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Database: PDB
Entry: 3KMZ
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HEADER    TRANSCRIPTION                           11-NOV-09   3KMZ              
TITLE     CRYSTAL STRUCTURE OF RARALPHA LIGAND BINDING DOMAIN IN COMPLEX WITH   
TITLE    2 THE INVERSE AGONIST BMS493 AND A COREPRESSOR FRAGMENT                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINOIC ACID RECEPTOR ALPHA;                              
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN;                                     
COMPND   5 SYNONYM: RAR-ALPHA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP B MEMBER 1;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: NUCLEAR RECEPTOR COREPRESSOR 1;                            
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: NR1;                                                       
COMPND  11 SYNONYM: N-COR1, N-COR;                                              
COMPND  12 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: NR1B1, RARA;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SYNTHETIC                                             
KEYWDS    NUCLEAR RECEPTOR TRANSCRIPTION FACTOR LIGAND BINDING DOMAIN, DNA-     
KEYWDS   2 BINDING, METAL-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE,     
KEYWDS   3 RECEPTOR, TRANSCRIPTION, TRANSCRIPTION REGULATION, ZINC-FINGER,      
KEYWDS   4 CHROMATIN REGULATOR, REPRESSOR                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BOURGUET,A.LE MAIRE                                                 
REVDAT   3   14-JUL-10 3KMZ    1       JRNL                                     
REVDAT   2   23-JUN-10 3KMZ    1       JRNL                                     
REVDAT   1   02-JUN-10 3KMZ    0                                                
JRNL        AUTH   A.LE MAIRE,C.TEYSSIER,C.ERB,M.GRIMALDI,S.ALVAREZ,            
JRNL        AUTH 2 A.R.DE LERA,P.BALAGUER,H.GRONEMEYER,C.A.ROYER,P.GERMAIN,     
JRNL        AUTH 3 W.BOURGUET                                                   
JRNL        TITL   A UNIQUE SECONDARY-STRUCTURE SWITCH CONTROLS CONSTITUTIVE    
JRNL        TITL 2 GENE REPRESSION BY RETINOIC ACID RECEPTOR.                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  17   801 2010              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   20543827                                                     
JRNL        DOI    10.1038/NSMB.1855                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0062                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 31093                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1666                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2319                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.51                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 124                          
REMARK   3   BIN FREE R VALUE                    : 0.2460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3798                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 116                                     
REMARK   3   SOLVENT ATOMS            : 298                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.205         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.120         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.837         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4026 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5441 ; 1.216 ; 2.017       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   498 ;11.860 ; 5.080       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   172 ;36.314 ;24.419       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   752 ;14.815 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;21.645 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   635 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2928 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2425 ; 0.526 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3956 ; 1.037 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1601 ; 1.569 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1476 ; 2.573 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 2                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1740 ;  0.18 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1740 ;  0.27 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : C D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    156 ;  0.17 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    156 ;  0.28 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   182        B   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.9020   1.2190 -20.0050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0594 T22:  -0.0453                                     
REMARK   3      T33:  -0.0003 T12:   0.0329                                     
REMARK   3      T13:  -0.0194 T23:   0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7596 L22:   0.8738                                     
REMARK   3      L33:   1.0644 L12:  -0.0287                                     
REMARK   3      L13:   0.2279 L23:   0.3083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0620 S12:  -0.0200 S13:  -0.1200                       
REMARK   3      S21:  -0.0133 S22:   0.0059 S23:   0.0179                       
REMARK   3      S31:   0.0381 S32:   0.0232 S33:  -0.0679                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   182        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.8820  49.5970  -6.6860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0632 T22:  -0.0437                                     
REMARK   3      T33:   0.0009 T12:  -0.0332                                     
REMARK   3      T13:   0.0277 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7990 L22:   0.8996                                     
REMARK   3      L33:   1.0317 L12:   0.0056                                     
REMARK   3      L13:  -0.2482 L23:   0.2693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0661 S12:   0.0167 S13:   0.1235                       
REMARK   3      S21:   0.0194 S22:  -0.0030 S23:   0.0157                       
REMARK   3      S31:  -0.0328 S32:   0.0165 S33:  -0.0631                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  2047        C  2065                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0510  14.6840 -29.9040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0142 T22:   0.0076                                     
REMARK   3      T33:  -0.0341 T12:  -0.0137                                     
REMARK   3      T13:   0.0290 T23:  -0.0389                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8826 L22:   6.3406                                     
REMARK   3      L33:   2.6984 L12:  -5.5187                                     
REMARK   3      L13:  -3.5969 L23:   3.9948                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1995 S12:   0.1188 S13:   0.3001                       
REMARK   3      S21:  -0.5351 S22:   0.0748 S23:  -0.1814                       
REMARK   3      S31:  -0.3331 S32:   0.2414 S33:  -0.2743                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D  2047        D  2065                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.0860  36.0830   3.1560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0030 T22:  -0.0027                                     
REMARK   3      T33:  -0.0417 T12:   0.0006                                     
REMARK   3      T13:  -0.0275 T23:  -0.0327                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7121 L22:   6.8487                                     
REMARK   3      L33:   4.2167 L12:   4.7736                                     
REMARK   3      L13:   3.9098 L23:   5.0900                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0928 S12:   0.0193 S13:  -0.3168                       
REMARK   3      S21:   0.4616 S22:   0.2138 S23:  -0.2630                       
REMARK   3      S31:   0.2671 S32:   0.2924 S33:  -0.3066                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     1        X     1                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.5150  10.3750 -17.9650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0240 T22:   0.0037                                     
REMARK   3      T33:  -0.0169 T12:   0.0514                                     
REMARK   3      T13:  -0.0155 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1879 L22:   4.1324                                     
REMARK   3      L33:   9.8029 L12:   6.2414                                     
REMARK   3      L13:   1.0072 L23:   2.3478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0942 S12:   0.9011 S13:   0.6543                       
REMARK   3      S21:   0.0662 S22:  -0.1708 S23:  -0.0025                       
REMARK   3      S31:  -0.2176 S32:  -0.0684 S33:   0.2651                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X     2        X     2                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4920  40.4140  -8.7410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0194 T22:   0.0207                                     
REMARK   3      T33:   0.0119 T12:  -0.0538                                     
REMARK   3      T13:   0.0092 T23:   0.0346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.0316 L22:   3.1331                                     
REMARK   3      L33:   7.7113 L12:  -5.4396                                     
REMARK   3      L13:  -0.5906 L23:   2.1521                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5406 S12:  -0.6981 S13:  -1.0704                       
REMARK   3      S21:  -0.7486 S22:  -0.0206 S23:  -0.1304                       
REMARK   3      S31:   0.3840 S32:  -0.0567 S33:   0.5611                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F   298                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.1050  26.3470 -12.7020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0534 T22:   0.0068                                     
REMARK   3      T33:  -0.0311 T12:  -0.0022                                     
REMARK   3      T13:   0.0071 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0682 L22:   0.5851                                     
REMARK   3      L33:   0.1462 L12:   0.0169                                     
REMARK   3      L13:   0.0289 L23:   0.0761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0302 S12:  -0.0027 S13:   0.0177                       
REMARK   3      S21:  -0.0109 S22:  -0.0306 S23:   0.0316                       
REMARK   3      S31:   0.0063 S32:   0.0656 S33:   0.0005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     1        G     9                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.5470  29.1480 -10.8490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0567 T22:   0.0674                                     
REMARK   3      T33:  -0.1372 T12:  -0.0191                                     
REMARK   3      T13:  -0.0419 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9754 L22:   2.0883                                     
REMARK   3      L33:   0.1434 L12:  -0.4504                                     
REMARK   3      L13:   0.0327 L23:   0.5021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0765 S12:  -0.0364 S13:   0.0945                       
REMARK   3      S21:  -0.0111 S22:   0.2731 S23:  -0.4529                       
REMARK   3      S31:   0.0115 S32:  -0.1293 S33:  -0.3496                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3KMZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056193.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32768                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.34100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1DKF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 3350 (W/V), 0.15M NH4CL, PH      
REMARK 280  7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       52.41550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.81250            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       52.41550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       52.81250            
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                                                 
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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, 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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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   BIOMT1   2 -1.000000  0.000000  0.000000     -104.90554            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -53.38195            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350   BIOMT1   2 -1.000000  0.000000  0.000000     -104.83100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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 B   156                                                      
REMARK 465     GLY B   157                                                      
REMARK 465     SER B   158                                                      
REMARK 465     SER B   159                                                      
REMARK 465     HIS B   160                                                      
REMARK 465     HIS B   161                                                      
REMARK 465     HIS B   162                                                      
REMARK 465     HIS B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     HIS B   165                                                      
REMARK 465     SER B   166                                                      
REMARK 465     SER B   167                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     LEU B   169                                                      
REMARK 465     VAL B   170                                                      
REMARK 465     PRO B   171                                                      
REMARK 465     ARG B   172                                                      
REMARK 465     GLY B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     HIS B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     SER B   177                                                      
REMARK 465     TYR B   178                                                      
REMARK 465     THR B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     ILE B   402                                                      
REMARK 465     PRO B   403                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     SER B   405                                                      
REMARK 465     MET B   406                                                      
REMARK 465     PRO B   407                                                      
REMARK 465     PRO B   408                                                      
REMARK 465     LEU B   409                                                      
REMARK 465     ILE B   410                                                      
REMARK 465     GLN B   411                                                      
REMARK 465     GLU B   412                                                      
REMARK 465     MET B   413                                                      
REMARK 465     LEU B   414                                                      
REMARK 465     GLU B   415                                                      
REMARK 465     ASN B   416                                                      
REMARK 465     SER B   417                                                      
REMARK 465     GLU B   418                                                      
REMARK 465     GLY B   419                                                      
REMARK 465     LEU B   420                                                      
REMARK 465     ASP B   421                                                      
REMARK 465     MET A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     HIS A   162                                                      
REMARK 465     HIS A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     HIS A   165                                                      
REMARK 465     SER A   166                                                      
REMARK 465     SER A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     LEU A   169                                                      
REMARK 465     VAL A   170                                                      
REMARK 465     PRO A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     HIS A   175                                                      
REMARK 465     GLU A   176                                                      
REMARK 465     SER A   177                                                      
REMARK 465     TYR A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     LEU A   180                                                      
REMARK 465     ILE A   402                                                      
REMARK 465     PRO A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     SER A   405                                                      
REMARK 465     MET A   406                                                      
REMARK 465     PRO A   407                                                      
REMARK 465     PRO A   408                                                      
REMARK 465     LEU A   409                                                      
REMARK 465     ILE A   410                                                      
REMARK 465     GLN A   411                                                      
REMARK 465     GLU A   412                                                      
REMARK 465     MET A   413                                                      
REMARK 465     LEU A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     ASN A   416                                                      
REMARK 465     SER A   417                                                      
REMARK 465     GLU A   418                                                      
REMARK 465     GLY A   419                                                      
REMARK 465     LEU A   420                                                      
REMARK 465     ASP A   421                                                      
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 B 401    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 401    CB   CG   CD   OE1  OE2                             
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    ASP B 341        9.26     80.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 255        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A  37        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH B 480        DISTANCE =  6.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQO B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 422                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EQO A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 422                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 8                   
DBREF  3KMZ B  176   421  UNP    P10276   RARA_HUMAN     176    421             
DBREF  3KMZ C 2047  2065  UNP    O75376   NCOR1_HUMAN   2047   2065             
DBREF  3KMZ A  176   421  UNP    P10276   RARA_HUMAN     176    421             
DBREF  3KMZ D 2047  2065  UNP    O75376   NCOR1_HUMAN   2047   2065             
SEQADV 3KMZ MET B  156  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY B  157  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER B  158  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER B  159  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  160  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  161  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  162  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  163  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  164  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  165  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER B  166  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER B  167  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY B  168  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ LEU B  169  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ VAL B  170  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ PRO B  171  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ ARG B  172  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY B  173  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER B  174  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS B  175  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ MET A  156  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY A  157  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER A  158  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER A  159  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  160  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  161  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  162  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  163  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  164  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  165  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER A  166  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER A  167  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY A  168  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ LEU A  169  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ VAL A  170  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ PRO A  171  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ ARG A  172  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ GLY A  173  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ SER A  174  UNP  P10276              EXPRESSION TAG                 
SEQADV 3KMZ HIS A  175  UNP  P10276              EXPRESSION TAG                 
SEQRES   1 B  266  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  266  LEU VAL PRO ARG GLY SER HIS GLU SER TYR THR LEU THR          
SEQRES   3 B  266  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   4 B  266  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   5 B  266  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   6 B  266  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   7 B  266  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   8 B  266  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   9 B  266  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES  10 B  266  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES  11 B  266  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  12 B  266  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  13 B  266  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  14 B  266  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  15 B  266  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  16 B  266  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  17 B  266  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  18 B  266  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  19 B  266  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  20 B  266  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES  21 B  266  ASN SER GLU GLY LEU ASP                                      
SEQRES   1 C   19  ARG LEU ILE THR LEU ALA ASP HIS ILE CSO GLN ILE ILE          
SEQRES   2 C   19  THR GLN ASP PHE ALA ARG                                      
SEQRES   1 A  266  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  266  LEU VAL PRO ARG GLY SER HIS GLU SER TYR THR LEU THR          
SEQRES   3 A  266  PRO GLU VAL GLY GLU LEU ILE GLU LYS VAL ARG LYS ALA          
SEQRES   4 A  266  HIS GLN GLU THR PHE PRO ALA LEU CYS GLN LEU GLY LYS          
SEQRES   5 A  266  TYR THR THR ASN ASN SER SER GLU GLN ARG VAL SER LEU          
SEQRES   6 A  266  ASP ILE ASP LEU TRP ASP LYS PHE SER GLU LEU SER THR          
SEQRES   7 A  266  LYS CYS ILE ILE LYS THR VAL GLU PHE ALA LYS GLN LEU          
SEQRES   8 A  266  PRO GLY PHE THR THR LEU THR ILE ALA ASP GLN ILE THR          
SEQRES   9 A  266  LEU LEU LYS ALA ALA CYS LEU ASP ILE LEU ILE LEU ARG          
SEQRES  10 A  266  ILE CYS THR ARG TYR THR PRO GLU GLN ASP THR MET THR          
SEQRES  11 A  266  PHE SER ASP GLY LEU THR LEU ASN ARG THR GLN MET HIS          
SEQRES  12 A  266  ASN ALA GLY PHE GLY PRO LEU THR ASP LEU VAL PHE ALA          
SEQRES  13 A  266  PHE ALA ASN GLN LEU LEU PRO LEU GLU MET ASP ASP ALA          
SEQRES  14 A  266  GLU THR GLY LEU LEU SER ALA ILE CYS LEU ILE CYS GLY          
SEQRES  15 A  266  ASP ARG GLN ASP LEU GLU GLN PRO ASP ARG VAL ASP MET          
SEQRES  16 A  266  LEU GLN GLU PRO LEU LEU GLU ALA LEU LYS VAL TYR VAL          
SEQRES  17 A  266  ARG LYS ARG ARG PRO SER ARG PRO HIS MET PHE PRO LYS          
SEQRES  18 A  266  MET LEU MET LYS ILE THR ASP LEU ARG SER ILE SER ALA          
SEQRES  19 A  266  LYS GLY ALA GLU ARG VAL ILE THR LEU LYS MET GLU ILE          
SEQRES  20 A  266  PRO GLY SER MET PRO PRO LEU ILE GLN GLU MET LEU GLU          
SEQRES  21 A  266  ASN SER GLU GLY LEU ASP                                      
SEQRES   1 D   19  ARG LEU ILE THR LEU ALA ASP HIS ILE CSO GLN ILE ILE          
SEQRES   2 D   19  THR GLN ASP PHE ALA ARG                                      
MODRES 3KMZ CSO C 2056  CYS  S-HYDROXYCYSTEINE                                  
MODRES 3KMZ CSO D 2056  CYS  S-HYDROXYCYSTEINE                                  
HET    CSO  C2056       7                                                       
HET    CSO  D2056       7                                                       
HET    EQO  B   1      31                                                       
HET    GOL  B 422       6                                                       
HET    GOL  B   4       6                                                       
HET    GOL  B   5       6                                                       
HET    GOL  B   9       6                                                       
HET    EQO  A   2      31                                                       
HET    GOL  A 422       6                                                       
HET    GOL  A   3       6                                                       
HET    GOL  A   6       6                                                       
HET    GOL  A   7       6                                                       
HET    GOL  A   8       6                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     EQO 4-{(E)-2-[5,5-DIMETHYL-8-(PHENYLETHYNYL)-5,6-                    
HETNAM   2 EQO  DIHYDRONAPHTHALEN-2-YL]ETHENYL}BENZOIC ACID                     
HETNAM     GOL GLYCEROL                                                         
FORMUL   2  CSO    2(C3 H7 N O3 S)                                              
FORMUL   5  EQO    2(C29 H24 O2)                                                
FORMUL   6  GOL    9(C3 H8 O3)                                                  
FORMUL  16  HOH   *298(H2 O)                                                    
HELIX    1   1 THR B  181  PHE B  199  1                                  19    
HELIX    2   2 ALA B  201  LEU B  205  5                                   5    
HELIX    3   3 ASP B  221  GLN B  245  1                                  25    
HELIX    4   4 GLY B  248  LEU B  252  5                                   5    
HELIX    5   5 THR B  253  THR B  275  1                                  23    
HELIX    6   6 ARG B  294  GLY B  301  1                                   8    
HELIX    7   7 PHE B  302  PRO B  304  5                                   3    
HELIX    8   8 LEU B  305  LEU B  317  1                                  13    
HELIX    9   9 PRO B  318  GLU B  320  5                                   3    
HELIX   10  10 ASP B  322  ILE B  335  1                                  14    
HELIX   11  11 GLN B  344  ARG B  367  1                                  24    
HELIX   12  12 HIS B  372  MET B  379  1                                   8    
HELIX   13  13 MET B  379  GLU B  393  1                                  15    
HELIX   14  14 LEU C 2051  ALA C 2064  1                                  14    
HELIX   15  15 THR A  181  PHE A  199  1                                  19    
HELIX   16  16 ALA A  201  LEU A  205  5                                   5    
HELIX   17  17 ASP A  221  GLN A  245  1                                  25    
HELIX   18  18 GLY A  248  LEU A  252  5                                   5    
HELIX   19  19 THR A  253  ARG A  276  1                                  24    
HELIX   20  20 ARG A  294  GLY A  301  1                                   8    
HELIX   21  21 PHE A  302  PRO A  304  5                                   3    
HELIX   22  22 LEU A  305  LEU A  317  1                                  13    
HELIX   23  23 PRO A  318  GLU A  320  5                                   3    
HELIX   24  24 ASP A  322  ILE A  335  1                                  14    
HELIX   25  25 GLN A  344  ARG A  367  1                                  24    
HELIX   26  26 HIS A  372  GLU A  393  1                                  22    
HELIX   27  27 LEU D 2051  PHE D 2063  1                                  13    
SHEET    1   A 3 TYR B 277  THR B 278  0                                        
SHEET    2   A 3 THR B 283  THR B 285 -1  O  THR B 283   N  THR B 278           
SHEET    3   A 3 THR B 291  ASN B 293 -1  O  LEU B 292   N  MET B 284           
SHEET    1   B 2 VAL B 395  THR B 397  0                                        
SHEET    2   B 2 LEU C2048  THR C2050 -1  O  ILE C2049   N  ILE B 396           
SHEET    1   C 3 TYR A 277  THR A 278  0                                        
SHEET    2   C 3 THR A 283  THR A 285 -1  O  THR A 283   N  THR A 278           
SHEET    3   C 3 THR A 291  ASN A 293 -1  O  LEU A 292   N  MET A 284           
SHEET    1   D 2 VAL A 395  THR A 397  0                                        
SHEET    2   D 2 LEU D2048  THR D2050 -1  O  ILE D2049   N  ILE A 396           
LINK         C   ILE C2055                 N   CSO C2056     1555   1555  1.33  
LINK         C   CSO C2056                 N   GLN C2057     1555   1555  1.33  
LINK         C   ILE D2055                 N   CSO D2056     1555   1555  1.33  
LINK         C   CSO D2056                 N   GLN D2057     1555   1555  1.33  
CISPEP   1 MET A  400    GLU A  401          0         1.93                     
SITE     1 AC1 15 HOH B  11  PHE B 199  PHE B 228  SER B 232                    
SITE     2 AC1 15 THR B 233  CYS B 235  ILE B 236  LEU B 269                    
SITE     3 AC1 15 ILE B 273  ARG B 276  PHE B 286  SER B 287                    
SITE     4 AC1 15 PHE B 302  LEU C2051  HIS C2054                               
SITE     1 AC2  5 THR B 210  ASN B 211  ASN B 293  GLN B 296                    
SITE     2 AC2  5 HOH B 445                                                     
SITE     1 AC3  4 THR B 210  ASN B 212  LEU B 224  LYS B 227                    
SITE     1 AC4  7 ALA B 263  LEU B 266  ASP B 267  ARG B 385                    
SITE     2 AC4  7 SER B 388  HOH B 429  HOH B 437                               
SITE     1 AC5  9 LEU B 319  GLU B 320  GLU B 325  VAL B 363                    
SITE     2 AC5  9 ARG B 366  ARG B 367  ARG B 370  MET B 373                    
SITE     3 AC5  9 MET B 377                                                     
SITE     1 AC6 15 HOH A  20  PHE A 199  TRP A 225  PHE A 228                    
SITE     2 AC6 15 SER A 232  CYS A 235  ILE A 236  LEU A 269                    
SITE     3 AC6 15 ILE A 273  ARG A 276  PHE A 286  SER A 287                    
SITE     4 AC6 15 PHE A 302  LEU D2051  HIS D2054                               
SITE     1 AC7  9 LEU A 319  GLU A 320  GLU A 325  VAL A 363                    
SITE     2 AC7  9 ARG A 366  ARG A 367  ARG A 370  MET A 373                    
SITE     3 AC7  9 MET A 377                                                     
SITE     1 AC8  6 HOH A  40  LEU A 220  GLY A 301  ARG A 394                    
SITE     2 AC8  6 ILE A 396  THR A 397                                          
SITE     1 AC9  5 THR A 210  ASN A 211  SER A 214  HOH A 423                    
SITE     2 AC9  5 HOH A 469                                                     
SITE     1 BC1  5 LYS A 360  ARG A 364  PRO A 371  PHE A 374                    
SITE     2 BC1  5 PRO A 375                                                     
SITE     1 BC2  8 HOH A  54  HOH A  88  ALA A 263  LEU A 266                    
SITE     2 BC2  8 ASP A 267  ARG A 385  SER A 388  ALA A 389                    
CRYST1  104.831  105.625   53.382  90.00  89.92  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009539  0.000000 -0.000013        0.00000                         
SCALE2      0.000000  0.009467  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018733        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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