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Database: PDB
Entry: 3FCS
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Original site: 3FCS 
HEADER    CELL ADHESION/BLOOD CLOTTING            22-NOV-08   3FCS              
TITLE     STRUCTURE OF COMPLETE ECTODOMAIN OF INTEGRIN AIIBB3                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN, ALPHA 2B;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-989, ECTODOMAIN;                           
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 27-716, EXTRACELLULAR DOMAIN;                 
COMPND  10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: 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;                                                        
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: 3.2.8.1;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1, PEF1;                           
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: ITGB3, GP3A;                                                   
SOURCE  16 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    BETA PROPELLER, ROSSMANN FOLD, EGF DOMAIN, CELL ADHESION, DISEASE     
KEYWDS   2 MUTATION, GLYCOPROTEIN, HOST-VIRUS INTERACTION, INTEGRIN, MEMBRANE,  
KEYWDS   3 PHOSPHOPROTEIN, RECEPTOR, TRANSMEMBRANE, CELL ADHESION-IMMUNE SYSTEM 
KEYWDS   4 COMPLEX, CELL ADHESION-BLOOD CLOTTING COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHU,B.-H.LUO,T.XIAO,C.ZHANG,N.NISHIDA,T.A.SPRINGER                  
REVDAT   2   13-JUL-11 3FCS    1       VERSN                                    
REVDAT   1   20-JAN-09 3FCS    0                                                
JRNL        AUTH   J.ZHU,B.H.LUO,T.XIAO,C.ZHANG,N.NISHIDA,T.A.SPRINGER          
JRNL        TITL   STRUCTURE OF A COMPLETE INTEGRIN ECTODOMAIN IN A PHYSIOLOGIC 
JRNL        TITL 2 RESTING STATE AND ACTIVATION AND DEACTIVATION BY APPLIED     
JRNL        TITL 3 FORCES.                                                      
JRNL        REF    MOL.CELL                      V.  32   849 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   19111664                                                     
JRNL        DOI    10.1016/J.MOLCEL.2008.11.018                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0066                                      
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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 133242                         
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1785                            
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) : 2.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8771                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 127                          
REMARK   3   BIN FREE R VALUE                    : 0.4230                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 23654                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 462                                     
REMARK   3   SOLVENT ATOMS            : 678                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : -0.01000                                             
REMARK   3    B33 (A**2) : 0.03000                                              
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): 0.516         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.297         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.317         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 29.421        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 24891 ; 0.003 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 16841 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 33907 ; 0.741 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 40845 ; 0.647 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3122 ; 4.263 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1104 ;28.826 ;24.583       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3967 ;11.482 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   151 ; 9.957 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3794 ; 0.046 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 27816 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4792 ; 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): 15479 ; 0.880 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  6292 ; 0.159 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 24955 ; 1.542 ;10.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9412 ; 0.777 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8943 ; 1.330 ;10.000       
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 : 12                                
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     221      2                      
REMARK   3           1     C      1       C     221      2                      
REMARK   3           2     A    224       A     271      2                      
REMARK   3           2     C    224       C     271      2                      
REMARK   3           3     A    275       A     276      2                      
REMARK   3           3     C    275       C     276      2                      
REMARK   3           4     A    280       A     452      2                      
REMARK   3           4     C    280       C     452      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2568 ; 0.050 ; 0.250           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   3097 ; 0.090 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):   2568 ; 0.020 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   3097 ; 0.020 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
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    453       A     600      2                      
REMARK   3           1     C    453       C     600      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   2    A    (A):    871 ; 0.050 ; 0.250           
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   1026 ; 0.100 ; 0.500           
REMARK   3   TIGHT THERMAL      2    A (A**2):    871 ; 0.020 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   1026 ; 0.010 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
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    610       A     743      2                      
REMARK   3           1     C    610       C     743      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):    774 ; 0.050 ; 0.250           
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    865 ; 0.100 ; 0.500           
REMARK   3   TIGHT THERMAL      3    A (A**2):    774 ; 0.010 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    865 ; 0.010 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    744       A     763      4                      
REMARK   3           1     C    744       C     763      4                      
REMARK   3           2     A    772       A     959      4                      
REMARK   3           2     C    772       C     959      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):   2050 ; 0.280 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    A (A**2):   2050 ; 0.090 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B       7      4                      
REMARK   3           1     D      1       D       7      4                      
REMARK   3           2     B      8       B      10      6                      
REMARK   3           2     D      8       D      10      6                      
REMARK   3           3     B     11       B      32      4                      
REMARK   3           3     D     11       D      32      4                      
REMARK   3           4     B     36       B      57      4                      
REMARK   3           4     D     36       D      57      4                      
REMARK   3           5     B    434       B     436      4                      
REMARK   3           5     D    434       D     436      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    B    (A):    663 ; 0.200 ; 0.500           
REMARK   3   LOOSE POSITIONAL   5    B    (A):     41 ; 0.260 ; 5.000           
REMARK   3   MEDIUM THERMAL     5    B (A**2):    663 ; 0.100 ; 2.000           
REMARK   3   LOOSE THERMAL      5    B (A**2):     41 ; 0.060 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     58       B     108      4                      
REMARK   3           1     D     58       D     108      4                      
REMARK   3           2     B    353       B     433      4                      
REMARK   3           2     D    353       D     433      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    B    (A):   1719 ; 0.170 ; 0.500           
REMARK   3   MEDIUM THERMAL     6    B (A**2):   1719 ; 0.120 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
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      4                      
REMARK   3           1     D    109       D     352      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  7    B    (A):   3174 ; 0.170 ; 0.500           
REMARK   3   MEDIUM THERMAL     7    B (A**2):   3174 ; 0.130 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 8                                  
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    437       B     472      4                      
REMARK   3           1     D    437       D     472      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  8    B    (A):    449 ; 0.140 ; 0.500           
REMARK   3   MEDIUM THERMAL     8    B (A**2):    449 ; 0.060 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 9                                  
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    473       B     522      4                      
REMARK   3           1     D    473       D     522      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  9    B    (A):    573 ; 0.170 ; 0.500           
REMARK   3   MEDIUM THERMAL     9    B (A**2):    573 ; 0.070 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 10                                 
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    523       B     559      4                      
REMARK   3           1     D    523       D     559      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 10    B    (A):    475 ; 0.240 ; 0.500           
REMARK   3   MEDIUM THERMAL    10    B (A**2):    475 ; 0.100 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 11                                 
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    560       B     605      4                      
REMARK   3           1     D    560       D     605      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 11    B    (A):    554 ; 0.180 ; 0.500           
REMARK   3   MEDIUM THERMAL    11    B (A**2):    554 ; 0.070 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 12                                 
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    601       A     609      5                      
REMARK   3           1     C    601       C     609      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL 12    A    (A):     53 ; 0.070 ; 0.500           
REMARK   3   LOOSE POSITIONAL  12    A    (A):     47 ; 0.110 ; 5.000           
REMARK   3   MEDIUM THERMAL    12    A (A**2):     53 ; 0.080 ; 2.000           
REMARK   3   LOOSE THERMAL     12    A (A**2):     47 ; 0.130 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 23                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   452                          
REMARK   3    RESIDUE RANGE :   A  2004        A  2007                          
REMARK   3    ORIGIN FOR THE GROUP (A): -82.6220 -53.3398 -79.4693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2536 T22:  -0.0294                                     
REMARK   3      T33:  -0.0934 T12:   0.0012                                     
REMARK   3      T13:  -0.0395 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6690 L22:   1.7658                                     
REMARK   3      L33:   1.9983 L12:  -0.2091                                     
REMARK   3      L13:   0.3571 L23:   0.4368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:   0.1589 S13:   0.0807                       
REMARK   3      S21:  -0.3133 S22:  -0.1161 S23:  -0.0579                       
REMARK   3      S31:  -0.0381 S32:  -0.1443 S33:   0.0921                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   452                          
REMARK   3    RESIDUE RANGE :   C  2004        C  2007                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7863  34.0230   9.4560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1907 T22:  -0.3062                                     
REMARK   3      T33:  -0.2377 T12:  -0.0161                                     
REMARK   3      T13:   0.0440 T23:  -0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6977 L22:   1.5980                                     
REMARK   3      L33:   2.0005 L12:  -0.0706                                     
REMARK   3      L13:   0.4183 L23:   0.4365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0925 S12:  -0.1413 S13:   0.0029                       
REMARK   3      S21:   0.0161 S22:   0.0148 S23:   0.0564                       
REMARK   3      S31:  -0.2180 S32:   0.0690 S33:   0.0776                       
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   453        A   600                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.4587 -31.6025 -42.6473              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0568 T22:  -0.2487                                     
REMARK   3      T33:  -0.0129 T12:  -0.0079                                     
REMARK   3      T13:  -0.0074 T23:  -0.2422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3148 L22:   2.3188                                     
REMARK   3      L33:   5.4415 L12:   1.4954                                     
REMARK   3      L13:   2.1381 L23:   0.4958                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1148 S12:  -0.3685 S13:  -0.0966                       
REMARK   3      S21:   0.0685 S22:   0.1690 S23:   0.2735                       
REMARK   3      S31:  -0.3069 S32:  -0.1493 S33:  -0.2838                       
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 :   C   453        C   600                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0567  -1.0633 -27.2439              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1904 T22:  -0.1838                                     
REMARK   3      T33:  -0.0730 T12:   0.0027                                     
REMARK   3      T13:  -0.2075 T23:  -0.0550                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2549 L22:   5.4267                                     
REMARK   3      L33:   5.4763 L12:   1.8080                                     
REMARK   3      L13:   0.6760 L23:   2.5660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1526 S12:   0.0046 S13:   0.1531                       
REMARK   3      S21:  -0.3714 S22:   0.1093 S23:  -0.0469                       
REMARK   3      S31:  -0.0290 S32:  -0.3162 S33:  -0.2619                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   601        A   746                          
REMARK   3    RESIDUE RANGE :   A  2008        A  2008                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.5079 -40.0846 -69.5152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0614 T22:   0.0632                                     
REMARK   3      T33:   0.0108 T12:  -0.0075                                     
REMARK   3      T13:  -0.0255 T23:  -0.2509                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6400 L22:   3.2304                                     
REMARK   3      L33:   7.8315 L12:   0.6586                                     
REMARK   3      L13:   2.7043 L23:   3.2151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0959 S12:   0.0111 S13:  -0.1684                       
REMARK   3      S21:  -0.5900 S22:   0.1266 S23:   0.1128                       
REMARK   3      S31:  -0.6464 S32:  -0.2333 S33:  -0.0307                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   601        C   746                          
REMARK   3    RESIDUE RANGE :   C  2008        C  2008                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5684 -15.1015  -0.2543              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1661 T22:  -0.1807                                     
REMARK   3      T33:   0.0788 T12:   0.0329                                     
REMARK   3      T13:  -0.1624 T23:   0.0438                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4101 L22:   2.8449                                     
REMARK   3      L33:   8.4651 L12:   0.4864                                     
REMARK   3      L13:   3.1575 L23:   2.8071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0809 S12:  -0.5502 S13:   0.1277                       
REMARK   3      S21:   0.0614 S22:   0.0350 S23:  -0.1708                       
REMARK   3      S31:  -0.4495 S32:  -0.6480 S33:  -0.1159                       
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 :   A   747        A   959                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.4014 -69.7992-114.9065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1336 T22:  -0.0461                                     
REMARK   3      T33:  -0.2978 T12:  -0.0842                                     
REMARK   3      T13:  -0.1262 T23:  -0.1501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5071 L22:   5.3303                                     
REMARK   3      L33:   7.4174 L12:  -0.3289                                     
REMARK   3      L13:   0.1689 L23:   3.8160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1320 S12:  -0.2677 S13:   0.1466                       
REMARK   3      S21:   0.1535 S22:   0.1325 S23:  -0.2849                       
REMARK   3      S31:  -0.1266 S32:   0.0819 S33:  -0.0005                       
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 :   C   747        C   959                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0292  -7.5729  44.5094              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7356 T22:   0.9487                                     
REMARK   3      T33:   0.2250 T12:   0.0093                                     
REMARK   3      T13:  -0.3013 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4053 L22:   0.7691                                     
REMARK   3      L33:   2.9958 L12:  -1.2308                                     
REMARK   3      L13:   1.3404 L23:  -0.1264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0772 S12:  -1.5190 S13:  -0.6034                       
REMARK   3      S21:   0.3089 S22:   0.3201 S23:  -0.0778                       
REMARK   3      S31:   0.0290 S32:  -0.7361 S33:  -0.3974                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    57                          
REMARK   3    RESIDUE RANGE :   B   434        B   436                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.5571 -73.4332 -42.1754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1138 T22:  -0.1409                                     
REMARK   3      T33:  -0.1827 T12:   0.0591                                     
REMARK   3      T13:  -0.0546 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1591 L22:   3.3539                                     
REMARK   3      L33:   3.8761 L12:  -1.5525                                     
REMARK   3      L13:   2.4936 L23:  -2.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1368 S12:   0.0249 S13:   0.6087                       
REMARK   3      S21:   0.2090 S22:  -0.1143 S23:  -0.4263                       
REMARK   3      S31:  -0.6482 S32:   0.0285 S33:  -0.0226                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D    57                          
REMARK   3    RESIDUE RANGE :   D   434        D   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.7938 -17.1445 -27.7742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0962 T22:   0.0323                                     
REMARK   3      T33:  -0.1150 T12:   0.0716                                     
REMARK   3      T13:   0.0062 T23:  -0.1133                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1362 L22:   8.1329                                     
REMARK   3      L33:   3.5169 L12:  -0.8401                                     
REMARK   3      L13:  -0.6825 L23:   3.1997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2129 S12:   0.2341 S13:  -0.1440                       
REMARK   3      S21:  -0.4366 S22:   0.2354 S23:   0.6762                       
REMARK   3      S31:   0.0488 S32:  -0.7095 S33:  -0.0225                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    58        B   108                          
REMARK   3    RESIDUE RANGE :   B   353        B   433                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.3761 -87.7205 -63.8100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3266 T22:  -0.5543                                     
REMARK   3      T33:  -0.0483 T12:   0.1416                                     
REMARK   3      T13:  -0.1422 T23:   0.1004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9949 L22:   2.4481                                     
REMARK   3      L33:   4.7672 L12:   1.5713                                     
REMARK   3      L13:   2.4641 L23:   2.9640                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0126 S12:  -0.2050 S13:  -0.6048                       
REMARK   3      S21:   0.0743 S22:   0.0089 S23:   0.1976                       
REMARK   3      S31:   0.7687 S32:   0.2044 S33:  -0.0216                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D    58        D   108                          
REMARK   3    RESIDUE RANGE :   D   353        D   433                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2056   3.7133  -6.2380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.6604 T22:   0.3088                                     
REMARK   3      T33:  -0.0366 T12:   0.1884                                     
REMARK   3      T13:   0.1573 T23:  -0.2235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3879 L22:   6.2464                                     
REMARK   3      L33:   6.3162 L12:   1.5258                                     
REMARK   3      L13:   4.1094 L23:   1.7135                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1903 S12:   0.1258 S13:  -0.1564                       
REMARK   3      S21:  -0.1709 S22:   0.0780 S23:  -0.7849                       
REMARK   3      S31:   0.3308 S32:   0.6615 S33:  -0.2683                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   109        B   352                          
REMARK   3    RESIDUE RANGE :   B  2001        B  2003                          
REMARK   3    ORIGIN FOR THE GROUP (A): -80.6029 -87.0349 -83.1536              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3006 T22:  -0.2293                                     
REMARK   3      T33:   0.1094 T12:  -0.0992                                     
REMARK   3      T13:  -0.1085 T23:  -0.1892                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9253 L22:   2.1482                                     
REMARK   3      L33:   0.7364 L12:  -0.7382                                     
REMARK   3      L13:  -0.4231 L23:   0.2485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1690 S12:   0.4181 S13:  -0.5928                       
REMARK   3      S21:  -0.0205 S22:  -0.1549 S23:   0.3545                       
REMARK   3      S31:   0.6881 S32:  -0.2861 S33:  -0.0141                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   109        D   352                          
REMARK   3    RESIDUE RANGE :   D  2001        D  2003                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5322  31.8298  13.0841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4633 T22:   0.2965                                     
REMARK   3      T33:  -0.0209 T12:  -0.0869                                     
REMARK   3      T13:  -0.0771 T23:  -0.1614                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2660 L22:   1.7838                                     
REMARK   3      L33:   0.5997 L12:  -0.2705                                     
REMARK   3      L13:   0.0287 L23:  -0.6392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1109 S12:   0.0469 S13:   0.1405                       
REMARK   3      S21:   0.2387 S22:   0.1108 S23:  -0.5378                       
REMARK   3      S31:  -0.3197 S32:   0.7132 S33:   0.0002                       
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 :   B   437        B   472                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.2518 -64.8909 -28.2604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2024 T22:   0.2486                                     
REMARK   3      T33:  -0.2543 T12:   0.1281                                     
REMARK   3      T13:   0.0000 T23:  -0.1832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6914 L22:   9.0510                                     
REMARK   3      L33:   3.9345 L12:  -1.3749                                     
REMARK   3      L13:  -3.0657 L23:  -0.3558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0750 S12:  -0.9920 S13:   0.4062                       
REMARK   3      S21:   0.2852 S22:  -0.0983 S23:   0.5756                       
REMARK   3      S31:   0.1899 S32:  -0.6163 S33:   0.1733                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   437        D   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2263  -9.3829 -41.7377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2535 T22:  -0.1291                                     
REMARK   3      T33:  -0.1918 T12:   0.0924                                     
REMARK   3      T13:  -0.2294 T23:   0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7855 L22:   2.6103                                     
REMARK   3      L33:   9.3659 L12:   1.0639                                     
REMARK   3      L13:  -0.1640 L23:   3.6656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1380 S12:   0.5513 S13:   0.4349                       
REMARK   3      S21:  -1.1430 S22:  -0.2722 S23:   0.1319                       
REMARK   3      S31:  -0.7323 S32:  -0.0913 S33:   0.1342                       
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 :   B   473        B   522                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.6151 -51.2952 -44.1610              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0282 T22:  -0.2974                                     
REMARK   3      T33:   0.0050 T12:   0.1950                                     
REMARK   3      T13:  -0.0913 T23:  -0.2338                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1837 L22:   5.7373                                     
REMARK   3      L33:   7.9206 L12:   2.9781                                     
REMARK   3      L13:   1.6035 L23:  -0.4844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2606 S12:  -0.1007 S13:   0.3085                       
REMARK   3      S21:   0.0753 S22:  -0.1167 S23:  -0.1295                       
REMARK   3      S31:   0.1489 S32:   0.2269 S33:   0.3773                       
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   473        D   522                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.6108 -16.0107 -25.8379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2428 T22:  -0.0823                                     
REMARK   3      T33:   0.0810 T12:   0.1658                                     
REMARK   3      T13:  -0.2171 T23:  -0.0773                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3956 L22:   8.9434                                     
REMARK   3      L33:   6.4364 L12:   1.0215                                     
REMARK   3      L13:  -0.7020 L23:  -0.9011                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0497 S12:  -0.0647 S13:  -0.0109                       
REMARK   3      S21:  -0.0982 S22:  -0.1751 S23:  -0.0452                       
REMARK   3      S31:   0.6239 S32:  -0.0030 S33:   0.2248                       
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 :   B   523        B   559                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.5219 -61.8840 -63.7301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2148 T22:  -0.4884                                     
REMARK   3      T33:  -0.0519 T12:   0.0522                                     
REMARK   3      T13:  -0.0408 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.7967 L22:   7.1888                                     
REMARK   3      L33:   9.3594 L12:   4.2165                                     
REMARK   3      L13:   5.0677 L23:   5.4206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:  -0.1388 S13:   0.9855                       
REMARK   3      S21:  -0.3198 S22:  -0.1430 S23:  -0.1647                       
REMARK   3      S31:  -0.3356 S32:  -0.6620 S33:   0.1414                       
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   523        D   559                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1921  -4.1175  -6.2051              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2786 T22:   0.2574                                     
REMARK   3      T33:   0.0422 T12:   0.0926                                     
REMARK   3      T13:  -0.0521 T23:  -0.0589                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3993 L22:   5.6015                                     
REMARK   3      L33:   6.1860 L12:   4.3050                                     
REMARK   3      L13:   2.8353 L23:   1.3158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1729 S12:  -0.2882 S13:  -0.2051                       
REMARK   3      S21:   0.0164 S22:   0.0657 S23:   1.0438                       
REMARK   3      S31:  -0.6047 S32:  -0.1218 S33:  -0.2386                       
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 :   B   560        B   612                          
REMARK   3    ORIGIN FOR THE GROUP (A): -45.0747 -76.7271 -89.5359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0353 T22:   0.2095                                     
REMARK   3      T33:  -0.2329 T12:   0.0667                                     
REMARK   3      T13:  -0.0698 T23:  -0.1093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7873 L22:   3.4245                                     
REMARK   3      L33:   9.8085 L12:   0.0399                                     
REMARK   3      L13:  -2.7694 L23:   0.3367                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3219 S12:   0.3554 S13:  -0.0970                       
REMARK   3      S21:   0.1850 S22:  -0.1038 S23:   0.1055                       
REMARK   3      S31:   0.3470 S32:  -0.1211 S33:   0.4257                       
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   560        D   612                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6652  -4.5346  19.7967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5140 T22:   0.1586                                     
REMARK   3      T33:   0.0095 T12:   0.0000                                     
REMARK   3      T13:  -0.2423 T23:  -0.1647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5751 L22:   2.0675                                     
REMARK   3      L33:   7.2795 L12:  -0.9910                                     
REMARK   3      L13:   1.1539 L23:  -3.8634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0954 S12:  -0.0441 S13:   0.0533                       
REMARK   3      S21:   0.7884 S22:  -0.5623 S23:  -0.6457                       
REMARK   3      S31:   0.0450 S32:   1.0880 S33:   0.4669                       
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 :   B   613        B   690                          
REMARK   3    ORIGIN FOR THE GROUP (A): -42.3353 -95.3977-102.1487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4678 T22:   0.4976                                     
REMARK   3      T33:   0.6048 T12:   0.0381                                     
REMARK   3      T13:   0.0082 T23:  -0.0190                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2241 L22:   1.1316                                     
REMARK   3      L33:   2.6345 L12:   0.2408                                     
REMARK   3      L13:  -0.7174 L23:  -0.2270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4013 S12:  -0.2037 S13:   0.9018                       
REMARK   3      S21:   0.1321 S22:  -0.4006 S23:  -0.1023                       
REMARK   3      S31:   1.1710 S32:   0.1712 S33:  -0.0008                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FCS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050430.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135066                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 4.550                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1700                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.15                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.130                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: COMBINATION OF PDB ENTRY 1JV2 AND 1TXV               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 3350, 50 MM MAGNESIUM ACETATE,   
REMARK 280  AND 0.1 M IMIDAZOLE, PH 7.0, VAPOR DIFFUSION, TEMPERATURE 298.0K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
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      327.31150            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      163.65575            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      490.96725            
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 300 REMARK: HETERO-DIMER                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 74630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 68970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   764                                                      
REMARK 465     GLU A   765                                                      
REMARK 465     GLY A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     ARG A   768                                                      
REMARK 465     GLU A   769                                                      
REMARK 465     GLN A   770                                                      
REMARK 465     ASN A   771                                                      
REMARK 465     SER A   772                                                      
REMARK 465     LEU A   773                                                      
REMARK 465     ASP A   774                                                      
REMARK 465     GLY A   840                                                      
REMARK 465     LEU A   841                                                      
REMARK 465     PRO A   842                                                      
REMARK 465     ILE A   843                                                      
REMARK 465     PRO A   844                                                      
REMARK 465     SER A   845                                                      
REMARK 465     PRO A   846                                                      
REMARK 465     SER A   847                                                      
REMARK 465     PRO A   848                                                      
REMARK 465     ILE A   849                                                      
REMARK 465     HIS A   850                                                      
REMARK 465     PRO A   851                                                      
REMARK 465     ALA A   852                                                      
REMARK 465     HIS A   853                                                      
REMARK 465     HIS A   854                                                      
REMARK 465     LYS A   855                                                      
REMARK 465     ARG A   856                                                      
REMARK 465     ASP A   857                                                      
REMARK 465     ARG A   858                                                      
REMARK 465     ARG A   859                                                      
REMARK 465     GLN A   860                                                      
REMARK 465     ILE A   861                                                      
REMARK 465     PHE A   862                                                      
REMARK 465     LEU A   863                                                      
REMARK 465     PRO A   864                                                      
REMARK 465     GLU A   865                                                      
REMARK 465     PRO A   866                                                      
REMARK 465     GLU A   867                                                      
REMARK 465     GLN A   868                                                      
REMARK 465     PRO A   869                                                      
REMARK 465     SER A   870                                                      
REMARK 465     ARG A   871                                                      
REMARK 465     LEU A   872                                                      
REMARK 465     GLN A   873                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     ASP B   477                                                      
REMARK 465     TYR B   478                                                      
REMARK 465     ARG B   479                                                      
REMARK 465     PRO B   480                                                      
REMARK 465     SER B   481                                                      
REMARK 465     GLN B   482                                                      
REMARK 465     SER C   758                                                      
REMARK 465     LEU C   759                                                      
REMARK 465     VAL C   760                                                      
REMARK 465     VAL C   761                                                      
REMARK 465     ALA C   762                                                      
REMARK 465     ALA C   763                                                      
REMARK 465     GLU C   764                                                      
REMARK 465     GLU C   765                                                      
REMARK 465     GLY C   766                                                      
REMARK 465     GLU C   767                                                      
REMARK 465     ARG C   768                                                      
REMARK 465     GLU C   769                                                      
REMARK 465     GLN C   770                                                      
REMARK 465     ASN C   771                                                      
REMARK 465     SER C   772                                                      
REMARK 465     LEU C   773                                                      
REMARK 465     ASP C   774                                                      
REMARK 465     SER C   775                                                      
REMARK 465     TRP C   776                                                      
REMARK 465     ASP C   838                                                      
REMARK 465     TRP C   839                                                      
REMARK 465     GLY C   840                                                      
REMARK 465     LEU C   841                                                      
REMARK 465     PRO C   842                                                      
REMARK 465     ILE C   843                                                      
REMARK 465     PRO C   844                                                      
REMARK 465     SER C   845                                                      
REMARK 465     PRO C   846                                                      
REMARK 465     SER C   847                                                      
REMARK 465     PRO C   848                                                      
REMARK 465     ILE C   849                                                      
REMARK 465     HIS C   850                                                      
REMARK 465     PRO C   851                                                      
REMARK 465     ALA C   852                                                      
REMARK 465     HIS C   853                                                      
REMARK 465     HIS C   854                                                      
REMARK 465     LYS C   855                                                      
REMARK 465     ARG C   856                                                      
REMARK 465     ASP C   857                                                      
REMARK 465     ARG C   858                                                      
REMARK 465     ARG C   859                                                      
REMARK 465     GLN C   860                                                      
REMARK 465     ILE C   861                                                      
REMARK 465     PHE C   862                                                      
REMARK 465     LEU C   863                                                      
REMARK 465     PRO C   864                                                      
REMARK 465     GLU C   865                                                      
REMARK 465     PRO C   866                                                      
REMARK 465     GLU C   867                                                      
REMARK 465     GLN C   868                                                      
REMARK 465     PRO C   869                                                      
REMARK 465     SER C   870                                                      
REMARK 465     ARG C   871                                                      
REMARK 465     LEU C   872                                                      
REMARK 465     GLN C   873                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     SER D    77                                                      
REMARK 465     SER D    78                                                      
REMARK 465     ASP D   477                                                      
REMARK 465     TYR D   478                                                      
REMARK 465     ARG D   479                                                      
REMARK 465     PRO D   480                                                      
REMARK 465     SER D   481                                                      
REMARK 465     GLN D   482                                                      
REMARK 465     GLU D   613                                                      
REMARK 465     CYS D   614                                                      
REMARK 465     VAL D   615                                                      
REMARK 465     GLU D   616                                                      
REMARK 465     CYS D   617                                                      
REMARK 465     LYS D   618                                                      
REMARK 465     LYS D   619                                                      
REMARK 465     PHE D   620                                                      
REMARK 465     ASP D   621                                                      
REMARK 465     ARG D   622                                                      
REMARK 465     GLY D   623                                                      
REMARK 465     ALA D   624                                                      
REMARK 465     LEU D   625                                                      
REMARK 465     HIS D   626                                                      
REMARK 465     ASP D   627                                                      
REMARK 465     GLU D   628                                                      
REMARK 465     ASN D   629                                                      
REMARK 465     THR D   630                                                      
REMARK 465     CYS D   631                                                      
REMARK 465     ASN D   632                                                      
REMARK 465     ARG D   633                                                      
REMARK 465     TYR D   634                                                      
REMARK 465     CYS D   635                                                      
REMARK 465     ARG D   636                                                      
REMARK 465     ASP D   637                                                      
REMARK 465     GLU D   638                                                      
REMARK 465     ILE D   639                                                      
REMARK 465     GLU D   640                                                      
REMARK 465     SER D   641                                                      
REMARK 465     VAL D   642                                                      
REMARK 465     LYS D   643                                                      
REMARK 465     GLU D   644                                                      
REMARK 465     LEU D   645                                                      
REMARK 465     LYS D   646                                                      
REMARK 465     ASP D   647                                                      
REMARK 465     THR D   648                                                      
REMARK 465     GLY D   649                                                      
REMARK 465     LYS D   650                                                      
REMARK 465     ASP D   651                                                      
REMARK 465     ALA D   652                                                      
REMARK 465     VAL D   653                                                      
REMARK 465     ASN D   654                                                      
REMARK 465     CYS D   655                                                      
REMARK 465     THR D   656                                                      
REMARK 465     TYR D   657                                                      
REMARK 465     LYS D   658                                                      
REMARK 465     ASN D   659                                                      
REMARK 465     GLU D   660                                                      
REMARK 465     ASP D   661                                                      
REMARK 465     ASP D   662                                                      
REMARK 465     CYS D   663                                                      
REMARK 465     VAL D   664                                                      
REMARK 465     VAL D   665                                                      
REMARK 465     ARG D   666                                                      
REMARK 465     PHE D   667                                                      
REMARK 465     GLN D   668                                                      
REMARK 465     TYR D   669                                                      
REMARK 465     TYR D   670                                                      
REMARK 465     GLU D   671                                                      
REMARK 465     ASP D   672                                                      
REMARK 465     SER D   673                                                      
REMARK 465     SER D   674                                                      
REMARK 465     GLY D   675                                                      
REMARK 465     LYS D   676                                                      
REMARK 465     SER D   677                                                      
REMARK 465     ILE D   678                                                      
REMARK 465     LEU D   679                                                      
REMARK 465     TYR D   680                                                      
REMARK 465     VAL D   681                                                      
REMARK 465     VAL D   682                                                      
REMARK 465     GLU D   683                                                      
REMARK 465     GLU D   684                                                      
REMARK 465     PRO D   685                                                      
REMARK 465     GLU D   686                                                      
REMARK 465     CYS D   687                                                      
REMARK 465     CYS D   688                                                      
REMARK 465     LYS D   689                                                      
REMARK 465     GLY D   690                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 667    C    O    CB   CG   CD   OE1  OE2                   
REMARK 470     GLY A 668    N    CA                                             
REMARK 470     TRP A 839    C    O    CB   CG   CD1  CD2  NE1                   
REMARK 470     TRP A 839    CE2  CE3  CZ2  CZ3  CH2                             
REMARK 470     GLU C 667    C    O    CB   CG   CD   OE1  OE2                   
REMARK 470     GLY C 668    N                                                   
REMARK 470     PHE C 669    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLY C 777    N                                                   
REMARK 470     VAL C 837    CA   C    O    CB   CG1  CG2                        
REMARK 470     ASP C 874    N    CB   CG   OD1  OD2                             
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    LEU D   573     O    HOH D   693              2.05            
REMARK 500   O    ARG C   516     O    HOH C  1134              2.08            
REMARK 500   O    HOH A  1021     O    HOH A  1022              2.12            
REMARK 500   O    HOH C  1029     O    HOH C  1226              2.13            
REMARK 500   O    HOH C  1008     O    HOH C  1094              2.17            
REMARK 500   O    HOH C   984     O    HOH D   720              2.17            
REMARK 500   O    ASP A   881     O    HOH A  1183              2.18            
REMARK 500   O    HOH C   983     O    HOH C  1108              2.19            
REMARK 500   O    HOH A  1003     O    HOH B   695              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     -122.91     50.95                                   
REMARK 500    LYS A 118     -116.09     51.00                                   
REMARK 500    GLU A 123      132.90     73.05                                   
REMARK 500    SER A 144       81.68   -152.74                                   
REMARK 500    SER A 217      -65.70      8.76                                   
REMARK 500    ARG A 320      104.35   -162.42                                   
REMARK 500    VAL A 325      -35.34   -139.16                                   
REMARK 500    GLN A 477      -52.77     71.99                                   
REMARK 500    MET A 580     -164.75     65.28                                   
REMARK 500    ALA A 581       80.85     99.64                                   
REMARK 500    ASP A 628       58.52   -107.95                                   
REMARK 500    MET A 660      -62.50   -106.75                                   
REMARK 500    ASN A 665       57.95   -105.41                                   
REMARK 500    ASN A 833       72.49     49.74                                   
REMARK 500    LYS A 836     -107.33    -74.92                                   
REMARK 500    VAL A 837      151.66     70.18                                   
REMARK 500    ARG A 917       67.49     72.02                                   
REMARK 500    ALA A 938      -71.30    -66.29                                   
REMARK 500    PRO A 940       70.14   -114.38                                   
REMARK 500    LEU A 942      -90.86   -130.49                                   
REMARK 500    THR B   7       49.21    -93.06                                   
REMARK 500    ARG B   8      -95.81   -152.78                                   
REMARK 500    VAL B 157      -78.39   -128.31                                   
REMARK 500    CYS B 177       49.45    -97.93                                   
REMARK 500    VAL B 193      -59.30   -125.20                                   
REMARK 500    GLN B 199       94.66    -69.99                                   
REMARK 500    ASP B 241       77.67   -100.79                                   
REMARK 500    LEU B 258       -9.16     88.93                                   
REMARK 500    CYS B 374     -133.54    -98.35                                   
REMARK 500    ASN B 376     -151.45     58.79                                   
REMARK 500    GLN B 440       39.91    -94.90                                   
REMARK 500    CYS B 448       66.34   -106.32                                   
REMARK 500    GLU B 472      -75.02    -76.98                                   
REMARK 500    GLU B 475      -71.08   -149.51                                   
REMARK 500    GLN B 505      117.79   -169.89                                   
REMARK 500    PHE B 526       23.26   -162.67                                   
REMARK 500    TYR B 531      -61.04   -107.11                                   
REMARK 500    SER B 576     -109.59     45.91                                   
REMARK 500    CYS B 601       86.31   -161.45                                   
REMARK 500    THR B 609      -78.22   -164.46                                   
REMARK 500    GLU B 616      -51.70   -142.92                                   
REMARK 500    THR B 630       38.17   -160.47                                   
REMARK 500    ARG B 636       48.31   -152.27                                   
REMARK 500    GLU B 644       74.18     60.41                                   
REMARK 500    ASP B 647       59.64   -167.64                                   
REMARK 500    LYS B 650      -56.45   -159.57                                   
REMARK 500    ASP B 651       32.91    -99.80                                   
REMARK 500    ALA B 652     -151.18   -177.99                                   
REMARK 500    ASN B 659     -169.39    -77.20                                   
REMARK 500    TYR B 670      -78.97   -169.68                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      93 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1112        DISTANCE =  5.76 ANGSTROMS                       
REMARK 525    HOH C1047        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH C1067        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH C1174        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C1183        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH C1209        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH D 751        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH D 757        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH D 758        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH D 771        DISTANCE =  9.17 ANGSTROMS                       
REMARK 525    HOH D 772        DISTANCE =  8.74 ANGSTROMS                       
REMARK 525    HOH D 773        DISTANCE = 10.24 ANGSTROMS                       
REMARK 525    HOH D 774        DISTANCE =  7.54 ANGSTROMS                       
REMARK 525    HOH D 775        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH D 776        DISTANCE =  7.59 ANGSTROMS                       
REMARK 525    HOH D 780        DISTANCE = 10.55 ANGSTROMS                       
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                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 243   OE1                                                    
REMARK 620 2 ASP A 245   OD1  96.9                                              
REMARK 620 3 ASP A 247   O    84.3  81.0                                        
REMARK 620 4 THR A 250   O    93.1 169.2  95.9                                  
REMARK 620 5 THR A 250   OG1 167.9  88.0  85.5  81.4                            
REMARK 620 6 GLU A 252   OE1  75.7  73.1 144.8 113.6 116.4                      
REMARK 620 7 GLU A 252   OE2 121.8  78.3 148.2  99.9  70.0  47.1                
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 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 299   OD1  73.2                                              
REMARK 620 3 ASP A 301   OD1  73.1  76.6                                        
REMARK 620 4 ARG A 303   O    82.2 155.5  97.5                                  
REMARK 620 5 ASP A 305   OD1 130.2 106.1 156.6  88.8                            
REMARK 620 6 ASP A 305   OD2  85.9  72.5 146.5 105.3  49.6                      
REMARK 620 7 HOH A 960   O   145.2  79.7  79.7 123.2  78.0 106.6                
REMARK 620 N                    1     2     3     4     5     6                 
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 ASP A 365   OD1                                                    
REMARK 620 2 ASP A 367   OD1  95.6                                              
REMARK 620 3 ASP A 369   OD1  87.0  93.8                                        
REMARK 620 4 TYR A 371   O    78.1 172.5  90.1                                  
REMARK 620 5 ASP A 373   OD1 131.3 111.3 128.5  70.8                            
REMARK 620 6 ASP A 373   OD2  99.6  83.1 172.9  93.7  48.0                      
REMARK 620 7 HOH A 961   O   148.3 105.7  68.7  81.7  61.6 106.0                
REMARK 620 N                    1     2     3     4     5     6                 
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 426   OD1                                                    
REMARK 620 2 ASP A 428   OD1  77.5                                              
REMARK 620 3 ASN A 430   OD1  85.8  85.0                                        
REMARK 620 4 TYR A 432   O    83.8 160.4  87.7                                  
REMARK 620 5 ASP A 434   OD1 134.5 117.1 135.5  80.5                            
REMARK 620 6 ASP A 434   OD2  91.3  86.2 171.1 100.3  50.7                      
REMARK 620 7 HOH A 962   O   148.4  73.4  79.7 123.1  71.8  98.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 602   O                                                      
REMARK 620 2 ASP A 605   OD1  78.1                                              
REMARK 620 3 VAL A 607   O    94.5 102.3                                        
REMARK 620 4 GLU A 642   OE1  94.8 172.9  77.1                                  
REMARK 620 5 GLU A 642   OE2  67.3 128.9 116.3  47.2                            
REMARK 620 6 HOH A1045   O    88.3  64.3 165.5 116.9  77.9                      
REMARK 620 7 HOH A1044   O   169.1  95.0  78.6  91.8 123.2  96.3                
REMARK 620 N                    1     2     3     4     5     6                 
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 SER B 121   OG                                                     
REMARK 620 2 GLU B 220   OE2 110.7                                              
REMARK 620 3 HOH B 692   O    91.1 139.7                                        
REMARK 620 4 HOH B 756   O   116.3  93.5 106.9                                  
REMARK 620 5 HOH B 757   O    87.5  72.3  75.4 155.8                            
REMARK 620 6 HOH B 761   O   160.9  68.8  79.7  82.5  74.1                      
REMARK 620 N                    1     2     3     4     5                       
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 SER B 123   O                                                      
REMARK 620 2 ASP B 126   OD1  73.4                                              
REMARK 620 3 ASP B 127   OD1 101.1  64.4                                        
REMARK 620 4 MET B 335   O   173.4 110.1  76.1                                  
REMARK 620 5 HOH B 694   O    96.5 163.9 130.9  81.2                            
REMARK 620 6 HOH B 693   O   114.0 139.4  75.1  59.6  56.0                      
REMARK 620 N                    1     2     3     4     5                       
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 158   OD2                                                    
REMARK 620 2 ASN B 215   OD1 118.3                                              
REMARK 620 3 ASP B 217   O   155.7  85.4                                        
REMARK 620 4 ASP B 217   OD1  98.9 116.9  72.4                                  
REMARK 620 5 PRO B 219   O    78.3 135.4  80.7  98.9                            
REMARK 620 6 GLU B 220   OE1  84.3  70.2 100.4 168.7  71.0                      
REMARK 620 N                    1     2     3     4     5                       
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 GLU C 243   OE1                                                    
REMARK 620 2 GLU C 243   OE2  46.1                                              
REMARK 620 3 ASP C 245   OD1 105.1  59.3                                        
REMARK 620 4 ASP C 247   O    78.5  71.2  84.7                                  
REMARK 620 5 THR C 250   O    84.2 129.1 168.9  91.5                            
REMARK 620 6 THR C 250   OG1 155.9 137.5  86.7  81.8  82.5                      
REMARK 620 7 GLU C 252   OE1  79.7  70.8  70.9 141.5 117.3 124.4                
REMARK 620 8 GLU C 252   OE2 122.8 119.8  86.1 158.5  93.9  78.3  50.9          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 297   OD1                                                    
REMARK 620 2 ASN C 299   OD1  82.5                                              
REMARK 620 3 ASP C 301   OD1  80.4  76.1                                        
REMARK 620 4 ARG C 303   O    89.1 171.3 104.5                                  
REMARK 620 5 ASP C 305   OD1 128.5 103.2 151.0  80.5                            
REMARK 620 6 ASP C 305   OD2  85.2  77.2 151.1 100.1  48.3                      
REMARK 620 7 HOH C 961   O   152.6  78.7  75.8 109.9  75.7 109.6                
REMARK 620 N                    1     2     3     4     5     6                 
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 ASP C 365   OD1                                                    
REMARK 620 2 ASP C 367   OD1  81.7                                              
REMARK 620 3 ASP C 369   OD1  79.6  83.1                                        
REMARK 620 4 TYR C 371   O    83.1 164.5  91.3                                  
REMARK 620 5 ASP C 373   OD1 139.2 115.1 136.6  78.8                            
REMARK 620 6 ASP C 373   OD2 100.0  83.8 166.9 101.8  49.7                      
REMARK 620 7 HOH C1012   O   151.1  99.2  71.9  92.7  66.6 108.8                
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 ASP C 426   OD1                                                    
REMARK 620 2 ASP C 428   OD1  76.9                                              
REMARK 620 3 ASN C 430   OD1  86.7  80.4                                        
REMARK 620 4 TYR C 432   O    79.8 155.1  89.8                                  
REMARK 620 5 ASP C 434   OD1 128.8 122.3 139.3  79.6                            
REMARK 620 6 ASP C 434   OD2  84.3  94.0 170.3  92.2  50.3                      
REMARK 620 7 HOH C 962   O   148.9  72.2  85.1 130.0  72.9 100.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2008  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 602   O                                                      
REMARK 620 2 ASP C 605   OD1  76.0                                              
REMARK 620 3 VAL C 607   O    92.7  94.6                                        
REMARK 620 4 GLU C 642   OE1  96.9 165.4  72.7                                  
REMARK 620 5 GLU C 642   OE2  71.1 135.7 115.5  49.7                            
REMARK 620 6 HOH C1056   O    85.8  60.8 154.9 132.3  87.7                      
REMARK 620 7 HOH C1007   O   173.6 104.6  80.9  81.0 111.4 100.1                
REMARK 620 N                    1     2     3     4     5     6                 
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 SER D 121   OG                                                     
REMARK 620 2 GLU D 220   OE2  91.0                                              
REMARK 620 3 HOH D 787   O    76.7 119.2                                        
REMARK 620 4 HOH D 782   O   157.1  99.3 114.7                                  
REMARK 620 5 HOH D 781   O    80.3 157.9  78.7  82.6                            
REMARK 620 6 HOH D 692   O    71.7  84.8 140.5  88.8  73.2                      
REMARK 620 N                    1     2     3     4     5                       
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 SER D 123   O                                                      
REMARK 620 2 ASP D 126   OD1  90.2                                              
REMARK 620 3 ASP D 127   OD1  98.8  69.1                                        
REMARK 620 4 MET D 335   O   146.9 118.4  78.3                                  
REMARK 620 5 HOH D 694   O    80.0 160.0  94.9  67.5                            
REMARK 620 N                    1     2     3     4                             
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 158   OD2                                                    
REMARK 620 2 ASN D 215   OD1 109.9                                              
REMARK 620 3 ASP D 217   O   167.1  82.6                                        
REMARK 620 4 ASP D 217   OD1 105.4  97.3  68.8                                  
REMARK 620 5 PRO D 219   O    81.4 157.1  88.0  98.6                            
REMARK 620 6 GLU D 220   OE1  87.2  81.1  98.2 167.0  79.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2005                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2006                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2007                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A2008                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A3570                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3559                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3560                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3561                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3562                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3563                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2005                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2006                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2007                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2008                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3570                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 960                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C5003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C5004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3452                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3453                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3559                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3560                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FCU   RELATED DB: PDB                                   
DBREF  3FCS A    1   958  UNP    Q17R67   Q17R67_HUMAN    32    989             
DBREF  3FCS B    1   690  UNP    P05106   ITB3_HUMAN      27    716             
DBREF  3FCS C    1   958  UNP    Q17R67   Q17R67_HUMAN    32    989             
DBREF  3FCS D    1   690  UNP    P05106   ITB3_HUMAN      27    716             
SEQADV 3FCS CYS A  959  UNP  Q17R67              EXPRESSION TAG                 
SEQADV 3FCS CYS B  688  UNP  P05106    PRO   714 ENGINEERED                     
SEQADV 3FCS CYS C  959  UNP  Q17R67              EXPRESSION TAG                 
SEQADV 3FCS CYS D  688  UNP  P05106    PRO   714 ENGINEERED                     
SEQRES   1 A  959  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  959  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  959  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  959  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  959  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  959  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  959  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  959  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  959  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  959  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  959  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  959  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  959  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  959  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  959  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  959  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  959  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  959  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  959  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  959  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  959  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  959  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  959  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  959  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  959  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  959  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  959  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  959  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  959  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  959  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  959  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  959  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  959  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  959  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  959  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  959  ALA SER VAL GLN LEU LEU VAL GLN ASP SER LEU ASN PRO          
SEQRES  37 A  959  ALA VAL LYS SER CYS VAL LEU PRO GLN THR LYS THR PRO          
SEQRES  38 A  959  VAL SER CYS PHE ASN ILE GLN MET CYS VAL GLY ALA THR          
SEQRES  39 A  959  GLY HIS ASN ILE PRO GLN LYS LEU SER LEU ASN ALA GLU          
SEQRES  40 A  959  LEU GLN LEU ASP ARG GLN LYS PRO ARG GLN GLY ARG ARG          
SEQRES  41 A  959  VAL LEU LEU LEU GLY SER GLN GLN ALA GLY THR THR LEU          
SEQRES  42 A  959  ASN LEU ASP LEU GLY GLY LYS HIS SER PRO ILE CYS HIS          
SEQRES  43 A  959  THR THR MET ALA PHE LEU ARG ASP GLU ALA ASP PHE ARG          
SEQRES  44 A  959  ASP LYS LEU SER PRO ILE VAL LEU SER LEU ASN VAL SER          
SEQRES  45 A  959  LEU PRO PRO THR GLU ALA GLY MET ALA PRO ALA VAL VAL          
SEQRES  46 A  959  LEU HIS GLY ASP THR HIS VAL GLN GLU GLN THR ARG ILE          
SEQRES  47 A  959  VAL LEU ASP CYS GLY GLU ASP ASP VAL CYS VAL PRO GLN          
SEQRES  48 A  959  LEU GLN LEU THR ALA SER VAL THR GLY SER PRO LEU LEU          
SEQRES  49 A  959  VAL GLY ALA ASP ASN VAL LEU GLU LEU GLN MET ASP ALA          
SEQRES  50 A  959  ALA ASN GLU GLY GLU GLY ALA TYR GLU ALA GLU LEU ALA          
SEQRES  51 A  959  VAL HIS LEU PRO GLN GLY ALA HIS TYR MET ARG ALA LEU          
SEQRES  52 A  959  SER ASN VAL GLU GLY PHE GLU ARG LEU ILE CYS ASN GLN          
SEQRES  53 A  959  LYS LYS GLU ASN GLU THR ARG VAL VAL LEU CYS GLU LEU          
SEQRES  54 A  959  GLY ASN PRO MET LYS LYS ASN ALA GLN ILE GLY ILE ALA          
SEQRES  55 A  959  MET LEU VAL SER VAL GLY ASN LEU GLU GLU ALA GLY GLU          
SEQRES  56 A  959  SER VAL SER PHE GLN LEU GLN ILE ARG SER LYS ASN SER          
SEQRES  57 A  959  GLN ASN PRO ASN SER LYS ILE VAL LEU LEU ASP VAL PRO          
SEQRES  58 A  959  VAL ARG ALA GLU ALA GLN VAL GLU LEU ARG GLY ASN SER          
SEQRES  59 A  959  PHE PRO ALA SER LEU VAL VAL ALA ALA GLU GLU GLY GLU          
SEQRES  60 A  959  ARG GLU GLN ASN SER LEU ASP SER TRP GLY PRO LYS VAL          
SEQRES  61 A  959  GLU HIS THR TYR GLU LEU HIS ASN ASN GLY PRO GLY THR          
SEQRES  62 A  959  VAL ASN GLY LEU HIS LEU SER ILE HIS LEU PRO GLY GLN          
SEQRES  63 A  959  SER GLN PRO SER ASP LEU LEU TYR ILE LEU ASP ILE GLN          
SEQRES  64 A  959  PRO GLN GLY GLY LEU GLN CYS PHE PRO GLN PRO PRO VAL          
SEQRES  65 A  959  ASN PRO LEU LYS VAL ASP TRP GLY LEU PRO ILE PRO SER          
SEQRES  66 A  959  PRO SER PRO ILE HIS PRO ALA HIS HIS LYS ARG ASP ARG          
SEQRES  67 A  959  ARG GLN ILE PHE LEU PRO GLU PRO GLU GLN PRO SER ARG          
SEQRES  68 A  959  LEU GLN ASP PRO VAL LEU VAL SER CYS ASP SER ALA PRO          
SEQRES  69 A  959  CYS THR VAL VAL GLN CYS ASP LEU GLN GLU MET ALA ARG          
SEQRES  70 A  959  GLY GLN ARG ALA MET VAL THR VAL LEU ALA PHE LEU TRP          
SEQRES  71 A  959  LEU PRO SER LEU TYR GLN ARG PRO LEU ASP GLN PHE VAL          
SEQRES  72 A  959  LEU GLN SER HIS ALA TRP PHE ASN VAL SER SER LEU PRO          
SEQRES  73 A  959  TYR ALA VAL PRO PRO LEU SER LEU PRO ARG GLY GLU ALA          
SEQRES  74 A  959  GLN VAL TRP THR GLN LEU LEU ARG ALA CYS                      
SEQRES   1 B  690  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  690  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  690  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  690  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  690  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  690  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  690  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  690  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  690  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  690  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  690  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  690  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  690  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  690  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  690  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  690  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  690  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  690  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  690  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  690  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  690  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  690  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  690  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  690  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  690  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  690  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  690  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  690  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  690  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  690  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  690  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  690  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  690  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  690  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  690  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  690  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  690  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 B  690  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 B  690  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 B  690  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 B  690  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 B  690  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 B  690  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 B  690  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 B  690  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 B  690  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 B  690  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 B  690  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 B  690  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 B  690  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 B  690  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 B  690  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 B  690  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS CYS LYS          
SEQRES  54 B  690  GLY                                                          
SEQRES   1 C  959  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  959  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  959  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  959  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  959  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  959  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  959  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  959  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  959  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  959  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  959  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  959  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  959  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  959  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  959  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  959  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  959  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  959  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  959  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  959  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  959  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  959  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  959  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  959  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  959  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  959  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  959  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  959  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  959  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  959  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  959  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  959  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  959  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  959  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  959  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  959  ALA SER VAL GLN LEU LEU VAL GLN ASP SER LEU ASN PRO          
SEQRES  37 C  959  ALA VAL LYS SER CYS VAL LEU PRO GLN THR LYS THR PRO          
SEQRES  38 C  959  VAL SER CYS PHE ASN ILE GLN MET CYS VAL GLY ALA THR          
SEQRES  39 C  959  GLY HIS ASN ILE PRO GLN LYS LEU SER LEU ASN ALA GLU          
SEQRES  40 C  959  LEU GLN LEU ASP ARG GLN LYS PRO ARG GLN GLY ARG ARG          
SEQRES  41 C  959  VAL LEU LEU LEU GLY SER GLN GLN ALA GLY THR THR LEU          
SEQRES  42 C  959  ASN LEU ASP LEU GLY GLY LYS HIS SER PRO ILE CYS HIS          
SEQRES  43 C  959  THR THR MET ALA PHE LEU ARG ASP GLU ALA ASP PHE ARG          
SEQRES  44 C  959  ASP LYS LEU SER PRO ILE VAL LEU SER LEU ASN VAL SER          
SEQRES  45 C  959  LEU PRO PRO THR GLU ALA GLY MET ALA PRO ALA VAL VAL          
SEQRES  46 C  959  LEU HIS GLY ASP THR HIS VAL GLN GLU GLN THR ARG ILE          
SEQRES  47 C  959  VAL LEU ASP CYS GLY GLU ASP ASP VAL CYS VAL PRO GLN          
SEQRES  48 C  959  LEU GLN LEU THR ALA SER VAL THR GLY SER PRO LEU LEU          
SEQRES  49 C  959  VAL GLY ALA ASP ASN VAL LEU GLU LEU GLN MET ASP ALA          
SEQRES  50 C  959  ALA ASN GLU GLY GLU GLY ALA TYR GLU ALA GLU LEU ALA          
SEQRES  51 C  959  VAL HIS LEU PRO GLN GLY ALA HIS TYR MET ARG ALA LEU          
SEQRES  52 C  959  SER ASN VAL GLU GLY PHE GLU ARG LEU ILE CYS ASN GLN          
SEQRES  53 C  959  LYS LYS GLU ASN GLU THR ARG VAL VAL LEU CYS GLU LEU          
SEQRES  54 C  959  GLY ASN PRO MET LYS LYS ASN ALA GLN ILE GLY ILE ALA          
SEQRES  55 C  959  MET LEU VAL SER VAL GLY ASN LEU GLU GLU ALA GLY GLU          
SEQRES  56 C  959  SER VAL SER PHE GLN LEU GLN ILE ARG SER LYS ASN SER          
SEQRES  57 C  959  GLN ASN PRO ASN SER LYS ILE VAL LEU LEU ASP VAL PRO          
SEQRES  58 C  959  VAL ARG ALA GLU ALA GLN VAL GLU LEU ARG GLY ASN SER          
SEQRES  59 C  959  PHE PRO ALA SER LEU VAL VAL ALA ALA GLU GLU GLY GLU          
SEQRES  60 C  959  ARG GLU GLN ASN SER LEU ASP SER TRP GLY PRO LYS VAL          
SEQRES  61 C  959  GLU HIS THR TYR GLU LEU HIS ASN ASN GLY PRO GLY THR          
SEQRES  62 C  959  VAL ASN GLY LEU HIS LEU SER ILE HIS LEU PRO GLY GLN          
SEQRES  63 C  959  SER GLN PRO SER ASP LEU LEU TYR ILE LEU ASP ILE GLN          
SEQRES  64 C  959  PRO GLN GLY GLY LEU GLN CYS PHE PRO GLN PRO PRO VAL          
SEQRES  65 C  959  ASN PRO LEU LYS VAL ASP TRP GLY LEU PRO ILE PRO SER          
SEQRES  66 C  959  PRO SER PRO ILE HIS PRO ALA HIS HIS LYS ARG ASP ARG          
SEQRES  67 C  959  ARG GLN ILE PHE LEU PRO GLU PRO GLU GLN PRO SER ARG          
SEQRES  68 C  959  LEU GLN ASP PRO VAL LEU VAL SER CYS ASP SER ALA PRO          
SEQRES  69 C  959  CYS THR VAL VAL GLN CYS ASP LEU GLN GLU MET ALA ARG          
SEQRES  70 C  959  GLY GLN ARG ALA MET VAL THR VAL LEU ALA PHE LEU TRP          
SEQRES  71 C  959  LEU PRO SER LEU TYR GLN ARG PRO LEU ASP GLN PHE VAL          
SEQRES  72 C  959  LEU GLN SER HIS ALA TRP PHE ASN VAL SER SER LEU PRO          
SEQRES  73 C  959  TYR ALA VAL PRO PRO LEU SER LEU PRO ARG GLY GLU ALA          
SEQRES  74 C  959  GLN VAL TRP THR GLN LEU LEU ARG ALA CYS                      
SEQRES   1 D  690  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  690  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  690  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  690  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  690  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  690  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  690  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  690  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  690  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  690  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  690  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  690  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  690  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  690  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  690  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  690  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  690  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  690  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  690  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  690  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  690  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  690  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  690  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  690  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  690  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  690  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  690  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  690  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  690  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  690  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  690  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  690  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  690  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  690  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  690  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  690  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  690  SER GLN CYS GLU CYS SER GLU GLU ASP TYR ARG PRO SER          
SEQRES  38 D  690  GLN GLN ASP GLU CYS SER PRO ARG GLU GLY GLN PRO VAL          
SEQRES  39 D  690  CYS SER GLN ARG GLY GLU CYS LEU CYS GLY GLN CYS VAL          
SEQRES  40 D  690  CYS HIS SER SER ASP PHE GLY LYS ILE THR GLY LYS TYR          
SEQRES  41 D  690  CYS GLU CYS ASP ASP PHE SER CYS VAL ARG TYR LYS GLY          
SEQRES  42 D  690  GLU MET CYS SER GLY HIS GLY GLN CYS SER CYS GLY ASP          
SEQRES  43 D  690  CYS LEU CYS ASP SER ASP TRP THR GLY TYR TYR CYS ASN          
SEQRES  44 D  690  CYS THR THR ARG THR ASP THR CYS MET SER SER ASN GLY          
SEQRES  45 D  690  LEU LEU CYS SER GLY ARG GLY LYS CYS GLU CYS GLY SER          
SEQRES  46 D  690  CYS VAL CYS ILE GLN PRO GLY SER TYR GLY ASP THR CYS          
SEQRES  47 D  690  GLU LYS CYS PRO THR CYS PRO ASP ALA CYS THR PHE LYS          
SEQRES  48 D  690  LYS GLU CYS VAL GLU CYS LYS LYS PHE ASP ARG GLY ALA          
SEQRES  49 D  690  LEU HIS ASP GLU ASN THR CYS ASN ARG TYR CYS ARG ASP          
SEQRES  50 D  690  GLU ILE GLU SER VAL LYS GLU LEU LYS ASP THR GLY LYS          
SEQRES  51 D  690  ASP ALA VAL ASN CYS THR TYR LYS ASN GLU ASP ASP CYS          
SEQRES  52 D  690  VAL VAL ARG PHE GLN TYR TYR GLU ASP SER SER GLY LYS          
SEQRES  53 D  690  SER ILE LEU TYR VAL VAL GLU GLU PRO GLU CYS CYS LYS          
SEQRES  54 D  690  GLY                                                          
MODRES 3FCS ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN A  570  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN B  452  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN B  559  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN C   15  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN C  249  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN C  570  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN D  452  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCS ASN D  559  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     CA  A2008       1                                                       
HET    NAG  A3015      14                                                       
HET    NAG  A3570      14                                                       
HET    IMD  A5001       5                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3100      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    MAN  B3373      11                                                       
HET    NAG  B3452      14                                                       
HET    NAG  B3453      14                                                       
HET    NAG  B3559      14                                                       
HET    NAG  B3560      14                                                       
HET    MAN  B3561      11                                                       
HET    MAN  B3562      11                                                       
HET    MAN  B3563      11                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET     CA  C2008       1                                                       
HET    NAG  C3015      14                                                       
HET    NAG  C3249      14                                                       
HET    NAG  C3250      14                                                       
HET    NAG  C3570      14                                                       
HET    IMD  C5001       5                                                       
HET    IMD  C 960       5                                                       
HET    IMD  C5002       5                                                       
HET    IMD  C5003       5                                                       
HET    IMD  C5004       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    NAG  D3371      14                                                       
HET    NAG  D3372      14                                                       
HET    NAG  D3452      14                                                       
HET    NAG  D3453      14                                                       
HET    NAG  D3559      14                                                       
HET    NAG  D3560      14                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     IMD IMIDAZOLE                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   5   CA    14(CA 2+)                                                    
FORMUL  10  NAG    25(C8 H15 N O6)                                              
FORMUL  12  IMD    6(C3 H5 N2 1+)                                               
FORMUL  13   MG    2(MG 2+)                                                     
FORMUL  17  MAN    6(C6 H12 O6)                                                 
FORMUL  42  HOH   *678(H2 O)                                                    
HELIX    1   1 SER A  152  GLU A  157  1                                   6    
HELIX    2   2 GLY A  188  PHE A  191  1                                   4    
HELIX    3   3 VAL A  200  SER A  206  1                                   7    
HELIX    4   4 PRO A  228  TYR A  230  1                                   3    
HELIX    5   5 TRP A  260  THR A  263  1                                   4    
HELIX    6   6 TYR A  440  ALA A  442  1                                   3    
HELIX    7   7 ARG A  516  GLY A  518  1                                   3    
HELIX    8   8 GLU A  555  ASP A  557  1                                   3    
HELIX    9   9 LEU A  911  LEU A  914  1                                   4    
HELIX   10  10 CYS B   13  VAL B   19  1                                   7    
HELIX   11  11 LYS B   41  LYS B   46  1                                   6    
HELIX   12  12 PRO B   51  SER B   53  1                                   3    
HELIX   13  13 TYR B  122  SER B  130  1                                   9    
HELIX   14  14 THR B  136  LEU B  145  1                                  10    
HELIX   15  15 VAL B  200  VAL B  207  1                                   8    
HELIX   16  16 GLY B  222  VAL B  231  1                                  10    
HELIX   17  17 ASP B  233  ILE B  236  1                                   4    
HELIX   18  18 ASP B  259  ALA B  263  1                                   5    
HELIX   19  19 SER B  282  THR B  285  1                                   4    
HELIX   20  20 LEU B  292  GLN B  301  1                                  10    
HELIX   21  21 GLU B  312  LEU B  324  1                                  13    
HELIX   22  22 VAL B  340  ILE B  351  1                                  12    
HELIX   23  23 ALA B  436  GLN B  438  1                                   3    
HELIX   24  24 VAL B  494  GLN B  497  1                                   4    
HELIX   25  25 CYS B  536  GLY B  538  1                                   3    
HELIX   26  26 GLU B  613  VAL B  615  1                                   3    
HELIX   27  27 SER C  152  GLU C  157  1                                   6    
HELIX   28  28 GLY C  188  PHE C  191  1                                   4    
HELIX   29  29 VAL C  200  SER C  206  1                                   7    
HELIX   30  30 PRO C  228  TYR C  230  1                                   3    
HELIX   31  31 TRP C  260  THR C  263  1                                   4    
HELIX   32  32 TYR C  440  ALA C  442  1                                   3    
HELIX   33  33 ARG C  516  GLY C  518  1                                   3    
HELIX   34  34 GLU C  555  ASP C  557  1                                   3    
HELIX   35  35 LEU C  911  LEU C  914  1                                   4    
HELIX   36  36 CYS D   13  VAL D   19  1                                   7    
HELIX   37  37 LYS D   41  LYS D   46  1                                   6    
HELIX   38  38 PRO D   51  SER D   53  1                                   3    
HELIX   39  39 TYR D  122  TRP D  129  1                                   8    
HELIX   40  40 THR D  136  MET D  142  1                                   7    
HELIX   41  41 PRO D  170  GLU D  174  1                                   5    
HELIX   42  42 THR D  201  LYS D  209  1                                   9    
HELIX   43  43 GLY D  222  VAL D  231  1                                  10    
HELIX   44  44 ASP D  233  ILE D  236  1                                   4    
HELIX   45  45 ASP D  259  ALA D  263  1                                   5    
HELIX   46  46 SER D  282  THR D  285  1                                   4    
HELIX   47  47 LEU D  292  GLN D  301  1                                  10    
HELIX   48  48 GLU D  312  LEU D  324  1                                  13    
HELIX   49  49 VAL D  340  ILE D  351  1                                  12    
HELIX   50  50 ALA D  436  GLN D  440  1                                   5    
HELIX   51  51 VAL D  494  GLN D  497  1                                   4    
HELIX   52  52 CYS D  536  GLY D  538  1                                   3    
HELIX   53  53 ALA D  607  PHE D  610  1                                   4    
SHEET    1   1 1 THR A   9  ALA A  12  0                                        
SHEET    1   2 1 SER A  22  LYS A  27  0                                        
SHEET    1   3 1 VAL A  33  ALA A  39  0                                        
SHEET    1   4 1 GLY A  52  PRO A  57  0                                        
SHEET    1   5 1 GLY A  62  GLN A  64  0                                        
SHEET    1   6 1 THR A  76  VAL A  79  0                                        
SHEET    1   7 1 GLN A  82  PHE A  87  0                                        
SHEET    1   8 1 SER A  96  TRP A 100  0                                        
SHEET    1   9 1 VAL A 103  ALA A 108  0                                        
SHEET    1  10 1 HIS A 112  GLU A 117  0                                        
SHEET    1  11 1 GLU A 120  GLU A 121  0                                        
SHEET    1  12 1 SER A 129  GLN A 134  0                                        
SHEET    1  13 1 ARG A 139  TYR A 143  0                                        
SHEET    1  14 1 SER A 172  VAL A 175  0                                        
SHEET    1  15 1 GLU A 180  ALA A 185  0                                        
SHEET    1  16 1 LEU A 194  PRO A 199  0                                        
SHEET    1  17 1 SER A 220  LEU A 221  0                                        
SHEET    1  18 1 SER A 238  GLY A 242  0                                        
SHEET    1  19 1 GLU A 252  ALA A 257  0                                        
SHEET    1  20 1 ALA A 266  LEU A 270  0                                        
SHEET    1  21 1 ARG A 276  ARG A 281  0                                        
SHEET    1  22 1 SER A 292  THR A 296  0                                        
SHEET    1  23 1 ASP A 305  ALA A 310  0                                        
SHEET    1  24 1 MET A 314  ARG A 317  0                                        
SHEET    1  25 1 ARG A 320  GLU A 324  0                                        
SHEET    1  26 1 ARG A 327  PHE A 331  0                                        
SHEET    1  27 1 LEU A 345  THR A 348  0                                        
SHEET    1  28 1 ALA A 359  GLY A 364  0                                        
SHEET    1  29 1 ASP A 373  ALA A 378  0                                        
SHEET    1  30 1 GLN A 388  PHE A 392  0                                        
SHEET    1  31 1 GLY A 394  GLN A 395  0                                        
SHEET    1  32 1 GLY A 398  LEU A 399  0                                        
SHEET    1  33 1 GLN A 405  ASP A 408  0                                        
SHEET    1  34 1 LEU A 421  VAL A 425  0                                        
SHEET    1  35 1 ASP A 434  ALA A 439  0                                        
SHEET    1  36 1 GLN A 444  TYR A 448  0                                        
SHEET    1  37 1 VAL A 453  VAL A 462  0                                        
SHEET    1  38 1 CYS A 473  VAL A 474  0                                        
SHEET    1  39 1 PRO A 481  THR A 494  0                                        
SHEET    1  41 1 SER A 503  LEU A 510  0                                        
SHEET    1  42 1 VAL A 521  LEU A 523  0                                        
SHEET    1  43 1 GLY A 530  ASP A 536  0                                        
SHEET    1  44 1 ILE A 544  LEU A 552  0                                        
SHEET    1  45 1 ILE A 565  SER A 572  0                                        
SHEET    1  46 1 VAL A 585  GLY A 588  0                                        
SHEET    1  47 1 HIS A 591  THR A 596  0                                        
SHEET    1  48 1 LEU A 612  THR A 619  0                                        
SHEET    1  49 1 LEU A 623  LEU A 624  0                                        
SHEET    1  50 1 LEU A 631  ASN A 639  0                                        
SHEET    1  51 1 ALA A 647  HIS A 652  0                                        
SHEET    1  52 1 ALA A 657  SER A 664  0                                        
SHEET    1  53 1 CYS A 674  LYS A 677  0                                        
SHEET    1  54 1 VAL A 684  GLY A 690  0                                        
SHEET    1  55 1 ALA A 697  VAL A 707  0                                        
SHEET    1  56 1 SER A 716  ARG A 724  0                                        
SHEET    1  57 1 VAL A 736  ARG A 743  0                                        
SHEET    1  58 1 VAL A 748  PHE A 755  0                                        
SHEET    1  59 1 SER A 758  VAL A 761  0                                        
SHEET    1  60 1 LYS A 779  ASN A 788  0                                        
SHEET    1  61 1 VAL A 794  PRO A 804  0                                        
SHEET    1  62 1 LEU A 813  GLN A 821  0                                        
SHEET    1  63 1 GLN A 825  GLN A 829  0                                        
SHEET    1  64 1 PRO A 875  VAL A 878  0                                        
SHEET    1  65 1 CYS A 885  MET A 895  0                                        
SHEET    1  66 1 ARG A 900  LEU A 909  0                                        
SHEET    1  67 1 GLN A 921  SER A 934  0                                        
SHEET    1  68 1 ARG A 946  ARG A 957  0                                        
SHEET    1  69 1 ALA B  24  CYS B  26  0                                        
SHEET    1  70 1 CYS B  38  ASP B  39  0                                        
SHEET    1  71 1 ILE B  54  GLU B  55  0                                        
SHEET    1  72 1 GLU B  60  GLU B  65  0                                        
SHEET    1  73 1 VAL B  83  SER B  84  0                                        
SHEET    1  74 1 ARG B  87  LEU B  92  0                                        
SHEET    1  75 1 SER B  97  ARG B 105  0                                        
SHEET    1  76 1 VAL B 112  ASP B 119  0                                        
SHEET    1  77 1 LEU B 149  PHE B 156  0                                        
SHEET    1  78 1 TYR B 190  THR B 197  0                                        
SHEET    1  79 1 SER B 243  THR B 250  0                                        
SHEET    1  80 1 ASN B 305  THR B 311  0                                        
SHEET    1  81 1 THR B 329  LEU B 333  0                                        
SHEET    1  82 1 VAL B 355  ARG B 360  0                                        
SHEET    1  83 1 LEU B 366  THR B 373  0                                        
SHEET    1  84 1 VAL B 379  PRO B 381  0                                        
SHEET    1  85 1 SER B 385  CYS B 386  0                                        
SHEET    1  86 1 THR B 394  VAL B 403  0                                        
SHEET    1  87 1 GLU B 411  PRO B 418  0                                        
SHEET    1  88 1 LEU B 425  PHE B 431  0                                        
SHEET    1  89 1 GLY B 453  GLU B 456  0                                        
SHEET    1  90 1 VAL B 459  CYS B 462  0                                        
SHEET    1  91 1 GLY B 499  CYS B 501  0                                        
SHEET    1  92 1 CYS B 506  CYS B 508  0                                        
SHEET    1  93 1 GLY B 540  SER B 543  0                                        
SHEET    1  94 1 ASP B 546  CYS B 549  0                                        
SHEET    1  95 1 TRP B 553  THR B 554  0                                        
SHEET    1  96 1 CYS B 560  THR B 561  0                                        
SHEET    1  97 1 LYS B 580  GLU B 582  0                                        
SHEET    1  98 1 SER B 585  VAL B 587  0                                        
SHEET    1  99 1 GLU B 638  GLU B 640  0                                        
SHEET    1 100 1 ASN B 654  LYS B 658  0                                        
SHEET    1 101 1 CYS B 663  GLN B 668  0                                        
SHEET    1 102 1 ILE B 678  TYR B 680  0                                        
SHEET    1 103 1 GLU B 686  CYS B 687  0                                        
SHEET    1 104 1 THR C   9  ALA C  12  0                                        
SHEET    1 105 1 SER C  22  LYS C  27  0                                        
SHEET    1 106 1 VAL C  33  ALA C  39  0                                        
SHEET    1 107 1 GLY C  52  PRO C  57  0                                        
SHEET    1 108 1 GLY C  63  GLN C  64  0                                        
SHEET    1 109 1 THR C  76  VAL C  79  0                                        
SHEET    1 110 1 GLN C  82  PHE C  87  0                                        
SHEET    1 111 1 SER C  96  TRP C 100  0                                        
SHEET    1 112 1 VAL C 103  ALA C 108  0                                        
SHEET    1 113 1 HIS C 112  GLU C 117  0                                        
SHEET    1 114 1 GLU C 120  GLU C 121  0                                        
SHEET    1 115 1 SER C 129  GLN C 134  0                                        
SHEET    1 116 1 ARG C 139  TYR C 143  0                                        
SHEET    1 117 1 SER C 172  VAL C 175  0                                        
SHEET    1 118 1 GLU C 180  ALA C 185  0                                        
SHEET    1 119 1 LEU C 194  PRO C 199  0                                        
SHEET    1 120 1 SER C 220  LEU C 221  0                                        
SHEET    1 121 1 SER C 238  GLY C 242  0                                        
SHEET    1 122 1 GLU C 252  ALA C 257  0                                        
SHEET    1 123 1 ALA C 266  LEU C 270  0                                        
SHEET    1 124 1 ARG C 276  ARG C 281  0                                        
SHEET    1 125 1 SER C 292  THR C 296  0                                        
SHEET    1 126 1 ASP C 305  ALA C 310  0                                        
SHEET    1 127 1 MET C 314  ARG C 317  0                                        
SHEET    1 128 1 ARG C 320  GLU C 324  0                                        
SHEET    1 129 1 ARG C 327  PHE C 331  0                                        
SHEET    1 130 1 LEU C 345  THR C 348  0                                        
SHEET    1 131 1 ALA C 359  GLY C 364  0                                        
SHEET    1 132 1 ASP C 373  ALA C 378  0                                        
SHEET    1 133 1 GLN C 388  PHE C 392  0                                        
SHEET    1 134 1 GLY C 394  GLN C 395  0                                        
SHEET    1 135 1 GLY C 398  LEU C 399  0                                        
SHEET    1 136 1 GLN C 405  ASP C 408  0                                        
SHEET    1 137 1 SER C 420  VAL C 425  0                                        
SHEET    1 138 1 ASP C 434  ALA C 439  0                                        
SHEET    1 139 1 GLN C 444  TYR C 448  0                                        
SHEET    1 140 1 VAL C 453  VAL C 462  0                                        
SHEET    1 141 1 CYS C 473  VAL C 474  0                                        
SHEET    1 142 1 PRO C 481  THR C 494  0                                        
SHEET    1 143 1 SER C 503  LEU C 510  0                                        
SHEET    1 144 1 VAL C 521  LEU C 523  0                                        
SHEET    1 145 1 GLY C 530  ASP C 536  0                                        
SHEET    1 146 1 ILE C 544  LEU C 552  0                                        
SHEET    1 147 1 ILE C 565  SER C 572  0                                        
SHEET    1 148 1 VAL C 585  GLY C 588  0                                        
SHEET    1 149 1 HIS C 591  THR C 596  0                                        
SHEET    1 150 1 LEU C 612  THR C 619  0                                        
SHEET    1 151 1 LEU C 623  LEU C 624  0                                        
SHEET    1 152 1 ASN C 629  ASN C 639  0                                        
SHEET    1 153 1 ALA C 647  HIS C 652  0                                        
SHEET    1 154 1 ALA C 657  SER C 664  0                                        
SHEET    1 155 1 CYS C 674  LYS C 677  0                                        
SHEET    1 156 1 VAL C 684  GLY C 690  0                                        
SHEET    1 157 1 ALA C 697  VAL C 707  0                                        
SHEET    1 158 1 SER C 716  ARG C 724  0                                        
SHEET    1 159 1 VAL C 736  ARG C 743  0                                        
SHEET    1 160 1 VAL C 748  PHE C 755  0                                        
SHEET    1 161 1 LYS C 779  ASN C 788  0                                        
SHEET    1 162 1 VAL C 794  PRO C 804  0                                        
SHEET    1 163 1 LEU C 813  GLN C 821  0                                        
SHEET    1 164 1 GLN C 825  GLN C 829  0                                        
SHEET    1 165 1 CYS C 885  MET C 895  0                                        
SHEET    1 166 1 ARG C 900  LEU C 909  0                                        
SHEET    1 167 1 PHE C 922  SER C 934  0                                        
SHEET    1 168 1 ARG C 946  LEU C 955  0                                        
SHEET    1 169 1 CYS D  23  CYS D  26  0                                        
SHEET    1 170 1 CYS D  38  LEU D  40  0                                        
SHEET    1 171 1 ILE D  54  GLU D  55  0                                        
SHEET    1 172 1 GLU D  60  GLU D  65  0                                        
SHEET    1 173 1 VAL D  83  SER D  84  0                                        
SHEET    1 174 1 ARG D  87  LEU D  92  0                                        
SHEET    1 175 1 SER D  97  ARG D 105  0                                        
SHEET    1 176 1 VAL D 112  ASP D 119  0                                        
SHEET    1 177 1 LEU D 149  PHE D 156  0                                        
SHEET    1 178 1 TYR D 190  THR D 197  0                                        
SHEET    1 179 1 SER D 243  THR D 250  0                                        
SHEET    1 180 1 ASN D 305  THR D 311  0                                        
SHEET    1 181 1 THR D 328  LEU D 333  0                                        
SHEET    1 182 1 VAL D 355  ARG D 360  0                                        
SHEET    1 183 1 LEU D 366  SER D 367  0                                        
SHEET    1 184 1 PHE D 370  THR D 373  0                                        
SHEET    1 185 1 VAL D 379  PRO D 381  0                                        
SHEET    1 186 1 SER D 385  CYS D 386  0                                        
SHEET    1 187 1 THR D 394  VAL D 403  0                                        
SHEET    1 188 1 GLU D 411  PRO D 418  0                                        
SHEET    1 189 1 LEU D 425  PHE D 431  0                                        
SHEET    1 190 1 GLY D 453  PHE D 455  0                                        
SHEET    1 191 1 CYS D 460  CYS D 462  0                                        
SHEET    1 192 1 GLY D 499  CYS D 501  0                                        
SHEET    1 193 1 CYS D 506  CYS D 508  0                                        
SHEET    1 194 1 GLY D 540  SER D 543  0                                        
SHEET    1 195 1 ASP D 546  CYS D 549  0                                        
SHEET    1 196 1 TRP D 553  THR D 554  0                                        
SHEET    1 197 1 CYS D 560  THR D 561  0                                        
SHEET    1 198 1 GLY D 579  GLU D 582  0                                        
SHEET    1 199 1 SER D 585  CYS D 588  0                                        
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.03  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.04  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS A  473    CYS A  484                          1555   1555  2.03  
SSBOND   5 CYS A  490    CYS A  545                          1555   1555  2.04  
SSBOND   6 CYS A  602    CYS A  608                          1555   1555  2.04  
SSBOND   7 CYS A  674    CYS A  687                          1555   1555  2.04  
SSBOND   8 CYS A  826    CYS A  890                          1555   1555  2.04  
SSBOND   9 CYS A  880    CYS A  885                          1555   1555  2.02  
SSBOND  10 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND  11 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND  12 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND  13 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND  14 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND  15 CYS B  232    CYS B  273                          1555   1555  2.03  
SSBOND  16 CYS B  374    CYS B  386                          1555   1555  2.03  
SSBOND  17 CYS B  406    CYS B  433                          1555   1555  2.04  
SSBOND  18 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  19 CYS B  448    CYS B  460                          1555   1555  2.03  
SSBOND  20 CYS B  462    CYS B  471                          1555   1555  2.03  
SSBOND  21 CYS B  473    CYS B  503                          1555   1555  2.04  
SSBOND  22 CYS B  486    CYS B  501                          1555   1555  2.03  
SSBOND  23 CYS B  495    CYS B  506                          1555   1555  2.03  
SSBOND  24 CYS B  508    CYS B  521                          1555   1555  2.04  
SSBOND  25 CYS B  523    CYS B  544                          1555   1555  2.04  
SSBOND  26 CYS B  528    CYS B  542                          1555   1555  2.03  
SSBOND  27 CYS B  536    CYS B  547                          1555   1555  2.03  
SSBOND  28 CYS B  549    CYS B  558                          1555   1555  2.04  
SSBOND  29 CYS B  560    CYS B  583                          1555   1555  2.04  
SSBOND  30 CYS B  567    CYS B  581                          1555   1555  2.03  
SSBOND  31 CYS B  575    CYS B  586                          1555   1555  2.04  
SSBOND  32 CYS B  588    CYS B  598                          1555   1555  2.03  
SSBOND  33 CYS B  601    CYS B  604                          1555   1555  2.03  
SSBOND  34 CYS B  631    CYS B  617                          1555   1555  2.03  
SSBOND  35 CYS B  635    CYS B  614                          1555   1555  2.03  
SSBOND  36 CYS B  655    CYS B  608                          1555   1555  2.03  
SSBOND  37 CYS B  687    CYS B  663                          1555   1555  2.03  
SSBOND  38 CYS B  688    CYS A  959                          1555   1555  2.03  
SSBOND  39 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  40 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  41 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  42 CYS C  473    CYS C  484                          1555   1555  2.04  
SSBOND  43 CYS C  490    CYS C  545                          1555   1555  2.04  
SSBOND  44 CYS C  602    CYS C  608                          1555   1555  2.04  
SSBOND  45 CYS C  674    CYS C  687                          1555   1555  2.04  
SSBOND  46 CYS C  826    CYS C  890                          1555   1555  2.03  
SSBOND  47 CYS C  880    CYS C  885                          1555   1555  2.03  
SSBOND  48 CYS D    5    CYS D   23                          1555   1555  2.03  
SSBOND  49 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  50 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  51 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  52 CYS D  177    CYS D  184                          1555   1555  2.04  
SSBOND  53 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  54 CYS D  374    CYS D  386                          1555   1555  2.03  
SSBOND  55 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  56 CYS D  437    CYS D  457                          1555   1555  2.03  
SSBOND  57 CYS D  448    CYS D  460                          1555   1555  2.04  
SSBOND  58 CYS D  462    CYS D  471                          1555   1555  2.03  
SSBOND  59 CYS D  473    CYS D  503                          1555   1555  2.03  
SSBOND  60 CYS D  486    CYS D  501                          1555   1555  2.04  
SSBOND  61 CYS D  495    CYS D  506                          1555   1555  2.04  
SSBOND  62 CYS D  508    CYS D  521                          1555   1555  2.03  
SSBOND  63 CYS D  523    CYS D  544                          1555   1555  2.04  
SSBOND  64 CYS D  528    CYS D  542                          1555   1555  2.03  
SSBOND  65 CYS D  536    CYS D  547                          1555   1555  2.04  
SSBOND  66 CYS D  549    CYS D  558                          1555   1555  2.04  
SSBOND  67 CYS D  560    CYS D  583                          1555   1555  2.04  
SSBOND  68 CYS D  567    CYS D  581                          1555   1555  2.03  
SSBOND  69 CYS D  575    CYS D  586                          1555   1555  2.03  
SSBOND  70 CYS D  588    CYS D  598                          1555   1555  2.03  
SSBOND  71 CYS D  601    CYS D  604                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.45  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.37  
LINK         OD1 ASP A 245                CA    CA A2004     1555   1555  2.48  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.15  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.40  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.66  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.59  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.85  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.51  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.26  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.51  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.21  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.38  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.77  
LINK         OD1 ASP A 365                CA    CA A2006     1555   1555  2.23  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.10  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.20  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.48  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.70  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.68  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.32  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.35  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.27  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.37  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.55  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.57  
LINK         ND2 ASN A 570                 C1  NAG A3570     1555   1555  1.44  
LINK         O   CYS A 602                CA    CA A2008     1555   1555  2.21  
LINK         OD1 ASP A 605                CA    CA A2008     1555   1555  2.53  
LINK         O   VAL A 607                CA    CA A2008     1555   1555  2.62  
LINK         OE1 GLU A 642                CA    CA A2008     1555   1555  2.56  
LINK         OE2 GLU A 642                CA    CA A2008     1555   1555  2.87  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         OG  SER B 121                MG    MG B2001     1555   1555  2.30  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.48  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.63  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.50  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.44  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.13  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.60  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.25  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.39  
LINK         OE1 GLU B 220                CA    CA B2003     1555   1555  2.69  
LINK         OE2 GLU B 220                MG    MG B2001     1555   1555  2.27  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.38  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         ND2 ASN B 452                 C1  NAG B3452     1555   1555  1.44  
LINK         ND2 ASN B 559                 C1  NAG B3559     1555   1555  1.44  
LINK         ND2 ASN C  15                 C1  NAG C3015     1555   1555  1.44  
LINK         OE1 GLU C 243                CA    CA C2004     1555   1555  2.47  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.99  
LINK         OD1 ASP C 245                CA    CA C2004     1555   1555  2.37  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.28  
LINK         ND2 ASN C 249                 C1  NAG C3249     1555   1555  1.43  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.13  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.51  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.55  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.54  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.27  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.29  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.42  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.16  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.36  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.87  
LINK         OD1 ASP C 365                CA    CA C2006     1555   1555  2.44  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.34  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.18  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.32  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.61  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.59  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.29  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.48  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.20  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.37  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.56  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.56  
LINK         ND2 ASN C 570                 C1  NAG C3570     1555   1555  1.44  
LINK         O   CYS C 602                CA    CA C2008     1555   1555  2.22  
LINK         OD1 ASP C 605                CA    CA C2008     1555   1555  2.58  
LINK         O   VAL C 607                CA    CA C2008     1555   1555  2.77  
LINK         OE1 GLU C 642                CA    CA C2008     1555   1555  2.61  
LINK         OE2 GLU C 642                CA    CA C2008     1555   1555  2.59  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         OG  SER D 121                MG    MG D2001     1555   1555  2.49  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.50  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.42  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.44  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.36  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.19  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.57  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.22  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.27  
LINK         OE1 GLU D 220                CA    CA D2003     1555   1555  2.40  
LINK         OE2 GLU D 220                MG    MG D2001     1555   1555  2.12  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         O   MET D 335                CA    CA D2002     1555   1555  2.51  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK         ND2 ASN D 452                 C1  NAG D3452     1555   1555  1.44  
LINK         ND2 ASN D 559                 C1  NAG D3559     1555   1555  1.44  
LINK         O4  NAG B3099                 C1  NAG B3100     1555   1555  1.45  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.44  
LINK         O3  MAN B3322                 C1  MAN B3323     1555   1555  1.45  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         O4  NAG B3372                 C1  MAN B3373     1555   1555  1.44  
LINK         O4  NAG B3452                 C1  NAG B3453     1555   1555  1.44  
LINK         O4  NAG B3559                 C1  NAG B3560     1555   1555  1.44  
LINK         O4  NAG B3560                 C1  MAN B3561     1555   1555  1.45  
LINK         O3  MAN B3561                 C1  MAN B3562     1555   1555  1.44  
LINK         O2  MAN B3562                 C1  MAN B3563     1555   1555  1.44  
LINK         O4  NAG C3249                 C1  NAG C3250     1555   1555  1.44  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
LINK         O4  NAG D3452                 C1  NAG D3453     1555   1555  1.44  
LINK         O4  NAG D3559                 C1  NAG D3560     1555   1555  1.45  
LINK        CA    CA A2005                 O   HOH A 960     1555   1555  2.50  
LINK        CA    CA A2006                 O   HOH A 961     1555   1555  2.26  
LINK        CA    CA A2007                 O   HOH A 962     1555   1555  2.38  
LINK        CA    CA A2008                 O   HOH A1045     1555   1555  2.16  
LINK        CA    CA A2008                 O   HOH A1044     1555   1555  2.29  
LINK        MG    MG B2001                 O   HOH B 692     1555   1555  1.84  
LINK        MG    MG B2001                 O   HOH B 756     1555   1555  1.76  
LINK        MG    MG B2001                 O   HOH B 757     1555   1555  2.35  
LINK        MG    MG B2001                 O   HOH B 761     1555   1555  2.47  
LINK        CA    CA B2002                 O   HOH B 694     1555   1555  2.66  
LINK        CA    CA B2002                 O   HOH B 693     1555   1555  2.63  
LINK        CA    CA C2005                 O   HOH C 961     1555   1555  2.04  
LINK        CA    CA C2006                 O   HOH C1012     1555   1555  2.60  
LINK        CA    CA C2007                 O   HOH C 962     1555   1555  2.29  
LINK        CA    CA C2008                 O   HOH C1056     1555   1555  2.54  
LINK        CA    CA C2008                 O   HOH C1007     1555   1555  2.57  
LINK        MG    MG D2001                 O   HOH D 787     1555   1555  1.85  
LINK        MG    MG D2001                 O   HOH D 782     1555   1555  2.11  
LINK        MG    MG D2001                 O   HOH D 781     1555   1555  1.95  
LINK        MG    MG D2001                 O   HOH D 692     1555   1555  2.44  
LINK        CA    CA D2002                 O   HOH D 694     1555   1555  2.38  
CISPEP   1 ASN A  691    PRO A  692          0         0.64                     
CISPEP   2 PHE A  755    PRO A  756          0         2.07                     
CISPEP   3 GLN A  829    PRO A  830          0         0.85                     
CISPEP   4 SER B   84    PRO B   85          0         3.29                     
CISPEP   5 SER B  162    PRO B  163          0         2.95                     
CISPEP   6 SER B  168    PRO B  169          0        -2.14                     
CISPEP   7 ASN C  691    PRO C  692          0         1.96                     
CISPEP   8 PHE C  755    PRO C  756          0         1.35                     
CISPEP   9 GLN C  829    PRO C  830          0         2.25                     
CISPEP  10 SER D   84    PRO D   85          0         4.53                     
CISPEP  11 SER D  162    PRO D  163          0         0.99                     
CISPEP  12 SER D  168    PRO D  169          0        -1.84                     
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 960                                          
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 961                                          
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 962                                          
SITE     1 AC5  6 CYS A 602  ASP A 605  VAL A 607  GLU A 642                    
SITE     2 AC5  6 HOH A1044  HOH A1045                                          
SITE     1 AC6  2 ASN A  15  HOH A1113                                          
SITE     1 AC7  6 ASN A 505  GLU A 507  ARG A 512  ASN A 570                    
SITE     2 AC7  6 VAL A 571  SER A 572                                          
SITE     1 AC8  4 GLN A 463  ASN A 467  SER A 483  CYS A 484                    
SITE     1 AC9  7 ASP B 119  SER B 121  GLU B 220  HOH B 692                    
SITE     2 AC9  7 HOH B 756  HOH B 757  HOH B 761                               
SITE     1 BC1  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 BC1  6 HOH B 693  HOH B 694                                          
SITE     1 BC2  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC2  5 GLU B 220                                                     
SITE     1 BC3  4 ASN B  99  HOH B 759  NAG B3100  NAG B3371                    
SITE     1 BC4  1 NAG B3099                                                     
SITE     1 BC5  6 MET A 285  ASN B 316  LEU B 317  ASN B 320                    
SITE     2 BC5  6 HOH B 736  NAG B3321                                          
SITE     1 BC6  4 ARG A 281  LYS B 600  NAG B3320  MAN B3322                    
SITE     1 BC7  2 NAG B3321  MAN B3323                                          
SITE     1 BC8  1 MAN B3322                                                     
SITE     1 BC9  6 SER B 369  ASN B 371  SER B 398  GLU B 400                    
SITE     2 BC9  6 NAG B3099  NAG B3372                                          
SITE     1 CC1  2 NAG B3371  MAN B3373                                          
SITE     1 CC2  1 NAG B3372                                                     
SITE     1 CC3  5 ASN B 449  ASN B 450  GLY B 451  ASN B 452                    
SITE     2 CC3  5 NAG B3453                                                     
SITE     1 CC4  1 NAG B3452                                                     
SITE     1 CC5  4 TYR B 531  ASN B 559  CYS B 583  NAG B3560                    
SITE     1 CC6  6 ASP A 628  VAL A 630  MET A 660  TYR B 557                    
SITE     2 CC6  6 NAG B3559  MAN B3561                                          
SITE     1 CC7  4 ASP A 628  HOH B 731  NAG B3560  MAN B3562                    
SITE     1 CC8  2 MAN B3561  MAN B3563                                          
SITE     1 CC9  2 SER A  46  MAN B3562                                          
SITE     1 DC1  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 DC1  5 GLU C 252                                                     
SITE     1 DC2  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 DC2  6 ASP C 305  HOH C 961                                          
SITE     1 DC3  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 DC3  6 ASP C 373  HOH C1012                                          
SITE     1 DC4  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 DC4  6 ASP C 434  HOH C 962                                          
SITE     1 DC5  6 CYS C 602  ASP C 605  VAL C 607  GLU C 642                    
SITE     2 DC5  6 HOH C1007  HOH C1056                                          
SITE     1 DC6  2 ASN C  15  HOH C1196                                          
SITE     1 DC7  3 ASP C 247  ASN C 249  NAG C3250                               
SITE     1 DC8  2 NAG C3249  LYS D 137                                          
SITE     1 DC9  3 GLU C 507  ASN C 570  SER C 572                               
SITE     1 EC1  3 ARG C 281  GLU C 283  PRO C 343                               
SITE     1 EC2  7 ASP C 232  TYR C 234  THR C 259  THR C 263                    
SITE     2 EC2  7 THR D 254  HIS D 255  ASP D 259                               
SITE     1 EC3  4 GLN C 463  ASN C 467  SER C 483  CYS C 484                    
SITE     1 EC4  3 THR C 348  SER C 401  ARG C 402                               
SITE     1 EC5  3 PRO C 410  PHE C 411  GLN C 444                               
SITE     1 EC6  7 ASP D 119  SER D 121  GLU D 220  HOH D 692                    
SITE     2 EC6  7 HOH D 781  HOH D 782  HOH D 787                               
SITE     1 EC7  5 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 EC7  5 HOH D 694                                                     
SITE     1 EC8  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 EC8  5 GLU D 220                                                     
SITE     1 EC9  2 ASN D  99  NAG D3371                                          
SITE     1 FC1  5 TRP C 262  MET C 285  LEU D 317  ASN D 320                    
SITE     2 FC1  5 NAG D3321                                                     
SITE     1 FC2  1 NAG D3320                                                     
SITE     1 FC3  6 SER D 369  ASN D 371  SER D 398  GLU D 400                    
SITE     2 FC3  6 NAG D3099  NAG D3372                                          
SITE     1 FC4  1 NAG D3371                                                     
SITE     1 FC5  5 ASN D 449  ASN D 450  GLY D 451  ASN D 452                    
SITE     2 FC5  5 NAG D3453                                                     
SITE     1 FC6  3 HOH D 727  HOH D 728  NAG D3452                               
SITE     1 FC7  5 TYR D 531  TYR D 557  ASN D 559  CYS D 583                    
SITE     2 FC7  5 NAG D3560                                                     
SITE     1 FC8  3 VAL C 630  HOH D 759  NAG D3559                               
CRYST1   81.300   81.300  654.623  90.00  90.00  90.00 P 41          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      0.012300  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012300  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.001528        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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