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Database: PDB
Entry: 1JMJ
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HEADER    BLOOD CLOTTING                          18-JUL-01   1JMJ              
TITLE     CRYSTAL STRUCTURE OF NATIVE HEPARIN COFACTOR II                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEPARIN COFACTOR II;                                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: HC-II; PROTEASE INHIBITOR LEUSERPIN 2; HLS2; SERINE (OR     
COMPND   5 CYSTEINE) PROTEINASE INHIBITOR, CLADE D (HEPARIN COFACTOR), MEMBER 1 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    SERPIN, THROMBIN INHIBITOR, HEPARIN, BLOOD CLOTTING                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.BAGLIN,R.W.CARRELL,F.C.CHURCH,J.A.HUNTINGTON                      
REVDAT   4   29-JUL-20 1JMJ    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 1JMJ    1       VERSN                                    
REVDAT   2   24-FEB-09 1JMJ    1       VERSN                                    
REVDAT   1   30-AUG-02 1JMJ    0                                                
JRNL        AUTH   T.P.BAGLIN,R.W.CARRELL,F.C.CHURCH,C.T.ESMON,J.A.HUNTINGTON   
JRNL        TITL   CRYSTAL STRUCTURES OF NATIVE AND THROMBIN-COMPLEXED HEPARIN  
JRNL        TITL 2 COFACTOR II REVEAL A MULTISTEP ALLOSTERIC MECHANISM.         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  99 11079 2002              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   12169660                                                     
JRNL        DOI    10.1073/PNAS.162232399                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 39156                          
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 SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 994                             
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) : 2.35                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.50                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 142                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.032                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6372                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 297                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.95000                                             
REMARK   3    B22 (A**2) : -9.52000                                             
REMARK   3    B33 (A**2) : -4.43000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 12.10000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.38                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.36                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.42                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.297 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.182 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.229 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.429 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 1JMJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000013938.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.4880                             
REMARK 200  MONOCHROMATOR                  : LIQUID GALLIUM                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40150                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 66.0                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.14000                            
REMARK 200  R SYM                      (I) : 0.14000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: SEVERAL SERPINS WERE TRIED BEST SOLUTION WITH        
REMARK 200  NATIVE ANTITHROMBIN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MGCL2, TRIS, PEG 4000, GLYCEROL, PH      
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP AT 298K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     ASP A     7                                                      
REMARK 465     GLN A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     GLN A    22                                                      
REMARK 465     TRP A    23                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     MET A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     LEU A    35                                                      
REMARK 465     LEU A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     ALA A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     PHE A    40                                                      
REMARK 465     HIS A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     GLU A    43                                                      
REMARK 465     ASN A    44                                                      
REMARK 465     THR A    45                                                      
REMARK 465     VAL A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     ASN A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     TRP A    50                                                      
REMARK 465     ILE A    51                                                      
REMARK 465     PRO A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     GLY A    54                                                      
REMARK 465     GLU A    55                                                      
REMARK 465     GLU A    56                                                      
REMARK 465     ASP A    57                                                      
REMARK 465     ASP A    58                                                      
REMARK 465     ASP A    59                                                      
REMARK 465     TYR A    60                                                      
REMARK 465     ASP A    72                                                      
REMARK 465     TYR A    73                                                      
REMARK 465     ILE A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     ILE A    76                                                      
REMARK 465     VAL A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     LEU A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     VAL A    82                                                      
REMARK 465     SER A    83                                                      
REMARK 465     PRO A    84                                                      
REMARK 465     THR A    85                                                      
REMARK 465     ASP A    86                                                      
REMARK 465     SER A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     VAL A    89                                                      
REMARK 465     SER A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     GLY A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     ILE A    94                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     LYS B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     ASP B     7                                                      
REMARK 465     GLN B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     THR B    15                                                      
REMARK 465     ALA B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     ASP B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     GLN B    22                                                      
REMARK 465     TRP B    23                                                      
REMARK 465     GLU B    24                                                      
REMARK 465     GLN B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     ASN B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     LEU B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     MET B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     LEU B    35                                                      
REMARK 465     LEU B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     ALA B    38                                                      
REMARK 465     ASP B    39                                                      
REMARK 465     PHE B    40                                                      
REMARK 465     HIS B    41                                                      
REMARK 465     LYS B    42                                                      
REMARK 465     GLU B    43                                                      
REMARK 465     ASN B    44                                                      
REMARK 465     THR B    45                                                      
REMARK 465     VAL B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     ASN B    48                                                      
REMARK 465     ASP B    49                                                      
REMARK 465     TRP B    50                                                      
REMARK 465     ILE B    51                                                      
REMARK 465     PRO B    52                                                      
REMARK 465     GLU B    53                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     ASP B    58                                                      
REMARK 465     ASP B    59                                                      
REMARK 465     TYR B    60                                                      
REMARK 465     LEU B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     LEU B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     ILE B    66                                                      
REMARK 465     PHE B    67                                                      
REMARK 465     SER B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     ASP B    70                                                      
REMARK 465     ASP B    71                                                      
REMARK 465     ASP B    72                                                      
REMARK 465     TYR B    73                                                      
REMARK 465     ILE B    74                                                      
REMARK 465     ASP B    75                                                      
REMARK 465     ILE B    76                                                      
REMARK 465     VAL B    77                                                      
REMARK 465     ASP B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     LEU B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     VAL B    82                                                      
REMARK 465     SER B    83                                                      
REMARK 465     PRO B    84                                                      
REMARK 465     THR B    85                                                      
REMARK 465     ASP B    86                                                      
REMARK 465     SER B    87                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     VAL B    89                                                      
REMARK 465     SER B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     GLY B    92                                                      
REMARK 465     ASN B    93                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  173   CD   CE   NZ                                        
REMARK 480     GLU A  175   CD   OE1  OE2                                       
REMARK 480     ARG A  189   NE   CZ   NH1  NH2                                  
REMARK 480     ASP A  216   OD2                                                 
REMARK 480     GLU A  300   OE1                                                 
REMARK 480     GLN A  411   OE1  NE2                                            
REMARK 480     ARG A  412   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B  165   CD   CE   NZ                                        
REMARK 480     ARG B  193   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG B  222   CD   NE   CZ   NH1  NH2                             
REMARK 480     LYS B  364   CE                                                  
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    GLN A  96      -63.27    108.80                                   
REMARK 500    ASP A 166      -35.08    -37.61                                   
REMARK 500    GLU A 175      170.52    176.83                                   
REMARK 500    PHE A 226       15.38     57.51                                   
REMARK 500    ASP A 233       85.01   -150.61                                   
REMARK 500    GLU A 300      127.43    174.82                                   
REMARK 500    ASP A 322       70.98     44.51                                   
REMARK 500    PHE A 441       -2.01   -158.28                                   
REMARK 500    PRO A 477       -7.18    -58.99                                   
REMARK 500    LEU B  95       62.39   -113.18                                   
REMARK 500    ASP B 233       86.57   -156.91                                   
REMARK 500    PHE B 234        5.73    -69.68                                   
REMARK 500    PHE B 441      -10.10   -154.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 290   NE2                                                    
REMARK 620 2 HIS A 292   ND1  94.2                                              
REMARK 620 3 HOH A 502   O    88.3 164.2                                        
REMARK 620 4 HOH A 551   O   139.2  97.8  70.6                                  
REMARK 620 5 HOH A 631   O    94.1  99.4  96.0 121.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JMO   RELATED DB: PDB                                   
DBREF  1JMJ A    1   480  UNP    P05546   HEP2_HUMAN      20    499             
DBREF  1JMJ B    1   480  UNP    P05546   HEP2_HUMAN      20    499             
SEQRES   1 A  480  GLY SER LYS GLY PRO LEU ASP GLN LEU GLU LYS GLY GLY          
SEQRES   2 A  480  GLU THR ALA GLN SER ALA ASP PRO GLN TRP GLU GLN LEU          
SEQRES   3 A  480  ASN ASN LYS ASN LEU SER MET PRO LEU LEU PRO ALA ASP          
SEQRES   4 A  480  PHE HIS LYS GLU ASN THR VAL THR ASN ASP TRP ILE PRO          
SEQRES   5 A  480  GLU GLY GLU GLU ASP ASP ASP TYR LEU ASP LEU GLU LYS          
SEQRES   6 A  480  ILE PHE SER GLU ASP ASP ASP TYR ILE ASP ILE VAL ASP          
SEQRES   7 A  480  SER LEU SER VAL SER PRO THR ASP SER ASP VAL SER ALA          
SEQRES   8 A  480  GLY ASN ILE LEU GLN LEU PHE HIS GLY LYS SER ARG ILE          
SEQRES   9 A  480  GLN ARG LEU ASN ILE LEU ASN ALA LYS PHE ALA PHE ASN          
SEQRES  10 A  480  LEU TYR ARG VAL LEU LYS ASP GLN VAL ASN THR PHE ASP          
SEQRES  11 A  480  ASN ILE PHE ILE ALA PRO VAL GLY ILE SER THR ALA MET          
SEQRES  12 A  480  GLY MET ILE SER LEU GLY LEU LYS GLY GLU THR HIS GLU          
SEQRES  13 A  480  GLN VAL HIS SER ILE LEU HIS PHE LYS ASP PHE VAL ASN          
SEQRES  14 A  480  ALA SER SER LYS TYR GLU ILE THR THR ILE HIS ASN LEU          
SEQRES  15 A  480  PHE ARG LYS LEU THR HIS ARG LEU PHE ARG ARG ASN PHE          
SEQRES  16 A  480  GLY TYR THR LEU ARG SER VAL ASN ASP LEU TYR ILE GLN          
SEQRES  17 A  480  LYS GLN PHE PRO ILE LEU LEU ASP PHE LYS THR LYS VAL          
SEQRES  18 A  480  ARG GLU TYR TYR PHE ALA GLU ALA GLN ILE ALA ASP PHE          
SEQRES  19 A  480  SER ASP PRO ALA PHE ILE SER LYS THR ASN ASN HIS ILE          
SEQRES  20 A  480  MET LYS LEU THR LYS GLY LEU ILE LYS ASP ALA LEU GLU          
SEQRES  21 A  480  ASN ILE ASP PRO ALA THR GLN MET MET ILE LEU ASN CYS          
SEQRES  22 A  480  ILE TYR PHE LYS GLY SER TRP VAL ASN LYS PHE PRO VAL          
SEQRES  23 A  480  GLU MET THR HIS ASN HIS ASN PHE ARG LEU ASN GLU ARG          
SEQRES  24 A  480  GLU VAL VAL LYS VAL SER MET MET GLN THR LYS GLY ASN          
SEQRES  25 A  480  PHE LEU ALA ALA ASN ASP GLN GLU LEU ASP CYS ASP ILE          
SEQRES  26 A  480  LEU GLN LEU GLU TYR VAL GLY GLY ILE SER MET LEU ILE          
SEQRES  27 A  480  VAL VAL PRO HIS LYS MET SER GLY MET LYS THR LEU GLU          
SEQRES  28 A  480  ALA GLN LEU THR PRO ARG VAL VAL GLU ARG TRP GLN LYS          
SEQRES  29 A  480  SER MET THR ASN ARG THR ARG GLU VAL LEU LEU PRO LYS          
SEQRES  30 A  480  PHE LYS LEU GLU LYS ASN TYR ASN LEU VAL GLU SER LEU          
SEQRES  31 A  480  LYS LEU MET GLY ILE ARG MET LEU PHE ASP LYS ASN GLY          
SEQRES  32 A  480  ASN MET ALA GLY ILE SER ASP GLN ARG ILE ALA ILE ASP          
SEQRES  33 A  480  LEU PHE LYS HIS GLN GLY THR ILE THR VAL ASN GLU GLU          
SEQRES  34 A  480  GLY THR GLN ALA THR THR VAL THR THR VAL GLY PHE MET          
SEQRES  35 A  480  PRO LEU SER THR GLN VAL ARG PHE THR VAL ASP ARG PRO          
SEQRES  36 A  480  PHE LEU PHE LEU ILE TYR GLU HIS ARG THR SER CYS LEU          
SEQRES  37 A  480  LEU PHE MET GLY ARG VAL ALA ASN PRO SER ARG SER              
SEQRES   1 B  480  GLY SER LYS GLY PRO LEU ASP GLN LEU GLU LYS GLY GLY          
SEQRES   2 B  480  GLU THR ALA GLN SER ALA ASP PRO GLN TRP GLU GLN LEU          
SEQRES   3 B  480  ASN ASN LYS ASN LEU SER MET PRO LEU LEU PRO ALA ASP          
SEQRES   4 B  480  PHE HIS LYS GLU ASN THR VAL THR ASN ASP TRP ILE PRO          
SEQRES   5 B  480  GLU GLY GLU GLU ASP ASP ASP TYR LEU ASP LEU GLU LYS          
SEQRES   6 B  480  ILE PHE SER GLU ASP ASP ASP TYR ILE ASP ILE VAL ASP          
SEQRES   7 B  480  SER LEU SER VAL SER PRO THR ASP SER ASP VAL SER ALA          
SEQRES   8 B  480  GLY ASN ILE LEU GLN LEU PHE HIS GLY LYS SER ARG ILE          
SEQRES   9 B  480  GLN ARG LEU ASN ILE LEU ASN ALA LYS PHE ALA PHE ASN          
SEQRES  10 B  480  LEU TYR ARG VAL LEU LYS ASP GLN VAL ASN THR PHE ASP          
SEQRES  11 B  480  ASN ILE PHE ILE ALA PRO VAL GLY ILE SER THR ALA MET          
SEQRES  12 B  480  GLY MET ILE SER LEU GLY LEU LYS GLY GLU THR HIS GLU          
SEQRES  13 B  480  GLN VAL HIS SER ILE LEU HIS PHE LYS ASP PHE VAL ASN          
SEQRES  14 B  480  ALA SER SER LYS TYR GLU ILE THR THR ILE HIS ASN LEU          
SEQRES  15 B  480  PHE ARG LYS LEU THR HIS ARG LEU PHE ARG ARG ASN PHE          
SEQRES  16 B  480  GLY TYR THR LEU ARG SER VAL ASN ASP LEU TYR ILE GLN          
SEQRES  17 B  480  LYS GLN PHE PRO ILE LEU LEU ASP PHE LYS THR LYS VAL          
SEQRES  18 B  480  ARG GLU TYR TYR PHE ALA GLU ALA GLN ILE ALA ASP PHE          
SEQRES  19 B  480  SER ASP PRO ALA PHE ILE SER LYS THR ASN ASN HIS ILE          
SEQRES  20 B  480  MET LYS LEU THR LYS GLY LEU ILE LYS ASP ALA LEU GLU          
SEQRES  21 B  480  ASN ILE ASP PRO ALA THR GLN MET MET ILE LEU ASN CYS          
SEQRES  22 B  480  ILE TYR PHE LYS GLY SER TRP VAL ASN LYS PHE PRO VAL          
SEQRES  23 B  480  GLU MET THR HIS ASN HIS ASN PHE ARG LEU ASN GLU ARG          
SEQRES  24 B  480  GLU VAL VAL LYS VAL SER MET MET GLN THR LYS GLY ASN          
SEQRES  25 B  480  PHE LEU ALA ALA ASN ASP GLN GLU LEU ASP CYS ASP ILE          
SEQRES  26 B  480  LEU GLN LEU GLU TYR VAL GLY GLY ILE SER MET LEU ILE          
SEQRES  27 B  480  VAL VAL PRO HIS LYS MET SER GLY MET LYS THR LEU GLU          
SEQRES  28 B  480  ALA GLN LEU THR PRO ARG VAL VAL GLU ARG TRP GLN LYS          
SEQRES  29 B  480  SER MET THR ASN ARG THR ARG GLU VAL LEU LEU PRO LYS          
SEQRES  30 B  480  PHE LYS LEU GLU LYS ASN TYR ASN LEU VAL GLU SER LEU          
SEQRES  31 B  480  LYS LEU MET GLY ILE ARG MET LEU PHE ASP LYS ASN GLY          
SEQRES  32 B  480  ASN MET ALA GLY ILE SER ASP GLN ARG ILE ALA ILE ASP          
SEQRES  33 B  480  LEU PHE LYS HIS GLN GLY THR ILE THR VAL ASN GLU GLU          
SEQRES  34 B  480  GLY THR GLN ALA THR THR VAL THR THR VAL GLY PHE MET          
SEQRES  35 B  480  PRO LEU SER THR GLN VAL ARG PHE THR VAL ASP ARG PRO          
SEQRES  36 B  480  PHE LEU PHE LEU ILE TYR GLU HIS ARG THR SER CYS LEU          
SEQRES  37 B  480  LEU PHE MET GLY ARG VAL ALA ASN PRO SER ARG SER              
MODRES 1JMJ ASN A  368  ASN  GLYCOSYLATION SITE                                 
MODRES 1JMJ ASN B  368  ASN  GLYCOSYLATION SITE                                 
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    BMA  C   3      11                                                       
HET     CA  A 501       1                                                       
HET    NAG  B 481      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   4   CA    CA 2+                                                        
FORMUL   6  HOH   *297(H2 O)                                                    
HELIX    1   1 ASP A   62  SER A   68  1                                   7    
HELIX    2   2 SER A  102  ASP A  124  1                                  23    
HELIX    3   3 ALA A  135  SER A  147  1                                  13    
HELIX    4   4 LEU A  148  LEU A  150  5                                   3    
HELIX    5   5 LYS A  151  LEU A  162  1                                  12    
HELIX    6   6 HIS A  163  SER A  171  1                                   9    
HELIX    7   7 GLU A  175  ARG A  192  1                                  18    
HELIX    8   8 LEU A  214  TYR A  225  1                                  12    
HELIX    9   9 ASP A  236  THR A  251  1                                  16    
HELIX   10  10 PRO A  285  THR A  289  5                                   5    
HELIX   11  11 SER A  345  LEU A  354  1                                  10    
HELIX   12  12 THR A  355  SER A  365  1                                  11    
HELIX   13  13 LEU A  386  GLY A  394  1                                   9    
HELIX   14  14 ARG A  396  ASP A  400  5                                   5    
HELIX   15  15 SER B  102  ASP B  124  1                                  23    
HELIX   16  16 ALA B  135  LEU B  148  1                                  14    
HELIX   17  17 LYS B  151  LEU B  162  1                                  12    
HELIX   18  18 HIS B  163  ASN B  169  1                                   7    
HELIX   19  19 GLU B  175  ARG B  192  1                                  18    
HELIX   20  20 LEU B  214  PHE B  226  1                                  13    
HELIX   21  21 ASP B  236  THR B  251  1                                  16    
HELIX   22  22 PRO B  285  THR B  289  5                                   5    
HELIX   23  23 SER B  345  LEU B  354  1                                  10    
HELIX   24  24 THR B  355  SER B  365  1                                  11    
HELIX   25  25 LEU B  386  GLY B  394  1                                   9    
HELIX   26  26 ARG B  396  ASP B  400  5                                   5    
SHEET    1   A 4 ARG A 449  THR A 451  0                                        
SHEET    2   A 4 THR A 367  PRO A 376  1  O  GLU A 372   N  PHE A 450           
SHEET    3   A 4 VAL A 301  ASP A 318 -1  N  MET A 307   O  LEU A 375           
SHEET    4   A 4 HIS A 290  ARG A 295 -1  O  HIS A 290   N  MET A 306           
SHEET    1   B 8 ARG A 449  THR A 451  0                                        
SHEET    2   B 8 THR A 367  PRO A 376  1  O  GLU A 372   N  PHE A 450           
SHEET    3   B 8 VAL A 301  ASP A 318 -1  N  MET A 307   O  LEU A 375           
SHEET    4   B 8 CYS A 323  TYR A 330 -1  O  CYS A 323   N  ASP A 318           
SHEET    5   B 8 ILE A 334  PRO A 341 -1  O  ILE A 334   N  TYR A 330           
SHEET    6   B 8 PHE A 456  GLU A 462 -1  O  LEU A 457   N  VAL A 339           
SHEET    7   B 8 CYS A 467  VAL A 474 -1  O  CYS A 467   N  GLU A 462           
SHEET    8   B 8 ILE A 132  ILE A 134 -1  N  ILE A 132   O  ARG A 473           
SHEET    1   C 5 ALA A 229  ALA A 232  0                                        
SHEET    2   C 5 THR A 198  GLN A 208  1  O  LEU A 205   N  GLN A 230           
SHEET    3   C 5 MET A 268  LYS A 277 -1  O  MET A 269   N  TYR A 206           
SHEET    4   C 5 ILE A 415  VAL A 426  1  N  ASP A 416   O  MET A 268           
SHEET    5   C 5 PHE A 378  GLU A 381 -1  O  PHE A 378   N  VAL A 426           
SHEET    1   D 5 ALA A 229  ALA A 232  0                                        
SHEET    2   D 5 THR A 198  GLN A 208  1  O  LEU A 205   N  GLN A 230           
SHEET    3   D 5 MET A 268  LYS A 277 -1  O  MET A 269   N  TYR A 206           
SHEET    4   D 5 ILE A 415  VAL A 426  1  N  ASP A 416   O  MET A 268           
SHEET    5   D 5 TYR A 384  ASN A 385 -1  N  TYR A 384   O  HIS A 420           
SHEET    1   E 4 ARG B 449  THR B 451  0                                        
SHEET    2   E 4 THR B 367  PRO B 376  1  O  GLU B 372   N  PHE B 450           
SHEET    3   E 4 VAL B 301  ASP B 318 -1  N  MET B 307   O  LEU B 375           
SHEET    4   E 4 HIS B 290  ARG B 295 -1  O  HIS B 290   N  MET B 306           
SHEET    1   F 8 ARG B 449  THR B 451  0                                        
SHEET    2   F 8 THR B 367  PRO B 376  1  O  GLU B 372   N  PHE B 450           
SHEET    3   F 8 VAL B 301  ASP B 318 -1  N  MET B 307   O  LEU B 375           
SHEET    4   F 8 CYS B 323  TYR B 330 -1  O  CYS B 323   N  ASP B 318           
SHEET    5   F 8 ILE B 334  PRO B 341 -1  O  ILE B 334   N  TYR B 330           
SHEET    6   F 8 PHE B 456  GLU B 462 -1  O  LEU B 457   N  VAL B 339           
SHEET    7   F 8 CYS B 467  VAL B 474 -1  O  CYS B 467   N  GLU B 462           
SHEET    8   F 8 ILE B 132  ILE B 134 -1  N  ILE B 132   O  ARG B 473           
SHEET    1   G 5 ALA B 229  ALA B 232  0                                        
SHEET    2   G 5 THR B 198  GLN B 208  1  O  LEU B 205   N  GLN B 230           
SHEET    3   G 5 MET B 268  LYS B 277 -1  O  MET B 269   N  TYR B 206           
SHEET    4   G 5 ILE B 415  VAL B 426  1  N  ASP B 416   O  MET B 268           
SHEET    5   G 5 PHE B 378  GLU B 381 -1  O  PHE B 378   N  VAL B 426           
SHEET    1   H 5 ALA B 229  ALA B 232  0                                        
SHEET    2   H 5 THR B 198  GLN B 208  1  O  LEU B 205   N  GLN B 230           
SHEET    3   H 5 MET B 268  LYS B 277 -1  O  MET B 269   N  TYR B 206           
SHEET    4   H 5 ILE B 415  VAL B 426  1  N  ASP B 416   O  MET B 268           
SHEET    5   H 5 TYR B 384  ASN B 385 -1  N  TYR B 384   O  HIS B 420           
LINK         ND2 ASN A 368                 C1  NAG C   1     1555   1555  1.45  
LINK         ND2 ASN B 368                 C1  NAG B 481     1555   1555  1.46  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.39  
LINK         O4  NAG C   2                 C1  BMA C   3     1555   1555  1.39  
LINK         NE2 HIS A 290                CA    CA A 501     1555   1555  2.55  
LINK         ND1 HIS A 292                CA    CA A 501     1555   1555  2.67  
LINK        CA    CA A 501                 O   HOH A 502     1555   1555  3.10  
LINK        CA    CA A 501                 O   HOH A 551     1555   1555  2.84  
LINK        CA    CA A 501                 O   HOH A 631     1555   1555  2.65  
CRYST1   74.730   80.000   92.240  90.00 102.04  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013382  0.000000  0.002854        0.00000                         
SCALE2      0.000000  0.012500  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011085        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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