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Database: PDB
Entry: 4EN2
LinkDB: 4EN2
Original site: 4EN2 
HEADER    VIRAL PROTEIN/IMMUNE SYSTEM             12-APR-12   4EN2              
TITLE     HIV-1 NEF IN COMPLEX WITH MHC-I CYTOPLASMIC DOMAIN AND MU1 ADAPTIN    
TITLE    2 SUBUNIT OF AP1 ADAPTOR (SECOND DOMAIN)                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AP-1 COMPLEX SUBUNIT MU-1;                                 
COMPND   3 CHAIN: M, A;                                                         
COMPND   4 FRAGMENT: SORTING MOTIF RECOGNITION DOMAIN;                          
COMPND   5 SYNONYM: AP-MU CHAIN FAMILY MEMBER MU1A, ADAPTOR PROTEIN COMPLEX AP-1
COMPND   6 MU-1 SUBUNIT, ADAPTOR-RELATED PROTEIN COMPLEX 1 MU-1 SUBUNIT,        
COMPND   7 CLATHRIN ASSEMBLY PROTEIN COMPLEX 1 MEDIUM CHAIN 1, CLATHRIN COAT    
COMPND   8 ASSEMBLY PROTEIN AP47, CLATHRIN COAT-ASSOCIATED PROTEIN AP47, GOLGI  
COMPND   9 ADAPTOR HA1/AP1 ADAPTIN MU-1 SUBUNIT, MU-ADAPTIN 1, MU1A-ADAPTIN;    
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: PROTEIN NEF;                                               
COMPND  13 CHAIN: B, C;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: MHC-I;                                                     
COMPND  17 CHAIN: D, E;                                                         
COMPND  18 FRAGMENT: CYTOPLASMIC DOMAIN;                                        
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: AP1M1, CLTNM;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  10 ORGANISM_TAXID: 11676;                                               
SOURCE  11 STRAIN: NL-43;                                                       
SOURCE  12 GENE: NEF;                                                           
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 GENE: HLA-2;                                                         
SOURCE  19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HUMAN IMMUNODEFICIENCY VIRUS 1, HIV, NEF, MHC-I, ANTIGEN              
KEYWDS   2 PRESENTATION, HOST DEFENSE, ADAPTOR PROTEIN COMPLEX 1, MU1 ADAPTIN   
KEYWDS   3 SUBUNIT, SORTING MOTIF RECOGNITION, CLASP, MEMBRANE TRAFFICKING,     
KEYWDS   4 VIRAL HIJACKING, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.JIA,Y.XIONG                                                         
REVDAT   3   15-NOV-17 4EN2    1       REMARK                                   
REVDAT   2   25-JUL-12 4EN2    1       JRNL                                     
REVDAT   1   20-JUN-12 4EN2    0                                                
JRNL        AUTH   X.JIA,R.SINGH,S.HOMANN,H.YANG,J.GUATELLI,Y.XIONG             
JRNL        TITL   STRUCTURAL BASIS OF EVASION OF CELLULAR ADAPTIVE IMMUNITY BY 
JRNL        TITL 2 HIV-1 NEF.                                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19   701 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22705789                                                     
JRNL        DOI    10.1038/NSMB.2328                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 29309                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1561                            
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) : 2.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1767                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.92                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 82                           
REMARK   3   BIN FREE R VALUE                    : 0.4020                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 53                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.33000                                             
REMARK   3    B22 (A**2) : 2.53000                                              
REMARK   3    B33 (A**2) : -1.20000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.477         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.328         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.276         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 28.523        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6908 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6578 ; 0.006 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9341 ; 1.594 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15138 ; 1.083 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   813 ; 7.148 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   335 ;37.925 ;22.955       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1198 ;20.327 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;17.452 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   980 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7681 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1666 ; 0.004 ; 0.020       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : M A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           0     M    160       M     422      0                      
REMARK   3           0     A    160       A     422      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           0     B      9       B     203      0                      
REMARK   3           0     C      9       C     203      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : D E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           0     D    319       D     329      0                      
REMARK   3           0     E    319       E     329      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
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 :   A   160        A   198                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.1360 -16.6320  -2.9500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3138 T22:   0.4598                                     
REMARK   3      T33:   0.2841 T12:   0.0636                                     
REMARK   3      T13:   0.0467 T23:   0.0180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0683 L22:   1.1413                                     
REMARK   3      L33:   2.3292 L12:   0.2457                                     
REMARK   3      L13:   1.2855 L23:  -0.5512                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1228 S12:  -0.2961 S13:   0.0207                       
REMARK   3      S21:   0.0068 S22:  -0.0324 S23:  -0.0052                       
REMARK   3      S31:   0.0072 S32:  -0.3966 S33:  -0.0904                       
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   199        A   271                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.7030 -21.6220 -12.5110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2997 T22:   0.3357                                     
REMARK   3      T33:   0.2540 T12:  -0.0351                                     
REMARK   3      T13:  -0.0234 T23:   0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3832 L22:   2.0452                                     
REMARK   3      L33:   2.1793 L12:  -0.6819                                     
REMARK   3      L13:  -0.2253 L23:   0.4908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0391 S12:  -0.0893 S13:  -0.1223                       
REMARK   3      S21:  -0.1074 S22:  -0.0053 S23:   0.0881                       
REMARK   3      S31:   0.0450 S32:  -0.5654 S33:  -0.0338                       
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 :   A   272        A   382                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0520 -17.0690  16.9400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2522 T22:   0.6183                                     
REMARK   3      T33:   0.2521 T12:  -0.0094                                     
REMARK   3      T13:   0.0122 T23:  -0.0713                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8865 L22:   1.3730                                     
REMARK   3      L33:   4.7872 L12:   0.4158                                     
REMARK   3      L13:   1.3972 L23:   0.0172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0027 S12:  -0.6537 S13:   0.1470                       
REMARK   3      S21:   0.1741 S22:  -0.0117 S23:  -0.1588                       
REMARK   3      S31:   0.0278 S32:  -0.1347 S33:   0.0144                       
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 :   A   383        A   423                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4130 -14.8640  -7.6940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3707 T22:   0.3683                                     
REMARK   3      T33:   0.3048 T12:  -0.0135                                     
REMARK   3      T13:   0.0260 T23:   0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3096 L22:   0.6698                                     
REMARK   3      L33:   3.6984 L12:  -0.2250                                     
REMARK   3      L13:   1.9172 L23:  -0.6001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0909 S12:  -0.3392 S13:   0.0714                       
REMARK   3      S21:  -0.1010 S22:   0.1981 S23:   0.1127                       
REMARK   3      S31:   0.0612 S32:  -0.5042 S33:  -0.2890                       
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 :   B     6        B    24                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1450 -16.7460 -24.7570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3221 T22:   0.3849                                     
REMARK   3      T33:   0.3836 T12:  -0.1339                                     
REMARK   3      T13:  -0.0600 T23:  -0.0784                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2089 L22:  11.6231                                     
REMARK   3      L33:   7.3796 L12:  -3.1170                                     
REMARK   3      L13:  -0.4843 L23:  -7.4223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2347 S12:   0.3525 S13:   0.5997                       
REMARK   3      S21:   0.2322 S22:  -0.2242 S23:  -1.0167                       
REMARK   3      S31:  -0.4730 S32:   0.6998 S33:   0.4589                       
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 :   B    64        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.3320 -13.8860 -20.9930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4327 T22:   0.2767                                     
REMARK   3      T33:   0.2923 T12:  -0.0938                                     
REMARK   3      T13:   0.0731 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2859 L22:   3.0648                                     
REMARK   3      L33:   0.3057 L12:  -1.7468                                     
REMARK   3      L13:  -0.6405 L23:   0.9221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0143 S12:   0.0149 S13:   0.1880                       
REMARK   3      S21:  -0.1262 S22:  -0.0484 S23:   0.1851                       
REMARK   3      S31:  -0.1143 S32:   0.0186 S33:   0.0341                       
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 :   B    91        B   148                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.7200 -24.3430 -28.0970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3979 T22:   0.3029                                     
REMARK   3      T33:   0.2570 T12:  -0.0348                                     
REMARK   3      T13:   0.0523 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3345 L22:   2.5686                                     
REMARK   3      L33:   0.9033 L12:  -0.7649                                     
REMARK   3      L13:   0.3406 L23:   1.2842                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0422 S12:   0.0883 S13:  -0.0664                       
REMARK   3      S21:  -0.1203 S22:   0.1601 S23:  -0.0819                       
REMARK   3      S31:  -0.1296 S32:   0.1047 S33:  -0.1180                       
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 :   B   149        B   178                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5120 -39.8430 -38.0840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3486 T22:   0.5717                                     
REMARK   3      T33:   0.2814 T12:   0.1914                                     
REMARK   3      T13:  -0.0573 T23:  -0.1883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.1939 L22:   7.4203                                     
REMARK   3      L33:   0.0434 L12:  -3.9779                                     
REMARK   3      L13:  -0.5814 L23:   0.4709                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6469 S12:   0.8554 S13:  -1.0359                       
REMARK   3      S21:  -0.7220 S22:  -0.6431 S23:   0.5075                       
REMARK   3      S31:  -0.0453 S32:  -0.0354 S33:  -0.0039                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   179        B   204                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.4770 -28.5450 -35.3460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4298 T22:   0.5201                                     
REMARK   3      T33:   0.2884 T12:   0.0521                                     
REMARK   3      T13:  -0.0027 T23:  -0.1002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3094 L22:   0.5553                                     
REMARK   3      L33:   6.4603 L12:   0.1314                                     
REMARK   3      L13:  -0.6977 L23:  -0.7923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0613 S12:   0.3482 S13:  -0.0893                       
REMARK   3      S21:  -0.2414 S22:  -0.0129 S23:   0.0777                       
REMARK   3      S31:   0.1053 S32:  -0.3774 S33:  -0.0484                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    12        C    21                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.0550 -24.9220  47.9560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5041 T22:   1.2296                                     
REMARK   3      T33:   0.6712 T12:  -0.4156                                     
REMARK   3      T13:   0.3936 T23:  -0.4425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.5794 L22:  26.1721                                     
REMARK   3      L33:  20.6948 L12:   4.3357                                     
REMARK   3      L13:  21.9217 L23:   6.8454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6644 S12:   2.9868 S13:  -2.6135                       
REMARK   3      S21:  -2.6477 S22:   1.6378 S23:   0.4269                       
REMARK   3      S31:   0.3228 S32:   2.9189 S33:  -2.3022                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    22        C    62                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9120 -11.7450  32.0650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5422 T22:   1.6849                                     
REMARK   3      T33:   1.2191 T12:  -0.1751                                     
REMARK   3      T13:   0.1923 T23:   0.2540                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7953 L22:   1.2778                                     
REMARK   3      L33:  17.0952 L12:  -3.8149                                     
REMARK   3      L13:  12.4854 L23:  -3.6725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2095 S12:  -1.8172 S13:  -2.1280                       
REMARK   3      S21:   0.0042 S22:   0.6708 S23:   0.8717                       
REMARK   3      S31:   0.3798 S32:  -0.4841 S33:  -0.8803                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    63        C    77                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9030 -10.5370  39.6180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2444 T22:   0.2033                                     
REMARK   3      T33:   0.4529 T12:   0.1519                                     
REMARK   3      T13:  -0.0959 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3419 L22:   4.8267                                     
REMARK   3      L33:  30.2548 L12:   4.5083                                     
REMARK   3      L13:  -3.4071 L23:  -5.3461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2896 S12:   0.0330 S13:  -0.4512                       
REMARK   3      S21:  -0.4035 S22:   0.0395 S23:  -0.3594                       
REMARK   3      S31:   1.2796 S32:  -0.3017 S33:   0.2500                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    78        C   117                          
REMARK   3    ORIGIN FOR THE GROUP (A): -26.4900 -17.5840  53.7170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5351 T22:   0.4211                                     
REMARK   3      T33:   0.1501 T12:  -0.0461                                     
REMARK   3      T13:   0.0433 T23:  -0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2862 L22:   3.7815                                     
REMARK   3      L33:   3.1369 L12:   1.9678                                     
REMARK   3      L13:  -0.9015 L23:  -2.1271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6174 S12:   0.7285 S13:  -0.2161                       
REMARK   3      S21:  -0.5203 S22:   0.5178 S23:   0.0641                       
REMARK   3      S31:   0.7724 S32:   0.0246 S33:   0.0996                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   118        C   203                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.8050  -8.2080  59.9550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3514 T22:   0.4706                                     
REMARK   3      T33:   0.2104 T12:   0.0076                                     
REMARK   3      T13:  -0.0269 T23:   0.0421                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5774 L22:   4.5710                                     
REMARK   3      L33:   0.8764 L12:   0.2992                                     
REMARK   3      L13:  -0.1609 L23:  -1.5034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1158 S12:   0.0854 S13:   0.1254                       
REMARK   3      S21:   0.2695 S22:   0.1141 S23:   0.0316                       
REMARK   3      S31:  -0.0397 S32:   0.3092 S33:   0.0016                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   319        D   329                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.0790  -7.5950  52.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3032 T22:   0.1207                                     
REMARK   3      T33:   0.5185 T12:  -0.0424                                     
REMARK   3      T13:  -0.0260 T23:   0.1271                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  27.5881 L22:   0.6383                                     
REMARK   3      L33:  15.0933 L12:   3.4066                                     
REMARK   3      L13:  12.1785 L23:   2.8481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1973 S12:  -0.6976 S13:  -0.1522                       
REMARK   3      S21:   0.0472 S22:  -0.1574 S23:  -0.1412                       
REMARK   3      S31:   0.3370 S32:  -0.6419 S33:  -0.0399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   317        E   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -37.5830 -11.9630 -18.1970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3964 T22:   0.4024                                     
REMARK   3      T33:   0.3472 T12:  -0.0358                                     
REMARK   3      T13:   0.0306 T23:   0.0752                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6067 L22:   3.7890                                     
REMARK   3      L33:  13.8983 L12:  -1.7030                                     
REMARK   3      L13:  -0.5647 L23:   5.6320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:   0.4395 S13:   0.2967                       
REMARK   3      S21:  -0.1335 S22:  -0.1865 S23:  -0.1093                       
REMARK   3      S31:  -0.1665 S32:   0.2057 S33:   0.2095                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   158        M   208                          
REMARK   3    ORIGIN FOR THE GROUP (A): -51.6400   3.5650  44.7080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3003 T22:   0.3852                                     
REMARK   3      T33:   0.2923 T12:   0.0025                                     
REMARK   3      T13:   0.0134 T23:  -0.0429                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7595 L22:   0.4190                                     
REMARK   3      L33:   6.4705 L12:   1.2316                                     
REMARK   3      L13:  -2.8932 L23:  -1.1817                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0437 S12:   0.1102 S13:  -0.2044                       
REMARK   3      S21:  -0.0206 S22:   0.0660 S23:  -0.0600                       
REMARK   3      S31:   0.0232 S32:  -0.0250 S33:  -0.0223                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   209        M   273                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.8380   6.9690  49.5170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3150 T22:   0.2471                                     
REMARK   3      T33:   0.2728 T12:  -0.0259                                     
REMARK   3      T13:  -0.0457 T23:  -0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9627 L22:   1.9756                                     
REMARK   3      L33:   0.6132 L12:   0.1741                                     
REMARK   3      L13:  -0.6367 L23:  -0.3375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0485 S12:  -0.1308 S13:  -0.0632                       
REMARK   3      S21:  -0.0069 S22:   0.0132 S23:  -0.1050                       
REMARK   3      S31:   0.0229 S32:  -0.0644 S33:   0.0353                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   274        M   294                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.7160  -0.8310   8.0370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4070 T22:   0.3759                                     
REMARK   3      T33:   0.2028 T12:  -0.0199                                     
REMARK   3      T13:   0.0366 T23:  -0.0446                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6370 L22:   0.3723                                     
REMARK   3      L33:  22.1845 L12:  -1.7336                                     
REMARK   3      L13:  11.1052 L23:  -1.2678                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2434 S12:   1.2547 S13:  -0.0807                       
REMARK   3      S21:  -0.0419 S22:  -0.1611 S23:   0.0189                       
REMARK   3      S31:  -0.0680 S32:   2.0186 S33:  -0.0822                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   295        M   381                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.7450  -2.7540  16.1250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3038 T22:   0.3301                                     
REMARK   3      T33:   0.2901 T12:  -0.0591                                     
REMARK   3      T13:   0.0011 T23:  -0.0510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2346 L22:   2.1438                                     
REMARK   3      L33:   7.5337 L12:  -1.2482                                     
REMARK   3      L13:   2.4084 L23:  -3.0743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0691 S12:   0.2648 S13:  -0.0084                       
REMARK   3      S21:  -0.1443 S22:   0.0537 S23:  -0.0030                       
REMARK   3      S31:   0.4173 S32:   0.3627 S33:  -0.1228                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   382        M   423                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.7190  -1.2660  43.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3682 T22:   0.2673                                     
REMARK   3      T33:   0.3646 T12:   0.0246                                     
REMARK   3      T13:  -0.0513 T23:  -0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9041 L22:   0.2530                                     
REMARK   3      L33:   6.0322 L12:   0.6509                                     
REMARK   3      L13:  -0.4816 L23:  -0.3496                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0493 S12:   0.1280 S13:  -0.1742                       
REMARK   3      S21:   0.1084 S22:   0.0402 S23:  -0.1030                       
REMARK   3      S31:  -0.1329 S32:   0.1835 S33:  -0.0895                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.73                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4EN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-APR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000071824.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31023                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 3% PEG8000, PH 6.5,          
REMARK 280  MICROBATCH UNDEROIL, TEMPERATURE 298K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       44.01650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.37000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.06400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.37000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.01650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       49.06400            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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: 19970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, C, 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                                                                      
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: 4560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     PRO M   363                                                      
REMARK 465     SER M   364                                                      
REMARK 465     VAL M   365                                                      
REMARK 465     GLU M   366                                                      
REMARK 465     ALA M   367                                                      
REMARK 465     GLU M   368                                                      
REMARK 465     ASP M   369                                                      
REMARK 465     LYS M   370                                                      
REMARK 465     GLU M   371                                                      
REMARK 465     GLY M   372                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     TRP B     5                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     GLY B    29                                                      
REMARK 465     VAL B    30                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     VAL B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     ASP B    36                                                      
REMARK 465     LEU B    37                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     LYS B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     GLY B    41                                                      
REMARK 465     ALA B    42                                                      
REMARK 465     ILE B    43                                                      
REMARK 465     THR B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     ASN B    47                                                      
REMARK 465     THR B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     ALA B    50                                                      
REMARK 465     ASN B    51                                                      
REMARK 465     ASN B    52                                                      
REMARK 465     ALA B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     CYS B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     TRP B    57                                                      
REMARK 465     LEU B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     ALA B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     GLU B    62                                                      
REMARK 465     GLU B    63                                                      
REMARK 465     THR B   162                                                      
REMARK 465     SER B   163                                                      
REMARK 465     LEU B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     PRO B   167                                                      
REMARK 465     VAL B   168                                                      
REMARK 465     SER B   169                                                      
REMARK 465     LEU B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     GLY B   172                                                      
REMARK 465     MET B   173                                                      
REMARK 465     ASP B   174                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     CYS B   206                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     LYS C     4                                                      
REMARK 465     TRP C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     SER C     8                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     ASP C    28                                                      
REMARK 465     GLY C    29                                                      
REMARK 465     VAL C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     ALA C    32                                                      
REMARK 465     VAL C    33                                                      
REMARK 465     SER C    34                                                      
REMARK 465     ARG C    35                                                      
REMARK 465     ASP C    36                                                      
REMARK 465     LEU C    37                                                      
REMARK 465     GLU C    38                                                      
REMARK 465     LYS C    39                                                      
REMARK 465     HIS C    40                                                      
REMARK 465     GLY C    41                                                      
REMARK 465     ALA C    42                                                      
REMARK 465     ILE C    43                                                      
REMARK 465     THR C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     SER C    46                                                      
REMARK 465     ASN C    47                                                      
REMARK 465     THR C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     ALA C    50                                                      
REMARK 465     ASN C    51                                                      
REMARK 465     ASN C    52                                                      
REMARK 465     ALA C    53                                                      
REMARK 465     ALA C    54                                                      
REMARK 465     CYS C    55                                                      
REMARK 465     ALA C    56                                                      
REMARK 465     GLU C   149                                                      
REMARK 465     PRO C   150                                                      
REMARK 465     ASP C   151                                                      
REMARK 465     LYS C   152                                                      
REMARK 465     VAL C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     GLU C   155                                                      
REMARK 465     ALA C   156                                                      
REMARK 465     ASN C   157                                                      
REMARK 465     LYS C   158                                                      
REMARK 465     GLY C   159                                                      
REMARK 465     GLU C   160                                                      
REMARK 465     ASN C   161                                                      
REMARK 465     THR C   162                                                      
REMARK 465     SER C   163                                                      
REMARK 465     LEU C   164                                                      
REMARK 465     LEU C   165                                                      
REMARK 465     HIS C   166                                                      
REMARK 465     PRO C   167                                                      
REMARK 465     VAL C   168                                                      
REMARK 465     SER C   169                                                      
REMARK 465     LEU C   170                                                      
REMARK 465     HIS C   171                                                      
REMARK 465     GLY C   172                                                      
REMARK 465     MET C   173                                                      
REMARK 465     ASP C   174                                                      
REMARK 465     ASP C   175                                                      
REMARK 465     PRO C   176                                                      
REMARK 465     GLU C   177                                                      
REMARK 465     ARG C   178                                                      
REMARK 465     LYS C   204                                                      
REMARK 465     ASN C   205                                                      
REMARK 465     CYS C   206                                                      
REMARK 465     SER A   158                                                      
REMARK 465     TRP A   159                                                      
REMARK 465     SER A   364                                                      
REMARK 465     VAL A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     ALA A   367                                                      
REMARK 465     GLU A   368                                                      
REMARK 465     ASP A   369                                                      
REMARK 465     LYS A   370                                                      
REMARK 465     GLU A   371                                                      
REMARK 465     GLY A   372                                                      
REMARK 465     ASP D   314                                                      
REMARK 465     ARG D   315                                                      
REMARK 465     LYS D   316                                                      
REMARK 465     GLY D   317                                                      
REMARK 465     GLY D   318                                                      
REMARK 465     GLY D   331                                                      
REMARK 465     SER D   332                                                      
REMARK 465     ASP D   333                                                      
REMARK 465     VAL D   334                                                      
REMARK 465     SER D   335                                                      
REMARK 465     LEU D   336                                                      
REMARK 465     THR D   337                                                      
REMARK 465     ALA D   338                                                      
REMARK 465     CYS D   339                                                      
REMARK 465     LYS D   340                                                      
REMARK 465     VAL D   341                                                      
REMARK 465     SER E   332                                                      
REMARK 465     ASP E   333                                                      
REMARK 465     VAL E   334                                                      
REMARK 465     SER E   335                                                      
REMARK 465     LEU E   336                                                      
REMARK 465     THR E   337                                                      
REMARK 465     ALA E   338                                                      
REMARK 465     CYS E   339                                                      
REMARK 465     LYS E   340                                                      
REMARK 465     VAL E   341                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   192     CG2  VAL A   273              1.55            
REMARK 500   O    SER A   205     OH   TYR A   403              1.79            
REMARK 500   O    SER A   289     O    LEU A   362              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS M   352     OE2  GLU B    24     4445     1.90            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG M 251   CG  -  CD  -  NE  ANGL. DEV. = -14.5 DEGREES          
REMARK 500    LEU M 269   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER M 192      118.80   -166.64                                   
REMARK 500    PHE M 203       75.33   -115.29                                   
REMARK 500    MET M 207       57.94   -152.25                                   
REMARK 500    PHE M 262      166.79    179.14                                   
REMARK 500    ASN M 270       38.40    -92.92                                   
REMARK 500    SER M 287      142.73   -171.55                                   
REMARK 500    HIS M 288     -135.08     49.70                                   
REMARK 500    SER M 289       58.97    -93.10                                   
REMARK 500    PHE M 385      133.30   -173.88                                   
REMARK 500    PRO B  25       -8.87    -47.83                                   
REMARK 500    GLN B  73      -15.89     80.68                                   
REMARK 500    GLN B 125       48.77    -91.27                                   
REMARK 500    ASP B 186      100.73   -163.24                                   
REMARK 500    GLN C 125       48.17    -90.53                                   
REMARK 500    ASP C 186      102.60   -162.62                                   
REMARK 500    PHE A 203       75.07   -115.35                                   
REMARK 500    MET A 207       62.88   -151.77                                   
REMARK 500    HIS A 272        8.90     80.19                                   
REMARK 500    HIS A 288      -56.03     71.05                                   
REMARK 500    LEU A 362      141.80   -174.38                                   
REMARK 500    PHE A 385      136.94   -173.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU C   64     GLU C   65                  144.41                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EMZ   RELATED DB: PDB                                   
REMARK 900 SE-MET DERIVATIVE OF THE SAME PROTEIN COMPLEX                        
DBREF  4EN2 M  158   423  UNP    P35585   AP1M1_MOUSE    158    423             
DBREF  4EN2 B    1   206  UNP    Q90VU7   Q90VU7_9HIV1     1    206             
DBREF  4EN2 C    1   206  UNP    Q90VU7   Q90VU7_9HIV1     1    206             
DBREF  4EN2 A  158   423  UNP    P35585   AP1M1_MOUSE    158    423             
DBREF  4EN2 D  314   341  PDB    4EN2     4EN2           314    341             
DBREF  4EN2 E  314   341  PDB    4EN2     4EN2           314    341             
SEQRES   1 M  266  SER TRP ARG SER GLU GLY ILE LYS TYR ARG LYS ASN GLU          
SEQRES   2 M  266  VAL PHE LEU ASP VAL ILE GLU ALA VAL ASN LEU LEU VAL          
SEQRES   3 M  266  SER ALA ASN GLY ASN VAL LEU ARG SER GLU ILE VAL GLY          
SEQRES   4 M  266  SER ILE LYS MET ARG VAL PHE LEU SER GLY MET PRO GLU          
SEQRES   5 M  266  LEU ARG LEU GLY LEU ASN ASP LYS VAL LEU PHE ASP ASN          
SEQRES   6 M  266  THR GLY ARG GLY LYS SER LYS SER VAL GLU LEU GLU ASP          
SEQRES   7 M  266  VAL LYS PHE HIS GLN CYS VAL ARG LEU SER ARG PHE GLU          
SEQRES   8 M  266  ASN ASP ARG THR ILE SER PHE ILE PRO PRO ASP GLY GLU          
SEQRES   9 M  266  PHE GLU LEU MET SER TYR ARG LEU ASN THR HIS VAL LYS          
SEQRES  10 M  266  PRO LEU ILE TRP ILE GLU SER VAL ILE GLU LYS HIS SER          
SEQRES  11 M  266  HIS SER ARG ILE GLU TYR MET VAL LYS ALA LYS SER GLN          
SEQRES  12 M  266  PHE LYS ARG ARG SER THR ALA ASN ASN VAL GLU ILE HIS          
SEQRES  13 M  266  ILE PRO VAL PRO ASN ASP ALA ASP SER PRO LYS PHE LYS          
SEQRES  14 M  266  THR THR VAL GLY SER VAL LYS TRP VAL PRO GLU ASN SER          
SEQRES  15 M  266  GLU ILE VAL TRP SER VAL LYS SER PHE PRO GLY GLY LYS          
SEQRES  16 M  266  GLU TYR LEU MET ARG ALA HIS PHE GLY LEU PRO SER VAL          
SEQRES  17 M  266  GLU ALA GLU ASP LYS GLU GLY LYS PRO PRO ILE SER VAL          
SEQRES  18 M  266  LYS PHE GLU ILE PRO TYR PHE THR THR SER GLY ILE GLN          
SEQRES  19 M  266  VAL ARG TYR LEU LYS ILE ILE GLU LYS SER GLY TYR GLN          
SEQRES  20 M  266  ALA LEU PRO TRP VAL ARG TYR ILE THR GLN ASN GLY ASP          
SEQRES  21 M  266  TYR GLN LEU ARG THR GLN                                      
SEQRES   1 B  206  MET GLY GLY LYS TRP SER LYS SER SER VAL ILE GLY TRP          
SEQRES   2 B  206  PRO ALA VAL ARG GLU ARG MET ARG ARG ALA GLU PRO ALA          
SEQRES   3 B  206  ALA ASP GLY VAL GLY ALA VAL SER ARG ASP LEU GLU LYS          
SEQRES   4 B  206  HIS GLY ALA ILE THR SER SER ASN THR ALA ALA ASN ASN          
SEQRES   5 B  206  ALA ALA CYS ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU          
SEQRES   6 B  206  VAL GLY PHE PRO VAL THR PRO GLN VAL PRO LEU ARG PRO          
SEQRES   7 B  206  MET THR TYR LYS ALA ALA VAL ASP LEU SER HIS PHE LEU          
SEQRES   8 B  206  LYS GLU LYS GLY GLY LEU GLU GLY LEU ILE HIS SER GLN          
SEQRES   9 B  206  ARG ARG GLN ASP ILE LEU ASP LEU TRP ILE TYR HIS THR          
SEQRES  10 B  206  GLN GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY          
SEQRES  11 B  206  PRO GLY VAL ARG TYR PRO LEU THR PHE GLY TRP CYS TYR          
SEQRES  12 B  206  LYS LEU VAL PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA          
SEQRES  13 B  206  ASN LYS GLY GLU ASN THR SER LEU LEU HIS PRO VAL SER          
SEQRES  14 B  206  LEU HIS GLY MET ASP ASP PRO GLU ARG GLU VAL LEU GLU          
SEQRES  15 B  206  TRP ARG PHE ASP SER ARG LEU ALA PHE HIS HIS VAL ALA          
SEQRES  16 B  206  ARG GLU LEU HIS PRO GLU TYR PHE LYS ASN CYS                  
SEQRES   1 C  206  MET GLY GLY LYS TRP SER LYS SER SER VAL ILE GLY TRP          
SEQRES   2 C  206  PRO ALA VAL ARG GLU ARG MET ARG ARG ALA GLU PRO ALA          
SEQRES   3 C  206  ALA ASP GLY VAL GLY ALA VAL SER ARG ASP LEU GLU LYS          
SEQRES   4 C  206  HIS GLY ALA ILE THR SER SER ASN THR ALA ALA ASN ASN          
SEQRES   5 C  206  ALA ALA CYS ALA TRP LEU GLU ALA GLN GLU GLU GLU GLU          
SEQRES   6 C  206  VAL GLY PHE PRO VAL THR PRO GLN VAL PRO LEU ARG PRO          
SEQRES   7 C  206  MET THR TYR LYS ALA ALA VAL ASP LEU SER HIS PHE LEU          
SEQRES   8 C  206  LYS GLU LYS GLY GLY LEU GLU GLY LEU ILE HIS SER GLN          
SEQRES   9 C  206  ARG ARG GLN ASP ILE LEU ASP LEU TRP ILE TYR HIS THR          
SEQRES  10 C  206  GLN GLY TYR PHE PRO ASP TRP GLN ASN TYR THR PRO GLY          
SEQRES  11 C  206  PRO GLY VAL ARG TYR PRO LEU THR PHE GLY TRP CYS TYR          
SEQRES  12 C  206  LYS LEU VAL PRO VAL GLU PRO ASP LYS VAL GLU GLU ALA          
SEQRES  13 C  206  ASN LYS GLY GLU ASN THR SER LEU LEU HIS PRO VAL SER          
SEQRES  14 C  206  LEU HIS GLY MET ASP ASP PRO GLU ARG GLU VAL LEU GLU          
SEQRES  15 C  206  TRP ARG PHE ASP SER ARG LEU ALA PHE HIS HIS VAL ALA          
SEQRES  16 C  206  ARG GLU LEU HIS PRO GLU TYR PHE LYS ASN CYS                  
SEQRES   1 A  266  SER TRP ARG SER GLU GLY ILE LYS TYR ARG LYS ASN GLU          
SEQRES   2 A  266  VAL PHE LEU ASP VAL ILE GLU ALA VAL ASN LEU LEU VAL          
SEQRES   3 A  266  SER ALA ASN GLY ASN VAL LEU ARG SER GLU ILE VAL GLY          
SEQRES   4 A  266  SER ILE LYS MET ARG VAL PHE LEU SER GLY MET PRO GLU          
SEQRES   5 A  266  LEU ARG LEU GLY LEU ASN ASP LYS VAL LEU PHE ASP ASN          
SEQRES   6 A  266  THR GLY ARG GLY LYS SER LYS SER VAL GLU LEU GLU ASP          
SEQRES   7 A  266  VAL LYS PHE HIS GLN CYS VAL ARG LEU SER ARG PHE GLU          
SEQRES   8 A  266  ASN ASP ARG THR ILE SER PHE ILE PRO PRO ASP GLY GLU          
SEQRES   9 A  266  PHE GLU LEU MET SER TYR ARG LEU ASN THR HIS VAL LYS          
SEQRES  10 A  266  PRO LEU ILE TRP ILE GLU SER VAL ILE GLU LYS HIS SER          
SEQRES  11 A  266  HIS SER ARG ILE GLU TYR MET VAL LYS ALA LYS SER GLN          
SEQRES  12 A  266  PHE LYS ARG ARG SER THR ALA ASN ASN VAL GLU ILE HIS          
SEQRES  13 A  266  ILE PRO VAL PRO ASN ASP ALA ASP SER PRO LYS PHE LYS          
SEQRES  14 A  266  THR THR VAL GLY SER VAL LYS TRP VAL PRO GLU ASN SER          
SEQRES  15 A  266  GLU ILE VAL TRP SER VAL LYS SER PHE PRO GLY GLY LYS          
SEQRES  16 A  266  GLU TYR LEU MET ARG ALA HIS PHE GLY LEU PRO SER VAL          
SEQRES  17 A  266  GLU ALA GLU ASP LYS GLU GLY LYS PRO PRO ILE SER VAL          
SEQRES  18 A  266  LYS PHE GLU ILE PRO TYR PHE THR THR SER GLY ILE GLN          
SEQRES  19 A  266  VAL ARG TYR LEU LYS ILE ILE GLU LYS SER GLY TYR GLN          
SEQRES  20 A  266  ALA LEU PRO TRP VAL ARG TYR ILE THR GLN ASN GLY ASP          
SEQRES  21 A  266  TYR GLN LEU ARG THR GLN                                      
SEQRES   1 D   28  ASP ARG LYS GLY GLY SER TYR SER GLN ALA ALA GLY SER          
SEQRES   2 D   28  ASP SER ALA GLN GLY SER ASP VAL SER LEU THR ALA CYS          
SEQRES   3 D   28  LYS VAL                                                      
SEQRES   1 E   28  ASP ARG LYS GLY GLY SER TYR SER GLN ALA ALA GLY SER          
SEQRES   2 E   28  ASP SER ALA GLN GLY SER ASP VAL SER LEU THR ALA CYS          
SEQRES   3 E   28  LYS VAL                                                      
FORMUL   7  HOH   *53(H2 O)                                                     
HELIX    1   1 ASP M  216  THR M  223  1                                   8    
HELIX    2   2 ARG M  243  ARG M  251  1                                   9    
HELIX    3   3 LYS B    7  ALA B   23  1                                  17    
HELIX    4   4 THR B   80  GLY B   95  1                                  16    
HELIX    5   5 SER B  103  GLY B  119  1                                  17    
HELIX    6   6 GLU B  149  GLY B  159  1                                  11    
HELIX    7   7 SER B  187  PHE B  191  5                                   5    
HELIX    8   8 HIS B  193  HIS B  199  1                                   7    
HELIX    9   9 PRO B  200  PHE B  203  5                                   4    
HELIX   10  10 ILE C   11  ALA C   23  1                                  13    
HELIX   11  11 THR C   80  GLY C   95  1                                  16    
HELIX   12  12 SER C  103  GLY C  119  1                                  17    
HELIX   13  13 SER C  187  PHE C  191  5                                   5    
HELIX   14  14 HIS C  193  HIS C  199  1                                   7    
HELIX   15  15 PRO C  200  PHE C  203  5                                   4    
HELIX   16  16 ASP A  216  THR A  223  1                                   8    
HELIX   17  17 ARG A  243  ARG A  251  1                                   9    
HELIX   18  18 ASP E  327  GLY E  331  5                                   5    
SHEET    1   A 8 SER D 321  GLN D 322  0                                        
SHEET    2   A 8 ALA M 405  GLN M 414 -1  N  VAL M 409   O  SER D 321           
SHEET    3   A 8 ILE M 376  PRO M 383 -1  N  ILE M 382   O  THR M 413           
SHEET    4   A 8 TYR M 418  LEU M 420 -1  O  LEU M 420   N  ILE M 376           
SHEET    5   A 8 ASN M 169  VAL M 183  1  N  LEU M 181   O  GLN M 419           
SHEET    6   A 8 VAL M 189  PHE M 203 -1  O  VAL M 195   N  ALA M 178           
SHEET    7   A 8 GLY M 260  LEU M 269 -1  O  PHE M 262   N  MET M 200           
SHEET    8   A 8 GLU M 234  PHE M 238 -1  N  LYS M 237   O  SER M 266           
SHEET    1   B 9 SER M 331  VAL M 335  0                                        
SHEET    2   B 9 GLU M 340  PRO M 349 -1  O  SER M 344   N  SER M 331           
SHEET    3   B 9 THR M 306  PRO M 315 -1  N  ILE M 314   O  ILE M 341           
SHEET    4   B 9 ILE M 376  PRO M 383 -1  O  SER M 377   N  HIS M 313           
SHEET    5   B 9 ALA M 405  GLN M 414 -1  O  THR M 413   N  ILE M 382           
SHEET    6   B 9 ASN M 169  VAL M 183  1  N  LEU M 173   O  TRP M 408           
SHEET    7   B 9 VAL M 189  PHE M 203 -1  O  VAL M 195   N  ALA M 178           
SHEET    8   B 9 GLY M 260  LEU M 269 -1  O  PHE M 262   N  MET M 200           
SHEET    9   B 9 GLU M 234  PHE M 238 -1  N  LYS M 237   O  SER M 266           
SHEET    1   C 3 SER M 254  PHE M 255  0                                        
SHEET    2   C 3 GLU M 209  LEU M 214 -1  N  LEU M 210   O  PHE M 255           
SHEET    3   C 3 VAL M 392  ILE M 398 -1  O  TYR M 394   N  GLY M 213           
SHEET    1   D 4 ILE M 277  SER M 287  0                                        
SHEET    2   D 4 ARG M 290  SER M 299 -1  O  MET M 294   N  VAL M 282           
SHEET    3   D 4 GLU M 353  GLY M 361 -1  O  ALA M 358   N  TYR M 293           
SHEET    4   D 4 ASP M 321  THR M 327 -1  N  LYS M 324   O  HIS M 359           
SHEET    1   E 2 PHE M 385  THR M 386  0                                        
SHEET    2   E 2 PHE C  68  PRO C  69 -1  O  PHE C  68   N  THR M 386           
SHEET    1   F 2 PHE B  68  PRO B  69  0                                        
SHEET    2   F 2 PHE A 385  THR A 386 -1  O  THR A 386   N  PHE B  68           
SHEET    1   G 2 TYR B 143  PRO B 147  0                                        
SHEET    2   G 2 LEU B 181  PHE B 185 -1  O  ARG B 184   N  LYS B 144           
SHEET    1   H 5 LEU C  58  GLU C  59  0                                        
SHEET    2   H 5 ASP A 321  THR A 327 -1  O  PHE A 325   N  LEU C  58           
SHEET    3   H 5 GLU A 353  GLY A 361 -1  O  HIS A 359   N  LYS A 324           
SHEET    4   H 5 ARG A 290  SER A 299 -1  N  TYR A 293   O  ALA A 358           
SHEET    5   H 5 ILE A 277  LYS A 285 -1  N  VAL A 282   O  MET A 294           
SHEET    1   I10 GLN C  61  GLU C  62  0                                        
SHEET    2   I10 SER A 331  VAL A 335  1  O  TRP A 334   N  GLN C  61           
SHEET    3   I10 GLU A 340  PRO A 349 -1  O  SER A 344   N  SER A 331           
SHEET    4   I10 THR A 306  PRO A 315 -1  N  ILE A 314   O  ILE A 341           
SHEET    5   I10 ILE A 376  PRO A 383 -1  O  SER A 377   N  HIS A 313           
SHEET    6   I10 ALA A 405  LEU A 420 -1  O  THR A 413   N  ILE A 382           
SHEET    7   I10 ASN A 169  VAL A 183  1  N  LEU A 181   O  GLN A 419           
SHEET    8   I10 VAL A 189  PHE A 203 -1  O  VAL A 195   N  ALA A 178           
SHEET    9   I10 GLY A 260  LEU A 269 -1  O  PHE A 262   N  MET A 200           
SHEET   10   I10 GLU A 234  PHE A 238 -1  N  LYS A 237   O  SER A 266           
SHEET    1   J 7 GLN C  61  GLU C  62  0                                        
SHEET    2   J 7 SER A 331  VAL A 335  1  O  TRP A 334   N  GLN C  61           
SHEET    3   J 7 GLU A 340  PRO A 349 -1  O  SER A 344   N  SER A 331           
SHEET    4   J 7 THR A 306  PRO A 315 -1  N  ILE A 314   O  ILE A 341           
SHEET    5   J 7 ILE A 376  PRO A 383 -1  O  SER A 377   N  HIS A 313           
SHEET    6   J 7 ALA A 405  LEU A 420 -1  O  THR A 413   N  ILE A 382           
SHEET    7   J 7 SER E 321  GLN E 322 -1  O  SER E 321   N  VAL A 409           
SHEET    1   K 2 TYR C 143  PRO C 147  0                                        
SHEET    2   K 2 LEU C 181  PHE C 185 -1  O  ARG C 184   N  LYS C 144           
SHEET    1   L 3 ILE A 253  PHE A 255  0                                        
SHEET    2   L 3 GLU A 209  LEU A 214 -1  N  LEU A 210   O  PHE A 255           
SHEET    3   L 3 VAL A 392  ILE A 398 -1  O  TYR A 394   N  GLY A 213           
CISPEP   1 GLY B  130    PRO B  131          0        -0.76                     
CISPEP   2 GLY C  130    PRO C  131          0         0.51                     
CRYST1   88.033   98.128  112.740  90.00  90.00  90.00 P 21 21 21    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      0.011359  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010191  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008870        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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