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Database: PDB
Entry: 1JMO
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HEADER    BLOOD CLOTTING                          19-JUL-01   1JMO              
TITLE     CRYSTAL STRUCTURE OF THE HEPARIN COFACTOR II-S195A THROMBIN COMPLEX   
CAVEAT     1JMO    NAG B 1 HAS WRONG CHIRALITY AT ATOM C1 NAG A 482 HAS WRONG   
CAVEAT   2 1JMO    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THROMBIN, LIGHT CHAIN;                                     
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: LIGHT CHAIN;                                               
COMPND   5 SYNONYM: COAGULATION FACTOR II;                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: CONTAINS EXTRA 13 AMINO ACIDS AT THE N-TERMINUS;      
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: THROMBIN, HEAVY CHAIN;                                     
COMPND  10 CHAIN: H;                                                            
COMPND  11 FRAGMENT: HEAVY CHAIN;                                               
COMPND  12 SYNONYM: COAGULATION FACTOR II;                                      
COMPND  13 EC: 3.4.21.5;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: HEPARIN COFACTOR II;                                       
COMPND  18 CHAIN: A;                                                            
COMPND  19 SYNONYM: HC-II; PROTEASE INHIBITOR LEUSERPIN 2; HLS2; SERINE (OR     
COMPND  20 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;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BHK CULTURE;                            
SOURCE   9 EXPRESSION_SYSTEM_ORGAN: KIDNEY;                                     
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  15 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: BHK CULTURE;                            
SOURCE  18 EXPRESSION_SYSTEM_ORGAN: KIDNEY;                                     
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  21 ORGANISM_COMMON: HUMAN;                                              
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 OTHER_DETAILS: PLASMA PURIFIED HUMAN HEPARIN COFACTOR II             
KEYWDS    SERPIN, THROMBIN, PROTEASE, INHIBITION, INHIBITOR, BLOOD CLOTTING     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.P.BAGLIN,R.W.CARRELL,C.T.ESMON,J.A.HUNTINGTON                       
REVDAT   5   27-OCT-21 1JMO    1       REMARK SEQADV HETSYN                     
REVDAT   4   29-JUL-20 1JMO    1       CAVEAT COMPND REMARK SEQADV              
REVDAT   4 2                   1       HET    HETNAM FORMUL LINK                
REVDAT   4 3                   1       SITE   ATOM                              
REVDAT   3   13-JUL-11 1JMO    1       VERSN                                    
REVDAT   2   24-FEB-09 1JMO    1       VERSN                                    
REVDAT   1   30-AUG-02 1JMO    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.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.44                          
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)   (%) : 91.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 77077                          
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) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 983                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3020                       
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 105                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.033                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5930                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 97                                      
REMARK   3   SOLVENT ATOMS            : 208                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.20000                                              
REMARK   3    B22 (A**2) : 3.02000                                              
REMARK   3    B33 (A**2) : -7.22000                                             
REMARK   3    B12 (A**2) : 6.15000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.33                            
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) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.406                           
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) : 1.450 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.452 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.428 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.794 ; 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: MAXIMUM LIKELIHOOD TARGET OF CNS          
REMARK   4                                                                      
REMARK   4 1JMO 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_1000013943.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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          : SCALA, CCP4 (SCALA)                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77077                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.21                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.35                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.43400                            
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: N-TERMINAL HALF OF NATIVE HEPARIN COFACTOR II AND    
REMARK 200  NATIVE S195A THROMBIN                                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NH4CL, PEG 3350, PH 7.4, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP AT 298K                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.26667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.53333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.40000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      105.66667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.13333            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9230 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33000 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, A, B                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     THR L     1U                                                     
REMARK 465     ARG H    15                                                      
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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C  SSEQI                                                     
REMARK 475     SER A    83                                                      
REMARK 475     PRO A    84                                                      
REMARK 475     THR A    85                                                      
REMARK 475     ASP A    86                                                      
REMARK 475     SER A    87                                                      
REMARK 475     ASP A    88                                                      
REMARK 475     VAL A    89                                                      
REMARK 475     SER A    90                                                      
REMARK 475     ALA A    91                                                      
REMARK 475     GLY A    92                                                      
REMARK 475     ASN A    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 H  240   CE   NZ                                             
REMARK 480     LYS A  185   NZ                                                  
REMARK 480     ASP A  216   OD2                                                 
REMARK 480     LYS A  249   CD   CE   NZ                                        
REMARK 480     GLU A  300   OE1                                                 
REMARK 480     LYS A  348   CE   NZ                                             
REMARK 480     ILE A  413   CD1                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP L  14L  N   -  CA  -  C   ANGL. DEV. =  19.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE L   7      -86.71   -132.03                                   
REMARK 500    ILE L  14K      79.24    -60.15                                   
REMARK 500    ASP L  14L     161.96     42.85                                   
REMARK 500    ARG H  50       -3.85   -140.57                                   
REMARK 500    TYR H  60A      85.85   -157.45                                   
REMARK 500    ASN H  60G      59.21   -163.08                                   
REMARK 500    HIS H  71      -61.06   -130.84                                   
REMARK 500    ASN H  78       17.30     56.35                                   
REMARK 500    ILE H  79      -54.89   -128.67                                   
REMARK 500    GLU H  97A     -61.37   -109.71                                   
REMARK 500    VAL H 147E     -52.70   -134.28                                   
REMARK 500    PHE H 245      -12.38   -142.86                                   
REMARK 500    VAL A  82     -177.49    -45.88                                   
REMARK 500    SER A  83      -88.05    -66.37                                   
REMARK 500    THR A  85      -80.74   -123.81                                   
REMARK 500    ASP A  86      100.64     93.69                                   
REMARK 500    ASP A  88     -177.41    176.99                                   
REMARK 500    VAL A  89      106.20   -162.24                                   
REMARK 500    SER A  90      175.64    -51.18                                   
REMARK 500    ALA A  91     -130.88   -110.48                                   
REMARK 500    ASN A  93       47.32    -93.01                                   
REMARK 500    ILE A  94      155.20    -37.90                                   
REMARK 500    LEU A  95       77.98   -109.64                                   
REMARK 500    ASN A 261       61.21     39.92                                   
REMARK 500    THR A 431      -90.13    -49.67                                   
REMARK 500    ALA A 433     -126.14     44.17                                   
REMARK 500    THR A 434       67.55     90.49                                   
REMARK 500    THR A 435      130.60     15.89                                   
REMARK 500    VAL A 436       55.70    -94.71                                   
REMARK 500    THR A 437      179.34    -57.88                                   
REMARK 500    THR A 438      118.71    158.16                                   
REMARK 500    VAL A 439     -135.61   -131.39                                   
REMARK 500    PHE A 441      119.75    -30.91                                   
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                              NA H 501  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS H 224   O                                                      
REMARK 620 2 HOH H2048   O   122.8                                              
REMARK 620 N                    1                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JMJ   RELATED DB: PDB                                   
DBREF  1JMO L    1U   14M UNP    P00734   THRB_HUMAN     315    362             
DBREF  1JMO H   15   247  UNP    P00734   THRB_HUMAN     363    622             
DBREF  1JMO A    1   480  UNP    P05546   HEP2_HUMAN      20    499             
SEQADV 1JMO ALA H  195  UNP  P00734    SER   568 ENGINEERED MUTATION            
SEQADV 1JMO TYS A   60  UNP  P05546    TYR    79 MODIFIED RESIDUE               
SEQADV 1JMO TYS A   73  UNP  P05546    TYR    92 MODIFIED RESIDUE               
SEQRES   1 L   48  THR ALA THR SER GLU TYR GLN THR PHE PHE ASN PRO ARG          
SEQRES   2 L   48  THR PHE GLY SER GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   3 L   48  LEU PHE GLU LYS LYS SER LEU GLU ASP LYS THR GLU ARG          
SEQRES   4 L   48  GLU LEU LEU GLU SER TYR ILE ASP GLY                          
SEQRES   1 H  260  ARG ILE VAL GLU GLY SER ASP ALA GLU ILE GLY MET SER          
SEQRES   2 H  260  PRO TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU          
SEQRES   3 H  260  LEU LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL          
SEQRES   4 H  260  LEU THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP          
SEQRES   5 H  260  LYS ASN PHE THR GLU ASN ASP LEU LEU VAL ARG ILE GLY          
SEQRES   6 H  260  LYS HIS SER ARG THR ARG TYR GLU ARG ASN ILE GLU LYS          
SEQRES   7 H  260  ILE SER MET LEU GLU LYS ILE TYR ILE HIS PRO ARG TYR          
SEQRES   8 H  260  ASN TRP ARG GLU ASN LEU ASP ARG ASP ILE ALA LEU MET          
SEQRES   9 H  260  LYS LEU LYS LYS PRO VAL ALA PHE SER ASP TYR ILE HIS          
SEQRES  10 H  260  PRO VAL CYS LEU PRO ASP ARG GLU THR ALA ALA SER LEU          
SEQRES  11 H  260  LEU GLN ALA GLY TYR LYS GLY ARG VAL THR GLY TRP GLY          
SEQRES  12 H  260  ASN LEU LYS GLU THR TRP THR ALA ASN VAL GLY LYS GLY          
SEQRES  13 H  260  GLN PRO SER VAL LEU GLN VAL VAL ASN LEU PRO ILE VAL          
SEQRES  14 H  260  GLU ARG PRO VAL CYS LYS ASP SER THR ARG ILE ARG ILE          
SEQRES  15 H  260  THR ASP ASN MET PHE CYS ALA GLY TYR LYS PRO ASP GLU          
SEQRES  16 H  260  GLY LYS ARG GLY ASP ALA CYS GLU GLY ASP ALA GLY GLY          
SEQRES  17 H  260  PRO PHE VAL MET LYS SER PRO PHE ASN ASN ARG TRP TYR          
SEQRES  18 H  260  GLN MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG          
SEQRES  19 H  260  ASP GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU          
SEQRES  20 H  260  LYS LYS TRP ILE GLN LYS VAL ILE ASP GLN PHE GLY GLU          
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 TYS LEU ASP LEU GLU LYS          
SEQRES   6 A  480  ILE PHE SER GLU ASP ASP ASP TYS 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              
MODRES 1JMO ASN H   60G ASN  GLYCOSYLATION SITE                                 
MODRES 1JMO ASN A  169  ASN  GLYCOSYLATION SITE                                 
MODRES 1JMO ASN A  368  ASN  GLYCOSYLATION SITE                                 
MODRES 1JMO TYS A   60  TYR  O-SULFO-L-TYROSINE                                 
MODRES 1JMO TYS A   73  TYR  O-SULFO-L-TYROSINE                                 
HET    TYS  A  60      16                                                       
HET    TYS  A  73      16                                                       
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET     NA  H 501       1                                                       
HET    MPD  H2003       8                                                       
HET    MPD  H2004       8                                                       
HET    NAG  A 481      14                                                       
HET    NAG  A 482      14                                                       
HET    MPD  A2001       8                                                       
HET    MPD  A2002       8                                                       
HET    MPD  A2005       8                                                       
HETNAM     TYS O-SULFO-L-TYROSINE                                               
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      NA SODIUM ION                                                       
HETNAM     MPD (4S)-2-METHYL-2,4-PENTANEDIOL                                    
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   3  TYS    2(C9 H11 N O6 S)                                             
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  MPD    5(C6 H14 O2)                                                 
FORMUL  13  HOH   *208(H2 O)                                                    
HELIX    1   1 ASN L    1K GLY L    1F 1                                   6    
HELIX    2   2 PHE L    7  SER L   11  5                                   5    
HELIX    3   3 THR L   14B TYR L   14J 1                                   9    
HELIX    4   4 ALA H   55  CYS H   58  5                                   4    
HELIX    5   5 PRO H   60B ASP H   60E 5                                   4    
HELIX    6   6 THR H   60I ASN H   62  5                                   3    
HELIX    7   7 ASP H  125  LEU H  130  1                                   9    
HELIX    8   8 GLU H  164  THR H  172  1                                   9    
HELIX    9   9 LYS H  185  GLY H  186C 5                                   5    
HELIX   10  10 LEU H  234  GLY H  246  1                                  13    
HELIX   11  11 ASP A   62  GLU A   69  1                                   8    
HELIX   12  12 SER A  102  ASP A  124  1                                  23    
HELIX   13  13 ALA A  135  SER A  147  1                                  13    
HELIX   14  14 LEU A  148  LEU A  150  5                                   3    
HELIX   15  15 LYS A  151  LEU A  162  1                                  12    
HELIX   16  16 HIS A  163  SER A  171  1                                   9    
HELIX   17  17 GLU A  175  ARG A  192  1                                  18    
HELIX   18  18 LEU A  214  PHE A  226  1                                  13    
HELIX   19  19 ASP A  236  THR A  251  1                                  16    
HELIX   20  20 PRO A  285  THR A  289  5                                   5    
HELIX   21  21 LYS A  343  SER A  345  5                                   3    
HELIX   22  22 GLY A  346  LEU A  354  1                                   9    
HELIX   23  23 THR A  355  MET A  366  1                                  12    
HELIX   24  24 LEU A  386  GLY A  394  1                                   9    
HELIX   25  25 ARG A  396  ASP A  400  5                                   5    
SHEET    1   A 7 MET H 180  ALA H 183  0                                        
SHEET    2   A 7 GLY H 226  HIS H 230 -1  O  GLY H 226   N  ALA H 183           
SHEET    3   A 7 TRP H 207  GLU H 217 -1  O  ILE H 212   N  THR H 229           
SHEET    4   A 7 PRO H 198  LYS H 202 -1  N  PHE H 199   O  GLY H 211           
SHEET    5   A 7 LYS H 135  GLY H 140 -1  N  ARG H 137   O  VAL H 200           
SHEET    6   A 7 GLN H 156  PRO H 161 -1  N  GLN H 156   O  GLY H 140           
SHEET    7   A 7 SER H  20  ASP H  21 -1  O  SER H  20   N  VAL H 157           
SHEET    1   B 4 MET H 180  ALA H 183  0                                        
SHEET    2   B 4 GLY H 226  HIS H 230 -1  O  GLY H 226   N  ALA H 183           
SHEET    3   B 4 TRP H 207  GLU H 217 -1  O  ILE H 212   N  THR H 229           
SHEET    4   B 4 PHE A 441  PRO A 443 -1  N  MET A 442   O  GLY H 216           
SHEET    1   C 7 GLN H  30  ARG H  35  0                                        
SHEET    2   C 7 GLU H  39  LEU H  46 -1  O  GLU H  39   N  ARG H  35           
SHEET    3   C 7 TRP H  51  THR H  54 -1  N  LEU H  53   O  SER H  45           
SHEET    4   C 7 ALA H 104  LEU H 108 -1  N  ALA H 104   O  THR H  54           
SHEET    5   C 7 LYS H  81  ILE H  90 -1  N  GLU H  86   O  LYS H 107           
SHEET    6   C 7 LEU H  64  ILE H  68 -1  O  LEU H  64   N  LEU H  85           
SHEET    7   C 7 GLN H  30  ARG H  35 -1  N  MET H  32   O  ARG H  67           
SHEET    1   E 4 ARG A 449  THR A 451  0                                        
SHEET    2   E 4 THR A 367  PRO A 376  1  O  GLU A 372   N  PHE A 450           
SHEET    3   E 4 VAL A 301  ASP A 318 -1  N  MET A 307   O  LEU A 375           
SHEET    4   E 4 HIS A 290  ARG A 295 -1  O  HIS A 290   N  MET A 306           
SHEET    1   F 8 ARG A 449  THR A 451  0                                        
SHEET    2   F 8 THR A 367  PRO A 376  1  O  GLU A 372   N  PHE A 450           
SHEET    3   F 8 VAL A 301  ASP A 318 -1  N  MET A 307   O  LEU A 375           
SHEET    4   F 8 CYS A 323  TYR A 330 -1  O  CYS A 323   N  ASP A 318           
SHEET    5   F 8 ILE A 334  PRO A 341 -1  O  ILE A 334   N  TYR A 330           
SHEET    6   F 8 PHE A 456  GLU A 462 -1  O  LEU A 457   N  VAL A 339           
SHEET    7   F 8 CYS A 467  VAL A 474 -1  O  CYS A 467   N  GLU A 462           
SHEET    8   F 8 ILE A 132  ILE A 134 -1  N  ILE A 132   O  ARG A 473           
SHEET    1   G 5 ALA A 229  ALA A 232  0                                        
SHEET    2   G 5 THR A 198  GLN A 208  1  O  LEU A 205   N  GLN A 230           
SHEET    3   G 5 MET A 268  LYS A 277 -1  O  MET A 269   N  TYR A 206           
SHEET    4   G 5 ILE A 415  VAL A 426  1  N  ASP A 416   O  MET A 268           
SHEET    5   G 5 PHE A 378  GLU A 381 -1  O  PHE A 378   N  VAL A 426           
SHEET    1   H 5 ALA A 229  ALA A 232  0                                        
SHEET    2   H 5 THR A 198  GLN A 208  1  O  LEU A 205   N  GLN A 230           
SHEET    3   H 5 MET A 268  LYS A 277 -1  O  MET A 269   N  TYR A 206           
SHEET    4   H 5 ILE A 415  VAL A 426  1  N  ASP A 416   O  MET A 268           
SHEET    5   H 5 TYR A 384  ASN A 385 -1  N  TYR A 384   O  HIS A 420           
SSBOND   1 CYS L    1    CYS H  122                          1555   1555  2.04  
SSBOND   2 CYS H   42    CYS H   58                          1555   1555  2.06  
SSBOND   3 CYS H  168    CYS H  182                          1555   1555  2.03  
SSBOND   4 CYS H  191    CYS H  220                          1555   1555  2.06  
LINK         ND2 ASN H  60G                C1  NAG B   1     1555   1555  1.45  
LINK         C   ASP A  59                 N   TYS A  60     1555   1555  1.33  
LINK         C   TYS A  60                 N   LEU A  61     1555   1555  1.32  
LINK         C   ASP A  72                 N   TYS A  73     1555   1555  1.33  
LINK         C   TYS A  73                 N   ILE A  74     1555   1555  1.33  
LINK         ND2 ASN A 169                 C1  NAG A 481     1555   1555  1.45  
LINK         ND2 ASN A 368                 C1  NAG A 482     1555   1555  1.46  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.40  
LINK         O   LYS H 224                NA    NA H 501     1555   1555  2.64  
LINK        NA    NA H 501                 O   HOH H2048     1555   1555  2.86  
CISPEP   1 SER H   36A   PRO H   37          0         0.21                     
CRYST1  152.310  152.310  126.800  90.00  90.00 120.00 P 61          6          
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      0.006566  0.003791  0.000000        0.00000                         
SCALE2      0.000000  0.007581  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007886        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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