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Database: PDB
Entry: 3FCU
LinkDB: 3FCU
Original site: 3FCU 
HEADER    CELL ADHESION/BLOOD CLOTTING            22-NOV-08   3FCU              
TITLE     STRUCTURE OF HEADPIECE OF INTEGRIN AIIBB3 IN OPEN CONFORMATION        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN, ALPHA 2B;                                        
COMPND   3 CHAIN: A, C, E;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 32-488, HEADPIECE;                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   8 CHAIN: B, D, F;                                                      
COMPND   9 FRAGMENT: UNP RESIDUES 27-487;                                       
COMPND  10 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ITGA2B;                                                        
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;                           
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: ITGB3, GP3A;                                                   
SOURCE  15 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    CRYSTAL STRUCTURE; PLATELET INTEGRIN ALPHAIIBBETA3; FIBRINOGEN        
KEYWDS   2 BINDING; ALLOSTERY; THERAPEUTIC ANTAGONISM, CELL ADHESION, INTEGRIN, 
KEYWDS   3 MEMBRANE, RECEPTOR, TRANSMEMBRANE, DISEASE MUTATION, GLYCOPROTEIN,   
KEYWDS   4 HOST-VIRUS INTERACTION, PHOSPHOPROTEIN, CELL ADHESION-IMMUNE SYSTEM  
KEYWDS   5 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 3FCU    1       VERSN                                    
REVDAT   1   20-JAN-09 3FCU    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.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.59                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 115380                         
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3098                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7316                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2790                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 168                          
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20990                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 323                                     
REMARK   3   SOLVENT ATOMS            : 298                                     
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) : 60.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.447         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.254         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.427        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 21878 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A): 14771 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 29791 ; 0.657 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 35772 ; 0.645 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2726 ; 5.541 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   992 ;31.407 ;24.123       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3425 ;12.696 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   143 ;11.570 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3301 ; 0.049 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 24519 ; 0.003 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  4399 ; 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): 13556 ; 2.238 ; 8.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  5536 ; 0.361 ; 8.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 21825 ; 3.887 ;16.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  8322 ; 2.536 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7964 ; 4.194 ;16.000       
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 : 7                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A      27      5                      
REMARK   3           1     C      2       C      27      5                      
REMARK   3           1     E      2       E      27      5                      
REMARK   3           2     A     33       A      43      4                      
REMARK   3           2     C     33       C      43      4                      
REMARK   3           2     E     33       E      43      4                      
REMARK   3           3     A     47       A     207      4                      
REMARK   3           3     C     47       C     207      4                      
REMARK   3           3     E     47       E     207      4                      
REMARK   3           4     A    209       A     212      4                      
REMARK   3           4     C    209       C     212      4                      
REMARK   3           4     E    209       E     212      4                      
REMARK   3           5     A    216       A     221      4                      
REMARK   3           5     C    216       C     221      4                      
REMARK   3           5     E    216       E     221      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2483 ; 0.280 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2483 ; 0.200 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  1    E    (A):   2483 ; 0.220 ; 0.500           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    197 ; 0.300 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    C    (A):    197 ; 0.250 ; 5.000           
REMARK   3   LOOSE POSITIONAL   1    E    (A):    197 ; 0.330 ; 5.000           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2483 ; 0.300 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2483 ; 0.300 ; 2.000           
REMARK   3   MEDIUM THERMAL     1    E (A**2):   2483 ; 0.310 ; 2.000           
REMARK   3   LOOSE THERMAL      1    A (A**2):    197 ; 0.190 ;10.000           
REMARK   3   LOOSE THERMAL      1    C (A**2):    197 ; 0.200 ;10.000           
REMARK   3   LOOSE THERMAL      1    E (A**2):    197 ; 0.190 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    224       A     271      5                      
REMARK   3           1     C    224       C     271      5                      
REMARK   3           1     E    224       E     271      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    280 ; 0.110 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    C    (A):    280 ; 0.080 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  2    E    (A):    280 ; 0.100 ; 0.500           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    329 ; 0.150 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    C    (A):    329 ; 0.130 ; 5.000           
REMARK   3   LOOSE POSITIONAL   2    E    (A):    329 ; 0.160 ; 5.000           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    280 ; 0.320 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    C (A**2):    280 ; 0.270 ; 2.000           
REMARK   3   MEDIUM THERMAL     2    E (A**2):    280 ; 0.320 ; 2.000           
REMARK   3   LOOSE THERMAL      2    A (A**2):    329 ; 0.250 ;10.000           
REMARK   3   LOOSE THERMAL      2    C (A**2):    329 ; 0.270 ;10.000           
REMARK   3   LOOSE THERMAL      2    E (A**2):    329 ; 0.230 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A C E                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    280       A     451      5                      
REMARK   3           1     C    280       C     451      5                      
REMARK   3           1     E    280       E     451      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    994 ; 0.090 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    C    (A):    994 ; 0.090 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  3    E    (A):    994 ; 0.090 ; 0.500           
REMARK   3   LOOSE POSITIONAL   3    A    (A):   1164 ; 0.170 ; 5.000           
REMARK   3   LOOSE POSITIONAL   3    C    (A):   1164 ; 0.130 ; 5.000           
REMARK   3   LOOSE POSITIONAL   3    E    (A):   1164 ; 0.150 ; 5.000           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    994 ; 0.270 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    C (A**2):    994 ; 0.220 ; 2.000           
REMARK   3   MEDIUM THERMAL     3    E (A**2):    994 ; 0.260 ; 2.000           
REMARK   3   LOOSE THERMAL      3    A (A**2):   1164 ; 0.180 ;10.000           
REMARK   3   LOOSE THERMAL      3    C (A**2):   1164 ; 0.190 ;10.000           
REMARK   3   LOOSE THERMAL      3    E (A**2):   1164 ; 0.170 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : B D F                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 4                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      1       B       7      5                      
REMARK   3           1     D      1       D       7      5                      
REMARK   3           1     F      1       F       7      5                      
REMARK   3           2     B     11       B      32      5                      
REMARK   3           2     D     11       D      32      5                      
REMARK   3           2     F     11       F      32      5                      
REMARK   3           3     B     36       B      57      5                      
REMARK   3           3     D     36       D      57      5                      
REMARK   3           3     F     36       F      57      5                      
REMARK   3           4     B    434       B     436      5                      
REMARK   3           4     D    434       D     436      5                      
REMARK   3           4     F    434       F     436      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    316 ; 0.170 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    C    (A):    316 ; 0.110 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  4    E    (A):    316 ; 0.120 ; 0.500           
REMARK   3   LOOSE POSITIONAL   4    A    (A):    362 ; 0.310 ; 5.000           
REMARK   3   LOOSE POSITIONAL   4    C    (A):    362 ; 0.200 ; 5.000           
REMARK   3   LOOSE POSITIONAL   4    E    (A):    362 ; 0.200 ; 5.000           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    316 ; 0.160 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    C (A**2):    316 ; 0.170 ; 2.000           
REMARK   3   MEDIUM THERMAL     4    E (A**2):    316 ; 0.140 ; 2.000           
REMARK   3   LOOSE THERMAL      4    A (A**2):    362 ; 0.150 ;10.000           
REMARK   3   LOOSE THERMAL      4    C (A**2):    362 ; 0.140 ;10.000           
REMARK   3   LOOSE THERMAL      4    E (A**2):    362 ; 0.100 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : B D F                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B     58       B     108      5                      
REMARK   3           1     D     58       D     108      5                      
REMARK   3           1     F     58       F     108      5                      
REMARK   3           2     B    353       B     433      5                      
REMARK   3           2     D    353       D     433      5                      
REMARK   3           2     F    353       F     433      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    B    (A):    744 ; 0.110 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  5    D    (A):    744 ; 0.090 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  5    F    (A):    744 ; 0.090 ; 0.500           
REMARK   3   LOOSE POSITIONAL   5    B    (A):    958 ; 0.200 ; 5.000           
REMARK   3   LOOSE POSITIONAL   5    D    (A):    958 ; 0.210 ; 5.000           
REMARK   3   LOOSE POSITIONAL   5    F    (A):    958 ; 0.160 ; 5.000           
REMARK   3   MEDIUM THERMAL     5    B (A**2):    744 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     5    D (A**2):    744 ; 0.130 ; 2.000           
REMARK   3   MEDIUM THERMAL     5    F (A**2):    744 ; 0.110 ; 2.000           
REMARK   3   LOOSE THERMAL      5    B (A**2):    958 ; 0.100 ;10.000           
REMARK   3   LOOSE THERMAL      5    D (A**2):    958 ; 0.110 ;10.000           
REMARK   3   LOOSE THERMAL      5    F (A**2):    958 ; 0.110 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : B D F                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    109       B     352      5                      
REMARK   3           1     D    109       D     352      5                      
REMARK   3           1     F    109       F     352      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    B    (A):   1438 ; 0.090 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  6    D    (A):   1438 ; 0.100 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  6    F    (A):   1438 ; 0.090 ; 0.500           
REMARK   3   LOOSE POSITIONAL   6    B    (A):   1765 ; 0.180 ; 5.000           
REMARK   3   LOOSE POSITIONAL   6    D    (A):   1765 ; 0.200 ; 5.000           
REMARK   3   LOOSE POSITIONAL   6    F    (A):   1765 ; 0.210 ; 5.000           
REMARK   3   MEDIUM THERMAL     6    B (A**2):   1438 ; 0.230 ; 2.000           
REMARK   3   MEDIUM THERMAL     6    D (A**2):   1438 ; 0.240 ; 2.000           
REMARK   3   MEDIUM THERMAL     6    F (A**2):   1438 ; 0.210 ; 2.000           
REMARK   3   LOOSE THERMAL      6    B (A**2):   1765 ; 0.210 ;10.000           
REMARK   3   LOOSE THERMAL      6    D (A**2):   1765 ; 0.210 ;10.000           
REMARK   3   LOOSE THERMAL      6    F (A**2):   1765 ; 0.180 ;10.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 7                                  
REMARK   3     CHAIN NAMES                    : B D F                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    437       B     461      5                      
REMARK   3           1     D    437       D     461      5                      
REMARK   3           1     F    437       F     461      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  7    B    (A):    146 ; 0.160 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  7    D    (A):    146 ; 0.210 ; 0.500           
REMARK   3   MEDIUM POSITIONAL  7    F    (A):    146 ; 0.310 ; 0.500           
REMARK   3   LOOSE POSITIONAL   7    B    (A):    169 ; 0.180 ; 5.000           
REMARK   3   LOOSE POSITIONAL   7    D    (A):    169 ; 0.260 ; 5.000           
REMARK   3   LOOSE POSITIONAL   7    F    (A):    169 ; 0.300 ; 5.000           
REMARK   3   MEDIUM THERMAL     7    B (A**2):    146 ; 0.070 ; 2.000           
REMARK   3   MEDIUM THERMAL     7    D (A**2):    146 ; 0.070 ; 2.000           
REMARK   3   MEDIUM THERMAL     7    F (A**2):    146 ; 0.070 ; 2.000           
REMARK   3   LOOSE THERMAL      7    B (A**2):    169 ; 0.060 ;10.000           
REMARK   3   LOOSE THERMAL      7    D (A**2):    169 ; 0.060 ;10.000           
REMARK   3   LOOSE THERMAL      7    F (A**2):    169 ; 0.070 ;10.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 15                                         
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  2006                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9738 329.1421  23.9453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2822 T22:  -0.2373                                     
REMARK   3      T33:  -0.1454 T12:  -0.0559                                     
REMARK   3      T13:   0.0378 T23:   0.0610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8760 L22:   1.3721                                     
REMARK   3      L33:   1.1353 L12:  -0.1752                                     
REMARK   3      L13:  -0.2604 L23:  -0.1992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1265 S12:   0.1265 S13:   0.1198                       
REMARK   3      S21:  -0.1923 S22:  -0.0026 S23:  -0.0685                       
REMARK   3      S31:  -0.2483 S32:   0.0441 S33:  -0.1238                       
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  2006                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.2886 287.5998   3.5237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0261 T22:  -0.1747                                     
REMARK   3      T33:  -0.0106 T12:   0.0074                                     
REMARK   3      T13:  -0.0993 T23:  -0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6219 L22:   1.8798                                     
REMARK   3      L33:   0.6575 L12:  -0.2096                                     
REMARK   3      L13:   0.0059 L23:   0.1952                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0537 S12:  -0.0875 S13:  -0.0356                       
REMARK   3      S21:   0.1476 S22:   0.0227 S23:  -0.3297                       
REMARK   3      S31:  -0.0308 S32:   0.1241 S33:  -0.0764                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     1        E   452                          
REMARK   3    RESIDUE RANGE :   E  2004        E  2006                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5458 325.6202 -24.0282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0667 T22:  -0.2194                                     
REMARK   3      T33:  -0.1055 T12:  -0.1234                                     
REMARK   3      T13:   0.0584 T23:  -0.0688                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4598 L22:   1.0875                                     
REMARK   3      L33:   1.1919 L12:   0.0033                                     
REMARK   3      L13:   0.1113 L23:  -0.2441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0233 S12:   0.0783 S13:  -0.0249                       
REMARK   3      S21:   0.0638 S22:   0.0047 S23:  -0.0714                       
REMARK   3      S31:  -0.2025 S32:   0.1037 S33:  -0.0279                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
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): -12.5815 319.3215  42.2503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0855 T22:  -0.2321                                     
REMARK   3      T33:   0.0215 T12:   0.0489                                     
REMARK   3      T13:   0.0123 T23:   0.1135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3412 L22:   0.7866                                     
REMARK   3      L33:   1.3272 L12:  -0.2006                                     
REMARK   3      L13:  -0.7959 L23:  -0.0762                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0400 S12:   0.2563 S13:  -0.1429                       
REMARK   3      S21:  -0.0794 S22:   0.0931 S23:   0.3786                       
REMARK   3      S31:  -0.1794 S32:  -0.2880 S33:  -0.0532                       
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 :   D   109        D   352                          
REMARK   3    RESIDUE RANGE :   D  2001        D  2003                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.5248 263.6294  -5.7713              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0693 T22:  -0.3404                                     
REMARK   3      T33:   0.0419 T12:   0.0291                                     
REMARK   3      T13:  -0.1137 T23:  -0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3189 L22:   2.7812                                     
REMARK   3      L33:   0.7799 L12:   0.4869                                     
REMARK   3      L13:   0.0525 L23:   0.5071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1357 S12:  -0.0156 S13:  -0.2119                       
REMARK   3      S21:   0.0681 S22:  -0.1127 S23:   0.3616                       
REMARK   3      S31:   0.0671 S32:   0.0217 S33:  -0.0230                       
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 :   F   109        F   352                          
REMARK   3    RESIDUE RANGE :   F  2001        F  2003                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1314 323.1791 -45.8958              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0314 T22:   0.2489                                     
REMARK   3      T33:   0.1482 T12:  -0.1871                                     
REMARK   3      T13:   0.1770 T23:  -0.0767                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1280 L22:   1.5608                                     
REMARK   3      L33:   0.8102 L12:   0.1304                                     
REMARK   3      L13:  -0.3956 L23:  -0.0535                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:   0.2596 S13:  -0.0157                       
REMARK   3      S21:  -0.2362 S22:   0.0044 S23:  -0.5150                       
REMARK   3      S31:  -0.0634 S32:   0.5422 S33:   0.0184                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    58        B   108                          
REMARK   3    RESIDUE RANGE :   B   353        B   433                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.6462 340.4174  40.5821              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0823 T22:  -0.3421                                     
REMARK   3      T33:  -0.0690 T12:   0.3006                                     
REMARK   3      T13:   0.1142 T23:   0.3276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4402 L22:   3.0206                                     
REMARK   3      L33:   4.4383 L12:  -3.0355                                     
REMARK   3      L13:   4.3372 L23:  -2.0292                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2892 S12:  -0.5950 S13:  -0.4398                       
REMARK   3      S21:  -0.1728 S22:   0.3925 S23:   0.1849                       
REMARK   3      S31:   0.0005 S32:  -0.2695 S33:  -0.1033                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
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):  23.8454 218.6586   4.5529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3477 T22:  -0.4243                                     
REMARK   3      T33:   0.0231 T12:   0.2519                                     
REMARK   3      T13:  -0.0444 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2114 L22:   9.2520                                     
REMARK   3      L33:   5.5579 L12:  -2.3639                                     
REMARK   3      L13:   1.9626 L23:  -5.3207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1655 S12:  -0.7329 S13:   0.2230                       
REMARK   3      S21:  -0.2590 S22:   0.2945 S23:   1.0265                       
REMARK   3      S31:  -0.2227 S32:   0.0992 S33:  -0.1290                       
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 :   F    58        F   108                          
REMARK   3    RESIDUE RANGE :   F   353        F   433                          
REMARK   3    ORIGIN FOR THE GROUP (A): 101.4461 349.0582 -42.0582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0772 T22:  -0.1712                                     
REMARK   3      T33:   0.4928 T12:  -0.2066                                     
REMARK   3      T13:   0.1814 T23:   0.0295                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.1226 L22:   5.2492                                     
REMARK   3      L33:   4.1269 L12:   4.2884                                     
REMARK   3      L13:   3.8653 L23:   3.1601                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5239 S12:   0.8234 S13:  -0.7580                       
REMARK   3      S21:   0.3585 S22:   0.5835 S23:  -0.9164                       
REMARK   3      S31:   0.4717 S32:  -0.2900 S33:  -0.0596                       
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 :   B     1        B    57                          
REMARK   3    RESIDUE RANGE :   B   434        B   436                          
REMARK   3    ORIGIN FOR THE GROUP (A): -81.3268 357.5117  33.8367              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1812 T22:   0.0174                                     
REMARK   3      T33:  -0.1037 T12:   0.3090                                     
REMARK   3      T13:   0.0510 T23:   0.4855                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0648 L22:   9.6004                                     
REMARK   3      L33:   8.0763 L12:  -1.5707                                     
REMARK   3      L13:  -2.2215 L23:   0.2923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3055 S12:  -0.8520 S13:  -0.5806                       
REMARK   3      S21:   0.3156 S22:   0.2912 S23:   0.8378                       
REMARK   3      S31:   0.0077 S32:  -0.8967 S33:   0.0143                       
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 :   D     1        D    57                          
REMARK   3    RESIDUE RANGE :   D   434        D   436                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.3707 188.4819  15.2911              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4143 T22:  -0.1805                                     
REMARK   3      T33:  -0.1828 T12:   0.2800                                     
REMARK   3      T13:  -0.0730 T23:   0.3151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2123 L22:   8.5314                                     
REMARK   3      L33:   4.7646 L12:   2.7962                                     
REMARK   3      L13:  -2.3186 L23:  -0.9773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6355 S12:  -0.7509 S13:  -1.2360                       
REMARK   3      S21:   0.0370 S22:  -0.0649 S23:  -0.0280                       
REMARK   3      S31:   0.3084 S32:  -0.1036 S33:  -0.5706                       
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 :   F     1        F    57                          
REMARK   3    RESIDUE RANGE :   F   434        F   436                          
REMARK   3    ORIGIN FOR THE GROUP (A): 126.9953 368.4969 -33.9701              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3835 T22:   0.0163                                     
REMARK   3      T33:   1.0591 T12:   0.0106                                     
REMARK   3      T13:  -0.1112 T23:  -0.1680                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3492 L22:   4.7408                                     
REMARK   3      L33:   7.9442 L12:  -0.6601                                     
REMARK   3      L13:  -0.7503 L23:   2.1612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0817 S12:  -0.2841 S13:  -0.4925                       
REMARK   3      S21:   0.3004 S22:   0.5713 S23:  -1.5356                       
REMARK   3      S31:  -0.1009 S32:   1.7743 S33:  -0.6530                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   437        B   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): -92.9542 345.9742  26.4548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1344 T22:   0.3462                                     
REMARK   3      T33:   0.2872 T12:   0.0701                                     
REMARK   3      T13:   0.0467 T23:  -0.0368                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8457 L22:   9.0251                                     
REMARK   3      L33:   1.9436 L12:   2.0424                                     
REMARK   3      L13:   2.3313 L23:  -0.8141                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1520 S12:   0.3822 S13:   0.1417                       
REMARK   3      S21:   0.0106 S22:  -0.3310 S23:   0.6809                       
REMARK   3      S31:   0.3250 S32:  -0.4176 S33:   0.1790                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   437        D   461                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.8413 182.7272  28.6945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0283 T22:   0.1720                                     
REMARK   3      T33:   0.0463 T12:  -0.0880                                     
REMARK   3      T13:  -0.0223 T23:   0.0532                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8090 L22:   6.3359                                     
REMARK   3      L33:  11.3125 L12:  -3.8696                                     
REMARK   3      L13:  -0.4155 L23:  -6.2350                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0432 S12:  -0.2513 S13:  -0.3565                       
REMARK   3      S21:   0.6283 S22:  -0.1177 S23:   0.0776                       
REMARK   3      S31:   0.0198 S32:  -0.3571 S33:   0.1608                       
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 :   F   437        F   461                          
REMARK   3    ORIGIN FOR THE GROUP (A): 139.4097 358.7966 -25.3761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4865 T22:   1.1106                                     
REMARK   3      T33:   1.5366 T12:   0.2384                                     
REMARK   3      T13:  -0.3268 T23:   0.1267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2895 L22:   4.8293                                     
REMARK   3      L33:   0.2651 L12:   1.1824                                     
REMARK   3      L13:  -0.2770 L23:  -1.1315                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9178 S12:  -0.9769 S13:   0.4618                       
REMARK   3      S21:   0.5165 S22:  -1.1181 S23:  -0.3661                       
REMARK   3      S31:   0.4329 S32:   0.3585 S33:   0.2003                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3FCU 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 RCSB050431.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-OCT-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : A1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9760                             
REMARK 200  MONOCHROMATOR                  : RH-COATED SI                       
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 122126                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : 0.09700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.60200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: PDB ENTRY 2VDR                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 0.4 M MAGNESIUM ACETATE,   
REMARK 280  0.1 M SODIUM CACODYLATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.85867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       29.42933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       58.85867            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       29.42933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: HETER-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: 5710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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: 5630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 5630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     ASP B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     LEU C     1                                                      
REMARK 465     VAL C   453                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
REMARK 465     GLY D    73                                                      
REMARK 465     SER D    74                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     ASP D    76                                                      
REMARK 465     SER D    77                                                      
REMARK 465     SER D    78                                                      
REMARK 465     VAL E   453                                                      
REMARK 465     VAL E   454                                                      
REMARK 465     LYS E   455                                                      
REMARK 465     ALA E   456                                                      
REMARK 465     SER E   457                                                      
REMARK 465     GLY F    73                                                      
REMARK 465     SER F    74                                                      
REMARK 465     GLY F    75                                                      
REMARK 465     ASP F    76                                                      
REMARK 465     SER F    77                                                      
REMARK 465     SER F    78                                                      
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  MG     MG D  2001     O2   CAC D   462              1.66            
REMARK 500  MG     MG F  2001     O2   CAC F   462              1.67            
REMARK 500   ND2  ASN E    15     C2   NAG E  3015              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  28      -83.51    -46.29                                   
REMARK 500    SER A  29       75.63   -171.08                                   
REMARK 500    HIS A  30       74.77   -154.90                                   
REMARK 500    PRO A  45       82.99    -60.28                                   
REMARK 500    SER A  46      -18.47    161.62                                   
REMARK 500    GLN A  47       31.22     70.96                                   
REMARK 500    SER A 101     -127.82     53.05                                   
REMARK 500    LYS A 118     -123.70     54.84                                   
REMARK 500    GLU A 123      135.38     84.04                                   
REMARK 500    LEU A 212      -45.13     79.26                                   
REMARK 500    SER A 261       70.55     38.67                                   
REMARK 500    VAL A 453     -154.08   -142.11                                   
REMARK 500    ASP B  47       35.74    -98.41                                   
REMARK 500    ASP B  71     -140.68   -107.85                                   
REMARK 500    VAL B 157      -74.93   -131.63                                   
REMARK 500    GLN B 199       82.63    -68.61                                   
REMARK 500    SER B 213     -157.59   -107.20                                   
REMARK 500    LEU B 258       -9.34     88.26                                   
REMARK 500    VAL B 275      -77.01    -83.50                                   
REMARK 500    ALA B 309       78.24   -110.04                                   
REMARK 500    CYS B 374     -154.33    -91.00                                   
REMARK 500    LYS B 410      -75.14     67.77                                   
REMARK 500    GLN B 440       55.31    -93.46                                   
REMARK 500    SER C  46      -18.53    124.92                                   
REMARK 500    SER C  81      -14.18     78.51                                   
REMARK 500    SER C 101     -126.11     50.85                                   
REMARK 500    LYS C 118     -121.05     55.58                                   
REMARK 500    GLU C 123      131.76     86.10                                   
REMARK 500    LEU C 212      -45.82     78.99                                   
REMARK 500    ASP D  47       31.57    -95.48                                   
REMARK 500    ASP D  71     -143.72   -107.94                                   
REMARK 500    ASN D 148       67.95   -103.01                                   
REMARK 500    VAL D 157      -76.48   -127.51                                   
REMARK 500    VAL D 193      -60.32   -100.89                                   
REMARK 500    SER D 213     -150.25   -105.00                                   
REMARK 500    LYS D 253     -179.63    -67.91                                   
REMARK 500    LEU D 258       -6.44     87.21                                   
REMARK 500    VAL D 275      -75.68    -83.38                                   
REMARK 500    CYS D 374     -153.51    -92.02                                   
REMARK 500    LYS D 410      -72.20     70.47                                   
REMARK 500    GLN D 440       43.26    -95.33                                   
REMARK 500    SER E 101     -124.48     53.17                                   
REMARK 500    LYS E 118     -125.36     54.31                                   
REMARK 500    GLU E 123      128.64     91.23                                   
REMARK 500    LEU E 212      -52.65     78.32                                   
REMARK 500    SER E 261       72.22     44.75                                   
REMARK 500    ASP F  71     -142.08   -118.34                                   
REMARK 500    PRO F  94      122.06    -38.22                                   
REMARK 500    VAL F 157      -76.02   -133.67                                   
REMARK 500    SER F 213     -152.28   -110.66                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 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 C 469        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C 474        DISTANCE =  5.12 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 GLU A 243   OE2  49.3                                              
REMARK 620 3 ASP A 245   OD2 111.6  63.6                                        
REMARK 620 4 ASP A 247   O    76.4  78.4 104.2                                  
REMARK 620 5 THR A 250   O    75.0 123.3 173.0  79.5                            
REMARK 620 6 THR A 250   OG1 153.0 146.3  92.3  85.8  81.9                      
REMARK 620 7 GLU A 252   OE1  77.8  69.3  67.1 147.1 113.1 125.0                
REMARK 620 8 GLU A 252   OE2 117.4 115.6  78.1 164.5  96.8  78.7  48.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 297   OD1                                                    
REMARK 620 2 ASN A 299   OD1  79.8                                              
REMARK 620 3 ASP A 301   OD1  76.5  78.6                                        
REMARK 620 4 ARG A 303   O    76.7 155.7 101.2                                  
REMARK 620 5 ASP A 305   OD1 134.2 105.0 149.2  87.6                            
REMARK 620 6 ASP A 305   OD2  92.0  77.7 155.1  97.4  47.2                      
REMARK 620 7 HOH A 583   O   155.1 106.1  80.9  97.8  68.6 112.8                
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   OD2                                                    
REMARK 620 2 ASP A 367   OD1  88.0                                              
REMARK 620 3 ASP A 369   OD1  80.9  80.8                                        
REMARK 620 4 TYR A 371   O    73.1 160.6  91.4                                  
REMARK 620 5 ASP A 373   OD1  96.2  93.3 173.5  93.3                            
REMARK 620 6 ASP A 373   OD2 129.4 121.8 138.5  75.5  47.5                      
REMARK 620 7 HOH A 512   O   146.4 106.3  72.0  87.9 112.7  68.4                
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  92.6                                              
REMARK 620 3 ASN A 430   OD1  87.7  88.4                                        
REMARK 620 4 TYR A 432   O    79.1 171.6  92.8                                  
REMARK 620 5 ASP A 434   OD1  95.6  84.5 172.3  94.6                            
REMARK 620 6 ASP A 434   OD2 137.6 101.8 131.8  83.5  47.5                      
REMARK 620 7 HOH A 589   O   159.3  70.0  80.8 118.4  93.9  60.0                
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 SER B 123   OG  104.9                                              
REMARK 620 3 GLU B 220   OE1  77.6 167.1                                        
REMARK 620 4 HOH C 463   O    78.9  82.8  85.3                                  
REMARK 620 5 HOH C 464   O   155.9  88.4  85.2  83.2                            
REMARK 620 N                    1     2     3     4                             
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  73.1                                              
REMARK 620 3 ASP B 127   OD1  85.6  88.9                                        
REMARK 620 4 ASP B 251   OD2  75.0 147.4  81.8                                  
REMARK 620 5 HOH A 550   O    85.8 104.7 161.1  79.7                            
REMARK 620 6 HOH A 590   O   146.5 128.4  71.3  77.8 108.3                      
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 101.4                                              
REMARK 620 3 ASP B 217   O   160.2  89.4                                        
REMARK 620 4 ASP B 217   OD1  91.0  85.5  73.2                                  
REMARK 620 5 PRO B 219   O    85.0 173.5  84.2  93.8                            
REMARK 620 6 GLU B 220   OE2 104.7  91.9  91.3 164.3  87.1                      
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  51.9                                              
REMARK 620 3 ASP C 245   OD2 119.2  67.6                                        
REMARK 620 4 ASP C 247   O    76.0  80.5 101.1                                  
REMARK 620 5 THR C 250   O    71.9 123.7 168.6  83.4                            
REMARK 620 6 THR C 250   OG1 146.4 145.3  88.3  80.2  82.2                      
REMARK 620 7 GLU C 252   OE1  85.3  77.6  76.5 157.1 103.4 122.1                
REMARK 620 8 GLU C 252   OE2 129.7 119.1  73.6 153.5  97.6  73.8  48.3          
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  82.2                                              
REMARK 620 3 ASP C 301   OD1  81.1  79.6                                        
REMARK 620 4 ARG C 303   O    83.6 165.5  95.1                                  
REMARK 620 5 ASP C 305   OD1 137.0 109.2 140.9  83.5                            
REMARK 620 6 ASP C 305   OD2  92.9  86.3 165.3  97.5  48.8                      
REMARK 620 7 HOH A 582   O   160.2  86.9  80.7 105.7  62.4 102.9                
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   OD2                                                    
REMARK 620 2 ASP C 367   OD1  88.7                                              
REMARK 620 3 ASP C 369   OD1  86.7  77.0                                        
REMARK 620 4 TYR C 371   O    77.9 165.0  95.5                                  
REMARK 620 5 ASP C 373   OD1  95.8  89.1 165.9  98.6                            
REMARK 620 6 ASP C 373   OD2 129.4 118.6 137.9  75.6  47.9                      
REMARK 620 7 HOH A 591   O   152.3  97.0  68.5  92.1 111.3  70.8                
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  82.0                                              
REMARK 620 3 ASN C 430   OD1  87.4  84.7                                        
REMARK 620 4 TYR C 432   O    80.4 161.9  99.0                                  
REMARK 620 5 ASP C 434   OD1  90.4  77.9 162.6  97.7                            
REMARK 620 6 ASP C 434   OD2 134.7 100.5 137.8  88.7  47.5                      
REMARK 620 7 HOH A 592   O   148.3  67.0  83.4 130.9  89.5  61.4                
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 SER D 123   OG  104.7                                              
REMARK 620 3 GLU D 220   OE1  82.1 172.8                                        
REMARK 620 4 HOH C 459   O    77.7  85.3  94.1                                  
REMARK 620 5 HOH C 460   O   157.3  91.8  81.0  88.5                            
REMARK 620 N                    1     2     3     4                             
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  72.8                                              
REMARK 620 3 ASP D 127   OD1  86.6  98.1                                        
REMARK 620 4 ASP D 251   OD2  72.2 145.0  79.0                                  
REMARK 620 5 HOH A 584   O   147.4 133.5  72.4  79.4                            
REMARK 620 6 HOH A 585   O    93.0 114.0 146.2  68.8  91.3                      
REMARK 620 N                    1     2     3     4     5                       
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 100.4                                              
REMARK 620 3 ASP D 217   O   163.2  95.2                                        
REMARK 620 4 ASP D 217   OD1 100.5  89.5  73.4                                  
REMARK 620 5 PRO D 219   O    84.9 171.2  80.4  96.4                            
REMARK 620 6 GLU D 220   OE2  97.4  87.8  89.3 162.1  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 243   OE1                                                    
REMARK 620 2 GLU E 243   OE2  50.5                                              
REMARK 620 3 ASP E 245   OD2 119.7  70.1                                        
REMARK 620 4 ASP E 247   O    74.9  75.5 101.3                                  
REMARK 620 5 THR E 250   O    71.3 121.5 168.1  85.5                            
REMARK 620 6 THR E 250   OG1 144.7 150.5  92.5  85.4  78.3                      
REMARK 620 7 GLU E 252   OE1  81.7  77.0  76.1 151.4 102.5 123.0                
REMARK 620 8 GLU E 252   OE2 123.5 122.1  77.9 159.6  92.3  74.3  48.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 297   OD1                                                    
REMARK 620 2 ASN E 299   OD1  85.3                                              
REMARK 620 3 ASP E 301   OD1  84.9  79.3                                        
REMARK 620 4 ARG E 303   O    91.1 175.7  97.9                                  
REMARK 620 5 ASP E 305   OD1 141.3 103.3 133.5  81.0                            
REMARK 620 6 ASP E 305   OD2  95.9  88.3 167.5  94.5  47.7                      
REMARK 620 7 HOH A 478   O   161.3  83.5  78.4  99.3  56.4  98.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 365   OD2                                                    
REMARK 620 2 ASP E 367   OD1  81.1                                              
REMARK 620 3 ASP E 369   OD1  80.0  75.3                                        
REMARK 620 4 TYR E 371   O    78.8 156.4  89.1                                  
REMARK 620 5 ASP E 373   OD1 100.7  92.8 167.9 102.9                            
REMARK 620 6 ASP E 373   OD2 134.3 125.4 137.9  77.9  48.3                      
REMARK 620 7 HOH A 586   O   149.1 104.1  72.3  87.3 109.3  67.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E 426   OD1                                                    
REMARK 620 2 ASP E 428   OD1  80.4                                              
REMARK 620 3 ASN E 430   OD1  83.6  82.8                                        
REMARK 620 4 TYR E 432   O    76.7 157.1  92.6                                  
REMARK 620 5 ASP E 434   OD1  91.1  82.7 165.3  99.6                            
REMARK 620 6 ASP E 434   OD2 136.6 104.5 139.5  93.5  48.4                      
REMARK 620 7 HOH A 523   O   146.3  70.6  76.2 130.2 101.7  69.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 121   OG                                                     
REMARK 620 2 SER F 123   OG  100.8                                              
REMARK 620 3 GLU F 220   OE1  83.9 173.0                                        
REMARK 620 4 HOH C 465   O    73.8  83.0  93.5                                  
REMARK 620 5 HOH C 466   O   160.0  88.3  85.6  89.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F 123   O                                                      
REMARK 620 2 ASP F 126   OD1  66.9                                              
REMARK 620 3 ASP F 127   OD1  89.3  90.5                                        
REMARK 620 4 ASP F 251   OD2  75.5 141.9  83.9                                  
REMARK 620 5 HOH A 588   O   157.1 121.5  70.2  91.9                            
REMARK 620 6 HOH A 587   O    68.8  85.7 157.5  85.5 130.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA F2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 158   OD2                                                    
REMARK 620 2 ASN F 215   OD1 104.2                                              
REMARK 620 3 ASP F 217   O   159.2  92.7                                        
REMARK 620 4 ASP F 217   OD1  94.5  87.9  73.7                                  
REMARK 620 5 PRO F 219   O    85.6 169.5  78.6  95.2                            
REMARK 620 6 GLU F 220   OE2 101.2  89.4  90.9 164.2  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 458  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 470   O                                                      
REMARK 620 2 HOH C 472   O    90.8                                              
REMARK 620 3 HOH C 467   O    67.7  70.0                                        
REMARK 620 4 HOH C 468   O   146.4  81.1 136.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 458  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 474   O                                                      
REMARK 620 2 HOH A 605   O    77.0                                              
REMARK 620 3 HOH C 477   O    80.0  84.2                                        
REMARK 620 4 HOH C 473   O   124.2 151.1 116.6                                  
REMARK 620 5 HOH C 475   O   153.5  84.0  79.8  80.5                            
REMARK 620 6 HOH C 478   O    81.0  81.3 158.3  83.0 114.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 458  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 607   O                                                      
REMARK 620 2 HOH A 608   O    75.2                                              
REMARK 620 3 HOH C 484   O   136.8  71.9                                        
REMARK 620 N                    1     2                                         
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 NAG A3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2005                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2006                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C2007                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E2004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E2005                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E2006                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E2007                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG E3015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F2001                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F2002                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F2003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN F3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN F3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN F3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG F3371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 458                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 458                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 458                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC D 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC F 462                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VDO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VDP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VDQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TYE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3FCS   RELATED DB: PDB                                   
DBREF  3FCU A    1   457  UNP    Q17R67   Q17R67_HUMAN    32    488             
DBREF  3FCU B    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  3FCU C    1   457  UNP    Q17R67   Q17R67_HUMAN    32    488             
DBREF  3FCU D    1   461  UNP    P05106   ITB3_HUMAN      27    487             
DBREF  3FCU E    1   457  UNP    Q17R67   Q17R67_HUMAN    32    488             
DBREF  3FCU F    1   461  UNP    P05106   ITB3_HUMAN      27    487             
SEQRES   1 A  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  457  ALA SER                                                      
SEQRES   1 B  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 C  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  457  ALA SER                                                      
SEQRES   1 D  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  461  GLU CYS GLY VAL CYS ARG                                      
SEQRES   1 E  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 E  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 E  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 E  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 E  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 E  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 E  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 E  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 E  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 E  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 E  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 E  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 E  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 E  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 E  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 E  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 E  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 E  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 E  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 E  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 E  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 E  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 E  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 E  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 E  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 E  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 E  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 E  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 E  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 E  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 E  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 E  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 E  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 E  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 E  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 E  457  ALA SER                                                      
SEQRES   1 F  461  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 F  461  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 F  461  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 F  461  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 F  461  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 F  461  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 F  461  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 F  461  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 F  461  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 F  461  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 F  461  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 F  461  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 F  461  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 F  461  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 F  461  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 F  461  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 F  461  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 F  461  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 F  461  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 F  461  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 F  461  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 F  461  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 F  461  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 F  461  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 F  461  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 F  461  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 F  461  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 F  461  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 F  461  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 F  461  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 F  461  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 F  461  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 F  461  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 F  461  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 F  461  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 F  461  GLU CYS GLY VAL CYS ARG                                      
MODRES 3FCU ASN A   15  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN C   15  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN E   15  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN F  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3FCU ASN F  371  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    NAG  A3015      14                                                       
HET     MG  A 458       1                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    CAC  B 462       5                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    NAG  C3015      14                                                       
HET     MG  C 458       1                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3099      14                                                       
HET    NAG  D3320      14                                                       
HET    NAG  D3321      14                                                       
HET    MAN  D3322      11                                                       
HET    MAN  D3323      11                                                       
HET    NAG  D3371      14                                                       
HET    CAC  D 462       5                                                       
HET     CA  E2004       1                                                       
HET     CA  E2005       1                                                       
HET     CA  E2006       1                                                       
HET     CA  E2007       1                                                       
HET    NAG  E3015      14                                                       
HET     MG  E 458       1                                                       
HET     MG  F2001       1                                                       
HET     CA  F2002       1                                                       
HET     CA  F2003       1                                                       
HET    NAG  F3320      14                                                       
HET    NAG  F3321      14                                                       
HET    MAN  F3322      11                                                       
HET    MAN  F3323      11                                                       
HET    MAN  F3324      11                                                       
HET    NAG  F3371      14                                                       
HET    CAC  F 462       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     CAC CACODYLATE ION                                                   
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   7   CA    18(CA 2+)                                                    
FORMUL  11  NAG    14(C8 H15 N O6)                                              
FORMUL  12   MG    6(MG 2+)                                                     
FORMUL  17  MAN    8(C6 H12 O6)                                                 
FORMUL  19  CAC    3(C2 H6 AS O2 1-)                                            
FORMUL  45  HOH   *298(H2 O)                                                    
HELIX    1   1 LEU A  151  ASP A  159  1                                   9    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 ALA A  318  ARG A  320  5                                   3    
HELIX    7   7 TYR A  440  ALA A  442  5                                   3    
HELIX    8   8 ASN B    3  ARG B    8  1                                   6    
HELIX    9   9 SER B   12  SER B   20  1                                   9    
HELIX   10  10 LEU B   40  ASP B   47  1                                   8    
HELIX   11  11 ALA B   50  GLU B   52  5                                   3    
HELIX   12  12 SER B  121  ASP B  126  5                                   6    
HELIX   13  13 ASP B  127  LYS B  144  1                                  18    
HELIX   14  14 PRO B  169  ASN B  175  1                                   7    
HELIX   15  15 CYS B  177  LYS B  181  5                                   5    
HELIX   16  16 GLN B  199  LYS B  209  1                                  11    
HELIX   17  17 GLY B  221  CYS B  232  1                                  12    
HELIX   18  18 CYS B  232  GLY B  237  1                                   6    
HELIX   19  19 LEU B  258  GLY B  264  5                                   7    
HELIX   20  20 SER B  291  LYS B  302  1                                  12    
HELIX   21  21 VAL B  314  ILE B  325  1                                  12    
HELIX   22  22 SER B  337  GLY B  349  1                                  13    
HELIX   23  23 CYS B  435  ALA B  439  5                                   5    
HELIX   24  24 LEU C  151  ASP C  159  1                                   9    
HELIX   25  25 GLY C  187  LEU C  192  1                                   6    
HELIX   26  26 VAL C  200  TYR C  207  1                                   8    
HELIX   27  27 ASN C  227  PHE C  231  5                                   5    
HELIX   28  28 THR C  259  LEU C  264  1                                   6    
HELIX   29  29 ALA C  318  ARG C  320  5                                   3    
HELIX   30  30 TYR C  440  ALA C  442  5                                   3    
HELIX   31  31 CYS D    5  GLY D    9  5                                   5    
HELIX   32  32 SER D   12  SER D   20  1                                   9    
HELIX   33  33 LEU D   40  ASP D   47  1                                   8    
HELIX   34  34 ALA D   50  GLU D   52  5                                   3    
HELIX   35  35 SER D  121  LYS D  125  5                                   5    
HELIX   36  36 ASP D  127  LYS D  144  1                                  18    
HELIX   37  37 PRO D  170  ASN D  175  1                                   6    
HELIX   38  38 CYS D  177  LYS D  181  5                                   5    
HELIX   39  39 GLN D  199  LYS D  209  1                                  11    
HELIX   40  40 GLY D  221  CYS D  232  1                                  12    
HELIX   41  41 CYS D  232  GLY D  237  1                                   6    
HELIX   42  42 ASP D  259  GLY D  264  5                                   6    
HELIX   43  43 SER D  291  LYS D  302  1                                  12    
HELIX   44  44 VAL D  314  LEU D  324  1                                  11    
HELIX   45  45 SER D  337  GLY D  349  1                                  13    
HELIX   46  46 CYS D  435  ALA D  439  5                                   5    
HELIX   47  47 GLY E   44  GLU E   48  5                                   5    
HELIX   48  48 LEU E  151  ASP E  159  1                                   9    
HELIX   49  49 GLY E  187  LEU E  192  1                                   6    
HELIX   50  50 VAL E  200  TYR E  207  1                                   8    
HELIX   51  51 ASN E  227  PHE E  231  5                                   5    
HELIX   52  52 THR E  259  LEU E  264  1                                   6    
HELIX   53  53 ALA E  318  ARG E  320  5                                   3    
HELIX   54  54 ASN F    3  ARG F    8  1                                   6    
HELIX   55  55 SER F   12  SER F   20  1                                   9    
HELIX   56  56 LEU F   40  ASP F   47  1                                   8    
HELIX   57  57 SER F  121  ASP F  126  5                                   6    
HELIX   58  58 ASP F  127  THR F  146  1                                  20    
HELIX   59  59 PRO F  169  ASN F  175  1                                   7    
HELIX   60  60 CYS F  177  LYS F  181  5                                   5    
HELIX   61  61 GLN F  199  GLN F  210  1                                  12    
HELIX   62  62 GLY F  221  CYS F  232  1                                  12    
HELIX   63  63 CYS F  232  GLY F  237  1                                   6    
HELIX   64  64 LEU F  258  GLY F  264  5                                   7    
HELIX   65  65 SER F  291  LYS F  302  1                                  12    
HELIX   66  66 VAL F  314  ILE F  325  1                                  12    
HELIX   67  67 SER F  337  GLY F  349  1                                  13    
HELIX   68  68 CYS F  435  ALA F  439  5                                   5    
SHEET    1   A 5 GLY A  62  GLY A  63  0                                        
SHEET    2   A 5 THR A   9  ALA A  12  1  N  ALA A  12   O  GLY A  63           
SHEET    3   A 5 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    4   A 5 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    5   A 5 SER A 420  VAL A 425 -1  N  ARG A 422   O  ILE A 436           
SHEET    1   B 4 LEU A  23  LYS A  27  0                                        
SHEET    2   B 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3   B 4 GLY A  52  PRO A  57 -1  O  CYS A  56   N  ILE A  35           
SHEET    4   B 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1   C 4 GLU A  75  VAL A  79  0                                        
SHEET    2   C 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3   C 4 HIS A 112  GLU A 117 -1  O  ASN A 114   N  GLN A  85           
SHEET    4   C 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1   D 4 VAL A  97  TRP A 100  0                                        
SHEET    2   D 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3   D 4 SER A 129  GLN A 134 -1  O  PHE A 131   N  ALA A 106           
SHEET    4   D 4 ARG A 139  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1   E 4 SER A 173  VAL A 175  0                                        
SHEET    2   E 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3   E 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4   E 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1   F 4 VAL A 239  GLY A 242  0                                        
SHEET    2   F 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3   F 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4   F 4 ARG A 276  ARG A 281 -1  O  LEU A 277   N  ILE A 269           
SHEET    1   G 4 VAL A 293  THR A 296  0                                        
SHEET    2   G 4 ASP A 305  ALA A 310 -1  O  LEU A 307   N  ALA A 294           
SHEET    3   G 4 ARG A 327  PHE A 331 -1  O  ARG A 327   N  ALA A 310           
SHEET    4   G 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1   H 2 MET A 314  ARG A 317  0                                        
SHEET    2   H 2 LYS A 321  GLU A 324 -1  O  ALA A 323   N  GLU A 315           
SHEET    1   I 4 ILE A 360  GLY A 364  0                                        
SHEET    2   I 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  GLY A 364           
SHEET    3   I 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
SHEET    4   I 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1   J 2 GLY A 394  GLN A 395  0                                        
SHEET    2   J 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1   K 3 CYS B  38  ASP B  39  0                                        
SHEET    2   K 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   K 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   L 6 GLU B  60  GLU B  65  0                                        
SHEET    2   L 6 ARG B  87  LEU B  92 -1  O  ARG B  91   N  GLU B  60           
SHEET    3   L 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   L 6 LYS B 412  PRO B 418 -1  N  PHE B 414   O  VAL B 427           
SHEET    5   L 6 SER B 353  ARG B 360 -1  N  ARG B 360   O  THR B 415           
SHEET    6   L 6 SER B 385  LEU B 389 -1  O  LEU B 389   N  SER B 353           
SHEET    1   M 5 VAL B  83  SER B  84  0                                        
SHEET    2   M 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   M 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   M 5 LEU B 366  THR B 373 -1  N  THR B 373   O  SER B 396           
SHEET    5   M 5 VAL B 379  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   N 6 TYR B 190  THR B 197  0                                        
SHEET    2   N 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   N 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4   N 6 SER B 243  THR B 250  1  O  LEU B 245   N  ASP B 113           
SHEET    5   N 6 ILE B 304  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   N 6 THR B 329  VAL B 332  1  O  GLY B 331   N  PHE B 308           
SHEET    1   O 2 PHE B 455  GLU B 456  0                                        
SHEET    2   O 2 VAL B 459  CYS B 460 -1  O  VAL B 459   N  GLU B 456           
SHEET    1   P 5 GLY C  63  GLN C  64  0                                        
SHEET    2   P 5 LEU C   3  ALA C  12  1  N  ALA C  12   O  GLY C  63           
SHEET    3   P 5 GLN C 444  ALA C 450 -1  O  ARG C 449   N  ASP C   4           
SHEET    4   P 5 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    5   P 5 SER C 420  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1   Q 4 LEU C  23  LYS C  27  0                                        
SHEET    2   Q 4 VAL C  33  ALA C  39 -1  O  ALA C  34   N  HIS C  26           
SHEET    3   Q 4 GLY C  52  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    4   Q 4 SER C  67  LEU C  68 -1  O  LEU C  68   N  VAL C  53           
SHEET    1   R 4 GLU C  75  VAL C  79  0                                        
SHEET    2   R 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3   R 4 HIS C 112  GLU C 117 -1  O  HIS C 112   N  PHE C  87           
SHEET    4   R 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1   S 4 VAL C  97  TRP C 100  0                                        
SHEET    2   S 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3   S 4 SER C 129  ALA C 133 -1  O  PHE C 131   N  ALA C 106           
SHEET    4   S 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   T 4 SER C 172  VAL C 175  0                                        
SHEET    2   T 4 GLU C 180  ALA C 185 -1  O  GLY C 184   N  SER C 172           
SHEET    3   T 4 LEU C 194  PRO C 199 -1  O  ALA C 196   N  LEU C 183           
SHEET    4   T 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1   U 4 VAL C 239  GLY C 242  0                                        
SHEET    2   U 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3   U 4 ALA C 266  ASP C 271 -1  O  ALA C 266   N  ALA C 257           
SHEET    4   U 4 ARG C 276  ARG C 281 -1  O  LEU C 277   N  ILE C 269           
SHEET    1   V 4 VAL C 293  THR C 296  0                                        
SHEET    2   V 4 ASP C 305  ALA C 310 -1  O  LEU C 307   N  ALA C 294           
SHEET    3   V 4 ARG C 327  PHE C 331 -1  O  PHE C 331   N  LEU C 306           
SHEET    4   V 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1   W 2 MET C 314  ARG C 317  0                                        
SHEET    2   W 2 LYS C 321  GLU C 324 -1  O  ALA C 323   N  GLU C 315           
SHEET    1   X 4 ILE C 360  GLY C 364  0                                        
SHEET    2   X 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  GLY C 364           
SHEET    3   X 4 GLN C 388  PHE C 392 -1  O  GLN C 388   N  ALA C 378           
SHEET    4   X 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1   Y 2 GLY C 394  GLN C 395  0                                        
SHEET    2   Y 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1   Z 3 CYS D  38  ASP D  39  0                                        
SHEET    2   Z 3 ALA D  24  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3   Z 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  AA 6 GLU D  60  GLU D  65  0                                        
SHEET    2  AA 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3  AA 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4  AA 6 LYS D 412  PRO D 418 -1  N  ILE D 416   O  LEU D 425           
SHEET    5  AA 6 SER D 353  ARG D 360 -1  N  ARG D 360   O  THR D 415           
SHEET    6  AA 6 SER D 385  LEU D 389 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  AB 5 VAL D  83  SER D  84  0                                        
SHEET    2  AB 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  AB 5 THR D 394  VAL D 403 -1  O  VAL D 395   N  VAL D 104           
SHEET    4  AB 5 LEU D 366  THR D 373 -1  N  THR D 373   O  SER D 396           
SHEET    5  AB 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  AC 6 TYR D 190  THR D 197  0                                        
SHEET    2  AC 6 LEU D 149  PHE D 156 -1  N  ALA D 155   O  LYS D 191           
SHEET    3  AC 6 VAL D 112  ASP D 119  1  N  MET D 118   O  GLY D 154           
SHEET    4  AC 6 SER D 243  THR D 250  1  O  LEU D 245   N  ASP D 113           
SHEET    5  AC 6 ILE D 304  VAL D 310  1  O  ALA D 309   N  PHE D 248           
SHEET    6  AC 6 THR D 329  VAL D 332  1  O  THR D 329   N  PHE D 308           
SHEET    1  AD 2 PHE D 455  GLU D 456  0                                        
SHEET    2  AD 2 VAL D 459  CYS D 460 -1  O  VAL D 459   N  GLU D 456           
SHEET    1  AE 5 GLY E  63  GLN E  64  0                                        
SHEET    2  AE 5 THR E   9  ALA E  12  1  N  PHE E  10   O  GLY E  63           
SHEET    3  AE 5 GLN E 444  TYR E 448 -1  O  VAL E 447   N  THR E   9           
SHEET    4  AE 5 ASP E 434  ALA E 439 -1  N  LEU E 435   O  TYR E 448           
SHEET    5  AE 5 SER E 420  VAL E 425 -1  N  ARG E 422   O  ILE E 436           
SHEET    1  AF 3 LEU E  23  LYS E  27  0                                        
SHEET    2  AF 3 VAL E  33  ALA E  39 -1  O  ALA E  34   N  HIS E  26           
SHEET    3  AF 3 GLY E  52  PRO E  57 -1  O  CYS E  56   N  ILE E  35           
SHEET    1  AG 4 THR E  76  VAL E  79  0                                        
SHEET    2  AG 4 GLN E  82  PHE E  87 -1  O  LEU E  84   N  ARG E  77           
SHEET    3  AG 4 HIS E 112  GLU E 117 -1  O  HIS E 112   N  PHE E  87           
SHEET    4  AG 4 GLU E 120  GLU E 121 -1  O  GLU E 120   N  GLU E 117           
SHEET    1  AH 4 VAL E  97  TRP E 100  0                                        
SHEET    2  AH 4 VAL E 103  ALA E 108 -1  O  VAL E 105   N  VAL E  98           
SHEET    3  AH 4 SER E 129  GLN E 134 -1  O  SER E 129   N  ALA E 108           
SHEET    4  AH 4 ARG E 139  TYR E 143 -1  O  ALA E 141   N  LEU E 132           
SHEET    1  AI 4 SER E 173  VAL E 175  0                                        
SHEET    2  AI 4 GLU E 180  ALA E 185 -1  O  VAL E 182   N  VAL E 174           
SHEET    3  AI 4 LEU E 194  PRO E 199 -1  O  ALA E 196   N  LEU E 183           
SHEET    4  AI 4 SER E 220  LEU E 221 -1  O  SER E 220   N  GLN E 197           
SHEET    1  AJ 4 VAL E 239  GLY E 242  0                                        
SHEET    2  AJ 4 GLU E 252  ALA E 257 -1  O  VAL E 254   N  ALA E 240           
SHEET    3  AJ 4 ALA E 266  LEU E 270 -1  O  ALA E 266   N  ALA E 257           
SHEET    4  AJ 4 ARG E 276  ARG E 281 -1  O  LEU E 277   N  ILE E 269           
SHEET    1  AK 4 VAL E 293  THR E 296  0                                        
SHEET    2  AK 4 ASP E 305  ALA E 310 -1  O  LEU E 307   N  ALA E 294           
SHEET    3  AK 4 ARG E 327  PHE E 331 -1  O  ARG E 327   N  ALA E 310           
SHEET    4  AK 4 LEU E 345  THR E 348 -1  O  LEU E 347   N  VAL E 328           
SHEET    1  AL 2 MET E 314  SER E 316  0                                        
SHEET    2  AL 2 LEU E 322  GLU E 324 -1  O  ALA E 323   N  GLU E 315           
SHEET    1  AM 4 ILE E 360  GLY E 364  0                                        
SHEET    2  AM 4 ASP E 373  ALA E 378 -1  O  ASP E 373   N  GLY E 364           
SHEET    3  AM 4 GLN E 388  PHE E 392 -1  O  GLN E 388   N  ALA E 378           
SHEET    4  AM 4 GLN E 405  ASP E 408 -1  O  LEU E 407   N  VAL E 389           
SHEET    1  AN 2 GLY E 394  GLN E 395  0                                        
SHEET    2  AN 2 GLY E 398  LEU E 399 -1  O  GLY E 398   N  GLN E 395           
SHEET    1  AO 3 CYS F  38  ASP F  39  0                                        
SHEET    2  AO 3 ALA F  24  CYS F  26 -1  N  ALA F  24   O  ASP F  39           
SHEET    3  AO 3 ILE F  54  GLU F  55 -1  O  GLU F  55   N  TRP F  25           
SHEET    1  AP 6 GLU F  60  GLU F  65  0                                        
SHEET    2  AP 6 ARG F  87  LEU F  92 -1  O  ALA F  89   N  ARG F  62           
SHEET    3  AP 6 LEU F 425  PHE F 431  1  O  THR F 430   N  LEU F  90           
SHEET    4  AP 6 LYS F 412  PRO F 418 -1  N  PHE F 414   O  VAL F 427           
SHEET    5  AP 6 SER F 353  ARG F 360 -1  N  ARG F 360   O  THR F 415           
SHEET    6  AP 6 SER F 385  LEU F 389 -1  O  CYS F 386   N  VAL F 355           
SHEET    1  AQ 5 VAL F  83  SER F  84  0                                        
SHEET    2  AQ 5 SER F  97  ARG F 105 -1  O  GLN F 103   N  SER F  84           
SHEET    3  AQ 5 THR F 394  VAL F 403 -1  O  ILE F 399   N  PHE F 100           
SHEET    4  AQ 5 LEU F 366  THR F 373 -1  N  THR F 373   O  SER F 396           
SHEET    5  AQ 5 VAL F 379  PRO F 381 -1  O  ILE F 380   N  ALA F 372           
SHEET    1  AR 6 TYR F 190  THR F 197  0                                        
SHEET    2  AR 6 LEU F 149  PHE F 156 -1  N  ALA F 155   O  LYS F 191           
SHEET    3  AR 6 VAL F 112  ASP F 119  1  N  MET F 118   O  GLY F 154           
SHEET    4  AR 6 SER F 243  THR F 250  1  O  LEU F 245   N  ASP F 113           
SHEET    5  AR 6 ILE F 304  VAL F 310  1  O  ALA F 309   N  PHE F 248           
SHEET    6  AR 6 THR F 329  VAL F 332  1  O  GLY F 331   N  PHE F 308           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.03  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.05  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.03  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.03  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.04  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.04  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.06  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.04  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.04  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.05  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.04  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.04  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.04  
SSBOND  27 CYS E   56    CYS E   65                          1555   1555  2.03  
SSBOND  28 CYS E  107    CYS E  130                          1555   1555  2.05  
SSBOND  29 CYS E  146    CYS E  167                          1555   1555  2.03  
SSBOND  30 CYS F    5    CYS F   23                          1555   1555  2.04  
SSBOND  31 CYS F   13    CYS F  435                          1555   1555  2.04  
SSBOND  32 CYS F   16    CYS F   38                          1555   1555  2.03  
SSBOND  33 CYS F   26    CYS F   49                          1555   1555  2.03  
SSBOND  34 CYS F  177    CYS F  184                          1555   1555  2.04  
SSBOND  35 CYS F  232    CYS F  273                          1555   1555  2.04  
SSBOND  36 CYS F  374    CYS F  386                          1555   1555  2.04  
SSBOND  37 CYS F  406    CYS F  433                          1555   1555  2.03  
SSBOND  38 CYS F  437    CYS F  457                          1555   1555  2.03  
SSBOND  39 CYS F  448    CYS F  460                          1555   1555  2.03  
LINK         ND2 ASN A  15                 C1  NAG A3015     1555   1555  1.44  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.42  
LINK         OE2 GLU A 243                CA    CA A2004     1555   1555  2.78  
LINK         OD2 ASP A 245                CA    CA A2004     1555   1555  2.35  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.32  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.36  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.44  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.88  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.42  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.37  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.27  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.36  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.30  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.85  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.63  
LINK         OD2 ASP A 365                CA    CA A2006     1555   1555  2.59  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.25  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.51  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.36  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.78  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.66  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.29  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.32  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.26  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.39  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.76  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.69  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         OG  SER B 121                MG    MG B2001     1555   1555  2.27  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.24  
LINK         OG  SER B 123                MG    MG B2001     1555   1555  2.08  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.73  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.27  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.26  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.17  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.32  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.17  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.11  
LINK         OE1 GLU B 220                MG    MG B2001     1555   1555  2.00  
LINK         OE2 GLU B 220                CA    CA B2003     1555   1555  2.35  
LINK         OD2 ASP B 251                CA    CA B2002     1555   1555  2.33  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     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  2.41  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.60  
LINK         OD2 ASP C 245                CA    CA C2004     1555   1555  2.34  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.41  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.36  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.38  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.57  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.79  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.27  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.14  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.34  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.26  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.81  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.45  
LINK         OD2 ASP C 365                CA    CA C2006     1555   1555  2.43  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.36  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.49  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.25  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.76  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.64  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.37  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.41  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.25  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.24  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.71  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.74  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         OG  SER D 121                MG    MG D2001     1555   1555  2.21  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.19  
LINK         OG  SER D 123                MG    MG D2001     1555   1555  2.01  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.95  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.24  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.20  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.18  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.41  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.16  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.14  
LINK         OE1 GLU D 220                MG    MG D2001     1555   1555  2.13  
LINK         OE2 GLU D 220                CA    CA D2003     1555   1555  2.27  
LINK         OD2 ASP D 251                CA    CA D2002     1555   1555  2.48  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.45  
LINK         ND2 ASN E  15                 C1  NAG E3015     1555   1555  1.44  
LINK         OE1 GLU E 243                CA    CA E2004     1555   1555  2.65  
LINK         OE2 GLU E 243                CA    CA E2004     1555   1555  2.50  
LINK         OD2 ASP E 245                CA    CA E2004     1555   1555  2.21  
LINK         O   ASP E 247                CA    CA E2004     1555   1555  2.30  
LINK         O   THR E 250                CA    CA E2004     1555   1555  2.16  
LINK         OG1 THR E 250                CA    CA E2004     1555   1555  2.49  
LINK         OE1 GLU E 252                CA    CA E2004     1555   1555  2.63  
LINK         OE2 GLU E 252                CA    CA E2004     1555   1555  2.70  
LINK         OD1 ASP E 297                CA    CA E2005     1555   1555  2.21  
LINK         OD1 ASN E 299                CA    CA E2005     1555   1555  2.22  
LINK         OD1 ASP E 301                CA    CA E2005     1555   1555  2.32  
LINK         O   ARG E 303                CA    CA E2005     1555   1555  2.24  
LINK         OD1 ASP E 305                CA    CA E2005     1555   1555  2.90  
LINK         OD2 ASP E 305                CA    CA E2005     1555   1555  2.40  
LINK         OD2 ASP E 365                CA    CA E2006     1555   1555  2.47  
LINK         OD1 ASP E 367                CA    CA E2006     1555   1555  2.40  
LINK         OD1 ASP E 369                CA    CA E2006     1555   1555  2.44  
LINK         O   TYR E 371                CA    CA E2006     1555   1555  2.23  
LINK         OD1 ASP E 373                CA    CA E2006     1555   1555  2.70  
LINK         OD2 ASP E 373                CA    CA E2006     1555   1555  2.64  
LINK         OD1 ASP E 426                CA    CA E2007     1555   1555  2.37  
LINK         OD1 ASP E 428                CA    CA E2007     1555   1555  2.39  
LINK         OD1 ASN E 430                CA    CA E2007     1555   1555  2.37  
LINK         O   TYR E 432                CA    CA E2007     1555   1555  2.30  
LINK         OD1 ASP E 434                CA    CA E2007     1555   1555  2.78  
LINK         OD2 ASP E 434                CA    CA E2007     1555   1555  2.57  
LINK         OG  SER F 121                MG    MG F2001     1555   1555  2.25  
LINK         O   SER F 123                CA    CA F2002     1555   1555  2.29  
LINK         OG  SER F 123                MG    MG F2001     1555   1555  2.07  
LINK         OD1 ASP F 126                CA    CA F2002     1555   1555  2.95  
LINK         OD1 ASP F 127                CA    CA F2002     1555   1555  2.12  
LINK         OD2 ASP F 158                CA    CA F2003     1555   1555  2.21  
LINK         OD1 ASN F 215                CA    CA F2003     1555   1555  2.14  
LINK         O   ASP F 217                CA    CA F2003     1555   1555  2.40  
LINK         OD1 ASP F 217                CA    CA F2003     1555   1555  2.25  
LINK         O   PRO F 219                CA    CA F2003     1555   1555  2.14  
LINK         OE1 GLU F 220                MG    MG F2001     1555   1555  2.11  
LINK         OE2 GLU F 220                CA    CA F2003     1555   1555  2.29  
LINK         OD2 ASP F 251                CA    CA F2002     1555   1555  2.35  
LINK         ND2 ASN F 320                 C1  NAG F3320     1555   1555  1.44  
LINK         ND2 ASN F 371                 C1  NAG F3371     1555   1555  1.45  
LINK        CA    CA A2005                 O   HOH A 583     1555   1555  2.29  
LINK        CA    CA A2006                 O   HOH A 512     1555   1555  2.29  
LINK        CA    CA A2007                 O   HOH A 589     1555   1555  2.33  
LINK        MG    MG B2001                 O   HOH C 463     1555   1555  2.19  
LINK        MG    MG B2001                 O   HOH C 464     1555   1555  1.93  
LINK        CA    CA B2002                 O   HOH A 550     1555   1555  2.19  
LINK        CA    CA B2002                 O   HOH A 590     1555   1555  2.20  
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         O6  MAN B3322                 C1  MAN B3324     1555   1555  1.45  
LINK        CA    CA C2005                 O   HOH A 582     1555   1555  2.31  
LINK        CA    CA C2006                 O   HOH A 591     1555   1555  2.32  
LINK        CA    CA C2007                 O   HOH A 592     1555   1555  2.40  
LINK        MG    MG D2001                 O   HOH C 459     1555   1555  1.97  
LINK        MG    MG D2001                 O   HOH C 460     1555   1555  1.86  
LINK        CA    CA D2002                 O   HOH A 584     1555   1555  2.38  
LINK        CA    CA D2002                 O   HOH A 585     1555   1555  2.21  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O4  NAG D3321                 C1  MAN D3322     1555   1555  1.44  
LINK         O3  MAN D3322                 C1  MAN D3323     1555   1555  1.45  
LINK        CA    CA E2005                 O   HOH A 478     1555   1555  2.21  
LINK        CA    CA E2006                 O   HOH A 586     1555   1555  2.12  
LINK        CA    CA E2007                 O   HOH A 523     1555   1555  2.56  
LINK        MG    MG F2001                 O   HOH C 465     1555   1555  2.03  
LINK        MG    MG F2001                 O   HOH C 466     1555   1555  2.12  
LINK        CA    CA F2002                 O   HOH A 588     1555   1555  2.57  
LINK        CA    CA F2002                 O   HOH A 587     1555   1555  2.36  
LINK         O4  NAG F3320                 C1  NAG F3321     1555   1555  1.44  
LINK         O4  NAG F3321                 C1  MAN F3322     1555   1555  1.45  
LINK         O3  MAN F3322                 C1  MAN F3323     1555   1555  1.45  
LINK         O6  MAN F3322                 C1  MAN F3324     1555   1555  1.44  
LINK        MG    MG A 458                 O   HOH C 470     1555   1555  2.03  
LINK        MG    MG A 458                 O   HOH C 472     1555   1555  2.02  
LINK        MG    MG A 458                 O   HOH C 467     1555   1555  2.38  
LINK        MG    MG A 458                 O   HOH C 468     1555   1555  2.23  
LINK        MG    MG C 458                 O   HOH C 474     1555   1555  2.21  
LINK        MG    MG C 458                 O   HOH A 605     1555   1555  1.97  
LINK        MG    MG C 458                 O   HOH C 477     1555   1555  2.07  
LINK        MG    MG C 458                 O   HOH C 473     1555   1555  2.03  
LINK        MG    MG C 458                 O   HOH C 475     1555   1555  2.04  
LINK        MG    MG C 458                 O   HOH C 478     1555   1555  1.88  
LINK        MG    MG E 458                 O   HOH A 607     1555   1555  2.09  
LINK        MG    MG E 458                 O   HOH A 608     1555   1555  2.47  
LINK        MG    MG E 458                 O   HOH C 484     1555   1555  2.15  
CISPEP   1 SER A   29    HIS A   30          0        -0.66                     
CISPEP   2 SER B   84    PRO B   85          0         7.04                     
CISPEP   3 SER B  162    PRO B  163          0         3.97                     
CISPEP   4 SER B  168    PRO B  169          0        -5.61                     
CISPEP   5 SER D   84    PRO D   85          0         3.24                     
CISPEP   6 SER D  162    PRO D  163          0         5.38                     
CISPEP   7 SER D  168    PRO D  169          0        -5.89                     
CISPEP   8 SER F   84    PRO F   85          0         3.86                     
CISPEP   9 SER F  162    PRO F  163          0         5.78                     
CISPEP  10 SER F  168    PRO F  169          0        -6.49                     
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 583                                          
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 512                                          
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 589                                          
SITE     1 AC5  3 ASN A  15  THR D 195  LYS D 235                               
SITE     1 AC6  6 SER B 121  SER B 123  GLU B 220  CAC B 462                    
SITE     2 AC6  6 HOH C 463  HOH C 464                                          
SITE     1 AC7  6 HOH A 550  HOH A 590  SER B 123  ASP B 126                    
SITE     2 AC7  6 ASP B 127  ASP B 251                                          
SITE     1 AC8  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 AC8  5 GLU B 220                                                     
SITE     1 AC9  1 ASN B  99                                                     
SITE     1 BC1  3 MET A 285  ASN B 320  NAG B3321                               
SITE     1 BC2  4 ARG A 281  NAG B3320  MAN B3322  MAN B3324                    
SITE     1 BC3  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC4  2 ARG A 281  MAN B3322                                          
SITE     1 BC5  2 NAG B3321  MAN B3322                                          
SITE     1 BC6  3 ASN B 371  SER B 398  GLU B 400                               
SITE     1 BC7  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 BC7  5 GLU C 252                                                     
SITE     1 BC8  6 HOH A 582  ASP C 297  ASN C 299  ASP C 301                    
SITE     2 BC8  6 ARG C 303  ASP C 305                                          
SITE     1 BC9  6 HOH A 591  ASP C 365  ASP C 367  ASP C 369                    
SITE     2 BC9  6 TYR C 371  ASP C 373                                          
SITE     1 CC1  6 HOH A 592  ASP C 426  ASP C 428  ASN C 430                    
SITE     2 CC1  6 TYR C 432  ASP C 434                                          
SITE     1 CC2  1 ASN C  15                                                     
SITE     1 CC3  6 HOH C 459  HOH C 460  SER D 121  SER D 123                    
SITE     2 CC3  6 GLU D 220  CAC D 462                                          
SITE     1 CC4  6 HOH A 584  HOH A 585  SER D 123  ASP D 126                    
SITE     2 CC4  6 ASP D 127  ASP D 251                                          
SITE     1 CC5  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 CC5  5 GLU D 220                                                     
SITE     1 CC6  1 ASN D  99                                                     
SITE     1 CC7  4 MET C 285  LEU D 317  ASN D 320  NAG D3321                    
SITE     1 CC8  2 NAG D3320  MAN D3322                                          
SITE     1 CC9  2 NAG D3321  MAN D3323                                          
SITE     1 DC1  2 ARG C 281  MAN D3322                                          
SITE     1 DC2  5 HOH A 649  ASN D 371  SER D 398  ILE D 399                    
SITE     2 DC2  5 GLU D 400                                                     
SITE     1 DC3  5 GLU E 243  ASP E 245  ASP E 247  THR E 250                    
SITE     2 DC3  5 GLU E 252                                                     
SITE     1 DC4  6 HOH A 478  ASP E 297  ASN E 299  ASP E 301                    
SITE     2 DC4  6 ARG E 303  ASP E 305                                          
SITE     1 DC5  6 HOH A 586  ASP E 365  ASP E 367  ASP E 369                    
SITE     2 DC5  6 TYR E 371  ASP E 373                                          
SITE     1 DC6  6 HOH A 523  ASP E 426  ASP E 428  ASN E 430                    
SITE     2 DC6  6 TYR E 432  ASP E 434                                          
SITE     1 DC7  1 ASN E  15                                                     
SITE     1 DC8  6 HOH C 465  HOH C 466  SER F 121  SER F 123                    
SITE     2 DC8  6 GLU F 220  CAC F 462                                          
SITE     1 DC9  6 HOH A 587  HOH A 588  SER F 123  ASP F 126                    
SITE     2 DC9  6 ASP F 127  ASP F 251                                          
SITE     1 EC1  5 ASP F 158  ASN F 215  ASP F 217  PRO F 219                    
SITE     2 EC1  5 GLU F 220                                                     
SITE     1 EC2  2 ASN F 320  NAG F3321                                          
SITE     1 EC3  2 NAG F3320  MAN F3322                                          
SITE     1 EC4  3 NAG F3321  MAN F3323  MAN F3324                               
SITE     1 EC5  2 ARG E 281  MAN F3322                                          
SITE     1 EC6  1 MAN F3322                                                     
SITE     1 EC7  3 ASN F 371  SER F 398  GLU F 400                               
SITE     1 EC8  6 SER A  99  HOH C 467  HOH C 468  HOH C 469                    
SITE     2 EC8  6 HOH C 470  HOH C 472                                          
SITE     1 EC9  7 HOH A 605  ASP C  24  HOH C 473  HOH C 474                    
SITE     2 EC9  7 HOH C 475  HOH C 477  HOH C 478                               
SITE     1 FC1  5 HOH A 606  HOH A 607  HOH A 608  HOH A 609                    
SITE     2 FC1  5 HOH C 484                                                     
SITE     1 FC2  8 SER B 121  TYR B 122  SER B 123  ARG B 214                    
SITE     2 FC2  8 ASN B 215  ASP B 217  GLU B 220   MG B2001                    
SITE     1 FC3  9 HOH C 460  SER D 121  TYR D 122  SER D 123                    
SITE     2 FC3  9 ARG D 214  ASN D 215  ASP D 217  GLU D 220                    
SITE     3 FC3  9  MG D2001                                                     
SITE     1 FC4  9 HOH C 466  SER F 121  TYR F 122  SER F 123                    
SITE     2 FC4  9 ARG F 214  ASN F 215  ASP F 217  GLU F 220                    
SITE     3 FC4  9  MG F2001                                                     
CRYST1  332.093  332.093   88.288  90.00  90.00 120.00 P 62         18          
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      0.003011  0.001739  0.000000        0.00000                         
SCALE2      0.000000  0.003477  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011327        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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