     LEU A   355                                                      
REMARK 465     ASN A   356                                                      
REMARK 465     VAL A   357                                                      
REMARK 465     CYS A   358                                                      
REMARK 465     GLN A   359                                                      
REMARK 465     PRO A   360                                                      
REMARK 465     PRO A   449                                                      
REMARK 465     TYR A   450                                                      
REMARK 465     SER A   451                                                      
REMARK 465     LYS A   465                                                      
REMARK 465     ASN A   466                                                      
REMARK 465     SER A   467                                                      
REMARK 465     SER A   468                                                      
REMARK 465     GLN A   469                                                      
REMARK 465     GLU A   470                                                      
REMARK 465     GLY B   582                                                      
REMARK 465     GLY C   582                                                      
REMARK 465     LYS C   630                                                      
REMARK 465     ILE C   631                                                      
REMARK 465     GLY D   350                                                      
REMARK 465     GLU D   351                                                      
REMARK 465     PHE D   352                                                      
REMARK 465     LYS D   353                                                      
REMARK 465     GLY D   354                                                      
REMARK 465     LEU D   355                                                      
REMARK 465     ASN D   356                                                      
REMARK 465     VAL D   357                                                      
REMARK 465     CYS D   358                                                      
REMARK 465     GLN D   359                                                      
REMARK 465     PRO D   360                                                      
REMARK 465     TYR D   450                                                      
REMARK 465     SER D   451                                                      
REMARK 465     ASP D   452                                                      
REMARK 465     LYS D   465                                                      
REMARK 465     ASN D   466                                                      
REMARK 465     SER D   467                                                      
REMARK 465     SER D   468                                                      
REMARK 465     GLN D   469                                                      
REMARK 465     GLU D   470                                                      
REMARK 465     GLY F   582                                                      
REMARK 465     GLY G   234                                                      
REMARK 465     GLU G   235                                                      
REMARK 465     PHE G   236                                                      
REMARK 465     LYS G   237                                                      
REMARK 465     GLY G   238                                                      
REMARK 465     PRO G   329                                                      
REMARK 465     ARG G   330                                                      
REMARK 465     ASN G   331                                                      
REMARK 465     LEU G   332                                                      
REMARK 465     GLN G   333                                                      
REMARK 465     PRO G   334                                                      
REMARK 465     SER G   345                                                      
REMARK 465     GLU G   346                                                      
REMARK 465     ILE G   347                                                      
REMARK 465     GLU G   348                                                      
REMARK 465     LYS G   349                                                      
REMARK 465     ASN G   350                                                      
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    LYS A 419       82.46     52.92                                   
REMARK 500    PHE A 444      144.86   -172.64                                   
REMARK 500    GLU A 453     -146.15    -93.50                                   
REMARK 500    LYS D 419       90.45     54.13                                   
REMARK 500    GLU E 583      -46.15   -131.22                                   
REMARK 500    VAL G 302      147.16   -170.70                                   
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 SO4 B 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 702                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LPZ   RELATED DB: PDB                                   
DBREF  4PKY A  356   470  UNP    P27540   ARNT_HUMAN     342    456             
DBREF  4PKY B  585   631  UNP    Q9JJ11   TACC3_MOUSE    496    542             
DBREF  4PKY C  585   631  UNP    Q9JJ11   TACC3_MOUSE    496    542             
DBREF  4PKY D  356   470  UNP    P27540   ARNT_HUMAN     342    456             
DBREF  4PKY E  585   631  UNP    Q9JJ11   TACC3_MOUSE    496    542             
DBREF  4PKY F  585   631  UNP    Q9JJ11   TACC3_MOUSE    496    542             
DBREF  4PKY G  239   350  UNP    Q99814   EPAS1_HUMAN    239    350             
SEQADV 4PKY GLY A  350  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY GLU A  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY PHE A  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY LYS A  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY GLY A  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY LEU A  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY ARG A  362  UNP  P27540    GLU   348 ENGINEERED MUTATION            
SEQADV 4PKY GLY B  582  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLU B  583  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY PHE B  584  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLY C  582  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLU C  583  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY PHE C  584  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLY D  350  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY GLU D  351  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY PHE D  352  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY LYS D  353  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY GLY D  354  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY LEU D  355  UNP  P27540              EXPRESSION TAG                 
SEQADV 4PKY ARG D  362  UNP  P27540    GLU   348 ENGINEERED MUTATION            
SEQADV 4PKY GLY E  582  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLU E  583  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY PHE E  584  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLY F  582  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLU F  583  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY PHE F  584  UNP  Q9JJ11              EXPRESSION TAG                 
SEQADV 4PKY GLY G  234  UNP  Q99814              EXPRESSION TAG                 
SEQADV 4PKY GLU G  235  UNP  Q99814              EXPRESSION TAG                 
SEQADV 4PKY PHE G  236  UNP  Q99814              EXPRESSION TAG                 
SEQADV 4PKY LYS G  237  UNP  Q99814              EXPRESSION TAG                 
SEQADV 4PKY GLY G  238  UNP  Q99814              EXPRESSION TAG                 
SEQADV 4PKY GLU G  247  UNP  Q99814    ARG   247 ENGINEERED MUTATION            
SEQRES   1 A  121  GLY GLU PHE LYS GLY LEU ASN VAL CYS GLN PRO THR ARG          
SEQRES   2 A  121  PHE ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE          
SEQRES   3 A  121  VAL ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO          
SEQRES   4 A  121  GLN GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS          
SEQRES   5 A  121  PRO GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN          
SEQRES   6 A  121  VAL VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE          
SEQRES   7 A  121  ARG PHE ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG          
SEQRES   8 A  121  THR SER SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU          
SEQRES   9 A  121  ILE GLU TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN          
SEQRES  10 A  121  SER SER GLN GLU                                              
SEQRES   1 B   50  GLY GLU PHE GLU VAL LEU ALA LEU GLN ALA SER LEU ARG          
SEQRES   2 B   50  LYS ALA GLN MET GLN ASN HIS SER LEU GLU MET THR LEU          
SEQRES   3 B   50  GLU GLN LYS THR LYS GLU ILE ASP GLU LEU THR ARG ILE          
SEQRES   4 B   50  CYS ASP ASP LEU ILE SER LYS MET GLU LYS ILE                  
SEQRES   1 C   50  GLY GLU PHE GLU VAL LEU ALA LEU GLN ALA SER LEU ARG          
SEQRES   2 C   50  LYS ALA GLN MET GLN ASN HIS SER LEU GLU MET THR LEU          
SEQRES   3 C   50  GLU GLN LYS THR LYS GLU ILE ASP GLU LEU THR ARG ILE          
SEQRES   4 C   50  CYS ASP ASP LEU ILE SER LYS MET GLU LYS ILE                  
SEQRES   1 D  121  GLY GLU PHE LYS GLY LEU ASN VAL CYS GLN PRO THR ARG          
SEQRES   2 D  121  PHE ILE SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE          
SEQRES   3 D  121  VAL ASP HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO          
SEQRES   4 D  121  GLN GLU LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS          
SEQRES   5 D  121  PRO GLU ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN          
SEQRES   6 D  121  VAL VAL LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE          
SEQRES   7 D  121  ARG PHE ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG          
SEQRES   8 D  121  THR SER SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU          
SEQRES   9 D  121  ILE GLU TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN          
SEQRES  10 D  121  SER SER GLN GLU                                              
SEQRES   1 E   50  GLY GLU PHE GLU VAL LEU ALA LEU GLN ALA SER LEU ARG          
SEQRES   2 E   50  LYS ALA GLN MET GLN ASN HIS SER LEU GLU MET THR LEU          
SEQRES   3 E   50  GLU GLN LYS THR LYS GLU ILE ASP GLU LEU THR ARG ILE          
SEQRES   4 E   50  CYS ASP ASP LEU ILE SER LYS MET GLU LYS ILE                  
SEQRES   1 F   50  GLY GLU PHE GLU VAL LEU ALA LEU GLN ALA SER LEU ARG          
SEQRES   2 F   50  LYS ALA GLN MET GLN ASN HIS SER LEU GLU MET THR LEU          
SEQRES   3 F   50  GLU GLN LYS THR LYS GLU ILE ASP GLU LEU THR ARG ILE          
SEQRES   4 F   50  CYS ASP ASP LEU ILE SER LYS MET GLU LYS ILE                  
SEQRES   1 G  117  GLY GLU PHE LYS GLY LEU ASP SER LYS THR PHE LEU SER          
SEQRES   2 G  117  GLU HIS SER MET ASP MET LYS PHE THR TYR CYS ASP ASP          
SEQRES   3 G  117  ARG ILE THR GLU LEU ILE GLY TYR HIS PRO GLU GLU LEU          
SEQRES   4 G  117  LEU GLY ARG SER ALA TYR GLU PHE TYR HIS ALA LEU ASP          
SEQRES   5 G  117  SER GLU ASN MET THR LYS SER HIS GLN ASN LEU CYS THR          
SEQRES   6 G  117  LYS GLY GLN VAL VAL SER GLY GLN TYR ARG MET LEU ALA          
SEQRES   7 G  117  LYS HIS GLY GLY TYR VAL TRP LEU GLU THR GLN GLY THR          
SEQRES   8 G  117  VAL ILE TYR ASN PRO ARG ASN LEU GLN PRO GLN CYS ILE          
SEQRES   9 G  117  MET CYS VAL ASN TYR VAL LEU SER GLU ILE GLU LYS ASN          
HET    SO4  B 701       5                                                       
HET    SO4  B 702       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   8  SO4    2(O4 S 2-)                                                   
HELIX    1 AA1 HIS A  378  GLY A  385  1                                   8    
HELIX    2 AA2 GLN A  387  LEU A  392  1                                   6    
HELIX    3 AA3 ASN A  395  CYS A  400  5                                   6    
HELIX    4 AA4 ASP A  404  LYS A  419  1                                  16    
HELIX    5 AA5 PHE B  584  ILE B  631  1                                  48    
HELIX    6 AA6 PHE C  584  GLU C  629  1                                  46    
HELIX    7 AA7 ARG D  379  GLY D  385  1                                   7    
HELIX    8 AA8 GLN D  387  LEU D  392  1                                   6    
HELIX    9 AA9 ASN D  395  CYS D  400  5                                   6    
HELIX   10 AB1 HIS D  401  GLU D  403  5                                   3    
HELIX   11 AB2 ASP D  404  LYS D  419  1                                  16    
HELIX   12 AB3 GLU E  583  ILE E  631  1                                  49    
HELIX   13 AB4 PHE F  584  MET F  628  1                                  45    
HELIX   14 AB5 ASP G  259  ILE G  265  1                                   7    
HELIX   15 AB6 SER G  276  PHE G  280  5                                   5    
HELIX   16 AB7 ASP G  285  GLY G  300  1                                  16    
SHEET    1 AA1 5 PHE A 373  VAL A 376  0                                        
SHEET    2 AA1 5 ARG A 362  HIS A 367 -1  N  ARG A 366   O  THR A 374           
SHEET    3 AA1 5 ILE A 454  ASN A 463 -1  O  ILE A 457   N  HIS A 367           
SHEET    4 AA1 5 TRP A 436  GLN A 447 -1  N  ARG A 440   O  THR A 462           
SHEET    5 AA1 5 LEU A 423  ARG A 430 -1  N  PHE A 427   O  MET A 439           
SHEET    1 AA2 5 PHE D 373  VAL D 376  0                                        
SHEET    2 AA2 5 ARG D 362  HIS D 367 -1  N  ARG D 366   O  THR D 374           
SHEET    3 AA2 5 ILE D 454  ASN D 463 -1  O  ILE D 457   N  HIS D 367           
SHEET    4 AA2 5 TRP D 436  GLN D 447 -1  N  PHE D 446   O  GLU D 455           
SHEET    5 AA2 5 LEU D 423  ARG D 430 -1  N  PHE D 427   O  MET D 439           
SHEET    1 AA3 5 PHE G 254  CYS G 257  0                                        
SHEET    2 AA3 5 THR G 243  HIS G 248 -1  N  GLU G 247   O  THR G 255           
SHEET    3 AA3 5 CYS G 336  VAL G 343 -1  O  ILE G 337   N  HIS G 248           
SHEET    4 AA3 5 TYR G 316  ILE G 326 -1  N  THR G 324   O  MET G 338           
SHEET    5 AA3 5 GLN G 301  VAL G 303 -1  N  VAL G 302   O  GLY G 323           
SHEET    1 AA4 5 PHE G 254  CYS G 257  0                                        
SHEET    2 AA4 5 THR G 243  HIS G 248 -1  N  GLU G 247   O  THR G 255           
SHEET    3 AA4 5 CYS G 336  VAL G 343 -1  O  ILE G 337   N  HIS G 248           
SHEET    4 AA4 5 TYR G 316  ILE G 326 -1  N  THR G 324   O  MET G 338           
SHEET    5 AA4 5 TYR G 307  LEU G 310 -1  N  TYR G 307   O  LEU G 319           
SSBOND   1 CYS E  621    CYS F  621                          1555   1555  2.05  
SITE     1 AC1  2 ARG B 594  ARG E 594                                          
SITE     1 AC2  2 HIS B 601  ARG E 594                                          
CRYST1   96.136   96.136  182.841  90.00  90.00  90.00 P 41 21 2    32          
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      0.010402  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010402  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005469        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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