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Database: PDB
Entry: 3NID
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HEADER    CELL ADHESION/BLOOD CLOTTING            15-JUN-10   3NID              
TITLE     THE CLOSED HEADPIECE OF INTEGRIN ALPHAIIB BETA3 AND ITS COMPLEX WITH  
TITLE    2 AN ALPAHIIB BETA3 -SPECIFIC ANTAGONIST THAT DOES NOT INDUCE OPENING  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: INTEGRIN ALPHA-IIB, RESIDUES 32-488;                       
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6 INTEGRIN ALPHA-IIB HEAVY CHAIN;                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: INTEGRIN BETA-3, RESIDUES 27-497;                          
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MMONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                     
COMPND  16 CHAIN: E, H;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: MMONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                     
COMPND  20 CHAIN: F, L;                                                         
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGA2B, GP2B, ITGAB;                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  10 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;                          
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 GENE: ITGB3, GP3A;                                                   
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  22 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  24 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;                          
SOURCE  25 MOL_ID: 3;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  27 ORGANISM_COMMON: MOUSE;                                              
SOURCE  28 ORGANISM_TAXID: 10090;                                               
SOURCE  29 STRAIN: BALB/C;                                                      
SOURCE  30 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  31 MOL_ID: 4;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  33 ORGANISM_COMMON: MOUSE;                                              
SOURCE  34 ORGANISM_TAXID: 10090;                                               
SOURCE  35 STRAIN: BALB/C;                                                      
SOURCE  36 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    INTEGRIN, HEADPIECE, ALPHAIIB, BETA3, CELL ADHESION-BLOOD CLOTTING    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   1   22-DEC-10 3NID    0                                                
JRNL        AUTH   J.H.ZHU,J.Q.ZHU,A.NEGRI,D.PROVASI,M.FILIZOLA,B.S.COLLER,     
JRNL        AUTH 2 T.A.SPRINGER                                                 
JRNL        TITL   CLOSED HEADPIECE OF INTEGRIN {ALPHA}IIB{BETA}3 AND ITS       
JRNL        TITL 2 COMPLEX WITH AN {ALPHA}IIB{BETA}3-SPECIFIC ANTAGONIST THAT   
JRNL        TITL 3 DOES NOT INDUCE OPENING.                                     
JRNL        REF    BLOOD                         V. 116  5050 2010              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   20679525                                                     
JRNL        DOI    10.1182/BLOOD-2010-04-281154                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 168819                         
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) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1029                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12241                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2430                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 87                           
REMARK   3   BIN FREE R VALUE                    : 0.2530                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20715                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 302                                     
REMARK   3   SOLVENT ATOMS            : 1059                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.16000                                             
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : -0.05000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.217         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.179         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.123         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.963        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21579 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 14427 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 29409 ; 1.068 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 35078 ; 0.780 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2712 ; 5.713 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   930 ;32.897 ;24.355       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3360 ;12.463 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   112 ;14.191 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3263 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24094 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4269 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 13454 ; 1.845 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5484 ; 0.391 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21723 ; 3.327 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8125 ; 6.419 ;20.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7676 ; 8.437 ;20.000       
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 : 9                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     454      6                      
REMARK   3           1     C      1       C     454      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   1    A    (A):   5857 ; 0.300 ;10.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):   5857 ; 3.150 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B      57      6                      
REMARK   3           1     D      1       D      57      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   2    B    (A):    719 ; 0.510 ;10.000           
REMARK   3   LOOSE THERMAL      2    B (A**2):    719 ; 2.820 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 0                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   3    B    (A):   1651 ; 0.440 ;10.000           
REMARK   3   LOOSE THERMAL      3    B (A**2):   1651 ; 2.740 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    109       B     352      6                      
REMARK   3           1     D    109       D     352      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   4    B    (A):   3151 ; 0.260 ;10.000           
REMARK   3   LOOSE THERMAL      4    B (A**2):   3151 ; 2.750 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    433       B     466      6                      
REMARK   3           1     D    433       D     466      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   5    B    (A):    418 ; 0.550 ;10.000           
REMARK   3   LOOSE THERMAL      5    B (A**2):    418 ; 2.960 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : H E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H      1       H     119      6                      
REMARK   3           1     E      1       E     119      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   6    H    (A):   1555 ; 0.270 ;10.000           
REMARK   3   LOOSE THERMAL      6    H (A**2):   1555 ; 2.050 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : H E                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     H    120       H     221      6                      
REMARK   3           1     E    120       E     221      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   7    H    (A):   1166 ; 0.430 ;10.000           
REMARK   3   LOOSE THERMAL      7    H (A**2):   1166 ; 2.110 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
REMARK   3     CHAIN NAMES                    : L F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L      1       L     108      6                      
REMARK   3           1     F      1       F     108      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   8    L    (A):   1358 ; 0.220 ;10.000           
REMARK   3   LOOSE THERMAL      8    L (A**2):   1358 ; 2.180 ;20.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
REMARK   3     CHAIN NAMES                    : L F                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     L    109       L     214      6                      
REMARK   3           1     F    109       F     214      6                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   LOOSE POSITIONAL   9    L    (A):   1388 ; 0.610 ;10.000           
REMARK   3   LOOSE THERMAL      9    L (A**2):   1388 ; 3.850 ;20.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 52                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.5300  91.1560  38.8290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1115 T22:   0.0930                                     
REMARK   3      T33:   0.0973 T12:   0.0063                                     
REMARK   3      T13:  -0.0188 T23:   0.0208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1594 L22:   2.8255                                     
REMARK   3      L33:   2.3799 L12:  -1.2771                                     
REMARK   3      L13:  -1.1732 L23:   1.0227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0298 S12:   0.2277 S13:   0.0685                       
REMARK   3      S21:  -0.2728 S22:  -0.0925 S23:   0.3246                       
REMARK   3      S31:  -0.0798 S32:  -0.3807 S33:   0.0627                       
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    74        A   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.0020  95.4830  62.6300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1108 T22:   0.0793                                     
REMARK   3      T33:   0.1222 T12:  -0.0129                                     
REMARK   3      T13:   0.0715 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7983 L22:   0.8745                                     
REMARK   3      L33:   0.9889 L12:  -0.1062                                     
REMARK   3      L13:  -0.0237 L23:   0.3816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0151 S12:  -0.0601 S13:  -0.0227                       
REMARK   3      S21:   0.1712 S22:  -0.0750 S23:   0.2380                       
REMARK   3      S31:   0.0990 S32:  -0.2620 S33:   0.0902                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   275        A   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.4820  86.1120  60.3930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1207 T22:   0.0472                                     
REMARK   3      T33:   0.0894 T12:   0.0523                                     
REMARK   3      T13:  -0.0028 T23:   0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1272 L22:   4.3203                                     
REMARK   3      L33:   2.0267 L12:   0.5630                                     
REMARK   3      L13:  -0.2273 L23:  -0.0188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:  -0.1472 S13:  -0.1364                       
REMARK   3      S21:   0.2839 S22:   0.0395 S23:  -0.4313                       
REMARK   3      S31:   0.1664 S32:   0.1514 S33:  -0.0447                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   335        A   454                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.6750  82.8310  45.0520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1086 T22:   0.0163                                     
REMARK   3      T33:   0.0714 T12:   0.0355                                     
REMARK   3      T13:   0.0482 T23:   0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5288 L22:   2.4086                                     
REMARK   3      L33:   1.6093 L12:   0.1475                                     
REMARK   3      L13:   0.2345 L23:   0.4449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0505 S12:   0.0057 S13:  -0.1365                       
REMARK   3      S21:   0.0878 S22:   0.0957 S23:  -0.1448                       
REMARK   3      S31:   0.1334 S32:   0.0865 S33:  -0.0452                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    25                          
REMARK   3    ORIGIN FOR THE GROUP (A): 117.7490  84.8540  37.1380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5513 T22:   0.8971                                     
REMARK   3      T33:   0.6934 T12:   0.4608                                     
REMARK   3      T13:  -0.0002 T23:  -0.1273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3065 L22:   7.9984                                     
REMARK   3      L33:  20.4155 L12:   3.4987                                     
REMARK   3      L13:  -0.5618 L23:   0.5429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4309 S12:  -0.4759 S13:  -1.3949                       
REMARK   3      S21:   0.3153 S22:   0.0177 S23:  -0.4621                       
REMARK   3      S31:   1.8949 S32:   0.8260 S33:   0.4132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    26        B    60                          
REMARK   3    ORIGIN FOR THE GROUP (A): 126.5140  91.0210  34.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3202 T22:   2.0489                                     
REMARK   3      T33:   0.9612 T12:   0.3624                                     
REMARK   3      T13:  -0.0737 T23:  -0.3760                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8713 L22:   3.9784                                     
REMARK   3      L33:   7.4353 L12:  -1.1401                                     
REMARK   3      L13:  -2.8208 L23:   1.5980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1840 S12:  -0.2316 S13:   0.5221                       
REMARK   3      S21:   0.1200 S22:   0.9776 S23:  -1.5618                       
REMARK   3      S31:   0.4601 S32:   3.2698 S33:  -0.7936                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    61        B   108                          
REMARK   3    ORIGIN FOR THE GROUP (A): 103.7180 113.1850  51.6740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1523 T22:   0.6441                                     
REMARK   3      T33:   0.6635 T12:  -0.0577                                     
REMARK   3      T13:   0.0373 T23:  -0.1897                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4651 L22:   7.5702                                     
REMARK   3      L33:   8.6167 L12:  -4.2968                                     
REMARK   3      L13:  -4.0426 L23:   7.1996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1963 S12:  -0.1214 S13:   0.8312                       
REMARK   3      S21:  -0.2965 S22:   0.6433 S23:  -0.5552                       
REMARK   3      S31:  -0.3503 S32:   1.0157 S33:  -0.8396                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   109        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.3760 123.0290  66.2230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1868 T22:   0.0487                                     
REMARK   3      T33:   0.1443 T12:   0.0264                                     
REMARK   3      T13:   0.0396 T23:  -0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0013 L22:   2.7139                                     
REMARK   3      L33:   1.4119 L12:   1.4921                                     
REMARK   3      L13:  -0.0728 L23:   0.5756                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0367 S12:  -0.3498 S13:   0.3114                       
REMARK   3      S21:   0.1224 S22:   0.0150 S23:  -0.1198                       
REMARK   3      S31:  -0.2215 S32:   0.0491 S33:  -0.0517                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   178        B   354                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.6710 116.0720  61.9200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1034 T22:   0.0220                                     
REMARK   3      T33:   0.1216 T12:   0.0096                                     
REMARK   3      T13:   0.0430 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9379 L22:   2.5530                                     
REMARK   3      L33:   1.3835 L12:   0.6905                                     
REMARK   3      L13:   0.2629 L23:   0.7715                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0153 S12:  -0.0313 S13:   0.1056                       
REMARK   3      S21:  -0.0135 S22:   0.1094 S23:  -0.1932                       
REMARK   3      S31:  -0.1230 S32:   0.1081 S33:  -0.0941                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   355        B   383                          
REMARK   3    ORIGIN FOR THE GROUP (A):  98.8810 101.7180  57.3860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1934 T22:   0.2895                                     
REMARK   3      T33:   0.4470 T12:   0.0854                                     
REMARK   3      T13:   0.0480 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6166 L22:   5.9118                                     
REMARK   3      L33:  14.1401 L12:  -0.9835                                     
REMARK   3      L13:   1.0837 L23:   3.0343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2167 S12:  -0.2775 S13:  -0.0252                       
REMARK   3      S21:   0.6746 S22:   0.2820 S23:   0.1867                       
REMARK   3      S31:   0.8229 S32:   0.9027 S33:  -0.0653                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   384        B   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  99.3080 104.7860  50.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1403 T22:   0.4096                                     
REMARK   3      T33:   0.4504 T12:   0.0233                                     
REMARK   3      T13:  -0.0222 T23:  -0.0648                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7586 L22:   3.6432                                     
REMARK   3      L33:   9.3908 L12:  -2.5965                                     
REMARK   3      L13:  -3.3303 L23:   4.7398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1181 S12:   0.0651 S13:  -0.1498                       
REMARK   3      S21:   0.2147 S22:   0.1659 S23:   0.0628                       
REMARK   3      S31:   0.3205 S32:   0.4981 S33:  -0.0478                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   433        B   466                          
REMARK   3    ORIGIN FOR THE GROUP (A): 115.9970  88.5430  19.2060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2302 T22:   0.7523                                     
REMARK   3      T33:   0.5872 T12:   0.1606                                     
REMARK   3      T13:   0.0907 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9120 L22:   1.5651                                     
REMARK   3      L33:  15.0908 L12:   0.8385                                     
REMARK   3      L13:   0.2888 L23:  -1.0224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2017 S12:   0.2711 S13:   0.2249                       
REMARK   3      S21:  -0.2492 S22:   0.4248 S23:  -0.2408                       
REMARK   3      S31:   0.2436 S32:   1.1079 S33:  -0.2231                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    73                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.8060  95.1680 130.2080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0877 T22:   0.3573                                     
REMARK   3      T33:   0.1313 T12:  -0.0136                                     
REMARK   3      T13:   0.0211 T23:  -0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4122 L22:   1.8398                                     
REMARK   3      L33:   3.2922 L12:   0.6674                                     
REMARK   3      L13:  -0.7807 L23:  -0.5998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0490 S12:  -0.3999 S13:   0.1188                       
REMARK   3      S21:   0.1329 S22:  -0.0347 S23:  -0.2733                       
REMARK   3      S31:  -0.0960 S32:   0.5939 S33:   0.0838                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    74        C   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  91.9610  89.7630 106.6780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1494 T22:   0.2888                                     
REMARK   3      T33:   0.1192 T12:   0.0380                                     
REMARK   3      T13:   0.1105 T23:  -0.0022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9501 L22:   1.1475                                     
REMARK   3      L33:   1.2238 L12:   0.5561                                     
REMARK   3      L13:   0.0046 L23:  -0.0870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0681 S12:   0.1170 S13:  -0.0402                       
REMARK   3      S21:  -0.2008 S22:   0.0095 S23:  -0.2401                       
REMARK   3      S31:   0.1749 S32:   0.5002 S33:   0.0586                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   275        C   334                          
REMARK   3    ORIGIN FOR THE GROUP (A):  71.2280  75.8330 114.6080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2253 T22:   0.0386                                     
REMARK   3      T33:   0.1296 T12:  -0.0352                                     
REMARK   3      T13:   0.0592 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9155 L22:   3.7696                                     
REMARK   3      L33:   3.3858 L12:  -1.8993                                     
REMARK   3      L13:   0.0732 L23:  -0.6202                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0751 S12:   0.0883 S13:  -0.5233                       
REMARK   3      S21:  -0.1409 S22:   0.0189 S23:   0.1801                       
REMARK   3      S31:   0.5204 S32:  -0.0389 S33:   0.0562                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   335        C   453                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.3360  80.3710 129.4100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1849 T22:   0.1582                                     
REMARK   3      T33:   0.0865 T12:   0.0427                                     
REMARK   3      T13:   0.0620 T23:   0.0356                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7348 L22:   1.8903                                     
REMARK   3      L33:   2.4722 L12:   0.2485                                     
REMARK   3      L13:   0.1388 L23:  -0.1158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0253 S12:  -0.2804 S13:  -0.3915                       
REMARK   3      S21:  -0.0138 S22:   0.0276 S23:  -0.0861                       
REMARK   3      S31:   0.4329 S32:   0.1906 S33:  -0.0023                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    25                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9070  68.5850 139.4080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6905 T22:   0.5196                                     
REMARK   3      T33:   0.4753 T12:  -0.3349                                     
REMARK   3      T13:   0.0918 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2185 L22:  11.1172                                     
REMARK   3      L33:  14.8679 L12:  -2.1740                                     
REMARK   3      L13:  -3.3589 L23:   5.5865                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2106 S12:   0.0546 S13:  -1.1613                       
REMARK   3      S21:   0.1127 S22:  -0.3101 S23:  -0.2709                       
REMARK   3      S31:   1.7333 S32:  -0.2125 S33:   0.5206                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    26        D    59                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2060  71.5570 140.3510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3918 T22:   0.9015                                     
REMARK   3      T33:   0.5799 T12:  -0.4741                                     
REMARK   3      T13:   0.0732 T23:  -0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1918 L22:   6.1559                                     
REMARK   3      L33:  16.0777 L12:  -1.1716                                     
REMARK   3      L13:  -4.5425 L23:  -1.9464                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4013 S12:   0.2205 S13:  -0.1430                       
REMARK   3      S21:   0.2550 S22:   0.2696 S23:   1.0402                       
REMARK   3      S31:   1.1969 S32:  -2.2618 S33:   0.1317                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    60        D    91                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.5090  95.7760 113.4460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1176 T22:   0.4740                                     
REMARK   3      T33:   0.2297 T12:   0.0219                                     
REMARK   3      T13:   0.0360 T23:   0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4013 L22:   6.4555                                     
REMARK   3      L33:  15.7556 L12:   2.1587                                     
REMARK   3      L13:  -2.9066 L23:  -7.2854                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2520 S12:   0.2154 S13:   0.2759                       
REMARK   3      S21:   0.4152 S22:   0.2600 S23:   0.2600                       
REMARK   3      S31:  -0.8639 S32:  -0.8008 S33:  -0.5120                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    92        D   176                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.3170 100.9320  98.9110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1994 T22:   0.1584                                     
REMARK   3      T33:   0.0995 T12:  -0.0262                                     
REMARK   3      T13:   0.0350 T23:   0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2741 L22:   0.8109                                     
REMARK   3      L33:   2.2242 L12:   0.1440                                     
REMARK   3      L13:  -0.2795 L23:  -0.5615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:   0.3508 S13:   0.2523                       
REMARK   3      S21:  -0.0595 S22:   0.0647 S23:   0.0714                       
REMARK   3      S31:  -0.0198 S32:  -0.3251 S33:  -0.0238                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   177        D   353                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7540 100.6150 101.1800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1586 T22:   0.0805                                     
REMARK   3      T33:   0.0704 T12:  -0.0232                                     
REMARK   3      T13:   0.0470 T23:   0.0177                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0520 L22:   0.9116                                     
REMARK   3      L33:   2.5049 L12:  -0.3463                                     
REMARK   3      L13:   0.7335 L23:  -0.2510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0637 S12:   0.0303 S13:   0.2430                       
REMARK   3      S21:  -0.0536 S22:   0.0527 S23:   0.0221                       
REMARK   3      S31:  -0.1443 S32:  -0.1603 S33:   0.0110                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   354        D   383                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.1000  81.4900 112.5570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1935 T22:   0.2131                                     
REMARK   3      T33:   0.2391 T12:  -0.0545                                     
REMARK   3      T13:   0.0829 T23:   0.0341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1774 L22:   3.0294                                     
REMARK   3      L33:  14.1530 L12:   0.0599                                     
REMARK   3      L13:   0.7932 L23:  -0.7923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1612 S12:   0.1808 S13:  -0.4332                       
REMARK   3      S21:  -0.2711 S22:  -0.0301 S23:  -0.1754                       
REMARK   3      S31:   1.0689 S32:   0.0750 S33:   0.1913                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   384        D   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):  33.2280  86.0160 119.2990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1375 T22:   0.2799                                     
REMARK   3      T33:   0.1934 T12:  -0.0789                                     
REMARK   3      T13:   0.0154 T23:   0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3754 L22:   1.5444                                     
REMARK   3      L33:  10.7579 L12:   0.3480                                     
REMARK   3      L13:  -1.5533 L23:  -1.8194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1497 S12:  -0.0034 S13:  -0.1563                       
REMARK   3      S21:  -0.0377 S22:  -0.0123 S23:  -0.1307                       
REMARK   3      S31:   0.5029 S32:  -0.3852 S33:   0.1620                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   437        D   468                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2560  79.3570 155.4240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2066 T22:   0.1992                                     
REMARK   3      T33:   0.2185 T12:  -0.1422                                     
REMARK   3      T13:   0.0818 T23:  -0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.6134 L22:   6.3151                                     
REMARK   3      L33:   5.7472 L12:   2.1181                                     
REMARK   3      L13:  -1.0434 L23:   4.7914                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0621 S12:  -0.5614 S13:  -0.2457                       
REMARK   3      S21:   0.1347 S22:  -0.1648 S23:   0.2339                       
REMARK   3      S31:   0.4225 S32:  -0.4836 S33:   0.2270                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E    33                          
REMARK   3    ORIGIN FOR THE GROUP (A): 115.5550  83.4160  86.1720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8949 T22:   0.6580                                     
REMARK   3      T33:   0.4725 T12:  -0.0916                                     
REMARK   3      T13:   0.2336 T23:  -0.1793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0473 L22:   7.0426                                     
REMARK   3      L33:   6.3586 L12:  -3.9841                                     
REMARK   3      L13:  -1.7571 L23:  -1.8413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1489 S12:   0.5040 S13:  -1.0838                       
REMARK   3      S21:  -1.2615 S22:  -0.2810 S23:  -0.1046                       
REMARK   3      S31:   1.8576 S32:  -0.0193 S33:   0.4299                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    34        E    64                          
REMARK   3    ORIGIN FOR THE GROUP (A): 114.5390  96.0790  85.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4977 T22:   0.6027                                     
REMARK   3      T33:   0.2677 T12:  -0.0330                                     
REMARK   3      T13:   0.2822 T23:   0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5617 L22:   6.0202                                     
REMARK   3      L33:   3.5678 L12:  -1.5463                                     
REMARK   3      L13:   2.5836 L23:   0.6792                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2424 S12:   0.5647 S13:   0.3448                       
REMARK   3      S21:  -0.8975 S22:  -0.3096 S23:  -0.3449                       
REMARK   3      S31:   0.3533 S32:   0.2415 S33:   0.0672                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E    65        E   113                          
REMARK   3    ORIGIN FOR THE GROUP (A): 114.8370  89.8840  87.1680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8965 T22:   0.5976                                     
REMARK   3      T33:   0.4264 T12:  -0.0403                                     
REMARK   3      T13:   0.3039 T23:  -0.0476                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0754 L22:   2.0659                                     
REMARK   3      L33:   5.1073 L12:  -1.6493                                     
REMARK   3      L13:  -1.1414 L23:   0.2777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1918 S12:   0.5580 S13:  -0.2263                       
REMARK   3      S21:  -1.1457 S22:  -0.1956 S23:  -0.2878                       
REMARK   3      S31:   0.6934 S32:   0.0586 S33:   0.0038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   114        E   151                          
REMARK   3    ORIGIN FOR THE GROUP (A): 149.5190  86.4050  76.1280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9088 T22:   0.6942                                     
REMARK   3      T33:   1.1397 T12:   0.0452                                     
REMARK   3      T13:   0.1180 T23:   0.2867                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.1808 L22:   2.3431                                     
REMARK   3      L33:   5.9808 L12:  -0.9336                                     
REMARK   3      L13:   1.3470 L23:   3.2778                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4694 S12:   1.4765 S13:  -0.5733                       
REMARK   3      S21:   0.0201 S22:  -0.1497 S23:  -0.6087                       
REMARK   3      S31:  -0.2834 S32:   0.3701 S33:  -0.3196                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   152        E   170                          
REMARK   3    ORIGIN FOR THE GROUP (A): 147.3350  80.2460  83.8380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1217 T22:   1.1826                                     
REMARK   3      T33:   1.4926 T12:  -0.1927                                     
REMARK   3      T13:   0.3052 T23:   0.3546                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.1384 L22:   5.9246                                     
REMARK   3      L33:   3.3796 L12:  -3.5521                                     
REMARK   3      L13:  -3.7111 L23:   3.8414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4233 S12:  -0.5207 S13:  -0.7275                       
REMARK   3      S21:  -0.5386 S22:  -0.4339 S23:  -1.1229                       
REMARK   3      S31:   0.0858 S32:  -0.5943 S33:   0.0106                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   171        E   187                          
REMARK   3    ORIGIN FOR THE GROUP (A): 143.4700  89.4790  78.2920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4721 T22:   0.9190                                     
REMARK   3      T33:   1.0173 T12:  -0.0207                                     
REMARK   3      T13:   0.4009 T23:  -0.0888                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2637 L22:   6.8748                                     
REMARK   3      L33:  19.2779 L12:   2.7161                                     
REMARK   3      L13:  11.7626 L23:   7.5373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9976 S12:   0.5687 S13:   0.6440                       
REMARK   3      S21:  -0.6600 S22:   0.1354 S23:  -0.5555                       
REMARK   3      S31:  -1.4391 S32:   0.4445 S33:   0.8622                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   188        E   221                          
REMARK   3    ORIGIN FOR THE GROUP (A): 157.5460  79.0120  79.3050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2121 T22:   1.4939                                     
REMARK   3      T33:   2.0502 T12:   0.1568                                     
REMARK   3      T13:   0.5145 T23:   0.3286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9500 L22:  10.2443                                     
REMARK   3      L33:   1.4262 L12:   3.2571                                     
REMARK   3      L13:   3.2935 L23:   2.4491                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2994 S12:   0.4432 S13:  -0.2461                       
REMARK   3      S21:  -0.9657 S22:   0.1153 S23:  -1.0512                       
REMARK   3      S31:   0.0742 S32:   0.2364 S33:   0.1841                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     1        F    24                          
REMARK   3    ORIGIN FOR THE GROUP (A): 130.3090 104.7950 101.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3135 T22:   1.0993                                     
REMARK   3      T33:   1.3404 T12:  -0.1379                                     
REMARK   3      T13:   0.0273 T23:  -0.0833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8368 L22:   7.3534                                     
REMARK   3      L33:   4.0285 L12:  -2.0225                                     
REMARK   3      L13:   4.9589 L23:  -1.7291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5260 S12:  -0.5582 S13:   2.3774                       
REMARK   3      S21:   0.1594 S22:  -0.4667 S23:  -1.8319                       
REMARK   3      S31:  -0.2669 S32:   0.3516 S33:   0.9927                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    25        F    79                          
REMARK   3    ORIGIN FOR THE GROUP (A): 122.6370  98.0100 104.4680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1326 T22:   0.6446                                     
REMARK   3      T33:   0.5106 T12:  -0.0830                                     
REMARK   3      T13:   0.1228 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3495 L22:   6.0006                                     
REMARK   3      L33:   4.4816 L12:  -1.3387                                     
REMARK   3      L13:  -0.2635 L23:  -1.5372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2463 S12:  -0.3472 S13:   0.2154                       
REMARK   3      S21:   0.2289 S22:  -0.2145 S23:  -0.8449                       
REMARK   3      S31:   0.0714 S32:   0.5001 S33:   0.4608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F    80        F   105                          
REMARK   3    ORIGIN FOR THE GROUP (A): 125.0060  99.1510  97.2840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2000 T22:   0.5856                                     
REMARK   3      T33:   0.5284 T12:  -0.0583                                     
REMARK   3      T13:   0.2627 T23:   0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3458 L22:   4.9615                                     
REMARK   3      L33:   6.1076 L12:  -2.1204                                     
REMARK   3      L13:   3.7655 L23:  -2.2088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1143 S12:   0.3031 S13:   0.1959                       
REMARK   3      S21:  -0.2770 S22:  -0.3825 S23:  -0.9986                       
REMARK   3      S31:   0.2975 S32:   0.8305 S33:   0.2681                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   106        F   156                          
REMARK   3    ORIGIN FOR THE GROUP (A): 153.5350  98.3150  82.2190              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6052 T22:   0.8077                                     
REMARK   3      T33:   1.1422 T12:  -0.0280                                     
REMARK   3      T13:   0.2247 T23:   0.2827                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7729 L22:   2.8893                                     
REMARK   3      L33:  14.1616 L12:  -0.6448                                     
REMARK   3      L13:  -1.6771 L23:   2.7838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0506 S12:   0.0835 S13:   0.1119                       
REMARK   3      S21:  -0.9791 S22:   0.0554 S23:  -0.1527                       
REMARK   3      S31:  -0.4362 S32:   0.7617 S33:  -0.0048                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   157        F   187                          
REMARK   3    ORIGIN FOR THE GROUP (A): 149.2860  95.4150  80.7120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6977 T22:   1.1272                                     
REMARK   3      T33:   1.2476 T12:   0.0048                                     
REMARK   3      T13:   0.3617 T23:   0.3056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3162 L22:   5.9235                                     
REMARK   3      L33:   4.3775 L12:  -2.8918                                     
REMARK   3      L13:  -3.2028 L23:   4.9875                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1091 S12:   0.2323 S13:  -0.1549                       
REMARK   3      S21:  -0.7247 S22:   0.0938 S23:  -0.1504                       
REMARK   3      S31:  -0.4169 S32:  -0.0413 S33:   0.0153                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   188        F   207                          
REMARK   3    ORIGIN FOR THE GROUP (A): 158.3360 104.9050  81.4030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0097 T22:   1.6619                                     
REMARK   3      T33:   1.7196 T12:  -0.4104                                     
REMARK   3      T13:   0.4766 T23:   0.3526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3958 L22:   6.0300                                     
REMARK   3      L33:   0.7594 L12:   0.3513                                     
REMARK   3      L13:  -0.0553 L23:  -2.1301                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2207 S12:  -0.3857 S13:   0.5428                       
REMARK   3      S21:  -1.0653 S22:  -0.3512 S23:  -1.6841                       
REMARK   3      S31:   0.3469 S32:   0.0642 S33:   0.5719                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   208        F   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): 166.3040  96.9150  70.8070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0456 T22:   1.4972                                     
REMARK   3      T33:   1.0203 T12:   0.0212                                     
REMARK   3      T13:   0.3525 T23:  -0.1357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  44.1430 L22:  13.6955                                     
REMARK   3      L33:   9.2115 L12: -21.9259                                     
REMARK   3      L13:  17.8488 L23: -11.2243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.3192 S12:   0.5650 S13:  -0.6625                       
REMARK   3      S21:  -1.1311 S22:  -1.1721 S23:   1.4226                       
REMARK   3      S31:   0.9529 S32:   1.0966 S33:  -1.1471                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     1        H    29                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4420  90.4760  86.4800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7230 T22:   0.4835                                     
REMARK   3      T33:   0.2774 T12:  -0.0819                                     
REMARK   3      T13:   0.0573 T23:   0.0836                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4421 L22:   4.9074                                     
REMARK   3      L33:   9.4900 L12:  -2.2063                                     
REMARK   3      L13:  -4.4083 L23:   2.5934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:  -0.6526 S13:  -0.6141                       
REMARK   3      S21:   1.3577 S22:  -0.0481 S23:   0.1229                       
REMARK   3      S31:   0.8025 S32:  -0.4273 S33:   0.0475                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    30        H    64                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6210 101.6070  79.3020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2573 T22:   0.2711                                     
REMARK   3      T33:   0.1896 T12:  -0.0389                                     
REMARK   3      T13:   0.1251 T23:  -0.0756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5058 L22:   5.8414                                     
REMARK   3      L33:   4.7140 L12:   1.2379                                     
REMARK   3      L13:   0.4547 L23:   0.8878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2772 S12:  -0.3664 S13:   0.3054                       
REMARK   3      S21:   0.7872 S22:  -0.2669 S23:   0.2445                       
REMARK   3      S31:   0.0234 S32:  -0.2016 S33:  -0.0103                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    65        H   113                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.7650  96.4560  81.0740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4876 T22:   0.3933                                     
REMARK   3      T33:   0.2620 T12:  -0.0674                                     
REMARK   3      T13:   0.1175 T23:  -0.0541                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4228 L22:   3.1673                                     
REMARK   3      L33:   4.3151 L12:   0.3805                                     
REMARK   3      L13:  -1.4033 L23:  -0.3649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1169 S12:  -0.6294 S13:   0.1044                       
REMARK   3      S21:   1.1309 S22:  -0.1606 S23:   0.1737                       
REMARK   3      S31:   0.1264 S32:  -0.2841 S33:   0.0437                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   114        H   151                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5770  86.3960  94.3470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5139 T22:   0.4228                                     
REMARK   3      T33:   1.1514 T12:   0.1050                                     
REMARK   3      T13:   0.3021 T23:   0.2278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1089 L22:   2.1977                                     
REMARK   3      L33:   7.8077 L12:   0.8922                                     
REMARK   3      L13:  -1.4439 L23:   1.5510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2221 S12:  -1.0240 S13:  -1.6111                       
REMARK   3      S21:  -0.0861 S22:  -0.1157 S23:   0.3833                       
REMARK   3      S31:   0.3682 S32:   0.1569 S33:   0.3378                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   152        H   167                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5750  78.8010  91.0110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8367 T22:   1.0006                                     
REMARK   3      T33:   1.8325 T12:   0.4864                                     
REMARK   3      T13:   0.2135 T23:  -0.0668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.0298 L22:  11.0024                                     
REMARK   3      L33:   8.4779 L12:   9.0199                                     
REMARK   3      L13:   5.2961 L23:   8.6085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4634 S12:   0.4561 S13:  -1.6308                       
REMARK   3      S21:   1.2359 S22:   0.6632 S23:  -0.3802                       
REMARK   3      S31:   1.9723 S32:   1.5274 S33:  -0.1998                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 44                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   168        H   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6460  88.7930  89.4260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1258 T22:   0.2331                                     
REMARK   3      T33:   0.6491 T12:   0.0848                                     
REMARK   3      T13:   0.2204 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.9637 L22:   2.9829                                     
REMARK   3      L33:  15.3038 L12:   6.6449                                     
REMARK   3      L13:   7.6945 L23:   1.6799                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3152 S12:   0.1509 S13:  -0.0891                       
REMARK   3      S21:  -0.0965 S22:   0.0117 S23:   0.0210                       
REMARK   3      S31:  -0.1250 S32:   0.4580 S33:   0.3034                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 45                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   188        H   221                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.9690  75.9880  94.8420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5538 T22:   0.6313                                     
REMARK   3      T33:   2.2721 T12:   0.1611                                     
REMARK   3      T13:   0.9088 T23:   0.2280                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5146 L22:   4.1876                                     
REMARK   3      L33:  11.8299 L12:   0.8562                                     
REMARK   3      L13:   5.6161 L23:  -0.0166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6136 S12:  -0.9507 S13:  -2.2469                       
REMARK   3      S21:   0.5743 S22:  -0.1721 S23:   0.0002                       
REMARK   3      S31:   2.8046 S32:  -0.3033 S33:   0.7857                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 46                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     1        L    24                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.9010  98.9090  62.9830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1109 T22:   0.9721                                     
REMARK   3      T33:   1.0959 T12:   0.0983                                     
REMARK   3      T13:  -0.0047 T23:  -0.4176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4143 L22:   6.3342                                     
REMARK   3      L33:   1.1736 L12:  -3.0312                                     
REMARK   3      L13:  -1.8567 L23:   0.9399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1034 S12:   1.0981 S13:  -0.6141                       
REMARK   3      S21:  -0.0828 S22:  -0.3566 S23:   1.6337                       
REMARK   3      S31:  -0.0641 S32:  -0.8012 S33:   0.2533                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 47                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    25        L    79                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.3230  94.1550  62.4660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0264 T22:   0.4200                                     
REMARK   3      T33:   0.3517 T12:  -0.0065                                     
REMARK   3      T13:   0.0528 T23:  -0.1279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0210 L22:   4.4476                                     
REMARK   3      L33:   3.2407 L12:   0.2183                                     
REMARK   3      L13:  -0.0224 L23:   0.6706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0141 S12:   0.2329 S13:  -0.2732                       
REMARK   3      S21:  -0.0620 S22:  -0.3474 S23:   0.6008                       
REMARK   3      S31:   0.1106 S32:  -0.6833 S33:   0.3334                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 48                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L    80        L   105                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0870  97.1740  68.6610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0823 T22:   0.4548                                     
REMARK   3      T33:   0.3829 T12:   0.0153                                     
REMARK   3      T13:   0.1464 T23:  -0.1419                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4661 L22:   6.3780                                     
REMARK   3      L33:   3.6912 L12:   3.8122                                     
REMARK   3      L13:   0.7484 L23:   2.6891                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0996 S12:  -0.1175 S13:  -0.1480                       
REMARK   3      S21:   0.3958 S22:  -0.5178 S23:   0.8518                       
REMARK   3      S31:   0.2220 S32:  -0.7033 S33:   0.4182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 49                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   106        L   128                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5480  87.8660  85.6180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2215 T22:   0.4457                                     
REMARK   3      T33:   1.3103 T12:  -0.0883                                     
REMARK   3      T13:   0.3127 T23:  -0.1886                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9369 L22:   3.2043                                     
REMARK   3      L33:   0.3946 L12:   0.0206                                     
REMARK   3      L13:  -1.0753 L23:   0.9142                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5104 S12:   0.6409 S13:  -2.1763                       
REMARK   3      S21:   0.5073 S22:   0.1394 S23:   0.3552                       
REMARK   3      S31:   0.2171 S32:  -0.0707 S33:   0.3710                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 50                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   129        L   155                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.3370  95.7460  83.2450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.4965                                     
REMARK   3      T33:   0.7063 T12:  -0.0077                                     
REMARK   3      T13:   0.0893 T23:  -0.0856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2898 L22:   3.4806                                     
REMARK   3      L33:   5.2664 L12:  -2.1659                                     
REMARK   3      L13:  -0.9969 L23:   3.6427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0923 S12:   0.5072 S13:  -0.8182                       
REMARK   3      S21:  -0.0632 S22:  -0.0516 S23:   0.3048                       
REMARK   3      S31:  -0.3547 S32:  -0.2589 S33:   0.1438                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 51                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   156        L   209                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1250  94.2290  85.2580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0820 T22:   0.3340                                     
REMARK   3      T33:   0.7181 T12:  -0.0511                                     
REMARK   3      T13:   0.1064 T23:  -0.0380                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3016 L22:   3.0125                                     
REMARK   3      L33:  10.7474 L12:  -1.5180                                     
REMARK   3      L13:  -3.6114 L23:   2.7050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3816 S12:   0.3285 S13:  -0.9363                       
REMARK   3      S21:   0.1765 S22:  -0.0394 S23:   0.3482                       
REMARK   3      S31:  -0.0577 S32:  -0.3191 S33:   0.4211                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 52                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   210        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): -34.4500  91.1550  97.2780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.5565 T22:   1.5270                                     
REMARK   3      T33:   0.9033 T12:   0.0446                                     
REMARK   3      T13:   0.4700 T23:  -0.3487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  76.2091 L22: 191.5262                                     
REMARK   3      L33:  12.2154 L12: 120.0856                                     
REMARK   3      L13:  23.8164 L23:  34.2220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   4.0626 S12:  -1.7034 S13:  -3.4924                       
REMARK   3      S21:   4.2853 S22:  -3.5156 S23:  -5.8307                       
REMARK   3      S31:   4.4528 S32:   0.4618 S33:  -0.5470                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3NID COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059866.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00695                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 169848                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
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     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.01000                            
REMARK 200  R SYM                      (I) : 0.01000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.83900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 2VDR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      129.48500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.24500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.48500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.24500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, 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 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     LYS A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     THR E   138                                                      
REMARK 465     GLY E   139                                                      
REMARK 465     GLY E   220                                                      
REMARK 465     PRO E   221                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
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   O    HOH A   987     O    HOH A   989              1.93            
REMARK 500   O    HOH A   988     O    HOH A   989              1.96            
REMARK 500   O    HOH D   488     O    HOH D   984              2.06            
REMARK 500   O    HOH A   865     O    HOH B   585              2.06            
REMARK 500   O    HOH A   705     O    HOH A   814              2.08            
REMARK 500   O    HOH B   496     O    HOH B   572              2.09            
REMARK 500   O    HOH A  1048     O    HOH B   608              2.09            
REMARK 500   O    HOH A   607     O    HOH B   700              2.13            
REMARK 500   O    HOH A   985     O    HOH A   987              2.14            
REMARK 500   O    HOH A   717     O    HOH A   772              2.15            
REMARK 500   O    HOH A   987     O    HOH A   988              2.15            
REMARK 500   O    HOH A   717     O    HOH A   721              2.18            
REMARK 500   O    HOH B   495     O    HOH B   572              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 101     -130.07     49.73                                   
REMARK 500    LYS A 118     -119.41     55.74                                   
REMARK 500    GLU A 123      137.11     95.56                                   
REMARK 500    LEU A 212      -46.73     74.11                                   
REMARK 500    SER A 222     -169.47    -71.51                                   
REMARK 500    SER A 261       70.52     53.87                                   
REMARK 500    ASP A 319       37.13     71.50                                   
REMARK 500    PRO B   2      101.29    -55.37                                   
REMARK 500    PRO B  32      162.26    -48.79                                   
REMARK 500    LEU B  33      -72.96    -40.56                                   
REMARK 500    PHE B  56       83.98   -154.06                                   
REMARK 500    ASP B  66       55.93   -148.79                                   
REMARK 500    ASP B  76     -174.36     61.12                                   
REMARK 500    SER B  77       65.35   -156.55                                   
REMARK 500    VAL B 157      -85.12   -122.71                                   
REMARK 500    SER B 213     -160.84   -120.95                                   
REMARK 500    ASP B 241       75.23   -107.13                                   
REMARK 500    LEU B 258       -7.68     87.94                                   
REMARK 500    LEU B 375      -84.34     60.03                                   
REMARK 500    ASP B 432       79.24   -100.82                                   
REMARK 500    SER C 101     -130.53     52.56                                   
REMARK 500    LYS C 118     -115.47     52.79                                   
REMARK 500    GLU C 123      138.28     92.31                                   
REMARK 500    LEU C 212      -43.76     72.98                                   
REMARK 500    ALA C 424        5.85     83.36                                   
REMARK 500    ASP D  47       35.31    -95.50                                   
REMARK 500    VAL D 157      -82.01   -127.30                                   
REMARK 500    LYS D 181       59.59   -100.57                                   
REMARK 500    SER D 213     -161.31   -118.05                                   
REMARK 500    ASP D 241       68.40   -110.63                                   
REMARK 500    LEU D 258      -12.49     88.05                                   
REMARK 500    SER D 337       17.61     58.74                                   
REMARK 500    CYS D 374      -92.37   -106.90                                   
REMARK 500    ASN D 376     -112.32     53.78                                   
REMARK 500    SER E  85       70.05     55.26                                   
REMARK 500    LEU E 100      -74.46    -82.07                                   
REMARK 500    TYR E 101      -61.35   -108.90                                   
REMARK 500    THR E 122       89.23    -68.77                                   
REMARK 500    SER E 178       70.66     50.80                                   
REMARK 500    SER F  77       79.98     60.21                                   
REMARK 500    SER F 127       42.49    -92.91                                   
REMARK 500    ALA F 130      124.78   -178.52                                   
REMARK 500    ALA F 196      117.21   -160.59                                   
REMARK 500    LEU H 100      -70.79    -85.67                                   
REMARK 500    ASP H 179      -15.99     71.22                                   
REMARK 500    SER L  30       54.77     38.95                                   
REMARK 500    SER L  77       80.36     68.14                                   
REMARK 500    ASN L 212      -43.00     68.65                                   
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 D2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 488   O                                                      
REMARK 620 2 HOH D 483   O    73.6                                              
REMARK 620 3 HOH D 482   O   175.4 107.8                                        
REMARK 620 4 GLU D 220   OE2  81.4 148.6  98.6                                  
REMARK 620 5 HOH D 481   O    96.0 116.8  79.5  83.9                            
REMARK 620 6 SER D 121   OG  115.7  78.8  68.9  95.8 148.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 493   O                                                      
REMARK 620 2 HOH B 492   O    93.6                                              
REMARK 620 3 HOH B 495   O   169.3  94.2                                        
REMARK 620 4 GLU B 220   OE2 118.9  97.5  67.3                                  
REMARK 620 5 SER B 121   OG   69.5 163.0 102.5  92.1                            
REMARK 620 6 HOH B 494   O   107.9 110.5  62.4 123.1  75.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 464   O                                                      
REMARK 620 2 ASP C 367   OD1  96.4                                              
REMARK 620 3 TYR C 371   O   100.5 157.7                                        
REMARK 620 4 ASP C 365   OD2 148.7  78.8  79.1                                  
REMARK 620 5 ASP C 373   OD1 117.6  87.0  97.9  93.2                            
REMARK 620 6 ASP C 373   OD2  72.5 116.5  82.8 137.4  51.7                      
REMARK 620 7 ASP C 369   OD1  71.4  81.0  90.6  77.3 165.9 141.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 250   O                                                      
REMARK 620 2 ASP C 245   OD2 165.1                                              
REMARK 620 3 ASP C 247   O    86.5  96.4                                        
REMARK 620 4 THR C 250   OG1  77.1  89.1  78.9                                  
REMARK 620 5 GLU C 243   OE1  74.1 120.8  74.3 141.4                            
REMARK 620 6 GLU C 252   OE2  90.4  80.6 154.4  75.7 129.0                      
REMARK 620 7 GLU C 252   OE1 106.2  77.0 154.4 125.1  87.7  49.9                
REMARK 620 8 GLU C 243   OE2 124.0  70.9  78.6 147.8  49.9 123.2  75.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   OD1                                                    
REMARK 620 2 GLU B 220   OE1 173.9                                              
REMARK 620 3 ASN B 215   OD1  87.9  90.3                                        
REMARK 620 4 PRO B 219   O   100.7  81.2 171.3                                  
REMARK 620 5 ASP B 158   OD2  94.9  91.1  96.7  82.0                            
REMARK 620 6 ASP B 217   O    76.8  97.5  93.6  89.1 166.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C 299   OD1                                                    
REMARK 620 2 ASP C 297   OD1  86.4                                              
REMARK 620 3 ARG C 303   O   163.1  78.3                                        
REMARK 620 4 HOH C 466   O    87.1 156.8 104.1                                  
REMARK 620 5 ASP C 305   OD1 111.4 134.0  84.8  68.9                            
REMARK 620 6 ASP C 305   OD2  85.2  91.0 102.1 110.6  51.2                      
REMARK 620 7 ASP C 301   OD1  83.3  76.6  86.1  80.6 144.8 163.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ARG A 303   O   159.1                                              
REMARK 620 3 ASP A 297   OD1  83.8  75.3                                        
REMARK 620 4 HOH A 471   O    86.8 111.7 154.7                                  
REMARK 620 5 ASP A 305   OD1 111.2  83.3 128.3  77.1                            
REMARK 620 6 ASP A 301   OD1  86.5  86.9  74.8  81.2 150.8                      
REMARK 620 7 ASP A 305   OD2  81.8  97.4  85.5 116.4  51.0 158.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 476   O                                                      
REMARK 620 2 ASP D 127   OD1 176.1                                              
REMARK 620 3 MET D 335   O    90.5  90.1                                        
REMARK 620 4 HOH D 475   O    84.1  99.8  77.1                                  
REMARK 620 5 SER D 123   O    84.5  96.2 160.5  83.6                            
REMARK 620 6 ASP D 126   OD1  93.5  83.0 127.4 155.5  71.9                      
REMARK 620 7 ASP D 126   OD2  92.5  83.9  77.3 154.1 121.7  50.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 250   O                                                      
REMARK 620 2 ASP A 245   OD2 159.2                                              
REMARK 620 3 GLU A 243   OE1  75.8 124.7                                        
REMARK 620 4 THR A 250   OG1  76.2  83.6 143.1                                  
REMARK 620 5 ASP A 247   O    86.5  93.2  80.6  74.1                            
REMARK 620 6 GLU A 243   OE2 128.4  72.0  52.7 144.9  82.2                      
REMARK 620 7 GLU A 252   OE2  81.9  86.6 127.0  71.5 145.4 129.8                
REMARK 620 8 GLU A 252   OE1 100.6  85.4  86.6 122.0 163.4  81.6  51.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 470   O                                                      
REMARK 620 2 TYR A 371   O    97.5                                              
REMARK 620 3 ASP A 367   OD1  97.4 164.2                                        
REMARK 620 4 ASP A 365   OD2 151.6  75.7  88.7                                  
REMARK 620 5 ASP A 373   OD2  70.9  77.5 112.6 131.8                            
REMARK 620 6 ASP A 369   OD1  76.4  90.3  88.1  76.1 143.0                      
REMARK 620 7 ASP A 373   OD1 117.5  92.7  85.1  90.6  51.6 165.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 217   OD1                                                    
REMARK 620 2 ASN D 215   OD1  93.4                                              
REMARK 620 3 PRO D 219   O    99.4 166.3                                        
REMARK 620 4 GLU D 220   OE1 162.9  85.9  80.4                                  
REMARK 620 5 ASP D 158   OD2  96.7  99.5  83.9 100.3                            
REMARK 620 6 ASP D 217   O    75.7  91.8  86.7  87.2 166.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 428   OD1                                                    
REMARK 620 2 ASP A 426   OD1  75.4                                              
REMARK 620 3 TYR A 432   O   156.9  81.9                                        
REMARK 620 4 ASN A 430   OD1  89.2  85.6  84.7                                  
REMARK 620 5 HOH A 472   O    72.8 144.6 127.5  79.0                            
REMARK 620 6 ASP A 434   OD2 116.1 136.2  83.5 133.7  73.3                      
REMARK 620 7 ASP A 434   OD1  87.2  89.2  96.8 174.4 104.1  52.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 465   O                                                      
REMARK 620 2 ASP C 428   OD1  77.2                                              
REMARK 620 3 TYR C 432   O   124.5 153.8                                        
REMARK 620 4 ASN C 430   OD1  78.6  90.9  80.6                                  
REMARK 620 5 ASP C 426   OD1 149.3  77.5  77.0  84.6                            
REMARK 620 6 ASP C 434   OD1 104.4  85.8 100.6 174.9  90.8                      
REMARK 620 7 ASP C 434   OD2  71.0 114.4  88.7 133.8 136.4  51.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 MET B 335   O    88.2                                              
REMARK 620 3 HOH B 474   O   167.9  99.1                                        
REMARK 620 4 HOH B 475   O    95.7  80.1  95.0                                  
REMARK 620 5 SER B 123   O    96.1 167.0  78.8  87.3                            
REMARK 620 6 ASP B 126   OD1  77.7 120.1  90.3 158.1  72.9                      
REMARK 620 7 ASP B 126   OD2  92.0  74.7  80.8 153.4 117.3  48.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 463                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 464                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3324                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 463                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 473                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 222                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NID   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NIF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NIG   RELATED DB: PDB                                   
DBREF  3NID A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3NID B    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  3NID C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3NID D    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  3NID E    1   221  PDB    3NID     3NID             1    221             
DBREF  3NID H    1   221  PDB    3NID     3NID             1    221             
DBREF  3NID F    1   214  PDB    3NID     3NID             1    214             
DBREF  3NID L    1   214  PDB    3NID     3NID             1    214             
SEQRES   1 A  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  457  ALA SER                                                      
SEQRES   1 B  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  471  SER GLN CYS                                                  
SEQRES   1 C  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  457  ALA SER                                                      
SEQRES   1 D  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  471  SER GLN CYS                                                  
SEQRES   1 E  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 F  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 F  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 F  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 F  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 F  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 F  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 F  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 F  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 F  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 F  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 F  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 F  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 F  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 F  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 F  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 F  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 F  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
MODRES 3NID ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3NID ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3NID ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3NID ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3NID ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3NID ASN B  320  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    GOL  A 458       6                                                       
HET    GOL  A 459       6                                                       
HET    GOL  A 460       6                                                       
HET    GOL  A 461       6                                                       
HET    GOL  A 462       6                                                       
HET    GOL  A 463       6                                                       
HET    SO4  A 464       5                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    GOL  B 472       6                                                       
HET    SO4  B 473       5                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    GOL  C 458       6                                                       
HET    GOL  C 459       6                                                       
HET    SO4  C 460       5                                                       
HET    SO4  C 461       5                                                       
HET    SO4  C 462       5                                                       
HET    SO4  C 463       5                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3099      14                                                       
HET    NAG  D3320      14                                                       
HET    NAG  D3321      14                                                       
HET    MAN  D3322      11                                                       
HET    NAG  D3371      14                                                       
HET    NAG  D3372      14                                                       
HET    SO4  D 472       5                                                       
HET    SO4  D 473       5                                                       
HET    SO4  H 222       5                                                       
HET    SO4  L 215       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9   CA    12(CA 2+)                                                    
FORMUL  13  GOL    9(C3 H8 O3)                                                  
FORMUL  19  SO4    10(O4 S 2-)                                                  
FORMUL  20   MG    2(MG 2+)                                                     
FORMUL  23  NAG    10(C8 H15 N O6)                                              
FORMUL  24  MAN    4(C6 H12 O6)                                                 
FORMUL  48  HOH   *1059(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 ASN B    3  ARG B    8  1                                   6    
HELIX    8   8 SER B   12  ALA B   18  1                                   7    
HELIX    9   9 LYS B   41  ASP B   47  1                                   7    
HELIX   10  10 ALA B   50  GLU B   52  5                                   3    
HELIX   11  11 SER B  121  SER B  123  5                                   3    
HELIX   12  12 MET B  124  ILE B  131  1                                   8    
HELIX   13  13 ASN B  133  ARG B  143  1                                  11    
HELIX   14  14 PRO B  169  ASN B  175  1                                   7    
HELIX   15  15 VAL B  200  GLN B  210  1                                  11    
HELIX   16  16 GLY B  221  CYS B  232  1                                  12    
HELIX   17  17 CYS B  232  GLY B  237  1                                   6    
HELIX   18  18 LEU B  258  GLY B  264  5                                   7    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  ILE B  325  1                                  12    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  441  5                                   7    
HELIX   23  23 LEU C  151  ASN C  158  1                                   8    
HELIX   24  24 GLY C  187  LEU C  192  1                                   6    
HELIX   25  25 VAL C  200  TYR C  207  1                                   8    
HELIX   26  26 ASN C  227  PHE C  231  5                                   5    
HELIX   27  27 THR C  259  LEU C  264  1                                   6    
HELIX   28  28 TYR C  440  ALA C  442  5                                   3    
HELIX   29  29 ASN D    3  GLY D    9  1                                   7    
HELIX   30  30 SER D   12  SER D   20  1                                   9    
HELIX   31  31 LYS D   41  ASP D   47  1                                   7    
HELIX   32  32 ALA D   50  GLU D   52  5                                   3    
HELIX   33  33 SER D  121  SER D  123  5                                   3    
HELIX   34  34 MET D  124  ILE D  131  1                                   8    
HELIX   35  35 ASN D  133  ARG D  143  1                                  11    
HELIX   36  36 PRO D  169  ASN D  175  1                                   7    
HELIX   37  37 GLN D  199  GLN D  210  1                                  12    
HELIX   38  38 GLY D  221  CYS D  232  1                                  12    
HELIX   39  39 CYS D  232  GLY D  237  1                                   6    
HELIX   40  40 LEU D  258  GLY D  264  5                                   7    
HELIX   41  41 SER D  291  ASN D  303  1                                  13    
HELIX   42  42 VAL D  314  GLU D  323  1                                  10    
HELIX   43  43 ASN D  339  ARG D  352  1                                  14    
HELIX   44  44 CYS D  435  ALA D  441  5                                   7    
HELIX   45  45 ASN E   28  THR E   32  5                                   5    
HELIX   46  46 PRO E   62  GLN E   65  5                                   4    
HELIX   47  47 THR E   87  THR E   91  5                                   5    
HELIX   48  48 ASP F   79  PHE F   83  5                                   5    
HELIX   49  49 SER F  121  SER F  127  1                                   7    
HELIX   50  50 THR F  182  GLU F  187  1                                   6    
HELIX   51  51 ASN H   28  THR H   32  5                                   5    
HELIX   52  52 PRO H   62  GLN H   65  5                                   4    
HELIX   53  53 THR H   87  THR H   91  5                                   5    
HELIX   54  54 ASP L   79  PHE L   83  5                                   5    
HELIX   55  55 SER L  121  GLY L  128  1                                   8    
HELIX   56  56 LYS L  183  GLU L  187  1                                   5    
SHEET    1   A 4 THR A   9  ALA A  12  0                                        
SHEET    2   A 4 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    3   A 4 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    4   A 4 SER A 420  VAL A 425 -1  N  ARG A 422   O  ILE A 436           
SHEET    1   B 3 LEU A  23  LYS A  27  0                                        
SHEET    2   B 3 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3   B 3 GLY A  52  PRO A  57 -1  O  CYS A  56   N  ILE A  35           
SHEET    1   C 4 THR A  76  VAL A  79  0                                        
SHEET    2   C 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3   C 4 HIS A 112  GLU A 117 -1  O  LEU A 116   N  THR A  83           
SHEET    4   C 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1   D 4 VAL A  97  TRP A 100  0                                        
SHEET    2   D 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3   D 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4   D 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1   E 4 SER A 173  VAL A 175  0                                        
SHEET    2   E 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3   E 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4   E 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1   F 4 VAL A 239  GLY A 242  0                                        
SHEET    2   F 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3   F 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4   F 4 ARG A 276  ARG A 281 -1  O  LEU A 280   N  VAL A 267           
SHEET    1   G 4 VAL A 293  THR A 296  0                                        
SHEET    2   G 4 ASP A 305  ALA A 310 -1  O  LEU A 307   N  ALA A 294           
SHEET    3   G 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4   G 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1   H 2 MET A 314  ARG A 317  0                                        
SHEET    2   H 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1   I 4 ILE A 360  GLY A 364  0                                        
SHEET    2   I 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3   I 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4   I 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1   J 2 GLY A 394  GLN A 395  0                                        
SHEET    2   J 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1   K 3 CYS B  38  LEU B  40  0                                        
SHEET    2   K 3 CYS B  23  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   K 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   L 6 GLU B  60  GLU B  65  0                                        
SHEET    2   L 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3   L 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   L 6 GLU B 411  PRO B 418 -1  N  ILE B 416   O  LEU B 425           
SHEET    5   L 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   L 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   M 5 VAL B  83  SER B  84  0                                        
SHEET    2   M 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   M 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   M 5 LEU B 366  CYS B 374 -1  N  SER B 367   O  LYS B 402           
SHEET    5   M 5 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   N 6 TYR B 190  THR B 197  0                                        
SHEET    2   N 6 LEU B 149  PHE B 156 -1  N  PHE B 153   O  LEU B 194           
SHEET    3   N 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 152           
SHEET    4   N 6 SER B 243  THR B 250  1  O  SER B 243   N  ASP B 113           
SHEET    5   N 6 ILE B 304  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   N 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1   O 2 GLY B 453  GLU B 456  0                                        
SHEET    2   O 2 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1   P 4 THR C   9  ALA C  12  0                                        
SHEET    2   P 4 GLN C 444  TYR C 448 -1  O  VAL C 447   N  THR C   9           
SHEET    3   P 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4   P 4 SER C 420  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1   Q 3 LEU C  23  LYS C  27  0                                        
SHEET    2   Q 3 VAL C  33  GLY C  38 -1  O  ALA C  34   N  HIS C  26           
SHEET    3   Q 3 VAL C  53  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    1   R 4 THR C  76  VAL C  79  0                                        
SHEET    2   R 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3   R 4 HIS C 112  GLU C 117 -1  O  ASN C 114   N  GLN C  85           
SHEET    4   R 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1   S 4 VAL C  97  TRP C 100  0                                        
SHEET    2   S 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3   S 4 SER C 129  GLN C 134 -1  O  SER C 129   N  ALA C 108           
SHEET    4   S 4 ARG C 139  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   T 4 SER C 172  VAL C 175  0                                        
SHEET    2   T 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3   T 4 LEU C 194  PRO C 199 -1  O  ALA C 196   N  LEU C 183           
SHEET    4   T 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1   U 4 VAL C 239  GLY C 242  0                                        
SHEET    2   U 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3   U 4 ALA C 266  LEU C 270 -1  O  LEU C 270   N  TYR C 253           
SHEET    4   U 4 ARG C 276  ARG C 281 -1  O  LEU C 277   N  ILE C 269           
SHEET    1   V 4 VAL C 293  THR C 296  0                                        
SHEET    2   V 4 ASP C 305  ALA C 310 -1  O  LEU C 307   N  ALA C 294           
SHEET    3   V 4 ARG C 327  PHE C 331 -1  O  PHE C 331   N  LEU C 306           
SHEET    4   V 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1   W 2 MET C 314  ARG C 317  0                                        
SHEET    2   W 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1   X 4 ILE C 360  GLY C 364  0                                        
SHEET    2   X 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  LEU C 363           
SHEET    3   X 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4   X 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1   Y 2 GLY C 394  GLN C 395  0                                        
SHEET    2   Y 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1   Z 3 CYS D  38  LEU D  40  0                                        
SHEET    2   Z 3 CYS D  23  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3   Z 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  AA 6 GLU D  60  GLU D  65  0                                        
SHEET    2  AA 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3  AA 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4  AA 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5  AA 6 VAL D 355  ARG D 360 -1  N  GLU D 358   O  LYS D 417           
SHEET    6  AA 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  AB 5 VAL D  83  SER D  84  0                                        
SHEET    2  AB 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  AB 5 THR D 394  VAL D 403 -1  O  ILE D 399   N  PHE D 100           
SHEET    4  AB 5 LEU D 366  THR D 373 -1  N  THR D 373   O  SER D 396           
SHEET    5  AB 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  AC 6 TYR D 190  THR D 197  0                                        
SHEET    2  AC 6 LEU D 149  PHE D 156 -1  N  PHE D 153   O  LEU D 194           
SHEET    3  AC 6 VAL D 112  ASP D 119  1  N  TYR D 116   O  GLY D 152           
SHEET    4  AC 6 SER D 243  THR D 250  1  O  LEU D 245   N  ASP D 113           
SHEET    5  AC 6 ILE D 304  THR D 311  1  O  ALA D 309   N  PHE D 248           
SHEET    6  AC 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  AD 2 THR D 454  GLU D 456  0                                        
SHEET    2  AD 2 VAL D 459  ARG D 461 -1  O  ARG D 461   N  THR D 454           
SHEET    1  AE 4 GLN E   3  GLN E   6  0                                        
SHEET    2  AE 4 VAL E  18  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3  AE 4 THR E  78  LEU E  83 -1  O  LEU E  83   N  VAL E  18           
SHEET    4  AE 4 ALA E  68  ASP E  73 -1  N  THR E  71   O  TYR E  80           
SHEET    1  AF 6 GLU E  10  VAL E  12  0                                        
SHEET    2  AF 6 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  AF 6 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4  AF 6 VAL E  34  ARG E  40 -1  N  VAL E  37   O  TYR E  95           
SHEET    5  AF 6 GLY E  44  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6  AF 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1  AG 4 GLU E  10  VAL E  12  0                                        
SHEET    2  AG 4 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  AG 4 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4  AG 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1  AH 4 SER E 126  LEU E 130  0                                        
SHEET    2  AH 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  AH 4 TYR E 181  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4  AH 4 VAL E 169  THR E 171 -1  N  HIS E 170   O  SER E 186           
SHEET    1  AI 4 SER E 126  LEU E 130  0                                        
SHEET    2  AI 4 SER E 141  TYR E 151 -1  O  GLY E 145   N  LEU E 130           
SHEET    3  AI 4 TYR E 181  THR E 190 -1  O  LEU E 183   N  VAL E 148           
SHEET    4  AI 4 VAL E 175  LEU E 176 -1  N  VAL E 175   O  THR E 182           
SHEET    1  AJ 3 THR E 157  TRP E 160  0                                        
SHEET    2  AJ 3 THR E 200  ALA E 204 -1  O  ASN E 202   N  THR E 159           
SHEET    3  AJ 3 ASP E 213  LYS E 215 -1  O  LYS E 214   N  CYS E 201           
SHEET    1  AK 4 MET F   4  SER F   7  0                                        
SHEET    2  AK 4 VAL F  19  ALA F  25 -1  O  HIS F  24   N  THR F   5           
SHEET    3  AK 4 ASP F  70  ILE F  75 -1  O  LEU F  73   N  ILE F  21           
SHEET    4  AK 4 PHE F  62  SER F  67 -1  N  SER F  63   O  THR F  74           
SHEET    1  AL 6 SER F  10  VAL F  13  0                                        
SHEET    2  AL 6 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AL 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AL 6 ILE F  33  GLN F  38 -1  N  GLY F  34   O  VAL F  89           
SHEET    5  AL 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6  AL 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1  AM 4 SER F  10  VAL F  13  0                                        
SHEET    2  AM 4 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AM 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AM 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1  AN 4 THR F 114  PHE F 118  0                                        
SHEET    2  AN 4 ALA F 130  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3  AN 4 TYR F 173  LEU F 181 -1  O  MET F 175   N  LEU F 136           
SHEET    4  AN 4 VAL F 159  TRP F 163 -1  N  SER F 162   O  SER F 176           
SHEET    1  AO 3 SER F 153  ARG F 155  0                                        
SHEET    2  AO 3 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3  AO 3 TYR F 192  THR F 197 -1  O  GLU F 195   N  LYS F 147           
SHEET    1  AP 4 GLN H   3  GLN H   6  0                                        
SHEET    2  AP 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  AP 4 THR H  78  LEU H  83 -1  O  LEU H  81   N  LEU H  20           
SHEET    4  AP 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1  AQ 6 GLU H  10  VAL H  12  0                                        
SHEET    2  AQ 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AQ 6 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4  AQ 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5  AQ 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AQ 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  AR 4 GLU H  10  VAL H  12  0                                        
SHEET    2  AR 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AR 4 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4  AR 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  AS 4 SER H 126  LEU H 130  0                                        
SHEET    2  AS 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3  AS 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  AS 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1  AT 4 SER H 126  LEU H 130  0                                        
SHEET    2  AT 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3  AT 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  AT 4 VAL H 175  GLN H 177 -1  N  VAL H 175   O  THR H 182           
SHEET    1  AU 3 THR H 157  TRP H 160  0                                        
SHEET    2  AU 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  AU 3 THR H 210  LYS H 215 -1  O  LYS H 214   N  CYS H 201           
SHEET    1  AV 4 MET L   4  SER L   7  0                                        
SHEET    2  AV 4 THR L  18  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3  AV 4 ASP L  70  SER L  76 -1  O  LEU L  73   N  ILE L  21           
SHEET    4  AV 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1  AW 6 SER L  10  VAL L  13  0                                        
SHEET    2  AW 6 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AW 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AW 6 ILE L  33  GLN L  38 -1  N  GLN L  38   O  ASP L  85           
SHEET    5  AW 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6  AW 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  AX 4 SER L  10  VAL L  13  0                                        
SHEET    2  AX 4 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AX 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AX 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AY 4 THR L 114  PHE L 118  0                                        
SHEET    2  AY 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  AY 4 TYR L 173  THR L 182 -1  O  LEU L 179   N  VAL L 132           
SHEET    4  AY 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1  AZ 4 SER L 153  ARG L 155  0                                        
SHEET    2  AZ 4 ILE L 144  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3  AZ 4 SER L 191  HIS L 198 -1  O  THR L 197   N  ASN L 145           
SHEET    4  AZ 4 SER L 201  ASN L 210 -1  O  LYS L 207   N  CYS L 194           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.08  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.07  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.06  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.10  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.09  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.05  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.05  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.07  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.04  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.04  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.04  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.09  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.08  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.04  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.04  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.05  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.06  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.04  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.04  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.04  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.04  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.06  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.04  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.07  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.45  
LINK         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG D3321                 C1  MAN D3322     1555   1555  1.45  
LINK        MG    MG D2001                 O   HOH D 488     1555   1555  1.88  
LINK        MG    MG B2001                 O   HOH B 493     1555   1555  2.07  
LINK        CA    CA C2006                 O   HOH C 464     1555   1555  2.11  
LINK        MG    MG D2001                 O   HOH D 483     1555   1555  2.13  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.14  
LINK        MG    MG D2001                 O   HOH D 482     1555   1555  2.14  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.18  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.19  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.19  
LINK        CA    CA D2002                 O   HOH D 476     1555   1555  2.20  
LINK         OE2 GLU D 220                MG    MG D2001     1555   1555  2.21  
LINK        MG    MG B2001                 O   HOH B 492     1555   1555  2.22  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.22  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.22  
LINK        CA    CA A2006                 O   HOH A 470     1555   1555  2.23  
LINK         OE1 GLU B 220                CA    CA B2003     1555   1555  2.24  
LINK         OD2 ASP A 245                CA    CA A2004     1555   1555  2.24  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.25  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.26  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.26  
LINK         OD2 ASP C 245                CA    CA C2004     1555   1555  2.26  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.28  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.29  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.29  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.29  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.29  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.30  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.30  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.30  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.31  
LINK        CA    CA C2007                 O   HOH C 465     1555   1555  2.32  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.32  
LINK         O   MET D 335                CA    CA D2002     1555   1555  2.32  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.33  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.34  
LINK         OD2 ASP A 365                CA    CA A2006     1555   1555  2.34  
LINK        MG    MG B2001                 O   HOH B 495     1555   1555  2.34  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.35  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.35  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.35  
LINK         OE1 GLU D 220                CA    CA D2003     1555   1555  2.36  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.36  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.37  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.37  
LINK        CA    CA B2002                 O   HOH B 474     1555   1555  2.38  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.38  
LINK        CA    CA D2002                 O   HOH D 475     1555   1555  2.39  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.39  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.40  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.40  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.40  
LINK        CA    CA B2002                 O   HOH B 475     1555   1555  2.40  
LINK        MG    MG D2001                 O   HOH D 481     1555   1555  2.40  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.41  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.41  
LINK         OG  SER D 121                MG    MG D2001     1555   1555  2.42  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.43  
LINK         OD2 ASP C 365                CA    CA C2006     1555   1555  2.43  
LINK        CA    CA A2005                 O   HOH A 471     1555   1555  2.43  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.43  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.43  
LINK         OE2 GLU B 220                MG    MG B2001     1555   1555  2.45  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.45  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.45  
LINK        CA    CA C2005                 O   HOH C 466     1555   1555  2.46  
LINK        CA    CA A2007                 O   HOH A 472     1555   1555  2.47  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.48  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.48  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.48  
LINK         OE1 GLU C 243                CA    CA C2004     1555   1555  2.49  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.49  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.50  
LINK         OE2 GLU A 243                CA    CA A2004     1555   1555  2.51  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.52  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.53  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.53  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.53  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.54  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.54  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.55  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.55  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.56  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.56  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.57  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.57  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.58  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.58  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.59  
LINK         OD2 ASP D 126                CA    CA D2002     1555   1555  2.59  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.60  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.63  
LINK         OG  SER B 121                MG    MG B2001     1555   1555  2.66  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.68  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.69  
LINK        MG    MG B2001                 O   HOH B 494     1555   1555  2.73  
LINK         OD2 ASP B 126                CA    CA B2002     1555   1555  2.74  
CISPEP   1 SER B   77    SER B   78          0        -1.75                     
CISPEP   2 SER B   84    PRO B   85          0        -6.60                     
CISPEP   3 SER B  162    PRO B  163          0         7.94                     
CISPEP   4 SER B  168    PRO B  169          0       -12.56                     
CISPEP   5 PRO B  464    GLY B  465          0        -9.33                     
CISPEP   6 SER D   77    SER D   78          0         3.69                     
CISPEP   7 SER D   84    PRO D   85          0        -7.23                     
CISPEP   8 SER D  162    PRO D  163          0         6.28                     
CISPEP   9 SER D  168    PRO D  169          0        -7.50                     
CISPEP  10 PHE E  152    PRO E  153          0        -5.50                     
CISPEP  11 GLU E  154    PRO E  155          0         0.96                     
CISPEP  12 TRP E  194    PRO E  195          0         2.37                     
CISPEP  13 SER F    7    PRO F    8          0        -9.46                     
CISPEP  14 LEU F   94    PRO F   95          0        -3.24                     
CISPEP  15 TYR F  140    PRO F  141          0         2.52                     
CISPEP  16 PHE H  152    PRO H  153          0        -4.89                     
CISPEP  17 GLU H  154    PRO H  155          0        -2.84                     
CISPEP  18 TRP H  194    PRO H  195          0         2.06                     
CISPEP  19 SER L    7    PRO L    8          0        -8.15                     
CISPEP  20 LEU L   94    PRO L   95          0        -2.81                     
CISPEP  21 TYR L  140    PRO L  141          0         0.56                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A 471                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A 470                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A 472                                          
SITE     1 AC5  5 GLN A 395  SER A 401  ARG A 402  HOH A 595                    
SITE     2 AC5  5 HOH A 632                                                     
SITE     1 AC6  6 PHE A 160  TYR A 190  GOL A 462  HOH A 644                    
SITE     2 AC6  6 HOH A 874  HOH A 875                                          
SITE     1 AC7  5 LEU A   1  LEU A   3  GLN A 405  PRO C 403                    
SITE     2 AC7  5 HOH C 635                                                     
SITE     1 AC8  6 ALA A  89  ARG A  90  HIS A 112  LYS A 124                    
SITE     2 AC8  6 HOH A 643  HOH A 845                                          
SITE     1 AC9  9 TYR A 190  LEU A 192  PHE A 231  GOL A 459                    
SITE     2 AC9  9 HOH A 487  HOH A 489  HOH A 575  HOH A 644                    
SITE     3 AC9  9 HOH A 874                                                     
SITE     1 BC1  5 PRO A 403  HOH A 697  LEU C   1  ASN C   2                    
SITE     2 BC1  5 LEU C   3                                                     
SITE     1 BC2  4 ILE A 154  TYR A 155  ASN A 158  SER A 161                    
SITE     1 BC3  6 SER B 121  GLU B 220  HOH B 492  HOH B 493                    
SITE     2 BC3  6 HOH B 494  HOH B 495                                          
SITE     1 BC4  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 BC4  6 HOH B 474  HOH B 475                                          
SITE     1 BC5  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC5  5 GLU B 220                                                     
SITE     1 BC6  4 LYS B  98  ASN B  99  PHE B 100  HOH B 539                    
SITE     1 BC7  9 MET A 285  LEU B 317  ASN B 320  HOH B 509                    
SITE     2 BC7  9 HOH B 547  HOH B 575  HOH B 763  HOH B 950                    
SITE     3 BC7  9 NAG B3321                                                     
SITE     1 BC8  7 ARG A 281  HOH B 950  HOH B 951  HOH B 952                    
SITE     2 BC8  7 NAG B3320  MAN B3322  MAN B3323                               
SITE     1 BC9  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 CC1  3 ARG A 281  NAG B3321  MAN B3322                               
SITE     1 CC2  1 MAN B3322                                                     
SITE     1 CC3  5 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 CC3  5 NAG B3372                                                     
SITE     1 CC4  1 NAG B3371                                                     
SITE     1 CC5  5 SER B 300  ASN B 303  ILE B 304  PRO B 326                    
SITE     2 CC5  5 HOH B 783                                                     
SITE     1 CC6  6 GLN B  82  GLN B 106  SER B 243  ARG B 352                    
SITE     2 CC6  6 GLY B 420  PHE B 421                                          
SITE     1 CC7  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 CC7  5 GLU C 252                                                     
SITE     1 CC8  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 CC8  6 ASP C 305  HOH C 466                                          
SITE     1 CC9  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 CC9  6 ASP C 373  HOH C 464                                          
SITE     1 DC1  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 DC1  6 ASP C 434  HOH C 465                                          
SITE     1 DC2  6 ARG C  90  TRP C 110  HOH C 850  HOH C 941                    
SITE     2 DC2  6 SER D 162  ALA D 263                                          
SITE     1 DC3  4 PHE C 160  HOH C 489  HOH C 870  HOH C 871                    
SITE     1 DC4  4 PHE A  10  PHE A 411  GLN A 444  PRO C 383                    
SITE     1 DC5  6 ARG C 281  GLY C 282  GLU C 283  TYR C 329                    
SITE     2 DC5  6 PHE C 331  PRO C 343                                          
SITE     1 DC6  2 ARG C 279  ARG C 281                                          
SITE     1 DC7  4 ASN C 227  TYR C 230  ARG C 276  ARG C 279                    
SITE     1 DC8  6 SER D 121  GLU D 220  HOH D 481  HOH D 482                    
SITE     2 DC8  6 HOH D 483  HOH D 488                                          
SITE     1 DC9  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 DC9  6 HOH D 475  HOH D 476                                          
SITE     1 EC1  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 EC1  5 GLU D 220                                                     
SITE     1 EC2  3 ASN D  99  SER D 101  NAG D3372                               
SITE     1 EC3 10 MET C 285  LEU D 317  ASN D 320  HOH D 509                    
SITE     2 EC3 10 HOH D 517  HOH D 543  HOH D 552  HOH D 553                    
SITE     3 EC3 10 HOH D 554  NAG D3321                                          
SITE     1 EC4  4 ARG C 281  HOH D 532  NAG D3320  MAN D3322                    
SITE     1 EC5  1 NAG D3321                                                     
SITE     1 EC6  5 SER D 369  ASN D 371  SER D 398  GLU D 400                    
SITE     2 EC6  5 NAG D3372                                                     
SITE     1 EC7  2 NAG D3099  NAG D3371                                          
SITE     1 EC8  6 GLN D  82  GLN D 106  TYR D 110  SER D 243                    
SITE     2 EC8  6 ARG D 352  PHE D 421                                          
SITE     1 EC9  4 GLN A 134  SER A 137  ARG D 461  CYS D 462                    
SITE     1 FC1  4 LYS H  38  ARG H  40  GLU H  46  PHE H  64                    
SITE     1 FC2  5 GLN L  37  LYS L  39  LEU L  47  PRO L  59                    
SITE     2 FC2  5 PHE L  62                                                     
CRYST1  258.970  144.490  104.200  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.003861  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006921  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009597        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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