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Entry: 5FGB
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HEADER    IMMUNE SYSTEM                           20-DEC-15   5FGB              
TITLE     THREE DIMENSIONAL STRUCTURE OF BROADLY NEUTRALIZING HUMAN ANTI -      
TITLE    2 HEPATITIS C VIRUS (HCV) GLYCOPROTEIN E2 FAB FRAGMENT HC33.4          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTI-HCV E2 FAB HC84-1 LIGHT CHAIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ANTI-HCV E2 FAB HC84-1 HEAVY CHAIN;                        
COMPND   7 CHAIN: C, E;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: GENOME POLYPROTEIN;                                        
COMPND  11 CHAIN: F, G;                                                         
COMPND  12 EC: 3.4.22.-,3.4.21.98,3.6.1.15,3.6.4.13,2.7.7.48;                   
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE   6 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2;                            
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PMT/BIP MODIFIED;                         
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 EXPRESSION_SYSTEM: DROSOPHILA;                                       
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 7215;                                       
SOURCE  14 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER 2;                            
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PMT/BIP MODIFIED;                         
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 SYNTHETIC: YES;                                                      
SOURCE  19 ORGANISM_SCIENTIFIC: HEPATITIS C VIRUS GENOTYPE 1A (ISOLATE H);      
SOURCE  20 ORGANISM_COMMON: HCV;                                                
SOURCE  21 ORGANISM_TAXID: 11108;                                               
SOURCE  22 OTHER_DETAILS: FRAGMENT RESIDUES 406-425 OF HCV STRAIN H77           
SOURCE  23 POLYPROTEIN                                                          
KEYWDS    FAB FRAGMENT, NEUTRALIZING ANTIBODY, HEPATITIS C VIRUS E2, IMMUNE     
KEYWDS   2 SYSTEM                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.GIRARD-BLANC,F.A.REY,T.KREY                                         
REVDAT   2   09-MAR-16 5FGB    1       JRNL                                     
REVDAT   1   20-JAN-16 5FGB    0                                                
JRNL        AUTH   Z.Y.KECK,C.GIRARD-BLANC,W.WANG,P.LAU,A.ZUIANI,F.A.REY,       
JRNL        AUTH 2 T.KREY,M.S.DIAMOND,S.K.FOUNG                                 
JRNL        TITL   ANTIBODY RESPONSE TO HYPERVARIABLE REGION 1 INTERFERES WITH  
JRNL        TITL 2 BROADLY NEUTRALIZING ANTIBODIES TO HEPATITIS C VIRUS.        
JRNL        REF    J.VIROL.                      V.  90  3112 2016              
JRNL        REFN                   ESSN 1098-5514                               
JRNL        PMID   26739044                                                     
JRNL        DOI    10.1128/JVI.02458-15                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 118727                         
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)  : 0.172                          
REMARK   3   R VALUE            (WORKING SET)  : 0.171                          
REMARK   3   FREE R VALUE                      : 0.190                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 5936                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.65                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.69                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.91                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 8689                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2352                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 8255                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2343                   
REMARK   3   BIN FREE R VALUE                        : 0.2516                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.99                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 434                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6510                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 604                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 23.98                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.20490                                              
REMARK   3    B22 (A**2) : 4.79200                                              
REMARK   3    B33 (A**2) : -7.99690                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.16560                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.194               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.081               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.077               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.080               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.077               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 6811   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 9298   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2251   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 140    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1015   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 6811   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 903    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : 6      ; 1.000  ; HARMONIC            
REMARK   3    UTILITY DISTANCES         : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY ANGLES            : 12     ; 1.000  ; HARMONIC            
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 7872   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.24                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.54                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {C|1 - 20}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.2812   26.8753   43.8978           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0584 T22:   -0.0340                                    
REMARK   3     T33:   -0.0179 T12:   -0.0071                                    
REMARK   3     T13:    0.0190 T23:   -0.0107                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4818 L22:    1.1706                                    
REMARK   3     L33:    3.2122 L12:   -0.9166                                    
REMARK   3     L13:    1.5145 L23:   -1.4926                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0177 S12:    0.0794 S13:   -0.1151                     
REMARK   3     S21:    0.0614 S22:    0.0113 S23:   -0.1000                     
REMARK   3     S31:   -0.0269 S32:    0.0994 S33:    0.0064                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {C|21 - 86}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.4112   33.4406   43.4052           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0084 T22:   -0.0349                                    
REMARK   3     T33:   -0.0062 T12:   -0.0044                                    
REMARK   3     T13:    0.0028 T23:    0.0015                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1272 L22:    1.9649                                    
REMARK   3     L33:    0.4469 L12:    0.0141                                    
REMARK   3     L13:    0.2719 L23:   -0.4015                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0082 S12:    0.0037 S13:   -0.0111                     
REMARK   3     S21:    0.0262 S22:    0.0860 S23:    0.0068                     
REMARK   3     S31:   -0.1274 S32:   -0.0667 S33:   -0.0778                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {C|87 - 126}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.9000   26.7181   46.7267           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0450 T22:   -0.0533                                    
REMARK   3     T33:   -0.0108 T12:   -0.0006                                    
REMARK   3     T13:    0.0058 T23:    0.0132                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7788 L22:    1.2188                                    
REMARK   3     L33:    1.2709 L12:   -0.3508                                    
REMARK   3     L13:    0.8921 L23:   -0.6683                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0025 S12:    0.0083 S13:   -0.0391                     
REMARK   3     S21:    0.0836 S22:    0.1072 S23:    0.1675                     
REMARK   3     S31:   -0.0950 S32:   -0.0367 S33:   -0.1047                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {C|127 - 214}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -16.0793    2.1209   48.0129           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0108 T22:    0.0165                                    
REMARK   3     T33:   -0.0312 T12:   -0.0039                                    
REMARK   3     T13:   -0.0105 T23:    0.0062                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8194 L22:    1.7918                                    
REMARK   3     L33:    0.8005 L12:    0.1834                                    
REMARK   3     L13:    0.1583 L23:    0.2650                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0069 S12:    0.0580 S13:   -0.0244                     
REMARK   3     S21:   -0.1278 S22:   -0.0374 S23:    0.0057                     
REMARK   3     S31:    0.0705 S32:    0.0135 S33:    0.0443                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {C|215 - 223}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -9.0226   -3.0502   44.2525           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0245 T22:    0.0109                                    
REMARK   3     T33:    0.0158 T12:    0.0231                                    
REMARK   3     T13:    0.0044 T23:    0.0139                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6738 L22:    0.2843                                    
REMARK   3     L33:    1.3070 L12:    0.0642                                    
REMARK   3     L13:   -0.2798 L23:    0.5340                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0119 S12:    0.0757 S13:   -0.0737                     
REMARK   3     S21:   -0.0595 S22:   -0.0026 S23:    0.0016                     
REMARK   3     S31:    0.0911 S32:    0.2044 S33:    0.0146                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: {B|1 - 90}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -45.6353   -7.8485   23.3598           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1245 T22:   -0.0729                                    
REMARK   3     T33:    0.0035 T12:   -0.0048                                    
REMARK   3     T13:   -0.0204 T23:    0.0417                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1630 L22:    2.6339                                    
REMARK   3     L33:    0.9975 L12:   -1.2392                                    
REMARK   3     L13:    0.5092 L23:   -1.1137                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0824 S12:   -0.0691 S13:   -0.3168                     
REMARK   3     S21:   -0.0469 S22:    0.0852 S23:    0.3034                     
REMARK   3     S31:    0.0763 S32:   -0.0953 S33:   -0.1677                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: {B|91 - 106}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -40.3555  -13.2464   18.1684           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0018 T22:   -0.0118                                    
REMARK   3     T33:    0.0828 T12:   -0.0017                                    
REMARK   3     T13:   -0.0694 T23:   -0.0068                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.5173 L22:    0.9093                                    
REMARK   3     L33:    1.8822 L12:   -0.8643                                    
REMARK   3     L13:    0.6523 L23:    0.1317                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1631 S12:    0.1436 S13:   -0.5429                     
REMARK   3     S21:   -0.2240 S22:    0.0944 S23:    0.0378                     
REMARK   3     S31:    0.3773 S32:   -0.0856 S33:   -0.2575                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: {B|107 - 147}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.3498   15.7375   13.5685           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0550 T22:   -0.0085                                    
REMARK   3     T33:   -0.0208 T12:    0.0085                                    
REMARK   3     T13:   -0.0028 T23:    0.0069                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6982 L22:    1.4475                                    
REMARK   3     L33:    0.4980 L12:    0.3355                                    
REMARK   3     L13:   -0.1944 L23:   -0.3751                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0445 S12:    0.0874 S13:    0.0737                     
REMARK   3     S21:    0.0079 S22:   -0.0100 S23:    0.1080                     
REMARK   3     S31:   -0.0227 S32:    0.0034 S33:   -0.0345                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: {B|148 - 161}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.1124   15.8525    2.2495           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0237 T22:   -0.0134                                    
REMARK   3     T33:   -0.0500 T12:   -0.0053                                    
REMARK   3     T13:   -0.0037 T23:    0.0392                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0034 L22:    2.0194                                    
REMARK   3     L33:    2.0614 L12:   -0.6594                                    
REMARK   3     L13:    0.4443 L23:   -0.3323                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0351 S12:    0.2005 S13:    0.1907                     
REMARK   3     S21:   -0.2776 S22:    0.0526 S23:    0.2097                     
REMARK   3     S31:   -0.0889 S32:    0.1143 S33:   -0.0176                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: {B|162 - 212}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.9784   17.5701   10.4280           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0529 T22:   -0.0138                                    
REMARK   3     T33:   -0.0173 T12:   -0.0008                                    
REMARK   3     T13:   -0.0113 T23:    0.0181                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3576 L22:    1.3442                                    
REMARK   3     L33:    1.2791 L12:    0.7962                                    
REMARK   3     L13:   -1.1684 L23:   -0.6175                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0094 S12:    0.1653 S13:    0.1944                     
REMARK   3     S21:   -0.0779 S22:   -0.0039 S23:    0.0871                     
REMARK   3     S31:   -0.0855 S32:    0.0161 S33:   -0.0055                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: {E|1 - 64}                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.6291  -20.0392   27.5355           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0348 T22:   -0.0563                                    
REMARK   3     T33:   -0.0072 T12:    0.0022                                    
REMARK   3     T13:   -0.0225 T23:    0.0096                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6546 L22:    1.3568                                    
REMARK   3     L33:    0.4367 L12:   -0.1835                                    
REMARK   3     L13:   -0.1989 L23:   -0.1965                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0521 S12:   -0.0654 S13:   -0.0547                     
REMARK   3     S21:   -0.0198 S22:    0.0457 S23:    0.1468                     
REMARK   3     S31:    0.0980 S32:   -0.0343 S33:   -0.0978                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: {E|65 - 83}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.8586  -25.4565   29.7485           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0141 T22:   -0.0263                                    
REMARK   3     T33:    0.0252 T12:    0.0158                                    
REMARK   3     T13:   -0.0206 T23:    0.0001                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3371 L22:    2.9292                                    
REMARK   3     L33:    1.8978 L12:    0.2285                                    
REMARK   3     L13:   -0.5111 L23:    1.1022                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0035 S12:   -0.1242 S13:   -0.1186                     
REMARK   3     S21:   -0.0044 S22:    0.0785 S23:   -0.0760                     
REMARK   3     S31:    0.1567 S32:    0.0188 S33:   -0.0820                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: {E|84 - 135}                                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.8688  -11.3258   23.4094           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0306 T22:   -0.0279                                    
REMARK   3     T33:    0.0043 T12:    0.0109                                    
REMARK   3     T13:   -0.0010 T23:   -0.0018                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4693 L22:    1.1539                                    
REMARK   3     L33:    0.4854 L12:    0.3825                                    
REMARK   3     L13:    0.0548 L23:   -0.5605                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0338 S12:    0.0221 S13:   -0.0025                     
REMARK   3     S21:   -0.0753 S22:    0.0642 S23:    0.1452                     
REMARK   3     S31:    0.0878 S32:   -0.0190 S33:   -0.0980                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: {E|143 - 193}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.8487    6.9943   21.3969           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1002 T22:   -0.0802                                    
REMARK   3     T33:   -0.1104 T12:    0.0118                                    
REMARK   3     T13:    0.0072 T23:   -0.0006                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8620 L22:    1.4774                                    
REMARK   3     L33:    0.7297 L12:    0.2065                                    
REMARK   3     L13:    0.1780 L23:   -0.1654                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0006 S12:   -0.0476 S13:   -0.0120                     
REMARK   3     S21:    0.1059 S22:   -0.0658 S23:    0.1138                     
REMARK   3     S31:   -0.0870 S32:   -0.0548 S33:    0.0652                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: {E|194 - 222}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -12.8972   11.3070   28.9811           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0512 T22:    0.0179                                    
REMARK   3     T33:    0.0206 T12:   -0.0018                                    
REMARK   3     T13:   -0.0134 T23:   -0.0008                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7573 L22:    3.4540                                    
REMARK   3     L33:    0.1120 L12:   -1.1461                                    
REMARK   3     L13:   -0.4992 L23:    0.8587                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0090 S12:   -0.1054 S13:    0.1770                     
REMARK   3     S21:    0.2948 S22:   -0.0155 S23:   -0.3699                     
REMARK   3     S31:   -0.0572 S32:    0.1017 S33:    0.0244                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: {A|1 - 107}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -44.9314   18.9833   48.9382           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1073 T22:   -0.0450                                    
REMARK   3     T33:    0.0420 T12:    0.0164                                    
REMARK   3     T13:    0.0323 T23:    0.0569                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1450 L22:    3.1633                                    
REMARK   3     L33:    1.0339 L12:    1.3961                                    
REMARK   3     L13:   -0.4727 L23:   -1.4588                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0756 S12:    0.0655 S13:    0.2403                     
REMARK   3     S21:    0.1565 S22:    0.1605 S23:    0.4895                     
REMARK   3     S31:   -0.1114 S32:   -0.1364 S33:   -0.2361                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: {A|108 - 142}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.8524   -5.3903   56.7057           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0688 T22:   -0.0238                                    
REMARK   3     T33:   -0.0691 T12:   -0.0017                                    
REMARK   3     T13:    0.0000 T23:    0.0101                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.4789 L22:    1.6208                                    
REMARK   3     L33:    0.5415 L12:   -0.2240                                    
REMARK   3     L13:    0.1706 L23:   -0.3555                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0838 S12:    0.0318 S13:   -0.1208                     
REMARK   3     S21:   -0.0147 S22:   -0.0421 S23:    0.0465                     
REMARK   3     S31:    0.0484 S32:    0.0409 S33:   -0.0417                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: {A|143 - 160}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.8929   -5.5474   68.9299           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0108 T22:   -0.0055                                    
REMARK   3     T33:   -0.0243 T12:    0.0061                                    
REMARK   3     T13:   -0.0062 T23:    0.0372                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5273 L22:    0.5551                                    
REMARK   3     L33:    2.0910 L12:    0.0448                                    
REMARK   3     L13:   -0.1622 L23:    0.1789                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0463 S12:   -0.2000 S13:   -0.1483                     
REMARK   3     S21:    0.2228 S22:    0.0360 S23:    0.2126                     
REMARK   3     S31:    0.0546 S32:   -0.0240 S33:    0.0102                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: {A|161 - 186}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.7884   -0.7875   57.6471           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0540 T22:    0.0076                                    
REMARK   3     T33:   -0.0168 T12:    0.0015                                    
REMARK   3     T13:   -0.0106 T23:    0.0094                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2673 L22:    1.1828                                    
REMARK   3     L33:    1.0059 L12:   -0.7300                                    
REMARK   3     L13:    0.9778 L23:   -0.7018                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0490 S12:    0.0158 S13:    0.1224                     
REMARK   3     S21:    0.0572 S22:   -0.0254 S23:    0.0451                     
REMARK   3     S31:   -0.0057 S32:    0.0722 S33:    0.0745                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: {A|187 - 213}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -18.8804  -12.8067   64.1249           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0394 T22:   -0.0218                                    
REMARK   3     T33:    0.0029 T12:    0.0026                                    
REMARK   3     T13:   -0.0012 T23:    0.0461                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.9726 L22:    2.3262                                    
REMARK   3     L33:    1.7007 L12:   -0.6754                                    
REMARK   3     L13:    2.0183 L23:   -1.0928                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0551 S12:   -0.3459 S13:   -0.5471                     
REMARK   3     S21:    0.0705 S22:    0.0135 S23:    0.0680                     
REMARK   3     S31:    0.1994 S32:   -0.0080 S33:   -0.0686                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5FGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216548.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97857                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118795                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.630                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: HYPTHETICAL FAB ASSEMBLED FROM THE LIGHT CHAIN OF    
REMARK 200  PDB 4JZO AND THE HEAVY CHAIN OF PDB 3KDM                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 5.2 300 MM      
REMARK 280  AMMONIUM SULFATE 100 MM POTASSIUM PHOSPHATE 1 M LITHIUM CHLORIDE,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       74.71500            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19160 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, G                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     CYS A   214                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLU B   213                                                      
REMARK 465     CYS B   214                                                      
REMARK 465     THR C   102A                                                     
REMARK 465     ASP C   102B                                                     
REMARK 465     SER C   102C                                                     
REMARK 465     SER C   102D                                                     
REMARK 465     ALA C   102E                                                     
REMARK 465     TYR C   102F                                                     
REMARK 465     SER C   136                                                      
REMARK 465     SER C   137                                                      
REMARK 465     LYS C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     THR C   140                                                      
REMARK 465     SER C   141                                                      
REMARK 465     GLY C   142                                                      
REMARK 465     SER C   224                                                      
REMARK 465     CYS C   225                                                      
REMARK 465     ASP C   226                                                      
REMARK 465     LYS C   227                                                      
REMARK 465     LEU C   228                                                      
REMARK 465     GLU C   229                                                      
REMARK 465     ASP C   230                                                      
REMARK 465     ASP C   231                                                      
REMARK 465     ASP C   232                                                      
REMARK 465     ASP C   233                                                      
REMARK 465     LYS C   234                                                      
REMARK 465     ALA C   235                                                      
REMARK 465     GLY C   236                                                      
REMARK 465     TRP C   237                                                      
REMARK 465     SER C   238                                                      
REMARK 465     HIS C   239                                                      
REMARK 465     PRO C   240                                                      
REMARK 465     GLN C   241                                                      
REMARK 465     PHE C   242                                                      
REMARK 465     GLU C   243                                                      
REMARK 465     LYS C   244                                                      
REMARK 465     GLY C   245                                                      
REMARK 465     GLY C   246                                                      
REMARK 465     GLY C   247                                                      
REMARK 465     SER C   248                                                      
REMARK 465     GLY C   249                                                      
REMARK 465     GLY C   250                                                      
REMARK 465     GLY C   251                                                      
REMARK 465     SER C   252                                                      
REMARK 465     GLY C   253                                                      
REMARK 465     GLY C   254                                                      
REMARK 465     GLY C   255                                                      
REMARK 465     SER C   256                                                      
REMARK 465     TRP C   257                                                      
REMARK 465     SER C   258                                                      
REMARK 465     HIS C   259                                                      
REMARK 465     PRO C   260                                                      
REMARK 465     GLN C   261                                                      
REMARK 465     PHE C   262                                                      
REMARK 465     GLU C   263                                                      
REMARK 465     LYS C   264                                                      
REMARK 465     THR E   102A                                                     
REMARK 465     ASP E   102B                                                     
REMARK 465     SER E   102C                                                     
REMARK 465     SER E   102D                                                     
REMARK 465     ALA E   102E                                                     
REMARK 465     TYR E   102F                                                     
REMARK 465     TYR E   102G                                                     
REMARK 465     TYR E   102H                                                     
REMARK 465     SER E   136                                                      
REMARK 465     SER E   137                                                      
REMARK 465     LYS E   138                                                      
REMARK 465     SER E   139                                                      
REMARK 465     THR E   140                                                      
REMARK 465     SER E   141                                                      
REMARK 465     LYS E   223                                                      
REMARK 465     SER E   224                                                      
REMARK 465     CYS E   225                                                      
REMARK 465     ASP E   226                                                      
REMARK 465     LYS E   227                                                      
REMARK 465     LEU E   228                                                      
REMARK 465     GLU E   229                                                      
REMARK 465     ASP E   230                                                      
REMARK 465     ASP E   231                                                      
REMARK 465     ASP E   232                                                      
REMARK 465     ASP E   233                                                      
REMARK 465     LYS E   234                                                      
REMARK 465     ALA E   235                                                      
REMARK 465     GLY E   236                                                      
REMARK 465     TRP E   237                                                      
REMARK 465     SER E   238                                                      
REMARK 465     HIS E   239                                                      
REMARK 465     PRO E   240                                                      
REMARK 465     GLN E   241                                                      
REMARK 465     PHE E   242                                                      
REMARK 465     GLU E   243                                                      
REMARK 465     LYS E   244                                                      
REMARK 465     GLY E   245                                                      
REMARK 465     GLY E   246                                                      
REMARK 465     GLY E   247                                                      
REMARK 465     SER E   248                                                      
REMARK 465     GLY E   249                                                      
REMARK 465     GLY E   250                                                      
REMARK 465     GLY E   251                                                      
REMARK 465     SER E   252                                                      
REMARK 465     GLY E   253                                                      
REMARK 465     GLY E   254                                                      
REMARK 465     GLY E   255                                                      
REMARK 465     SER E   256                                                      
REMARK 465     TRP E   257                                                      
REMARK 465     SER E   258                                                      
REMARK 465     HIS E   259                                                      
REMARK 465     PRO E   260                                                      
REMARK 465     GLN E   261                                                      
REMARK 465     PHE E   262                                                      
REMARK 465     GLU E   263                                                      
REMARK 465     LYS E   264                                                      
REMARK 465     PRO F   405                                                      
REMARK 465     GLY F   406                                                      
REMARK 465     ALA F   407                                                      
REMARK 465     LYS F   408                                                      
REMARK 465     GLN F   409                                                      
REMARK 465     ASN F   410                                                      
REMARK 465     ILE F   411                                                      
REMARK 465     GLN F   412                                                      
REMARK 465     LEU F   413                                                      
REMARK 465     ILE F   414                                                      
REMARK 465     ASN F   415                                                      
REMARK 465     THR F   416                                                      
REMARK 465     ILE F   422                                                      
REMARK 465     ASN F   423                                                      
REMARK 465     SER F   424                                                      
REMARK 465     THR F   425                                                      
REMARK 465     PRO G   405                                                      
REMARK 465     GLY G   406                                                      
REMARK 465     ALA G   407                                                      
REMARK 465     LYS G   408                                                      
REMARK 465     GLN G   409                                                      
REMARK 465     ASN G   410                                                      
REMARK 465     ILE G   411                                                      
REMARK 465     GLN G   412                                                      
REMARK 465     LEU G   413                                                      
REMARK 465     ILE G   414                                                      
REMARK 465     ASN G   415                                                      
REMARK 465     THR G   416                                                      
REMARK 465     ASN G   417                                                      
REMARK 465     ILE G   422                                                      
REMARK 465     ASN G   423                                                      
REMARK 465     SER G   424                                                      
REMARK 465     THR G   425                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER C   196     O    HOH C   401              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU E 187   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  50      -51.84     71.49                                   
REMARK 500    ASP A  95     -121.32     69.51                                   
REMARK 500    ASP B  50      -51.67     69.15                                   
REMARK 500    ASP B  95     -118.91     71.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 301                 
DBREF  5FGB A   -1   214  PDB    5FGB     5FGB            -1    214             
DBREF  5FGB B   -1   214  PDB    5FGB     5FGB            -1    214             
DBREF  5FGB C    1   264  PDB    5FGB     5FGB             1    264             
DBREF  5FGB E    1   264  PDB    5FGB     5FGB             1    264             
DBREF  5FGB F  405   425  UNP    P27958   POLG_HCVH      405    425             
DBREF  5FGB G  405   425  UNP    P27958   POLG_HCVH      405    425             
SEQRES   1 A  216  ARG SER SER TYR GLU LEU THR GLN LEU PRO SER LEU SER          
SEQRES   2 A  216  VAL SER LEU GLY GLN THR ALA SER ILE THR CYS SER GLY          
SEQRES   3 A  216  ASP ASN LEU GLY ASP LYS PHE VAL CYS TRP TYR GLN GLN          
SEQRES   4 A  216  LYS PRO GLY GLN THR PRO VAL LEU VAL MET TYR GLU ASP          
SEQRES   5 A  216  THR LYS ARG PRO SER GLY ILE PRO GLU ARG PHE ALA GLY          
SEQRES   6 A  216  SER ASN SER GLY ASN THR ALA THR LEU THR ILE THR GLY          
SEQRES   7 A  216  THR GLN ALA MET ASP GLU ALA ASP TYR TYR CYS GLN THR          
SEQRES   8 A  216  TRP ASP SER SER THR ASP VAL VAL PHE GLY GLY GLY THR          
SEQRES   9 A  216  LYS LEU THR VAL LEU ARG THR VAL ALA ALA PRO SER VAL          
SEQRES  10 A  216  PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY          
SEQRES  11 A  216  THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO          
SEQRES  12 A  216  ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU          
SEQRES  13 A  216  GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP          
SEQRES  14 A  216  SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR          
SEQRES  15 A  216  LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA          
SEQRES  16 A  216  CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR          
SEQRES  17 A  216  LYS SER PHE ASN ARG GLY GLU CYS                              
SEQRES   1 B  216  ARG SER SER TYR GLU LEU THR GLN LEU PRO SER LEU SER          
SEQRES   2 B  216  VAL SER LEU GLY GLN THR ALA SER ILE THR CYS SER GLY          
SEQRES   3 B  216  ASP ASN LEU GLY ASP LYS PHE VAL CYS TRP TYR GLN GLN          
SEQRES   4 B  216  LYS PRO GLY GLN THR PRO VAL LEU VAL MET TYR GLU ASP          
SEQRES   5 B  216  THR LYS ARG PRO SER GLY ILE PRO GLU ARG PHE ALA GLY          
SEQRES   6 B  216  SER ASN SER GLY ASN THR ALA THR LEU THR ILE THR GLY          
SEQRES   7 B  216  THR GLN ALA MET ASP GLU ALA ASP TYR TYR CYS GLN THR          
SEQRES   8 B  216  TRP ASP SER SER THR ASP VAL VAL PHE GLY GLY GLY THR          
SEQRES   9 B  216  LYS LEU THR VAL LEU ARG THR VAL ALA ALA PRO SER VAL          
SEQRES  10 B  216  PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY          
SEQRES  11 B  216  THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO          
SEQRES  12 B  216  ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU          
SEQRES  13 B  216  GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP          
SEQRES  14 B  216  SER LYS ASP SER THR TYR SER LEU SER SER THR LEU THR          
SEQRES  15 B  216  LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA          
SEQRES  16 B  216  CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR          
SEQRES  17 B  216  LYS SER PHE ASN ARG GLY GLU CYS                              
SEQRES   1 C  269  GLU VAL GLN LEU VAL GLN SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 C  269  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 C  269  PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN          
SEQRES   4 C  269  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER          
SEQRES   5 C  269  GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 C  269  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN ILE          
SEQRES   7 C  269  LEU TYR LEU GLN MET ASN SER LEU LYS ALA GLU ASP THR          
SEQRES   8 C  269  ALA THR TYR TYR CYS ALA ARG ALA VAL VAL PHE THR ASP          
SEQRES   9 C  269  SER SER ALA TYR TYR TYR SER LYS TYR PHE ASP TYR TRP          
SEQRES  10 C  269  SER GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR          
SEQRES  11 C  269  LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS          
SEQRES  12 C  269  SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL          
SEQRES  13 C  269  LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN          
SEQRES  14 C  269  SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA          
SEQRES  15 C  269  VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL          
SEQRES  16 C  269  VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR          
SEQRES  17 C  269  ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL          
SEQRES  18 C  269  ASP LYS LYS ALA GLU PRO LYS SER CYS ASP LYS LEU GLU          
SEQRES  19 C  269  ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE          
SEQRES  20 C  269  GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY          
SEQRES  21 C  269  SER TRP SER HIS PRO GLN PHE GLU LYS                          
SEQRES   1 E  269  GLU VAL GLN LEU VAL GLN SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 E  269  PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY          
SEQRES   3 E  269  PHE THR PHE SER SER TYR ALA MET SER TRP VAL ARG GLN          
SEQRES   4 E  269  ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ALA ILE SER          
SEQRES   5 E  269  GLY SER GLY GLY SER THR TYR TYR ALA ASP SER VAL LYS          
SEQRES   6 E  269  GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN ILE          
SEQRES   7 E  269  LEU TYR LEU GLN MET ASN SER LEU LYS ALA GLU ASP THR          
SEQRES   8 E  269  ALA THR TYR TYR CYS ALA ARG ALA VAL VAL PHE THR ASP          
SEQRES   9 E  269  SER SER ALA TYR TYR TYR SER LYS TYR PHE ASP TYR TRP          
SEQRES  10 E  269  SER GLN GLY THR LEU VAL THR VAL SER SER ALA SER THR          
SEQRES  11 E  269  LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS          
SEQRES  12 E  269  SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL          
SEQRES  13 E  269  LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN          
SEQRES  14 E  269  SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA          
SEQRES  15 E  269  VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL          
SEQRES  16 E  269  VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR          
SEQRES  17 E  269  ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL          
SEQRES  18 E  269  ASP LYS LYS ALA GLU PRO LYS SER CYS ASP LYS LEU GLU          
SEQRES  19 E  269  ASP ASP ASP ASP LYS ALA GLY TRP SER HIS PRO GLN PHE          
SEQRES  20 E  269  GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY GLY          
SEQRES  21 E  269  SER TRP SER HIS PRO GLN PHE GLU LYS                          
SEQRES   1 F   21  PRO GLY ALA LYS GLN ASN ILE GLN LEU ILE ASN THR ASN          
SEQRES   2 F   21  GLY SER TRP HIS ILE ASN SER THR                              
SEQRES   1 G   21  PRO GLY ALA LYS GLN ASN ILE GLN LEU ILE ASN THR ASN          
SEQRES   2 G   21  GLY SER TRP HIS ILE ASN SER THR                              
HET    GOL  A 301       6                                                       
HET    SO4  A 302       5                                                       
HET    SO4  A 303       5                                                       
HET    SO4  A 304       5                                                       
HET    GOL  B 301       6                                                       
HET    SO4  B 302       5                                                       
HET    SO4  B 303       5                                                       
HET    GOL  C 301       6                                                       
HET    SO4  C 302       5                                                       
HET    SO4  C 303       5                                                       
HET    GOL  E 301       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL   8  SO4    7(O4 S 2-)                                                   
FORMUL  18  HOH   *604(H2 O)                                                    
HELIX    1 AA1 ASN A   26  LYS A   30  5                                   5    
HELIX    2 AA2 GLN A   78  GLU A   82  5                                   5    
HELIX    3 AA3 SER A  121  LYS A  126  1                                   6    
HELIX    4 AA4 LYS A  183  LYS A  188  1                                   6    
HELIX    5 AA5 GLN B   78  GLU B   82  5                                   5    
HELIX    6 AA6 SER B  121  LYS B  126  1                                   6    
HELIX    7 AA7 LYS B  183  LYS B  188  1                                   6    
HELIX    8 AA8 THR C   28  TYR C   32  5                                   5    
HELIX    9 AA9 LYS C   87  THR C   91  5                                   5    
HELIX   10 AB1 SER C  165  ALA C  167  5                                   3    
HELIX   11 AB2 SER C  196  LEU C  198  5                                   3    
HELIX   12 AB3 LYS C  210  ASN C  213  5                                   4    
HELIX   13 AB4 THR E   28  TYR E   32  5                                   5    
HELIX   14 AB5 LYS E   87  THR E   91  5                                   5    
HELIX   15 AB6 SER E  165  ALA E  167  5                                   3    
HELIX   16 AB7 SER E  196  LEU E  198  5                                   3    
HELIX   17 AB8 LYS E  210  ASN E  213  5                                   4    
SHEET    1 AA1 5 SER A   9  SER A  13  0                                        
SHEET    2 AA1 5 THR A 102  LEU A 107  1  O  LEU A 107   N  VAL A  12           
SHEET    3 AA1 5 ALA A  83  ASP A  91 -1  N  ALA A  83   O  LEU A 104           
SHEET    4 AA1 5 CYS A  33  GLN A  37 -1  N  GLN A  37   O  ASP A  84           
SHEET    5 AA1 5 VAL A  44  MET A  47 -1  O  VAL A  46   N  TRP A  34           
SHEET    1 AA2 4 SER A   9  SER A  13  0                                        
SHEET    2 AA2 4 THR A 102  LEU A 107  1  O  LEU A 107   N  VAL A  12           
SHEET    3 AA2 4 ALA A  83  ASP A  91 -1  N  ALA A  83   O  LEU A 104           
SHEET    4 AA2 4 ASP A  95  PHE A  98 -1  O  ASP A  95   N  ASP A  91           
SHEET    1 AA3 3 ALA A  18  SER A  23  0                                        
SHEET    2 AA3 3 THR A  69  ILE A  74 -1  O  ALA A  70   N  CYS A  22           
SHEET    3 AA3 3 PHE A  61  SER A  66 -1  N  ALA A  62   O  THR A  73           
SHEET    1 AA4 4 SER A 114  PHE A 118  0                                        
SHEET    2 AA4 4 THR A 129  PHE A 139 -1  O  ASN A 137   N  SER A 114           
SHEET    3 AA4 4 TYR A 173  SER A 182 -1  O  LEU A 181   N  ALA A 130           
SHEET    4 AA4 4 SER A 159  VAL A 163 -1  N  GLN A 160   O  THR A 178           
SHEET    1 AA5 4 ALA A 153  LEU A 154  0                                        
SHEET    2 AA5 4 LYS A 145  VAL A 150 -1  N  VAL A 150   O  ALA A 153           
SHEET    3 AA5 4 VAL A 191  THR A 197 -1  O  GLU A 195   N  GLN A 147           
SHEET    4 AA5 4 VAL A 205  ASN A 210 -1  O  VAL A 205   N  VAL A 196           
SHEET    1 AA6 5 SER B   9  SER B  13  0                                        
SHEET    2 AA6 5 THR B 102  LEU B 107  1  O  LEU B 107   N  VAL B  12           
SHEET    3 AA6 5 ALA B  83  ASP B  91 -1  N  ALA B  83   O  LEU B 104           
SHEET    4 AA6 5 CYS B  33  GLN B  37 -1  N  GLN B  37   O  ASP B  84           
SHEET    5 AA6 5 VAL B  44  MET B  47 -1  O  VAL B  46   N  TRP B  34           
SHEET    1 AA7 4 SER B   9  SER B  13  0                                        
SHEET    2 AA7 4 THR B 102  LEU B 107  1  O  LEU B 107   N  VAL B  12           
SHEET    3 AA7 4 ALA B  83  ASP B  91 -1  N  ALA B  83   O  LEU B 104           
SHEET    4 AA7 4 ASP B  95  PHE B  98 -1  O  ASP B  95   N  ASP B  91           
SHEET    1 AA8 3 ALA B  18  SER B  23  0                                        
SHEET    2 AA8 3 THR B  69  ILE B  74 -1  O  LEU B  72   N  ILE B  20           
SHEET    3 AA8 3 PHE B  61  SER B  66 -1  N  ALA B  62   O  THR B  73           
SHEET    1 AA9 4 SER B 114  PHE B 118  0                                        
SHEET    2 AA9 4 THR B 129  PHE B 139 -1  O  ASN B 137   N  SER B 114           
SHEET    3 AA9 4 TYR B 173  SER B 182 -1  O  LEU B 181   N  ALA B 130           
SHEET    4 AA9 4 SER B 159  VAL B 163 -1  N  GLN B 160   O  THR B 178           
SHEET    1 AB1 4 ALA B 153  LEU B 154  0                                        
SHEET    2 AB1 4 LYS B 145  VAL B 150 -1  N  VAL B 150   O  ALA B 153           
SHEET    3 AB1 4 VAL B 191  THR B 197 -1  O  GLU B 195   N  GLN B 147           
SHEET    4 AB1 4 VAL B 205  ASN B 210 -1  O  VAL B 205   N  VAL B 196           
SHEET    1 AB2 4 GLN C   3  SER C   7  0                                        
SHEET    2 AB2 4 LEU C  18  SER C  25 -1  O  ALA C  23   N  VAL C   5           
SHEET    3 AB2 4 ILE C  78  MET C  83 -1  O  MET C  83   N  LEU C  18           
SHEET    4 AB2 4 PHE C  68  ASP C  73 -1  N  THR C  69   O  GLN C  82           
SHEET    1 AB3 6 GLY C  10  VAL C  12  0                                        
SHEET    2 AB3 6 THR C 116  VAL C 120  1  O  LEU C 117   N  GLY C  10           
SHEET    3 AB3 6 ALA C  92  PHE C 102 -1  N  ALA C  92   O  VAL C 118           
SHEET    4 AB3 6 ALA C  33  GLN C  39 -1  N  VAL C  37   O  TYR C  95           
SHEET    5 AB3 6 LEU C  45  ILE C  51 -1  O  GLU C  46   N  ARG C  38           
SHEET    6 AB3 6 THR C  58  TYR C  60 -1  O  TYR C  59   N  ALA C  50           
SHEET    1 AB4 4 GLY C  10  VAL C  12  0                                        
SHEET    2 AB4 4 THR C 116  VAL C 120  1  O  LEU C 117   N  GLY C  10           
SHEET    3 AB4 4 ALA C  92  PHE C 102 -1  N  ALA C  92   O  VAL C 118           
SHEET    4 AB4 4 SER C 106  TRP C 112 -1  O  TYR C 108   N  VAL C 100           
SHEET    1 AB5 4 SER C 129  LEU C 133  0                                        
SHEET    2 AB5 4 THR C 144  TYR C 154 -1  O  LEU C 150   N  PHE C 131           
SHEET    3 AB5 4 TYR C 185  PRO C 194 -1  O  LEU C 187   N  VAL C 151           
SHEET    4 AB5 4 VAL C 172  THR C 174 -1  N  HIS C 173   O  VAL C 190           
SHEET    1 AB6 4 SER C 129  LEU C 133  0                                        
SHEET    2 AB6 4 THR C 144  TYR C 154 -1  O  LEU C 150   N  PHE C 131           
SHEET    3 AB6 4 TYR C 185  PRO C 194 -1  O  LEU C 187   N  VAL C 151           
SHEET    4 AB6 4 VAL C 178  LEU C 179 -1  N  VAL C 178   O  SER C 186           
SHEET    1 AB7 3 THR C 160  TRP C 163  0                                        
SHEET    2 AB7 3 ILE C 204  HIS C 209 -1  O  ASN C 206   N  SER C 162           
SHEET    3 AB7 3 THR C 214  LYS C 219 -1  O  VAL C 216   N  VAL C 207           
SHEET    1 AB8 4 GLN E   3  SER E   7  0                                        
SHEET    2 AB8 4 LEU E  18  SER E  25 -1  O  ALA E  23   N  VAL E   5           
SHEET    3 AB8 4 ILE E  78  MET E  83 -1  O  MET E  83   N  LEU E  18           
SHEET    4 AB8 4 PHE E  68  ASP E  73 -1  N  SER E  71   O  TYR E  80           
SHEET    1 AB9 6 GLY E  10  VAL E  12  0                                        
SHEET    2 AB9 6 THR E 116  VAL E 120  1  O  LEU E 117   N  GLY E  10           
SHEET    3 AB9 6 ALA E  92  VAL E 100 -1  N  TYR E  94   O  THR E 116           
SHEET    4 AB9 6 MET E  34  GLN E  39 -1  N  VAL E  37   O  TYR E  95           
SHEET    5 AB9 6 LEU E  45  ILE E  51 -1  O  GLU E  46   N  ARG E  38           
SHEET    6 AB9 6 THR E  58  TYR E  60 -1  O  TYR E  59   N  ALA E  50           
SHEET    1 AC1 4 GLY E  10  VAL E  12  0                                        
SHEET    2 AC1 4 THR E 116  VAL E 120  1  O  LEU E 117   N  GLY E  10           
SHEET    3 AC1 4 ALA E  92  VAL E 100 -1  N  TYR E  94   O  THR E 116           
SHEET    4 AC1 4 TYR E 108  TRP E 112 -1  O  TYR E 108   N  VAL E 100           
SHEET    1 AC2 4 SER E 129  LEU E 133  0                                        
SHEET    2 AC2 4 THR E 144  TYR E 154 -1  O  LEU E 150   N  PHE E 131           
SHEET    3 AC2 4 TYR E 185  PRO E 194 -1  O  VAL E 193   N  ALA E 145           
SHEET    4 AC2 4 VAL E 172  THR E 174 -1  N  HIS E 173   O  VAL E 190           
SHEET    1 AC3 4 SER E 129  LEU E 133  0                                        
SHEET    2 AC3 4 THR E 144  TYR E 154 -1  O  LEU E 150   N  PHE E 131           
SHEET    3 AC3 4 TYR E 185  PRO E 194 -1  O  VAL E 193   N  ALA E 145           
SHEET    4 AC3 4 VAL E 178  LEU E 179 -1  N  VAL E 178   O  SER E 186           
SHEET    1 AC4 3 THR E 160  TRP E 163  0                                        
SHEET    2 AC4 3 ILE E 204  HIS E 209 -1  O  ASN E 206   N  SER E 162           
SHEET    3 AC4 3 THR E 214  LYS E 219 -1  O  VAL E 216   N  VAL E 207           
SSBOND   1 CYS A   22    CYS A   87                          1555   1555  2.06  
SSBOND   2 CYS A  134    CYS A  194                          1555   1555  2.04  
SSBOND   3 CYS B   22    CYS B   87                          1555   1555  2.06  
SSBOND   4 CYS B  134    CYS B  194                          1555   1555  2.04  
SSBOND   5 CYS C   22    CYS C   96                          1555   1555  2.04  
SSBOND   6 CYS C  149    CYS C  205                          1555   1555  2.04  
SSBOND   7 CYS E   22    CYS E   96                          1555   1555  2.04  
SSBOND   8 CYS E  149    CYS E  205                          1555   1555  2.04  
CISPEP   1 TYR A  140    PRO A  141          0         3.33                     
CISPEP   2 TYR B  140    PRO B  141          0         3.34                     
CISPEP   3 PHE C  155    PRO C  156          0        -8.05                     
CISPEP   4 GLU C  157    PRO C  158          0         2.60                     
CISPEP   5 PHE E  155    PRO E  156          0        -8.36                     
CISPEP   6 GLU E  157    PRO E  158          0         1.44                     
SITE     1 AC1 11 SER A 162  SER A 176  SER A 177  THR A 178                    
SITE     2 AC1 11 HOH A 433  PHE C 175  PRO C 176  VAL C 178                    
SITE     3 AC1 11 SER C 186  LEU C 187  SER C 188                               
SITE     1 AC2  1 ARG A 211                                                     
SITE     1 AC3  3 THR A 109  VAL A 110  HOH A 409                               
SITE     1 AC4  7 SER A 156  GLY A 157  SER A 159  HOH A 401                    
SITE     2 AC4  7 HOH A 445  HOH A 470  HOH A 527                               
SITE     1 AC5 11 SER B 162  SER B 176  SER B 177  THR B 178                    
SITE     2 AC5 11 HOH B 603  PHE E 175  PRO E 176  VAL E 178                    
SITE     3 AC5 11 SER E 186  LEU E 187  SER E 188                               
SITE     1 AC6  1 ARG B 211                                                     
SITE     1 AC7  5 SER B 156  GLY B 157  HOH B 612  HOH B 624                    
SITE     2 AC7  5 HOH B 651                                                     
SITE     1 AC8  4 SER C  54  ARG C  72  ASP C  73  ASN C  74                    
SITE     1 AC9  7 SER C  52  SER C  54  GLY C  56  SER C  57                    
SITE     2 AC9  7 HOH C 426  HOH C 472  SER F 419                               
SITE     1 AD1  4 TYR C  59  HOH C 410  HOH C 453  HIS F 421                    
SITE     1 AD2  4 GLY E  10  THR E 116  LEU E 117  PRO E 158                    
CRYST1   49.810  149.430   67.950  90.00  90.08  90.00 P 1 21 1      4          
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      0.020076  0.000000  0.000028        0.00000                         
SCALE2      0.000000  0.006692  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014717        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system