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Database: PDB
Entry: 4EMZ
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HEADER    VIRAL PROTEIN/IMMUNE SYSTEM             12-APR-12   4EMZ              
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: PROTEIN NEF;                                               
COMPND   3 CHAIN: C, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: MHC-I;                                                     
COMPND   7 CHAIN: D, E;                                                         
COMPND   8 FRAGMENT: CYTOPLASMIC DOMAIN;                                        
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: AP-1 COMPLEX SUBUNIT MU-1;                                 
COMPND  12 CHAIN: A, M;                                                         
COMPND  13 FRAGMENT: SORTING MOTIF RECOGNITION DOMAIN;                          
COMPND  14 SYNONYM: AP-MU CHAIN FAMILY MEMBER MU1A, ADAPTOR PROTEIN COMPLEX AP-1
COMPND  15 MU-1 SUBUNIT, ADAPTOR-RELATED PROTEIN COMPLEX 1 MU-1 SUBUNIT,        
COMPND  16 CLATHRIN ASSEMBLY PROTEIN COMPLEX 1 MEDIUM CHAIN 1, CLATHRIN COAT    
COMPND  17 ASSEMBLY PROTEIN AP47, CLATHRIN COAT-ASSOCIATED PROTEIN AP47, GOLGI  
COMPND  18 ADAPTOR HA1/AP1 ADAPTIN MU-1 SUBUNIT, MU-ADAPTIN 1, MU1A-ADAPTIN;    
COMPND  19 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 STRAIN: NL-43;                                                       
SOURCE   5 GENE: NEF;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: HLA-2;                                                         
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  16 ORGANISM_COMMON: MOUSE;                                              
SOURCE  17 ORGANISM_TAXID: 10090;                                               
SOURCE  18 GENE: AP1M1, CLTNM;                                                  
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   2   25-JUL-12 4EMZ    1       JRNL                                     
REVDAT   1   20-JUN-12 4EMZ    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.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0025                                      
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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 24623                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1317                            
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) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1765                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6755                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 18                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 117.86                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.99000                                              
REMARK   3    B22 (A**2) : -2.48000                                             
REMARK   3    B33 (A**2) : 1.49000                                              
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): 0.833         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.432         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.364         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 43.897        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.932                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6953 ; 0.014 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6633 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9397 ; 1.765 ; 1.955       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 15257 ; 1.553 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   818 ; 8.078 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   336 ;35.864 ;22.738       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1171 ;22.350 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;20.727 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   981 ; 0.093 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7724 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1694 ; 0.007 ; 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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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                    : C B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           0     C      7       C     204      0                      
REMARK   3           0     B      7       B     204      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
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    315       D     330      0                      
REMARK   3           0     E    315       E     330      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A M                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           0     A    159       A     423      0                      
REMARK   3           0     M    159       M     423      0                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 22                                         
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   159        A   211                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1926 -31.8361  11.8930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4263 T22:   0.3550                                     
REMARK   3      T33:   0.5543 T12:  -0.0991                                     
REMARK   3      T13:   0.1052 T23:  -0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5951 L22:   3.7854                                     
REMARK   3      L33:   0.7198 L12:  -1.2740                                     
REMARK   3      L13:   0.5546 L23:  -0.8220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0439 S12:  -0.1142 S13:   0.0809                       
REMARK   3      S21:  -0.2802 S22:   0.2016 S23:  -0.6027                       
REMARK   3      S31:  -0.0515 S32:  -0.0993 S33:  -0.2455                       
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   212        A   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1285 -39.3725   2.5189              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6074 T22:   0.3307                                     
REMARK   3      T33:   0.4386 T12:  -0.0190                                     
REMARK   3      T13:   0.2123 T23:   0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5640 L22:   2.6276                                     
REMARK   3      L33:   0.2320 L12:   0.5694                                     
REMARK   3      L13:   0.3410 L23:   0.6185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2346 S12:   0.0361 S13:   0.1350                       
REMARK   3      S21:  -0.6863 S22:  -0.0889 S23:  -0.5743                       
REMARK   3      S31:  -0.1946 S32:  -0.0793 S33:  -0.1457                       
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   271        A   288                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.8506 -13.6168   1.8590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6727 T22:   0.3541                                     
REMARK   3      T33:   0.6045 T12:  -0.1810                                     
REMARK   3      T13:  -0.3380 T23:   0.1232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5716 L22:   0.3875                                     
REMARK   3      L33:   7.1820 L12:  -0.7185                                     
REMARK   3      L13:  -2.0284 L23:   1.6038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3864 S12:  -0.0253 S13:   0.9534                       
REMARK   3      S21:  -0.1126 S22:  -0.1633 S23:  -0.0451                       
REMARK   3      S31:  -0.0015 S32:  -0.6934 S33:  -0.2232                       
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   289        A   423                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.1447 -18.8874  10.9753              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3562 T22:   0.3726                                     
REMARK   3      T33:   0.4998 T12:  -0.0347                                     
REMARK   3      T13:  -0.0185 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4683 L22:   3.9690                                     
REMARK   3      L33:   0.4356 L12:  -1.7793                                     
REMARK   3      L13:   0.4964 L23:  -0.0265                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0669 S12:  -0.3082 S13:   0.3203                       
REMARK   3      S21:  -0.1740 S22:  -0.0084 S23:  -0.3681                       
REMARK   3      S31:   0.0553 S32:  -0.2323 S33:   0.0753                       
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    12        B    61                          
REMARK   3    ORIGIN FOR THE GROUP (A): -54.2522 -50.4186   6.2545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4011 T22:   0.3348                                     
REMARK   3      T33:   1.0226 T12:   0.1138                                     
REMARK   3      T13:  -0.3724 T23:   0.0954                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8526 L22:   2.0129                                     
REMARK   3      L33:   4.7696 L12:   1.2943                                     
REMARK   3      L13:  -1.9629 L23:  -3.0865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1905 S12:   0.3805 S13:   0.3106                       
REMARK   3      S21:   0.0463 S22:   0.5997 S23:   0.5826                       
REMARK   3      S31:  -0.0102 S32:  -0.7274 S33:  -0.7902                       
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    62        B    82                          
REMARK   3    ORIGIN FOR THE GROUP (A): -38.2302 -43.3391  12.6215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4848 T22:   0.3854                                     
REMARK   3      T33:   0.5012 T12:  -0.1197                                     
REMARK   3      T13:   0.0955 T23:   0.0498                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0052 L22:   3.8791                                     
REMARK   3      L33:   0.5848 L12:  -0.4716                                     
REMARK   3      L13:   0.2827 L23:   1.2098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1494 S12:   0.1445 S13:   0.0894                       
REMARK   3      S21:   0.1498 S22:  -0.1840 S23:   0.0815                       
REMARK   3      S31:   0.0973 S32:   0.0647 S33:   0.0345                       
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    83        B   131                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.8819 -55.5791   6.1268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5508 T22:   0.2089                                     
REMARK   3      T33:   0.6160 T12:  -0.0031                                     
REMARK   3      T13:  -0.3313 T23:   0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4575 L22:   1.8288                                     
REMARK   3      L33:   2.2369 L12:   1.3816                                     
REMARK   3      L13:  -0.2438 L23:   0.3958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1402 S12:  -0.1347 S13:   0.0000                       
REMARK   3      S21:  -0.2590 S22:  -0.1037 S23:   0.3849                       
REMARK   3      S31:  -0.0377 S32:  -0.0848 S33:  -0.0365                       
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   132        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5824 -63.4332  -2.6885              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9060 T22:   0.1613                                     
REMARK   3      T33:   0.7566 T12:   0.0318                                     
REMARK   3      T13:  -0.3546 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2063 L22:   2.2498                                     
REMARK   3      L33:   5.0383 L12:  -3.2130                                     
REMARK   3      L13:  -1.8990 L23:  -1.0710                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8533 S12:   0.7094 S13:  -0.5518                       
REMARK   3      S21:  -0.4365 S22:  -0.0461 S23:   0.6052                       
REMARK   3      S31:   0.0640 S32:  -0.7605 S33:  -0.8072                       
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   180        B   203                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.6572 -64.6621   0.4938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8998 T22:   0.1722                                     
REMARK   3      T33:   0.3935 T12:   0.1217                                     
REMARK   3      T13:  -0.1444 T23:  -0.1003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2185 L22:   5.7500                                     
REMARK   3      L33:   2.4187 L12:   0.3624                                     
REMARK   3      L13:  -1.0309 L23:   0.9801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2557 S12:   0.1884 S13:  -0.5754                       
REMARK   3      S21:  -0.9142 S22:   0.0853 S23:  -0.1769                       
REMARK   3      S31:   0.9617 S32:   0.1252 S33:   0.1704                       
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     8        C    16                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.1317  21.6560   3.9446              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5422 T22:   0.4562                                     
REMARK   3      T33:   0.3093 T12:  -0.0524                                     
REMARK   3      T13:  -0.0669 T23:  -0.1254                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1195 L22:  14.7632                                     
REMARK   3      L33:   1.9456 L12:   1.2776                                     
REMARK   3      L13:   0.4655 L23:   5.3575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0676 S12:   0.0492 S13:  -0.0170                       
REMARK   3      S21:  -0.9337 S22:  -0.0374 S23:   0.2810                       
REMARK   3      S31:  -0.3225 S32:   0.0006 S33:   0.1050                       
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    17        C    64                          
REMARK   3    ORIGIN FOR THE GROUP (A): -46.2229   7.5949  13.8053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4603 T22:   0.3772                                     
REMARK   3      T33:   0.8010 T12:  -0.0954                                     
REMARK   3      T13:  -0.3621 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4072 L22:   0.0043                                     
REMARK   3      L33:   3.8393 L12:   0.0203                                     
REMARK   3      L13:  -1.2465 L23:  -0.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0230 S12:   0.1728 S13:  -0.0153                       
REMARK   3      S21:   0.0186 S22:  -0.0303 S23:  -0.0492                       
REMARK   3      S31:  -0.1287 S32:  -0.4843 S33:   0.0533                       
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    65        C    81                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.0040  18.0827  19.0607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5054 T22:   0.4831                                     
REMARK   3      T33:   0.3807 T12:   0.0162                                     
REMARK   3      T13:  -0.0495 T23:  -0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4053 L22:   4.1180                                     
REMARK   3      L33:   0.3878 L12:  -1.7697                                     
REMARK   3      L13:   0.7070 L23:  -0.7592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1375 S12:  -0.0669 S13:  -0.2391                       
REMARK   3      S21:  -0.6512 S22:   0.0396 S23:   0.2122                       
REMARK   3      S31:   0.0043 S32:   0.0457 S33:  -0.1771                       
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    82        C   179                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.2036  27.1583  17.0700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4333 T22:   0.3541                                     
REMARK   3      T33:   0.4343 T12:   0.0871                                     
REMARK   3      T13:  -0.1008 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1812 L22:   1.6644                                     
REMARK   3      L33:   3.8836 L12:   0.6622                                     
REMARK   3      L13:  -0.9666 L23:   0.7733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1902 S12:  -0.0111 S13:   0.0010                       
REMARK   3      S21:  -0.3470 S22:   0.0376 S23:   0.3183                       
REMARK   3      S31:  -0.2918 S32:  -0.4273 S33:   0.1526                       
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   180        C   203                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.6761  36.2403  23.2209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4528 T22:   0.2520                                     
REMARK   3      T33:   1.3907 T12:   0.1726                                     
REMARK   3      T13:  -0.1347 T23:   0.2116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5142 L22:   4.5023                                     
REMARK   3      L33:   0.2351 L12:  -5.7025                                     
REMARK   3      L13:  -0.2470 L23:  -0.4969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2494 S12:  -0.6490 S13:   1.5297                       
REMARK   3      S21:   0.1000 S22:   0.7658 S23:   0.6422                       
REMARK   3      S31:  -0.0035 S32:  -0.1455 S33:  -0.5164                       
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   314        D   319                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.4649  11.2190  20.4251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4586 T22:   0.5056                                     
REMARK   3      T33:   0.3572 T12:   0.0197                                     
REMARK   3      T13:  -0.0314 T23:  -0.0848                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.6989 L22:  29.0159                                     
REMARK   3      L33:   5.2913 L12:   1.8891                                     
REMARK   3      L13:  -9.6167 L23:   5.5461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8408 S12:  -0.2124 S13:  -0.8060                       
REMARK   3      S21:  -0.4495 S22:  -0.8217 S23:  -1.3201                       
REMARK   3      S31:  -0.4577 S32:  -0.0463 S33:  -0.0190                       
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 :   D   320        D   332                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.2469  27.5523  24.0279              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4503 T22:   0.4300                                     
REMARK   3      T33:   0.2647 T12:   0.0248                                     
REMARK   3      T13:  -0.0329 T23:   0.0519                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.4894 L22:   3.8155                                     
REMARK   3      L33:   0.6846 L12:  -4.6741                                     
REMARK   3      L13:  -2.0733 L23:   1.5983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0342 S12:  -0.0034 S13:   0.2782                       
REMARK   3      S21:  -0.3351 S22:   0.0283 S23:  -0.0393                       
REMARK   3      S31:  -0.1978 S32:  -0.0044 S33:   0.0059                       
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 :   E   315        E   319                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8836 -29.2608  23.1019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7318 T22:   0.3636                                     
REMARK   3      T33:   0.7011 T12:  -0.0025                                     
REMARK   3      T13:   0.0021 T23:   0.0693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1737 L22:  16.9858                                     
REMARK   3      L33:  11.9992 L12:  10.9071                                     
REMARK   3      L13:  10.9157 L23:  10.5090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0914 S12:   0.1877 S13:  -0.0265                       
REMARK   3      S21:   1.8604 S22:   0.1733 S23:  -0.3213                       
REMARK   3      S31:  -0.5377 S32:   0.1683 S33:  -0.0819                       
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 :   E   320        E   331                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0710 -47.5030  14.2337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4854 T22:   0.3786                                     
REMARK   3      T33:   0.4235 T12:  -0.0886                                     
REMARK   3      T13:  -0.0857 T23:   0.0781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9045 L22:   1.3985                                     
REMARK   3      L33:   0.0437 L12:   0.1937                                     
REMARK   3      L13:   0.0262 L23:   0.2042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1496 S12:  -0.5608 S13:  -0.6736                       
REMARK   3      S21:  -0.2541 S22:  -0.1378 S23:  -0.0650                       
REMARK   3      S31:  -0.0932 S32:   0.0366 S33:  -0.0119                       
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   159        M   211                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4055  16.3063  33.6797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5298 T22:   0.5075                                     
REMARK   3      T33:   0.2619 T12:   0.0583                                     
REMARK   3      T13:  -0.0761 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4701 L22:   5.2847                                     
REMARK   3      L33:   0.1672 L12:   1.2187                                     
REMARK   3      L13:  -0.4514 L23:  -0.2350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3064 S12:  -0.2081 S13:   0.0004                       
REMARK   3      S21:   0.6614 S22:   0.3401 S23:  -0.1746                       
REMARK   3      S31:   0.0566 S32:   0.0524 S33:  -0.0337                       
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   212        M   270                          
REMARK   3    ORIGIN FOR THE GROUP (A): -23.1667  21.5536  37.9154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5397 T22:   0.4936                                     
REMARK   3      T33:   0.1860 T12:   0.1417                                     
REMARK   3      T13:   0.0414 T23:  -0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8310 L22:   1.0888                                     
REMARK   3      L33:   1.8146 L12:  -0.1251                                     
REMARK   3      L13:   0.3952 L23:  -0.9437                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1533 S12:  -0.4148 S13:  -0.1773                       
REMARK   3      S21:   0.5303 S22:   0.2853 S23:   0.0256                       
REMARK   3      S31:  -0.2369 S32:  -0.2843 S33:  -0.1320                       
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   271        M   381                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2454 -14.2241  26.8482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3116 T22:   0.3926                                     
REMARK   3      T33:   0.4587 T12:  -0.0481                                     
REMARK   3      T13:  -0.1161 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2101 L22:   5.6955                                     
REMARK   3      L33:   2.1215 L12:  -0.9525                                     
REMARK   3      L13:   0.4168 L23:  -0.6325                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0026 S12:  -0.0163 S13:  -0.0428                       
REMARK   3      S21:   0.0047 S22:   0.1344 S23:   0.1571                       
REMARK   3      S31:   0.1939 S32:  -0.1485 S33:  -0.1370                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
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): -17.2917  15.1121  28.8891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4511 T22:   0.4634                                     
REMARK   3      T33:   0.3198 T12:   0.0171                                     
REMARK   3      T13:  -0.0452 T23:   0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3155 L22:   2.1539                                     
REMARK   3      L33:   0.2808 L12:  -0.2304                                     
REMARK   3      L13:  -0.2345 L23:  -0.6645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1042 S12:  -0.1011 S13:  -0.0835                       
REMARK   3      S21:   0.0833 S22:   0.0846 S23:   0.0668                       
REMARK   3      S31:  -0.0343 S32:  -0.0132 S33:   0.0197                       
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 4EMZ 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 RCSB ID CODE IS RCSB071821.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-10                          
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) : 0.9792                             
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                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26098                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.04                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51                     
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       44.66200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.20350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.23550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       57.20350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.66200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.23550            
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: 4690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, M, 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: 4610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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     MSE 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     GLU C    24                                                      
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     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     MSE C   173                                                      
REMARK 465     ASP C   174                                                      
REMARK 465     ASP C   175                                                      
REMARK 465     PRO C   176                                                      
REMARK 465     GLU C   177                                                      
REMARK 465     ASN C   205                                                      
REMARK 465     CYS C   206                                                      
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     ASP E   314                                                      
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 465     MSE B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ALA B    26                                                      
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     ASP B   151                                                      
REMARK 465     LYS B   152                                                      
REMARK 465     VAL B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     GLU B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     ASN B   157                                                      
REMARK 465     LYS B   158                                                      
REMARK 465     GLY B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     ASN B   161                                                      
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     MSE B   173                                                      
REMARK 465     ASP B   174                                                      
REMARK 465     ASP B   175                                                      
REMARK 465     PRO B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     ASN B   205                                                      
REMARK 465     CYS B   206                                                      
REMARK 465     SER A   158                                                      
REMARK 465     PRO A   363                                                      
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     SER M   158                                                      
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 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   NH1  ARG A   290     C    PHE A   360              1.62            
REMARK 500   NH1  ARG A   290     CA   PHE A   360              1.89            
REMARK 500   OE1  GLU A   177     OG   SER A   388              1.96            
REMARK 500   OE1  GLU M   177     OG   SER M   388              2.02            
REMARK 500   O    SER M   205     OH   TYR M   403              2.09            
REMARK 500   NH1  ARG M   160     O    GLY M   206              2.10            
REMARK 500   NH1  ARG A   290     N    GLY A   361              2.13            
REMARK 500   NE2  HIS B   192     OE2  GLU B   197              2.14            
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    ILE C  11       34.21    -98.16                                   
REMARK 500    CYS C 142       31.13    -97.03                                   
REMARK 500    GLU C 149      -60.51    -94.69                                   
REMARK 500    LYS D 316     -131.46     45.29                                   
REMARK 500    LYS E 316      -73.23   -143.01                                   
REMARK 500    GLU B  64       75.40   -112.56                                   
REMARK 500    PRO B 122       40.71    -85.08                                   
REMARK 500    GLU B 149      -71.02    -75.98                                   
REMARK 500    SER A 161      170.51    -55.69                                   
REMARK 500    ASN A 215       34.71    -90.52                                   
REMARK 500    ASP A 250        0.42     81.67                                   
REMARK 500    ARG A 251       32.72     77.48                                   
REMARK 500    THR A 271       75.76     52.33                                   
REMARK 500    HIS A 286      -92.50   -117.30                                   
REMARK 500    SER A 289        7.87     83.09                                   
REMARK 500    ASN A 338       -8.88     80.09                                   
REMARK 500    TYR A 403       70.99     54.08                                   
REMARK 500    PRO M 258     -177.08    -62.74                                   
REMARK 500    PHE M 360      -90.66   -120.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EN2   RELATED DB: PDB                                   
DBREF  4EMZ C    1   206  UNP    Q90VU7   Q90VU7_9HIV1     1    206             
DBREF  4EMZ B    1   206  UNP    Q90VU7   Q90VU7_9HIV1     1    206             
DBREF  4EMZ A  158   423  UNP    P35585   AP1M1_MOUSE    158    423             
DBREF  4EMZ M  158   423  UNP    P35585   AP1M1_MOUSE    158    423             
DBREF  4EMZ D  314   341  PDB    4EMZ     4EMZ           314    341             
DBREF  4EMZ E  314   341  PDB    4EMZ     4EMZ           314    341             
SEQRES   1 C  206  MSE GLY GLY LYS TRP SER LYS SER SER VAL ILE GLY TRP          
SEQRES   2 C  206  PRO ALA VAL ARG GLU ARG MSE 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  MSE 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 MSE 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 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                                                      
SEQRES   1 B  206  MSE GLY GLY LYS TRP SER LYS SER SER VAL ILE GLY TRP          
SEQRES   2 B  206  PRO ALA VAL ARG GLU ARG MSE 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  MSE 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 MSE 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 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 MSE ARG VAL PHE LEU SER GLY MSE 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 MSE 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 MSE 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 MSE 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 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 MSE ARG VAL PHE LEU SER GLY MSE 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 MSE 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 MSE 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 MSE 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                                      
MODRES 4EMZ MSE C   20  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE C   79  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE B   20  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE B   79  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE A  200  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE A  207  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE A  265  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE A  294  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE A  356  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE M  200  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE M  207  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE M  265  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE M  294  MET  SELENOMETHIONINE                                   
MODRES 4EMZ MSE M  356  MET  SELENOMETHIONINE                                   
HET    MSE  C  20       8                                                       
HET    MSE  C  79       8                                                       
HET    MSE  B  20       8                                                       
HET    MSE  B  79       8                                                       
HET    MSE  A 200       8                                                       
HET    MSE  A 207       8                                                       
HET    MSE  A 265       8                                                       
HET    MSE  A 294       8                                                       
HET    MSE  A 356       8                                                       
HET    MSE  M 200       8                                                       
HET    MSE  M 207       8                                                       
HET    MSE  M 265       8                                                       
HET    MSE  M 294       8                                                       
HET    MSE  M 356       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    14(C5 H11 N O2 SE)                                           
FORMUL   7  HOH   *18(H2 O)                                                     
HELIX    1   1 SER C    9  ILE C   11  5                                   3    
HELIX    2   2 GLY C   12  ARG C   21  1                                  10    
HELIX    3   3 THR C   80  GLY C   95  1                                  16    
HELIX    4   4 SER C  103  GLY C  119  1                                  17    
HELIX    5   5 SER C  187  PHE C  191  5                                   5    
HELIX    6   6 HIS C  193  HIS C  199  1                                   7    
HELIX    7   7 PRO C  200  PHE C  203  5                                   4    
HELIX    8   8 SER B    6  ILE B   11  1                                   6    
HELIX    9   9 ILE B   11  ARG B   21  1                                  11    
HELIX   10  10 THR B   80  GLY B   95  1                                  16    
HELIX   11  11 SER B  103  GLY B  119  1                                  17    
HELIX   12  12 SER B  187  PHE B  191  5                                   5    
HELIX   13  13 VAL B  194  HIS B  199  1                                   6    
HELIX   14  14 PRO B  200  PHE B  203  5                                   4    
HELIX   15  15 ASP A  216  THR A  223  1                                   8    
HELIX   16  16 LEU A  244  ASN A  249  1                                   6    
HELIX   17  17 ASP M  216  THR M  223  1                                   8    
HELIX   18  18 LEU M  244  ARG M  251  1                                   8    
HELIX   19  19 PRO M  336  ASN M  338  5                                   3    
SHEET    1   A 5 LEU C  58  GLU C  59  0                                        
SHEET    2   A 5 ASP A 321  THR A 327 -1  O  PHE A 325   N  LEU C  58           
SHEET    3   A 5 LYS A 352  GLY A 361 -1  O  ARG A 357   N  LYS A 326           
SHEET    4   A 5 ARG A 290  SER A 299 -1  N  TYR A 293   O  ALA A 358           
SHEET    5   A 5 ILE A 277  LYS A 285 -1  N  TRP A 278   O  LYS A 298           
SHEET    1   B 2 PHE C  68  PRO C  69  0                                        
SHEET    2   B 2 PHE M 385  THR M 386 -1  O  THR M 386   N  PHE C  68           
SHEET    1   C 2 TYR C 143  PRO C 147  0                                        
SHEET    2   C 2 LEU C 181  PHE C 185 -1  O  ARG C 184   N  LYS C 144           
SHEET    1   D 8 SER D 321  GLN D 322  0                                        
SHEET    2   D 8 ALA M 405  GLN M 414 -1  O  VAL M 409   N  SER D 321           
SHEET    3   D 8 ASN M 169  VAL M 183  1  N  GLU M 177   O  GLN M 414           
SHEET    4   D 8 TYR M 418  LEU M 420  1  O  GLN M 419   N  VAL M 183           
SHEET    5   D 8 ILE M 376  PRO M 383 -1  N  ILE M 376   O  LEU M 420           
SHEET    6   D 8 THR M 306  PRO M 315 -1  N  ASN M 308   O  GLU M 381           
SHEET    7   D 8 GLU M 340  PRO M 349 -1  O  PHE M 348   N  ALA M 307           
SHEET    8   D 8 SER M 331  VAL M 335 -1  N  VAL M 335   O  GLU M 340           
SHEET    1   E 9 GLU M 234  PHE M 238  0                                        
SHEET    2   E 9 GLY M 260  ASN M 270 -1  O  SER M 266   N  LYS M 237           
SHEET    3   E 9 VAL M 189  PHE M 203 -1  N  ILE M 198   O  MSE M 265           
SHEET    4   E 9 ASN M 169  VAL M 183 -1  N  ASN M 180   O  GLU M 193           
SHEET    5   E 9 ALA M 405  GLN M 414  1  O  GLN M 414   N  GLU M 177           
SHEET    6   E 9 ILE M 376  PRO M 383 -1  N  ILE M 382   O  THR M 413           
SHEET    7   E 9 THR M 306  PRO M 315 -1  N  ASN M 308   O  GLU M 381           
SHEET    8   E 9 GLU M 340  PRO M 349 -1  O  PHE M 348   N  ALA M 307           
SHEET    9   E 9 SER M 331  VAL M 335 -1  N  VAL M 335   O  GLU M 340           
SHEET    1   F 6 SER E 321  GLN E 322  0                                        
SHEET    2   F 6 ALA A 405  LEU A 420 -1  O  VAL A 409   N  SER E 321           
SHEET    3   F 6 ASN A 169  VAL A 183  1  N  VAL A 175   O  ILE A 412           
SHEET    4   F 6 ILE A 194  PHE A 203 -1  O  LYS A 199   N  ASP A 174           
SHEET    5   F 6 GLY A 260  LEU A 269 -1  O  MSE A 265   N  ILE A 198           
SHEET    6   F 6 GLU A 234  PHE A 238 -1  N  GLU A 234   O  ARG A 268           
SHEET    1   G 7 VAL A 189  ARG A 191  0                                        
SHEET    2   G 7 ASN A 169  VAL A 183 -1  N  LEU A 182   O  LEU A 190           
SHEET    3   G 7 ALA A 405  LEU A 420  1  O  ILE A 412   N  VAL A 175           
SHEET    4   G 7 ILE A 376  PRO A 383 -1  N  ILE A 382   O  THR A 413           
SHEET    5   G 7 THR A 306  PRO A 315 -1  N  HIS A 313   O  SER A 377           
SHEET    6   G 7 GLU A 340  PRO A 349 -1  O  PHE A 348   N  ALA A 307           
SHEET    7   G 7 SER A 331  VAL A 335 -1  N  SER A 331   O  SER A 344           
SHEET    1   H 2 PHE B  68  PRO B  69  0                                        
SHEET    2   H 2 PHE A 385  THR A 386 -1  O  THR A 386   N  PHE B  68           
SHEET    1   I 2 TYR B 143  PRO B 147  0                                        
SHEET    2   I 2 LEU B 181  PHE B 185 -1  O  ARG B 184   N  LYS B 144           
SHEET    1   J 4 VAL A 242  ARG A 243  0                                        
SHEET    2   J 4 SER A 254  PHE A 255 -1  O  SER A 254   N  ARG A 243           
SHEET    3   J 4 GLU A 209  LEU A 214 -1  N  LEU A 210   O  PHE A 255           
SHEET    4   J 4 VAL A 392  ILE A 398 -1  O  ILE A 398   N  GLU A 209           
SHEET    1   K 4 VAL M 242  ARG M 243  0                                        
SHEET    2   K 4 ILE M 253  PHE M 255 -1  O  SER M 254   N  ARG M 243           
SHEET    3   K 4 GLU M 209  LEU M 214 -1  N  LEU M 210   O  PHE M 255           
SHEET    4   K 4 VAL M 392  ILE M 398 -1  O  TYR M 394   N  GLY M 213           
SHEET    1   L 4 ILE M 277  HIS M 286  0                                        
SHEET    2   L 4 ARG M 290  SER M 299 -1  O  ARG M 290   N  HIS M 286           
SHEET    3   L 4 LYS M 352  HIS M 359 -1  O  ALA M 358   N  TYR M 293           
SHEET    4   L 4 LYS M 324  THR M 327 -1  N  LYS M 326   O  ARG M 357           
LINK         C   ARG C  19                 N   MSE C  20     1555   1555  1.31  
LINK         C   MSE C  20                 N   ARG C  21     1555   1555  1.33  
LINK         C   PRO C  78                 N   MSE C  79     1555   1555  1.32  
LINK         C   MSE C  79                 N   THR C  80     1555   1555  1.33  
LINK         C   ARG B  19                 N   MSE B  20     1555   1555  1.32  
LINK         C   MSE B  20                 N   ARG B  21     1555   1555  1.33  
LINK         C   PRO B  78                 N   MSE B  79     1555   1555  1.34  
LINK         C   MSE B  79                 N   THR B  80     1555   1555  1.32  
LINK         C   LYS A 199                 N   MSE A 200     1555   1555  1.32  
LINK         C   MSE A 200                 N   ARG A 201     1555   1555  1.33  
LINK         C   GLY A 206                 N   MSE A 207     1555   1555  1.33  
LINK         C   MSE A 207                 N   PRO A 208     1555   1555  1.36  
LINK         C   LEU A 264                 N   MSE A 265     1555   1555  1.32  
LINK         C   MSE A 265                 N   SER A 266     1555   1555  1.33  
LINK         C   TYR A 293                 N   MSE A 294     1555   1555  1.32  
LINK         C   MSE A 294                 N   VAL A 295     1555   1555  1.32  
LINK         C   LEU A 355                 N   MSE A 356     1555   1555  1.33  
LINK         C   MSE A 356                 N   ARG A 357     1555   1555  1.33  
LINK         C   LYS M 199                 N   MSE M 200     1555   1555  1.33  
LINK         C   MSE M 200                 N   ARG M 201     1555   1555  1.34  
LINK         C   GLY M 206                 N   MSE M 207     1555   1555  1.33  
LINK         C   MSE M 207                 N   PRO M 208     1555   1555  1.34  
LINK         C   LEU M 264                 N   MSE M 265     1555   1555  1.33  
LINK         C   MSE M 265                 N   SER M 266     1555   1555  1.34  
LINK         C   TYR M 293                 N   MSE M 294     1555   1555  1.33  
LINK         C   MSE M 294                 N   VAL M 295     1555   1555  1.33  
LINK         C   LEU M 355                 N   MSE M 356     1555   1555  1.32  
LINK         C   MSE M 356                 N   ARG M 357     1555   1555  1.34  
CISPEP   1 GLY C  130    PRO C  131          0        -7.30                     
CISPEP   2 GLY B  130    PRO B  131          0        -5.08                     
CRYST1   89.324  112.471  114.407  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      0.011195  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008891  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008741        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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