GenomeNet

Database: PDB
Entry: 2GO7
LinkDB: 2GO7
Original site: 2GO7 
HEADER    HYDROLASE                               12-APR-06   2GO7              
TITLE     CRYSTAL STRUCTURE OF A HYDROLASE FROM HALOACID DEHALOGENASE-LIKE      
TITLE    2 FAMILY (SP_2064) FROM STREPTOCOCCUS PNEUMONIAE TIGR4 AT 2.10 A       
TITLE    3 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYDROLASE, HALOACID DEHALOGENASE-LIKE FAMILY;              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 170187;                                              
SOURCE   4 STRAIN: TIGR4;                                                       
SOURCE   5 GENE: NP_346487.1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,      
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, PSI-2, HYDROLASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   5   25-OCT-17 2GO7    1       REMARK                                   
REVDAT   4   13-JUL-11 2GO7    1       VERSN                                    
REVDAT   3   28-JUL-10 2GO7    1       TITLE  KEYWDS                            
REVDAT   2   24-FEB-09 2GO7    1       VERSN                                    
REVDAT   1   23-MAY-06 2GO7    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF (NP_346487.1) FROM STREPTOCOCCUS        
JRNL        TITL 2 PNEUMONIAE TIGR4 AT 2.10 A RESOLUTION                        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 70427                          
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) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3555                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4820                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.88                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 257                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6478                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 492                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 35.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.27000                                             
REMARK   3    B22 (A**2) : -0.27000                                             
REMARK   3    B33 (A**2) : 0.40000                                              
REMARK   3    B12 (A**2) : -0.13000                                             
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): 0.156         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.145         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.105         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.502         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6645 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  4368 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9022 ; 1.439 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10648 ; 0.958 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   820 ; 6.096 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   344 ;36.984 ;25.029       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1113 ;14.564 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;13.835 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1016 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7501 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1392 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1374 ; 0.211 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4547 ; 0.184 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3286 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3257 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   387 ; 0.162 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.087 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    15 ; 0.253 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    28 ; 0.257 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.112 ; 0.200       
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):  4245 ; 1.905 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1654 ; 0.685 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6545 ; 2.665 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2833 ; 4.559 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2472 ; 6.427 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A     204      4                      
REMARK   3           1     B      4       B     204      4                      
REMARK   3           1     C      4       C     204      4                      
REMARK   3           1     D      4       D     204      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2568 ; 0.480 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2568 ; 0.510 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2568 ; 0.550 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   2568 ; 0.410 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2568 ; 1.140 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2568 ; 1.250 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2568 ; 1.190 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   2568 ; 0.990 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    16                          
REMARK   3    RESIDUE RANGE :   A    84        A   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.9851   4.4000  12.1470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0582 T22:  -0.1302                                     
REMARK   3      T33:  -0.0859 T12:  -0.0107                                     
REMARK   3      T13:  -0.0042 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8579 L22:   1.6614                                     
REMARK   3      L33:   0.9428 L12:   0.4976                                     
REMARK   3      L13:  -0.3660 L23:  -0.0914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0220 S12:   0.1456 S13:   0.3638                       
REMARK   3      S21:  -0.0698 S22:   0.0238 S23:   0.1207                       
REMARK   3      S31:  -0.1341 S32:  -0.1147 S33:  -0.0458                       
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    17        A    83                          
REMARK   3    ORIGIN FOR THE GROUP (A): 113.7161  -0.0923  13.2457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0650 T22:  -0.1092                                     
REMARK   3      T33:  -0.0054 T12:  -0.0464                                     
REMARK   3      T13:   0.0008 T23:   0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6393 L22:   2.3191                                     
REMARK   3      L33:   0.8681 L12:  -0.4829                                     
REMARK   3      L13:  -0.1280 L23:   0.2223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0356 S12:  -0.0271 S13:   0.1904                       
REMARK   3      S21:  -0.0490 S22:  -0.0013 S23:  -0.4283                       
REMARK   3      S31:  -0.0648 S32:   0.1655 S33:  -0.0344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B    16                          
REMARK   3    RESIDUE RANGE :   B    84        B   204                          
REMARK   3    ORIGIN FOR THE GROUP (A): 106.5618 -27.1226  16.8918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0936 T22:  -0.1315                                     
REMARK   3      T33:  -0.0640 T12:   0.0100                                     
REMARK   3      T13:  -0.0375 T23:   0.0354                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6830 L22:   1.7556                                     
REMARK   3      L33:   1.1877 L12:  -0.4913                                     
REMARK   3      L13:  -0.4327 L23:  -0.0387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0188 S12:  -0.0144 S13:  -0.2000                       
REMARK   3      S21:  -0.0172 S22:   0.0573 S23:  -0.0439                       
REMARK   3      S31:   0.0633 S32:   0.0048 S33:  -0.0384                       
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 :   B    17        B    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.8593 -17.0685  30.9728              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0098 T22:  -0.0794                                     
REMARK   3      T33:  -0.1305 T12:   0.0006                                     
REMARK   3      T13:   0.0152 T23:   0.0330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2681 L22:   1.0794                                     
REMARK   3      L33:   0.8885 L12:  -0.7943                                     
REMARK   3      L13:  -0.4611 L23:   0.3101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1960 S12:  -0.3144 S13:  -0.1133                       
REMARK   3      S21:   0.2670 S22:   0.0935 S23:   0.0783                       
REMARK   3      S31:   0.0879 S32:  -0.0197 S33:   0.1025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     0        C    16                          
REMARK   3    RESIDUE RANGE :   C    84        C   204                          
REMARK   3    ORIGIN FOR THE GROUP (A):  73.0233 -30.8618   8.4993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0360 T22:  -0.0167                                     
REMARK   3      T33:   0.0239 T12:  -0.0563                                     
REMARK   3      T13:   0.0214 T23:  -0.0951                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1266 L22:   1.4022                                     
REMARK   3      L33:   1.6523 L12:  -0.0997                                     
REMARK   3      L13:  -0.0322 L23:   0.0951                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0454 S12:   0.3065 S13:  -0.5371                       
REMARK   3      S21:  -0.0986 S22:  -0.0661 S23:   0.0533                       
REMARK   3      S31:   0.2839 S32:  -0.0135 S33:   0.1115                       
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 :   C    17        C    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1533 -11.0459  21.2440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0974 T22:  -0.0938                                     
REMARK   3      T33:  -0.0839 T12:  -0.0274                                     
REMARK   3      T13:  -0.0086 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2628 L22:   1.0660                                     
REMARK   3      L33:   1.2774 L12:   1.2178                                     
REMARK   3      L13:  -0.4981 L23:  -0.0580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0700 S12:  -0.0855 S13:   0.0127                       
REMARK   3      S21:   0.0906 S22:  -0.0436 S23:   0.1200                       
REMARK   3      S31:  -0.0694 S32:  -0.1770 S33:  -0.0264                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D    16                          
REMARK   3    RESIDUE RANGE :   D    84        D   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9251 -22.3174  15.3858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0756 T22:   0.1182                                     
REMARK   3      T33:   0.0155 T12:  -0.0192                                     
REMARK   3      T13:  -0.0440 T23:  -0.0095                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9976 L22:   1.2914                                     
REMARK   3      L33:   3.0466 L12:   0.3673                                     
REMARK   3      L13:  -0.7458 L23:   0.0524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0126 S12:   0.3985 S13:  -0.0339                       
REMARK   3      S21:  -0.1083 S22:   0.0350 S23:   0.3103                       
REMARK   3      S31:   0.0694 S32:  -0.4910 S33:  -0.0224                       
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 :   D    17        D    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4935 -28.1759  -6.8765              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0495 T22:   0.2415                                     
REMARK   3      T33:  -0.0370 T12:  -0.1243                                     
REMARK   3      T13:  -0.0610 T23:  -0.0787                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3327 L22:   2.2765                                     
REMARK   3      L33:   4.0154 L12:  -1.3856                                     
REMARK   3      L13:  -0.4009 L23:   0.6660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0871 S12:   0.2326 S13:  -0.1974                       
REMARK   3      S21:  -0.2077 S22:   0.1954 S23:   0.0446                       
REMARK   3      S31:   0.0984 S32:  -0.4025 S33:  -0.1083                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: (1) HYDROGENS HAVE BEEN ADDED IN THE      
REMARK   3  RIDING POSITIONS. (2) A MET-INHIBITION PROTOCOL WAS USED FOR        
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO        
REMARK   3  0.75 TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL     
REMARK   3  S-MET INCORPORATION. (3) THERE IS UNKNOWN DENSITY NEAR TYR18 IN     
REMARK   3  CHAINS B AND C, WHICH IS ABSENT FROM CHAINS A AND D. THIS WAS       
REMARK   3  LEFT UNMODELED. SINCE THE UNKNOWN DENSITY IS LOCATED NEAR THE       
REMARK   3  ACTIVE SITE OF THE PROTEIN, THIS COULD BE POSSIBLE TO BE A          
REMARK   3  SUBSTRATE MOLECULE, SUCH AS HALOACID. (4) ATOM RECORD CONTAINS      
REMARK   3  RESIDUAL B FACTORS ONLY.                                            
REMARK   4                                                                      
REMARK   4 2GO7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000037353.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979224, 0.918370, 0.978940       
REMARK 200  MONOCHROMATOR                  : SINGLE CRYSTAL SI(111) BENT        
REMARK 200                                   MONOCHROMATOR (HORIZONTAL          
REMARK 200                                   FOCUSING)                          
REMARK 200  OPTICS                         : FLAT MIRROR (VERTICAL FOCUSING)    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70459                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.760                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MGCL2, 40.0% PEG-400, 0.1M          
REMARK 280  CITRATE, PH 5.5, VAPOR DIFFUSION, SITTING DROP, NANODROP,           
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.48000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.96000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.22000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       73.70000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       14.74000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1,2,3,4                                                 
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300 SIZE EXCLUSION CHROMATOGRAPHY DATA SUPPORTS THE                      
REMARK 300 ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT                
REMARK 300 OLIGOMERIZATION STATE.                                               
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR B   205                                                      
REMARK 465     LYS B   206                                                      
REMARK 465     THR C   205                                                      
REMARK 465     LYS C   206                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     LYS D   206                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   3    CE   NZ                                             
REMARK 470     LYS A  47    CD   CE   NZ                                        
REMARK 470     GLN A  70    OE1  NE2                                            
REMARK 470     LYS A 118    CE   NZ                                             
REMARK 470     GLU A 188    CD   OE1  OE2                                       
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     LYS B  40    CD   CE   NZ                                        
REMARK 470     ARG B  42    NH1  NH2                                            
REMARK 470     LYS B 118    CD   CE   NZ                                        
REMARK 470     ARG B 201    CZ   NH1  NH2                                       
REMARK 470     MSE C   1    CG  SE    CE                                        
REMARK 470     GLU C  39    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  40    NZ                                                  
REMARK 470     GLU C  98    OE1  OE2                                            
REMARK 470     LYS C 118    CD   CE   NZ                                        
REMARK 470     GLU C 188    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 201    CZ   NH1  NH2                                       
REMARK 470     TYR D  18    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     LYS D  40    NZ                                                  
REMARK 470     LYS D  47    CD   CE   NZ                                        
REMARK 470     GLN D  74    CD   OE1  NE2                                       
REMARK 470     LYS D 118    CD   CE   NZ                                        
REMARK 470     GLU D 143    OE1  OE2                                            
REMARK 470     GLU D 184    CD   OE1  OE2                                       
REMARK 470     GLU D 188    CD   OE1  OE2                                       
REMARK 470     ARG D 192    CZ   NH1  NH2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  10      -80.78    -98.14                                   
REMARK 500    THR A  13      -70.90   -114.78                                   
REMARK 500    TYR A  48     -109.27   -115.55                                   
REMARK 500    LEU B  10      -78.53    -93.80                                   
REMARK 500    THR B  13      -72.17   -119.06                                   
REMARK 500    TYR B  48     -106.62   -118.71                                   
REMARK 500    THR B 131     -168.69   -119.83                                   
REMARK 500    LEU C  10      -77.53    -95.52                                   
REMARK 500    THR C  13      -79.98   -120.32                                   
REMARK 500    TYR C  48     -119.17   -120.72                                   
REMARK 500    THR C 131     -169.72   -118.30                                   
REMARK 500    LEU D  10      -75.98   -100.77                                   
REMARK 500    THR D  13      -68.63   -121.69                                   
REMARK 500    TYR D  48     -118.47   -129.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 207  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   9   OD2                                                    
REMARK 620 2 HOH A 215   O    90.4                                              
REMARK 620 3 ASP A 164   OD1  84.2  83.5                                        
REMARK 620 4 HOH A 213   O   168.6  93.6  85.6                                  
REMARK 620 5 ASP A  11   O    95.5 173.8  98.9  80.9                            
REMARK 620 6 HOH A 214   O   100.5  81.3 164.1  90.7  95.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 207  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 164   OD1                                                    
REMARK 620 2 HOH B 212   O    88.3                                              
REMARK 620 3 ASP B   9   OD2  82.6  92.9                                        
REMARK 620 4 HOH B 211   O   173.0  91.7  90.4                                  
REMARK 620 5 HOH B 210   O    94.2  99.5 167.1  92.8                            
REMARK 620 6 ASP B  11   O    91.1 178.0  85.1  88.6  82.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 207  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C   9   OD2                                                    
REMARK 620 2 HOH C 212   O   170.2                                              
REMARK 620 3 HOH C 213   O    93.6  95.5                                        
REMARK 620 4 HOH C 214   O    89.1  94.9  88.6                                  
REMARK 620 5 ASP C 164   OD1  82.7  89.0 169.1  81.1                            
REMARK 620 6 ASP C  11   O    90.2  85.5  93.5 177.8  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 207  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 211   O                                                      
REMARK 620 2 HOH D 213   O    81.5                                              
REMARK 620 3 ASP D  11   O    92.5 173.3                                        
REMARK 620 4 HOH D 212   O    94.6  82.7  94.9                                  
REMARK 620 5 ASP D   9   OD2 170.3  96.9  89.5  94.6                            
REMARK 620 6 ASP D 164   OD1  81.1  87.5  94.5 169.8  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 207                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 210                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 208                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 211                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 210                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 209                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 211                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 210                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 212                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 359637   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION                      
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV                
REMARK 999 PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE                  
REMARK 999 TARGET SEQUENCE.                                                     
DBREF  2GO7 A    1   206  UNP    Q97NG6   Q97NG6_STRPN     1    206             
DBREF  2GO7 B    1   206  UNP    Q97NG6   Q97NG6_STRPN     1    206             
DBREF  2GO7 C    1   206  UNP    Q97NG6   Q97NG6_STRPN     1    206             
DBREF  2GO7 D    1   206  UNP    Q97NG6   Q97NG6_STRPN     1    206             
SEQADV 2GO7 GLY A    0  UNP  Q97NG6              LEADER SEQUENCE                
SEQADV 2GO7 MSE A    1  UNP  Q97NG6    MET     1 MODIFIED RESIDUE               
SEQADV 2GO7 MSE A   86  UNP  Q97NG6    MET    86 MODIFIED RESIDUE               
SEQADV 2GO7 GLY B    0  UNP  Q97NG6              LEADER SEQUENCE                
SEQADV 2GO7 MSE B    1  UNP  Q97NG6    MET     1 MODIFIED RESIDUE               
SEQADV 2GO7 MSE B   86  UNP  Q97NG6    MET    86 MODIFIED RESIDUE               
SEQADV 2GO7 GLY C    0  UNP  Q97NG6              LEADER SEQUENCE                
SEQADV 2GO7 MSE C    1  UNP  Q97NG6    MET     1 MODIFIED RESIDUE               
SEQADV 2GO7 MSE C   86  UNP  Q97NG6    MET    86 MODIFIED RESIDUE               
SEQADV 2GO7 GLY D    0  UNP  Q97NG6              LEADER SEQUENCE                
SEQADV 2GO7 MSE D    1  UNP  Q97NG6    MET     1 MODIFIED RESIDUE               
SEQADV 2GO7 MSE D   86  UNP  Q97NG6    MET    86 MODIFIED RESIDUE               
SEQRES   1 A  207  GLY MSE GLN LYS THR ALA PHE ILE TRP ASP LEU ASP GLY          
SEQRES   2 A  207  THR LEU LEU ASP SER TYR GLU ALA ILE LEU SER GLY ILE          
SEQRES   3 A  207  GLU GLU THR PHE ALA GLN PHE SER ILE PRO TYR ASP LYS          
SEQRES   4 A  207  GLU LYS VAL ARG GLU PHE ILE PHE LYS TYR SER VAL GLN          
SEQRES   5 A  207  ASP LEU LEU VAL ARG VAL ALA GLU ASP ARG ASN LEU ASP          
SEQRES   6 A  207  VAL GLU VAL LEU ASN GLN VAL ARG ALA GLN SER LEU ALA          
SEQRES   7 A  207  GLU LYS ASN ALA GLN VAL VAL LEU MSE PRO GLY ALA ARG          
SEQRES   8 A  207  GLU VAL LEU ALA TRP ALA ASP GLU SER GLY ILE GLN GLN          
SEQRES   9 A  207  PHE ILE TYR THR HIS LYS GLY ASN ASN ALA PHE THR ILE          
SEQRES  10 A  207  LEU LYS ASP LEU GLY VAL GLU SER TYR PHE THR GLU ILE          
SEQRES  11 A  207  LEU THR SER GLN SER GLY PHE VAL ARG LYS PRO SER PRO          
SEQRES  12 A  207  GLU ALA ALA THR TYR LEU LEU ASP LYS TYR GLN LEU ASN          
SEQRES  13 A  207  SER ASP ASN THR TYR TYR ILE GLY ASP ARG THR LEU ASP          
SEQRES  14 A  207  VAL GLU PHE ALA GLN ASN SER GLY ILE GLN SER ILE ASN          
SEQRES  15 A  207  PHE LEU GLU SER THR TYR GLU GLY ASN HIS ARG ILE GLN          
SEQRES  16 A  207  ALA LEU ALA ASP ILE SER ARG ILE PHE GLU THR LYS              
SEQRES   1 B  207  GLY MSE GLN LYS THR ALA PHE ILE TRP ASP LEU ASP GLY          
SEQRES   2 B  207  THR LEU LEU ASP SER TYR GLU ALA ILE LEU SER GLY ILE          
SEQRES   3 B  207  GLU GLU THR PHE ALA GLN PHE SER ILE PRO TYR ASP LYS          
SEQRES   4 B  207  GLU LYS VAL ARG GLU PHE ILE PHE LYS TYR SER VAL GLN          
SEQRES   5 B  207  ASP LEU LEU VAL ARG VAL ALA GLU ASP ARG ASN LEU ASP          
SEQRES   6 B  207  VAL GLU VAL LEU ASN GLN VAL ARG ALA GLN SER LEU ALA          
SEQRES   7 B  207  GLU LYS ASN ALA GLN VAL VAL LEU MSE PRO GLY ALA ARG          
SEQRES   8 B  207  GLU VAL LEU ALA TRP ALA ASP GLU SER GLY ILE GLN GLN          
SEQRES   9 B  207  PHE ILE TYR THR HIS LYS GLY ASN ASN ALA PHE THR ILE          
SEQRES  10 B  207  LEU LYS ASP LEU GLY VAL GLU SER TYR PHE THR GLU ILE          
SEQRES  11 B  207  LEU THR SER GLN SER GLY PHE VAL ARG LYS PRO SER PRO          
SEQRES  12 B  207  GLU ALA ALA THR TYR LEU LEU ASP LYS TYR GLN LEU ASN          
SEQRES  13 B  207  SER ASP ASN THR TYR TYR ILE GLY ASP ARG THR LEU ASP          
SEQRES  14 B  207  VAL GLU PHE ALA GLN ASN SER GLY ILE GLN SER ILE ASN          
SEQRES  15 B  207  PHE LEU GLU SER THR TYR GLU GLY ASN HIS ARG ILE GLN          
SEQRES  16 B  207  ALA LEU ALA ASP ILE SER ARG ILE PHE GLU THR LYS              
SEQRES   1 C  207  GLY MSE GLN LYS THR ALA PHE ILE TRP ASP LEU ASP GLY          
SEQRES   2 C  207  THR LEU LEU ASP SER TYR GLU ALA ILE LEU SER GLY ILE          
SEQRES   3 C  207  GLU GLU THR PHE ALA GLN PHE SER ILE PRO TYR ASP LYS          
SEQRES   4 C  207  GLU LYS VAL ARG GLU PHE ILE PHE LYS TYR SER VAL GLN          
SEQRES   5 C  207  ASP LEU LEU VAL ARG VAL ALA GLU ASP ARG ASN LEU ASP          
SEQRES   6 C  207  VAL GLU VAL LEU ASN GLN VAL ARG ALA GLN SER LEU ALA          
SEQRES   7 C  207  GLU LYS ASN ALA GLN VAL VAL LEU MSE PRO GLY ALA ARG          
SEQRES   8 C  207  GLU VAL LEU ALA TRP ALA ASP GLU SER GLY ILE GLN GLN          
SEQRES   9 C  207  PHE ILE TYR THR HIS LYS GLY ASN ASN ALA PHE THR ILE          
SEQRES  10 C  207  LEU LYS ASP LEU GLY VAL GLU SER TYR PHE THR GLU ILE          
SEQRES  11 C  207  LEU THR SER GLN SER GLY PHE VAL ARG LYS PRO SER PRO          
SEQRES  12 C  207  GLU ALA ALA THR TYR LEU LEU ASP LYS TYR GLN LEU ASN          
SEQRES  13 C  207  SER ASP ASN THR TYR TYR ILE GLY ASP ARG THR LEU ASP          
SEQRES  14 C  207  VAL GLU PHE ALA GLN ASN SER GLY ILE GLN SER ILE ASN          
SEQRES  15 C  207  PHE LEU GLU SER THR TYR GLU GLY ASN HIS ARG ILE GLN          
SEQRES  16 C  207  ALA LEU ALA ASP ILE SER ARG ILE PHE GLU THR LYS              
SEQRES   1 D  207  GLY MSE GLN LYS THR ALA PHE ILE TRP ASP LEU ASP GLY          
SEQRES   2 D  207  THR LEU LEU ASP SER TYR GLU ALA ILE LEU SER GLY ILE          
SEQRES   3 D  207  GLU GLU THR PHE ALA GLN PHE SER ILE PRO TYR ASP LYS          
SEQRES   4 D  207  GLU LYS VAL ARG GLU PHE ILE PHE LYS TYR SER VAL GLN          
SEQRES   5 D  207  ASP LEU LEU VAL ARG VAL ALA GLU ASP ARG ASN LEU ASP          
SEQRES   6 D  207  VAL GLU VAL LEU ASN GLN VAL ARG ALA GLN SER LEU ALA          
SEQRES   7 D  207  GLU LYS ASN ALA GLN VAL VAL LEU MSE PRO GLY ALA ARG          
SEQRES   8 D  207  GLU VAL LEU ALA TRP ALA ASP GLU SER GLY ILE GLN GLN          
SEQRES   9 D  207  PHE ILE TYR THR HIS LYS GLY ASN ASN ALA PHE THR ILE          
SEQRES  10 D  207  LEU LYS ASP LEU GLY VAL GLU SER TYR PHE THR GLU ILE          
SEQRES  11 D  207  LEU THR SER GLN SER GLY PHE VAL ARG LYS PRO SER PRO          
SEQRES  12 D  207  GLU ALA ALA THR TYR LEU LEU ASP LYS TYR GLN LEU ASN          
SEQRES  13 D  207  SER ASP ASN THR TYR TYR ILE GLY ASP ARG THR LEU ASP          
SEQRES  14 D  207  VAL GLU PHE ALA GLN ASN SER GLY ILE GLN SER ILE ASN          
SEQRES  15 D  207  PHE LEU GLU SER THR TYR GLU GLY ASN HIS ARG ILE GLN          
SEQRES  16 D  207  ALA LEU ALA ASP ILE SER ARG ILE PHE GLU THR LYS              
MODRES 2GO7 MSE A   86  MET  SELENOMETHIONINE                                   
MODRES 2GO7 MSE B   86  MET  SELENOMETHIONINE                                   
MODRES 2GO7 MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 2GO7 MSE C   86  MET  SELENOMETHIONINE                                   
MODRES 2GO7 MSE D   86  MET  SELENOMETHIONINE                                   
HET    MSE  A  86       8                                                       
HET    MSE  B  86       8                                                       
HET    MSE  C   1       5                                                       
HET    MSE  C  86       8                                                       
HET    MSE  D  86       8                                                       
HET     MG  A 207       1                                                       
HET     CL  A 208       1                                                       
HET     CL  A 209       1                                                       
HET     CL  A 210       1                                                       
HET     CL  A 211       1                                                       
HET     CL  A 212       1                                                       
HET     MG  B 207       1                                                       
HET     CL  B 208       1                                                       
HET     CL  B 209       1                                                       
HET     MG  C 207       1                                                       
HET     CL  C 208       1                                                       
HET     CL  C 209       1                                                       
HET     CL  C 210       1                                                       
HET     CL  C 211       1                                                       
HET     MG  D 207       1                                                       
HET     CL  D 208       1                                                       
HET     CL  D 209       1                                                       
HET     CL  D 210       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   5   MG    4(MG 2+)                                                     
FORMUL   6   CL    14(CL 1-)                                                    
FORMUL  23  HOH   *492(H2 O)                                                    
HELIX    1   1 SER A   17  SER A   33  1                                  17    
HELIX    2   2 ASP A   37  TYR A   48  1                                  12    
HELIX    3   3 SER A   49  ASN A   62  1                                  14    
HELIX    4   4 ASP A   64  ALA A   77  1                                  14    
HELIX    5   5 GLU A   78  VAL A   83  5                                   6    
HELIX    6   6 GLY A   88  SER A   99  1                                  12    
HELIX    7   7 ASN A  111  LEU A  120  1                                  10    
HELIX    8   8 VAL A  122  SER A  124  5                                   3    
HELIX    9   9 THR A  131  GLY A  135  5                                   5    
HELIX   10  10 PRO A  142  GLN A  153  1                                  12    
HELIX   11  11 ASN A  155  ASP A  157  5                                   3    
HELIX   12  12 ARG A  165  GLY A  176  1                                  12    
HELIX   13  13 ALA A  197  PHE A  203  1                                   7    
HELIX   14  14 SER B   17  PHE B   32  1                                  16    
HELIX   15  15 ASP B   37  TYR B   48  1                                  12    
HELIX   16  16 SER B   49  ASN B   62  1                                  14    
HELIX   17  17 ASP B   64  GLU B   78  1                                  15    
HELIX   18  18 LYS B   79  VAL B   83  5                                   5    
HELIX   19  19 GLY B   88  GLY B  100  1                                  13    
HELIX   20  20 ASN B  111  LEU B  120  1                                  10    
HELIX   21  21 VAL B  122  PHE B  126  5                                   5    
HELIX   22  22 THR B  131  GLY B  135  5                                   5    
HELIX   23  23 PRO B  142  TYR B  152  1                                  11    
HELIX   24  24 ASN B  155  ASP B  157  5                                   3    
HELIX   25  25 ARG B  165  GLY B  176  1                                  12    
HELIX   26  26 ALA B  197  GLU B  204  1                                   8    
HELIX   27  27 SER C   17  PHE C   32  1                                  16    
HELIX   28  28 ASP C   37  TYR C   48  1                                  12    
HELIX   29  29 SER C   49  ASN C   62  1                                  14    
HELIX   30  30 ASP C   64  GLU C   78  1                                  15    
HELIX   31  31 LYS C   79  VAL C   83  5                                   5    
HELIX   32  32 GLY C   88  SER C   99  1                                  12    
HELIX   33  33 ASN C  111  LEU C  120  1                                  10    
HELIX   34  34 VAL C  122  PHE C  126  5                                   5    
HELIX   35  35 THR C  131  GLY C  135  5                                   5    
HELIX   36  36 PRO C  142  TYR C  152  1                                  11    
HELIX   37  37 ASN C  155  ASP C  157  5                                   3    
HELIX   38  38 ARG C  165  GLY C  176  1                                  12    
HELIX   39  39 ALA C  197  ILE C  202  1                                   6    
HELIX   40  40 SER D   17  PHE D   32  1                                  16    
HELIX   41  41 ASP D   37  TYR D   48  1                                  12    
HELIX   42  42 SER D   49  ASN D   62  1                                  14    
HELIX   43  43 ASP D   64  GLU D   78  1                                  15    
HELIX   44  44 LYS D   79  VAL D   83  5                                   5    
HELIX   45  45 GLY D   88  SER D   99  1                                  12    
HELIX   46  46 ASN D  111  LEU D  120  1                                  10    
HELIX   47  47 VAL D  122  PHE D  126  5                                   5    
HELIX   48  48 THR D  131  GLY D  135  5                                   5    
HELIX   49  49 PRO D  142  TYR D  152  1                                  11    
HELIX   50  50 ASN D  155  ASP D  157  5                                   3    
HELIX   51  51 ARG D  165  GLY D  176  1                                  12    
HELIX   52  52 ALA D  197  GLU D  204  1                                   8    
SHEET    1   A 6 PHE A 126  LEU A 130  0                                        
SHEET    2   A 6 GLN A 102  TYR A 106  1  N  GLN A 103   O  THR A 127           
SHEET    3   A 6 ALA A   5  TRP A   8  1  N  TRP A   8   O  PHE A 104           
SHEET    4   A 6 THR A 159  GLY A 163  1  O  TYR A 160   N  ILE A   7           
SHEET    5   A 6 GLN A 178  ASN A 181  1  O  GLN A 178   N  THR A 159           
SHEET    6   A 6 ASN A 190  ARG A 192  1  O  HIS A 191   N  ASN A 181           
SHEET    1   B 2 LEU A  15  ASP A  16  0                                        
SHEET    2   B 2 VAL A  84  LEU A  85 -1  O  VAL A  84   N  ASP A  16           
SHEET    1   C 6 GLU B 128  LEU B 130  0                                        
SHEET    2   C 6 GLN B 102  TYR B 106  1  N  ILE B 105   O  LEU B 130           
SHEET    3   C 6 ALA B   5  TRP B   8  1  N  PHE B   6   O  GLN B 102           
SHEET    4   C 6 THR B 159  GLY B 163  1  O  TYR B 160   N  ILE B   7           
SHEET    5   C 6 GLN B 178  ASN B 181  1  O  ILE B 180   N  TYR B 161           
SHEET    6   C 6 ASN B 190  ARG B 192  1  O  HIS B 191   N  ASN B 181           
SHEET    1   D 2 LEU B  15  ASP B  16  0                                        
SHEET    2   D 2 VAL B  84  LEU B  85 -1  O  VAL B  84   N  ASP B  16           
SHEET    1   E 6 GLU C 128  LEU C 130  0                                        
SHEET    2   E 6 GLN C 102  TYR C 106  1  N  ILE C 105   O  LEU C 130           
SHEET    3   E 6 ALA C   5  TRP C   8  1  N  TRP C   8   O  PHE C 104           
SHEET    4   E 6 THR C 159  GLY C 163  1  O  TYR C 160   N  ILE C   7           
SHEET    5   E 6 GLN C 178  ASN C 181  1  O  GLN C 178   N  THR C 159           
SHEET    6   E 6 ASN C 190  ARG C 192  1  O  HIS C 191   N  ASN C 181           
SHEET    1   F 2 LEU C  15  ASP C  16  0                                        
SHEET    2   F 2 VAL C  84  LEU C  85 -1  O  VAL C  84   N  ASP C  16           
SHEET    1   G 6 GLU D 128  LEU D 130  0                                        
SHEET    2   G 6 GLN D 102  TYR D 106  1  N  ILE D 105   O  LEU D 130           
SHEET    3   G 6 ALA D   5  TRP D   8  1  N  PHE D   6   O  GLN D 102           
SHEET    4   G 6 THR D 159  GLY D 163  1  O  TYR D 160   N  ILE D   7           
SHEET    5   G 6 GLN D 178  ASN D 181  1  O  ILE D 180   N  TYR D 161           
SHEET    6   G 6 ASN D 190  ARG D 192  1  O  HIS D 191   N  SER D 179           
SHEET    1   H 2 LEU D  15  ASP D  16  0                                        
SHEET    2   H 2 VAL D  84  LEU D  85 -1  O  VAL D  84   N  ASP D  16           
LINK         C   LEU A  85                 N   MSE A  86     1555   1555  1.32  
LINK         C   MSE A  86                 N   PRO A  87     1555   1555  1.34  
LINK        MG    MG A 207                 OD2 ASP A   9     1555   1555  1.94  
LINK        MG    MG A 207                 O   HOH A 215     1555   1555  2.04  
LINK        MG    MG A 207                 OD1 ASP A 164     1555   1555  2.10  
LINK        MG    MG A 207                 O   HOH A 213     1555   1555  2.16  
LINK        MG    MG A 207                 O   ASP A  11     1555   1555  2.02  
LINK        MG    MG A 207                 O   HOH A 214     1555   1555  2.11  
LINK         C   LEU B  85                 N   MSE B  86     1555   1555  1.32  
LINK         C   MSE B  86                 N   PRO B  87     1555   1555  1.35  
LINK        MG    MG B 207                 OD1 ASP B 164     1555   1555  2.11  
LINK        MG    MG B 207                 O   HOH B 212     1555   1555  2.07  
LINK        MG    MG B 207                 OD2 ASP B   9     1555   1555  2.08  
LINK        MG    MG B 207                 O   HOH B 211     1555   1555  2.05  
LINK        MG    MG B 207                 O   HOH B 210     1555   1555  2.02  
LINK        MG    MG B 207                 O   ASP B  11     1555   1555  2.16  
LINK         C   GLY C   0                 N   MSE C   1     1555   1555  1.34  
LINK         C   MSE C   1                 N   GLN C   2     1555   1555  1.34  
LINK         C   LEU C  85                 N   MSE C  86     1555   1555  1.31  
LINK         C   MSE C  86                 N   PRO C  87     1555   1555  1.34  
LINK        MG    MG C 207                 OD2 ASP C   9     1555   1555  2.05  
LINK        MG    MG C 207                 O   HOH C 212     1555   1555  2.05  
LINK        MG    MG C 207                 O   HOH C 213     1555   1555  1.92  
LINK        MG    MG C 207                 O   HOH C 214     1555   1555  2.10  
LINK        MG    MG C 207                 OD1 ASP C 164     1555   1555  2.06  
LINK        MG    MG C 207                 O   ASP C  11     1555   1555  2.08  
LINK         C   LEU D  85                 N   MSE D  86     1555   1555  1.34  
LINK         C   MSE D  86                 N   PRO D  87     1555   1555  1.36  
LINK        MG    MG D 207                 O   HOH D 211     1555   1555  2.28  
LINK        MG    MG D 207                 O   HOH D 213     1555   1555  2.20  
LINK        MG    MG D 207                 O   ASP D  11     1555   1555  2.02  
LINK        MG    MG D 207                 O   HOH D 212     1555   1555  1.87  
LINK        MG    MG D 207                 OD2 ASP D   9     1555   1555  2.03  
LINK        MG    MG D 207                 OD1 ASP D 164     1555   1555  2.14  
CISPEP   1 LYS A  139    PRO A  140          0         5.94                     
CISPEP   2 LYS B  139    PRO B  140          0         6.04                     
CISPEP   3 LYS C  139    PRO C  140          0         4.60                     
CISPEP   4 LYS D  139    PRO D  140          0         3.77                     
SITE     1 AC1  6 ASP A   9  ASP A  11  ASP A 164  HOH A 213                    
SITE     2 AC1  6 HOH A 214  HOH A 215                                          
SITE     1 AC2  6 ASP B   9  ASP B  11  ASP B 164  HOH B 210                    
SITE     2 AC2  6 HOH B 211  HOH B 212                                          
SITE     1 AC3  6 ASP C   9  ASP C  11  ASP C 164  HOH C 212                    
SITE     2 AC3  6 HOH C 213  HOH C 214                                          
SITE     1 AC4  6 ASP D   9  ASP D  11  ASP D 164  HOH D 211                    
SITE     2 AC4  6 HOH D 212  HOH D 213                                          
SITE     1 AC5  4 GLY D 121  VAL D 122  GLU D 123  SER D 124                    
SITE     1 AC6  3 GLY C 121  GLU C 123  SER C 124                               
SITE     1 AC7  5 GLY A 121  VAL A 122  GLU A 123  SER A 124                    
SITE     2 AC7  5 HOH A 341                                                     
SITE     1 AC8  1 ARG A  72                                                     
SITE     1 AC9  3 ARG A 138  LYS A 139  HOH A 335                               
SITE     1 BC1  1 ARG C  72                                                     
SITE     1 BC2  2 ARG D  72  LEU D  76                                          
SITE     1 BC3  4 GLY B 121  VAL B 122  GLU B 123  SER B 124                    
SITE     1 BC4  2 ARG A 138  ARG B 138                                          
SITE     1 BC5  2 ARG C 138  ARG D 138                                          
SITE     1 BC6  4 ASP B   9  LEU B  10  ASP B  11  THR B 107                    
SITE     1 BC7  5 ASP C   9  LEU C  10  ASP C  11  THR C 107                    
SITE     2 BC7  5 HIS C 108                                                     
SITE     1 BC8  5 ASP D   9  LEU D  10  ASP D  11  THR D 107                    
SITE     2 BC8  5 HIS D 108                                                     
SITE     1 BC9  5 ASP A   9  LEU A  10  ASP A  11  THR A 107                    
SITE     2 BC9  5 HIS A 108                                                     
CRYST1  155.000  155.000   88.440  90.00  90.00 120.00 P 61         24          
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      0.006450  0.003720  0.000000        0.00000                         
SCALE2      0.000000  0.007450  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011310        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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