HEADER    TEXTURE OF CONNECTIVE TISSUE            20-NOV-77   4HYA              
TITLE     HYALURONIC ACID, THE ROLE OF DIVALENT CATIONS IN CONFORMATION AND     
TITLE    2 PACKING                                                              
CAVEAT     4HYA    GCU A 1 HAS WRONG CHIRALITY AT ATOM C1 GCU A 3 HAS WRONG     
CAVEAT   2 4HYA    CHIRALITY AT ATOM C1 GCU A 5 HAS WRONG CHIRALITY AT ATOM C1  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE-(1-4)-ALPHA-D-    
COMPND   3 GLUCOPYRANURONIC ACID-(1-3)-2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE-
COMPND   4 (1-4)-ALPHA-D-GLUCOPYRANURONIC ACID-(1-3)-2-ACETAMIDO-2-DEOXY-BETA-D-
COMPND   5 GLUCOPYRANOSE-(1-4)-ALPHA-D-GLUCOPYRANURONIC ACID;                   
COMPND   6 CHAIN: A;                                                            
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1                                                             
KEYWDS    TEXTURE OF CONNECTIVE TISSUE                                          
EXPDTA    FIBER DIFFRACTION                                                     
AUTHOR    S.ARNOTT                                                              
REVDAT  12   28-FEB-24 4HYA    1       HETSYN                                   
REVDAT  11   29-JUL-20 4HYA    1       CAVEAT COMPND REMARK DBREF               
REVDAT  11 2                   1       HETNAM LINK   SITE   ATOM                
REVDAT  10   04-FEB-15 4HYA    1       LINK                                     
REVDAT   9   13-JUL-11 4HYA    1       VERSN                                    
REVDAT   8   25-AUG-09 4HYA    1       SOURCE                                   
REVDAT   7   24-FEB-09 4HYA    1       VERSN                                    
REVDAT   6   01-APR-03 4HYA    1       JRNL                                     
REVDAT   5   15-JUL-92 4HYA    1       FORMUL                                   
REVDAT   4   30-SEP-83 4HYA    1       REVDAT                                   
REVDAT   3   06-JAN-82 4HYA    3       ORIGX  SCALE  HETATM                     
REVDAT   2   01-OCT-80 4HYA    1       REMARK                                   
REVDAT   1   28-MAR-80 4HYA    0                                                
JRNL        AUTH   W.T.WINTER,S.ARNOTT                                          
JRNL        TITL   HYALURONIC ACID: THE ROLE OF DIVALENT CATIONS IN             
JRNL        TITL 2 CONFORMATION AND PACKING.                                    
JRNL        REF    J.MOL.BIOL.                   V. 117   761 1977              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   609101                                                       
JRNL        DOI    10.1016/0022-2836(77)90068-7                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.J.C.SMITH,S.ARNOTT                                         
REMARK   1  TITL   LALS, A LINKED-ATOM LEAST-SQUARES RECIPROCAL-SPACE           
REMARK   1  TITL 2 REFINEMENT SYSTEM INCORPORATING STEREOCHEMICAL RESTRAINTS TO 
REMARK   1  TITL 3 SUPPLEMENT SPARSE DIFFRACTION DATA                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.A      V.  34     3 1978              
REMARK   1  REFN                   ISSN 0108-7673                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.T.WINTER,P.J.C.SMITH,S.ARNOTT                              
REMARK   1  TITL   HYALURONIC ACID, STRUCTURE OF A FULLY EXTENDED 3-FOLD        
REMARK   1  TITL 2 HELICAL SODIUM SALT AND COMPARISON WITH THE LESS EXTENDED    
REMARK   1  TITL 3 4-FOLD HELICAL FORMS                                         
REMARK   1  REF    J.MOL.BIOL.                   V.  99   219 1975              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.M.GUSS,D.W.L.HUKINS,P.J.C.SMITH,W.T.WINTER,S.ARNOTT,       
REMARK   1  AUTH 2 R.MOORHOUSE,D.A.REES                                         
REMARK   1  TITL   HYALURONIC ACID, MOLECULAR CONFORMATIONS AND INTERACTIONS IN 
REMARK   1  TITL 2 TWO SODIUM SALTS                                             
REMARK   1  REF    J.MOL.BIOL.                   V.  95   384 1975              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : LINKED-ATOM LEAST-SQUARES MODEL-BUILDING PROCEDURE   
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 0                                       
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 81                                      
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000179345.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : FIBER DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 205                                                                      
REMARK 205 FIBER DIFFRACTION                                                    
REMARK 205 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM FIBER              
REMARK 205 DIFFRACTION DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE             
REMARK 205 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE                   
REMARK 205 VALUES ON THESE RECORDS ARE MEANINGLESS.                             
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: UNKNOWN                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O1   GCU A     1     C3   NAG A     6     1554     1.43            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A    6                                                       
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 A   9  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCU A   1   O6A                                                    
REMARK 620 2 HOH A  12   O    80.7                                              
REMARK 620 3 HOH A  15   O    57.7 102.4                                        
REMARK 620 4 HOH A  18   O    55.0  74.7 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   8  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCU A   3   O6A                                                    
REMARK 620 2 HOH A  11   O    77.4                                              
REMARK 620 3 HOH A  14   O    68.9 106.4                                        
REMARK 620 4 HOH A  17   O    74.7 118.6 112.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A   7  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GCU A   5   O6A                                                    
REMARK 620 2 HOH A  10   O    61.6                                              
REMARK 620 3 HOH A  13   O   117.0 171.5                                        
REMARK 620 4 HOH A  16   O    88.5  61.2 127.2                                  
REMARK 620 N                    1     2     3                                   
HET    GCU  A   1      18                                                       
HET    NAG  A   2      25                                                       
HET    GCU  A   3      17                                                       
HET    NAG  A   4      25                                                       
HET    GCU  A   5      17                                                       
HET    NAG  A   6      24                                                       
HET     CA  A   7       1                                                       
HET     CA  A   8       1                                                       
HET     CA  A   9       1                                                       
HETNAM     GCU ALPHA-D-GLUCOPYRANURONIC ACID                                    
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     GCU ALPHA-D-GLUCURONIC ACID; D-GLUCURONIC ACID; GLUCURONIC           
HETSYN   2 GCU  ACID                                                            
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   1  GCU    3(C6 H10 O7)                                                 
FORMUL   1  NAG    3(C8 H15 N O6)                                               
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   5  HOH   *9(H2 O)                                                      
LINK         O4  GCU A   1                 C1  NAG A   2     1555   1555  1.39  
LINK         O3  NAG A   2                 C1  GCU A   3     1555   1555  1.39  
LINK         O4  GCU A   3                 C1  NAG A   4     1555   1555  1.39  
LINK         O3  NAG A   4                 C1  GCU A   5     1555   1555  1.39  
LINK         O4  GCU A   5                 C1  NAG A   6     1555   1555  1.39  
LINK         O6A GCU A   1                CA    CA A   9     1555   1555  2.92  
LINK         O6A GCU A   3                CA    CA A   8     1555   1555  2.51  
LINK         O6A GCU A   5                CA    CA A   7     1555   1555  2.77  
LINK        CA    CA A   7                 O   HOH A  10     1555   1555  2.55  
LINK        CA    CA A   7                 O   HOH A  13     1555   1555  2.51  
LINK        CA    CA A   7                 O   HOH A  16     1555   1555  2.52  
LINK        CA    CA A   8                 O   HOH A  11     1555   1555  2.47  
LINK        CA    CA A   8                 O   HOH A  14     1555   1555  2.57  
LINK        CA    CA A   8                 O   HOH A  17     1555   1555  2.56  
LINK        CA    CA A   9                 O   HOH A  12     1555   1555  2.67  
LINK        CA    CA A   9                 O   HOH A  15     1555   1555  2.44  
LINK        CA    CA A   9                 O   HOH A  18     1555   1555  2.52  
CRYST1   20.930   20.930   28.300  90.00  90.00 120.00 P 32 1 2     18          
ORIGX1      0.047778  0.027585  0.000000        0.00000                         
ORIGX2      0.000000  0.055170  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  0.035336        0.00000                         
SCALE1      0.047778  0.027585  0.000000        0.00000                         
SCALE2      0.000000  0.055170  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.035336        0.00000                         
HETATM    1  C1  GCU A   1       7.359  13.511  -8.694  1.00  0.00           C  
HETATM    2  C2  GCU A   1       7.289  14.655  -7.689  1.00  0.00           C  
HETATM    3  C3  GCU A   1       8.176  14.365  -6.489  1.00  0.00           C  
HETATM    4  C4  GCU A   1       7.836  13.004  -5.895  1.00  0.00           C  
HETATM    5  C5  GCU A   1       7.862  11.936  -6.984  1.00  0.00           C  
HETATM    6  C6  GCU A   1       7.422  10.578  -6.481  1.00  0.00           C  
HETATM    7  O1  GCU A   1       6.438  13.758  -9.704  1.00  0.00           O  
HETATM    8  O2  GCU A   1       7.680  15.866  -8.326  1.00  0.00           O  
HETATM    9  O3  GCU A   1       7.991  15.382  -5.502  1.00  0.00           O  
HETATM   10  O4  GCU A   1       8.780  12.652  -4.887  1.00  0.00           O  
HETATM   11  O5  GCU A   1       6.973  12.295  -8.051  1.00  0.00           O  
HETATM   12  O6A GCU A   1       7.750   9.614  -7.205  1.00  0.00           O  
HETATM   13  O6B GCU A   1       6.784  10.595  -5.405  1.00  0.00           O  
HETATM   14  H1  GCU A   1       8.389  13.417  -9.070  1.00  0.00           H  
HETATM   15  H2  GCU A   1       6.250  14.787  -7.355  1.00  0.00           H  
HETATM   16  H3  GCU A   1       9.230  14.377  -6.800  1.00  0.00           H  
HETATM   17  H4  GCU A   1       6.835  13.042  -5.442  1.00  0.00           H  
HETATM   18  H5  GCU A   1       8.887  11.836  -7.375  1.00  0.00           H  
HETATM   19  C1  NAG A   2       8.486  13.060  -3.594  1.00  0.00           C  
HETATM   20  C2  NAG A   2       8.988  11.994  -2.626  1.00  0.00           C  
HETATM   21  C3  NAG A   2       8.821  12.458  -1.189  1.00  0.00           C  
HETATM   22  C4  NAG A   2       9.472  13.821  -0.993  1.00  0.00           C  
HETATM   23  C5  NAG A   2       8.964  14.802  -2.043  1.00  0.00           C  
HETATM   24  C6  NAG A   2       9.658  16.145  -1.975  1.00  0.00           C  
HETATM   25  C7  NAG A   2       8.957   9.551  -2.938  1.00  0.00           C  
HETATM   26  C8  NAG A   2       8.078   8.347  -3.181  1.00  0.00           C  
HETATM   27  N2  NAG A   2       8.251  10.734  -2.861  1.00  0.00           N  
HETATM   28  O3  NAG A   2       9.422  11.508  -0.306  1.00  0.00           O  
HETATM   29  O4  NAG A   2       9.162  14.339   0.300  1.00  0.00           O  
HETATM   30  O5  NAG A   2       9.195  14.280  -3.362  1.00  0.00           O  
HETATM   31  O6  NAG A   2      10.045  16.609  -3.269  1.00  0.00           O  
HETATM   32  O7  NAG A   2      10.168   9.483  -2.824  1.00  0.00           O  
HETATM   33  H1  NAG A   2       7.432  13.188  -3.433  1.00  0.00           H  
HETATM   34  H2  NAG A   2      10.051  11.789  -2.824  1.00  0.00           H  
HETATM   35  H3  NAG A   2       7.750  12.525  -0.945  1.00  0.00           H  
HETATM   36  H4  NAG A   2      10.564  13.723  -1.081  1.00  0.00           H  
HETATM   37  H5  NAG A   2       7.885  14.970  -1.899  1.00  0.00           H  
HETATM   38  H61 NAG A   2      10.561  16.060  -1.356  1.00  0.00           H  
HETATM   39  H62 NAG A   2       8.978  16.888  -1.531  1.00  0.00           H  
HETATM   40  H81 NAG A   2       7.692   7.975  -2.222  1.00  0.00           H  
HETATM   41  H82 NAG A   2       7.238   8.632  -3.829  1.00  0.00           H  
HETATM   42  H83 NAG A   2       8.664   7.557  -3.671  1.00  0.00           H  
HETATM   43  HN2 NAG A   2       7.305  10.749  -2.957  1.00  0.00           H  
HETATM   44  C1  GCU A   3       8.610  10.997   0.699  1.00  0.00           C  
HETATM   45  C2  GCU A   3       9.440  10.866   1.970  1.00  0.00           C  
HETATM   46  C3  GCU A   3       8.564  10.446   3.138  1.00  0.00           C  
HETATM   47  C4  GCU A   3       7.375  11.389   3.274  1.00  0.00           C  
HETATM   48  C5  GCU A   3       6.644  11.512   1.939  1.00  0.00           C  
HETATM   49  C6  GCU A   3       5.520  12.523   1.978  1.00  0.00           C  
HETATM   50  O2  GCU A   3      10.483   9.924   1.755  1.00  0.00           O  
HETATM   51  O3  GCU A   3       9.330  10.464   4.344  1.00  0.00           O  
HETATM   52  O4  GCU A   3       6.457  10.897   4.251  1.00  0.00           O  
HETATM   53  O5  GCU A   3       7.557  11.940   0.917  1.00  0.00           O  
HETATM   54  O6A GCU A   3       4.553  12.269   1.228  1.00  0.00           O  
HETATM   55  O6B GCU A   3       5.701  13.486   2.756  1.00  0.00           O  
HETATM   56  H1  GCU A   3       8.178  10.018   0.441  1.00  0.00           H  
HETATM   57  H2  GCU A   3       9.917  11.833   2.196  1.00  0.00           H  
HETATM   58  H3  GCU A   3       8.201   9.420   2.977  1.00  0.00           H  
HETATM   59  H4  GCU A   3       7.726  12.382   3.591  1.00  0.00           H  
HETATM   60  H5  GCU A   3       6.215  10.537   1.664  1.00  0.00           H  
HETATM   61  C1  NAG A   4       6.957  10.709   5.530  1.00  0.00           C  
HETATM   62  C2  NAG A   4       5.882  11.109   6.532  1.00  0.00           C  
HETATM   63  C3  NAG A   4       6.326  10.787   7.949  1.00  0.00           C  
HETATM   64  C4  NAG A   4       6.750   9.328   8.054  1.00  0.00           C  
HETATM   65  C5  NAG A   4       7.774   9.000   6.970  1.00  0.00           C  
HETATM   66  C6  NAG A   4       8.150   7.533   6.948  1.00  0.00           C  
HETATM   67  C7  NAG A   4       4.306  12.947   6.085  1.00  0.00           C  
HETATM   68  C8  NAG A   4       4.155  14.446   5.966  1.00  0.00           C  
HETATM   69  N2  NAG A   4       5.594  12.552   6.387  1.00  0.00           N  
HETATM   70  O3  NAG A   4       5.253  11.042   8.858  1.00  0.00           O  
HETATM   71  O4  NAG A   4       7.335   9.068   9.328  1.00  0.00           O  
HETATM   72  O5  NAG A   4       7.243   9.315   5.674  1.00  0.00           O  
HETATM   73  O6  NAG A   4       9.527   7.334   7.267  1.00  0.00           O  
HETATM   74  O7  NAG A   4       3.381  12.168   5.929  1.00  0.00           O  
HETATM   75  H1  NAG A   4       7.873  11.291   5.719  1.00  0.00           H  
HETATM   76  H2  NAG A   4       4.952  10.567   6.305  1.00  0.00           H  
HETATM   77  H3  NAG A   4       7.173  11.434   8.227  1.00  0.00           H  
HETATM   78  H4  NAG A   4       5.868   8.680   7.932  1.00  0.00           H  
HETATM   79  H5  NAG A   4       8.693   9.580   7.146  1.00  0.00           H  
HETATM   80  H61 NAG A   4       7.964   7.123   5.943  1.00  0.00           H  
HETATM   81  H62 NAG A   4       7.542   6.988   7.686  1.00  0.00           H  
HETATM   82  H81 NAG A   4       3.981  14.878   6.965  1.00  0.00           H  
HETATM   83  H82 NAG A   4       5.071  14.874   5.535  1.00  0.00           H  
HETATM   84  H83 NAG A   4       3.301  14.678   5.315  1.00  0.00           H  
HETATM   85  HN2 NAG A   4       6.286  13.190   6.501  1.00  0.00           H  
HETATM   86  C1  GCU A   5       5.550  11.831   9.962  1.00  0.00           C  
HETATM   87  C2  GCU A   5       4.333  11.854  10.879  1.00  0.00           C  
HETATM   88  C3  GCU A   5       4.653  12.587  12.172  1.00  0.00           C  
HETATM   89  C4  GCU A   5       5.896  11.996  12.820  1.00  0.00           C  
HETATM   90  C5  GCU A   5       7.063  11.911  11.812  1.00  0.00           C  
HETATM   91  C6  GCU A   5       8.276  11.263  12.361  1.00  0.00           C  
HETATM   92  O2  GCU A   5       3.246  12.478  10.199  1.00  0.00           O  
HETATM   93  O3  GCU A   5       3.544  12.480  13.069  1.00  0.00           O  
HETATM   94  O4  GCU A   5       6.304  12.790  13.932  1.00  0.00           O  
HETATM   95  O5  GCU A   5       6.642  11.211  10.646  1.00  0.00           O  
HETATM   96  O6A GCU A   5       9.363  11.740  11.971  1.00  0.00           O  
HETATM   97  O6B GCU A   5       8.048  10.310  13.137  1.00  0.00           O  
HETATM   98  H1  GCU A   5       5.824  12.860   9.690  1.00  0.00           H  
HETATM   99  H2  GCU A   5       4.023  10.825  11.105  1.00  0.00           H  
HETATM  100  H3  GCU A   5       4.820  13.652  11.960  1.00  0.00           H  
HETATM  101  H4  GCU A   5       5.677  10.979  13.176  1.00  0.00           H  
HETATM  102  H5  GCU A   5       7.319  12.971  11.524  1.00  0.00           H  
HETATM  103  C1  NAG A   6       6.180  12.208  15.186  1.00  0.00           C  
HETATM  104  C2  NAG A   6       6.510  13.259  16.239  1.00  0.00           C  
HETATM  105  C3  NAG A   6       6.253  12.715  17.637  1.00  0.00           C  
HETATM  106  C4  NAG A   6       4.834  12.172  17.736  1.00  0.00           C  
HETATM  107  C5  NAG A   6       4.570  11.182  16.606  1.00  0.00           C  
HETATM  108  C6  NAG A   6       3.137  10.691  16.584  1.00  0.00           C  
HETATM  109  C7  NAG A   6       8.258  14.996  16.292  1.00  0.00           C  
HETATM  110  C8  NAG A   6       9.730  15.273  16.108  1.00  0.00           C  
HETATM  111  N2  NAG A   6       7.925  13.672  16.089  1.00  0.00           N  
HETATM  112  O4  NAG A   6       4.645  11.501  18.981  1.00  0.00           O  
HETATM  113  O5  NAG A   6       4.818  11.804  15.336  1.00  0.00           O  
HETATM  114  O6  NAG A   6       2.320  11.392  17.518  1.00  0.00           O  
HETATM  115  O7  NAG A   6       7.447  15.857  16.592  1.00  0.00           O  
HETATM  116  H1  NAG A   6       6.838  11.336  15.319  1.00  0.00           H  
HETATM  117  H2  NAG A   6       5.893  14.155  16.072  1.00  0.00           H  
HETATM  118  H3  NAG A   6       6.972  11.912  17.857  1.00  0.00           H  
HETATM  119  H4  NAG A   6       4.116  13.002  17.673  1.00  0.00           H  
HETATM  120  H5  NAG A   6       5.226  10.306  16.725  1.00  0.00           H  
HETATM  121  H61 NAG A   6       2.714  10.837  15.579  1.00  0.00           H  
HETATM  122  H62 NAG A   6       3.112   9.621  16.839  1.00  0.00           H  
HETATM  123  H81 NAG A   6      10.265  15.064  17.045  1.00  0.00           H  
HETATM  124  H82 NAG A   6      10.128  14.631  15.307  1.00  0.00           H  
HETATM  125  H83 NAG A   6       9.873  16.331  15.831  1.00  0.00           H  
HETATM  126  HN2 NAG A   6       8.584  13.031  15.856  1.00  0.00           H  
HETATM  127 CA    CA A   7      10.465  11.858   9.432  0.50  0.00          CA  
HETATM  128 CA    CA A   8       3.006  13.819   0.000  0.50  0.00          CA  
HETATM  129 CA    CA A   9       7.524   7.740  -9.432  0.50  0.00          CA  
HETATM  130  O   HOH A  10       9.926  14.046  10.624  1.00  0.00           O  
HETATM  131  O   HOH A  11       1.447  12.472   1.370  1.00  0.00           O  
HETATM  132  O   HOH A  12       9.580   6.634  -8.145  1.00  0.00           O  
HETATM  133  O   HOH A  13      11.312   9.706   8.456  1.00  0.00           O  
HETATM  134  O   HOH A  14       4.150  12.181  -1.616  1.00  0.00           O  
HETATM  135  O   HOH A  15       8.272  10.038  -9.735  1.00  0.00           O  
HETATM  136  O   HOH A  16       8.455  13.179   8.691  1.00  0.00           O  
HETATM  137  O   HOH A  17       4.681  15.340   1.189  1.00  0.00           O  
HETATM  138  O   HOH A  18       6.694   7.314  -7.095  1.00  0.00           O  
CONECT    1    2    7   11   14                                                 
CONECT    2    1    3    8   15                                                 
CONECT    3    2    4    9   16                                                 
CONECT    4    3    5   10   17                                                 
CONECT    5    4    6   11   18                                                 
CONECT    6    5   12   13                                                      
CONECT    7    1                                                                
CONECT    8    2                                                                
CONECT    9    3                                                                
CONECT   10    4   19                                                           
CONECT   11    1    5                                                           
CONECT   12    6  129                                                           
CONECT   13    6                                                                
CONECT   14    1                                                                
CONECT   15    2                                                                
CONECT   16    3                                                                
CONECT   17    4                                                                
CONECT   18    5                                                                
CONECT   19   10   20   30   33                                                 
CONECT   20   19   21   27   34                                                 
CONECT   21   20   22   28   35                                                 
CONECT   22   21   23   29   36                                                 
CONECT   23   22   24   30   37                                                 
CONECT   24   23   31   38   39                                                 
CONECT   25   26   27   32                                                      
CONECT   26   25   40   41   42                                                 
CONECT   27   20   25   43                                                      
CONECT   28   21   44                                                           
CONECT   29   22                                                                
CONECT   30   19   23                                                           
CONECT   31   24                                                                
CONECT   32   25                                                                
CONECT   33   19                                                                
CONECT   34   20                                                                
CONECT   35   21                                                                
CONECT   36   22                                                                
CONECT   37   23                                                                
CONECT   38   24                                                                
CONECT   39   24                                                                
CONECT   40   26                                                                
CONECT   41   26                                                                
CONECT   42   26                                                                
CONECT   43   27                                                                
CONECT   44   28   45   53   56                                                 
CONECT   45   44   46   50   57                                                 
CONECT   46   45   47   51   58                                                 
CONECT   47   46   48   52   59                                                 
CONECT   48   47   49   53   60                                                 
CONECT   49   48   54   55                                                      
CONECT   50   45                                                                
CONECT   51   46                                                                
CONECT   52   47   61                                                           
CONECT   53   44   48                                                           
CONECT   54   49  128                                                           
CONECT   55   49                                                                
CONECT   56   44                                                                
CONECT   57   45                                                                
CONECT   58   46                                                                
CONECT   59   47                                                                
CONECT   60   48                                                                
CONECT   61   52   62   72   75                                                 
CONECT   62   61   63   69   76                                                 
CONECT   63   62   64   70   77                                                 
CONECT   64   63   65   71   78                                                 
CONECT   65   64   66   72   79                                                 
CONECT   66   65   73   80   81                                                 
CONECT   67   68   69   74                                                      
CONECT   68   67   82   83   84                                                 
CONECT   69   62   67   85                                                      
CONECT   70   63   86                                                           
CONECT   71   64                                                                
CONECT   72   61   65                                                           
CONECT   73   66                                                                
CONECT   74   67                                                                
CONECT   75   61                                                                
CONECT   76   62                                                                
CONECT   77   63                                                                
CONECT   78   64                                                                
CONECT   79   65                                                                
CONECT   80   66                                                                
CONECT   81   66                                                                
CONECT   82   68                                                                
CONECT   83   68                                                                
CONECT   84   68                                                                
CONECT   85   69                                                                
CONECT   86   70   87   95   98                                                 
CONECT   87   86   88   92   99                                                 
CONECT   88   87   89   93  100                                                 
CONECT   89   88   90   94  101                                                 
CONECT   90   89   91   95  102                                                 
CONECT   91   90   96   97                                                      
CONECT   92   87                                                                
CONECT   93   88                                                                
CONECT   94   89  103                                                           
CONECT   95   86   90                                                           
CONECT   96   91  127                                                           
CONECT   97   91                                                                
CONECT   98   86                                                                
CONECT   99   87                                                                
CONECT  100   88                                                                
CONECT  101   89                                                                
CONECT  102   90                                                                
CONECT  103   94  104  113  116                                                 
CONECT  104  103  105  111  117                                                 
CONECT  105  104  106  118                                                      
CONECT  106  105  107  112  119                                                 
CONECT  107  106  108  113  120                                                 
CONECT  108  107  114  121  122                                                 
CONECT  109  110  111  115                                                      
CONECT  110  109  123  124  125                                                 
CONECT  111  104  109  126                                                      
CONECT  112  106                                                                
CONECT  113  103  107                                                           
CONECT  114  108                                                                
CONECT  115  109                                                                
CONECT  116  103                                                                
CONECT  117  104                                                                
CONECT  118  105                                                                
CONECT  119  106                                                                
CONECT  120  107                                                                
CONECT  121  108                                                                
CONECT  122  108                                                                
CONECT  123  110                                                                
CONECT  124  110                                                                
CONECT  125  110                                                                
CONECT  126  111                                                                
CONECT  127   96  130  133  136                                                 
CONECT  128   54  131  134  137                                                 
CONECT  129   12  132  135  138                                                 
CONECT  130  127                                                                
CONECT  131  128                                                                
CONECT  132  129                                                                
CONECT  133  127                                                                
CONECT  134  128                                                                
CONECT  135  129                                                                
CONECT  136  127                                                                
CONECT  137  128                                                                
CONECT  138  129                                                                
MASTER      245    0    9    0    0    0    0    6   90    0  138    0          
END                                                                             
