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Database: PDB
Entry: 3KCG
LinkDB: 3KCG
Original site: 3KCG 
HEADER    HYDROLASE, HYDROLASE INHIBITOR          21-OCT-09   3KCG              
TITLE     CRYSTAL STRUCTURE OF THE ANTITHROMBIN-FACTOR IXA-PENTASACCHARIDE      
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COAGULATION FACTOR IXA LIGHT CHAIN;                        
COMPND   3 CHAIN: L;                                                            
COMPND   4 FRAGMENT: EGF2;                                                      
COMPND   5 SYNONYM: FACTOR IX, CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN          
COMPND   6 COMPONENT, PTC;                                                      
COMPND   7 EC: 3.4.21.22;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: COAGULATION FACTOR IXA HEAVY CHAIN;                        
COMPND  11 CHAIN: H;                                                            
COMPND  12 SYNONYM: FACTOR IX, CHRISTMAS FACTOR, PLASMA THROMBOPLASTIN          
COMPND  13 COMPONENT, PTC;                                                      
COMPND  14 EC: 3.4.21.22;                                                       
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MUTATION: YES;                                                       
COMPND  17 MOL_ID: 3;                                                           
COMPND  18 MOLECULE: ANTITHROMBIN-III;                                          
COMPND  19 CHAIN: I;                                                            
COMPND  20 SYNONYM: ATIII;                                                      
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: F9;                                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: F9;                                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: SERPINC1, AT3, PRO0309;                                        
SOURCE  20 EXPRESSION_SYSTEM_CELL: BHK                                          
KEYWDS    MICHAELIS COMPLEX, BLOOD COAGULATION, CALCIUM, DISULFIDE BOND, EGF-   
KEYWDS   2 LIKE DOMAIN, GLYCOPROTEIN, HEMOPHILIA, HYDROLASE, PHARMACEUTICAL,    
KEYWDS   3 PROTEASE, SECRETED, SERINE PROTEASE, SULFATION, ZYMOGEN, HEPARIN-    
KEYWDS   4 BINDING, PROTEASE INHIBITOR, SERINE PROTEASE INHIBITOR,              
KEYWDS   5 THROMBOPHILIA, HYDROLASE INHIBITOR                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.HUNTINGTON,D.J.D.JOHNSON                                          
REVDAT   3   10-NOV-21 3KCG    1       SEQADV HETSYN                            
REVDAT   2   29-JUL-20 3KCG    1       COMPND REMARK SEQADV HET                 
REVDAT   2 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   2 3                   1       ATOM                                     
REVDAT   1   02-FEB-10 3KCG    0                                                
JRNL        AUTH   D.J.JOHNSON,J.LANGDOWN,J.A.HUNTINGTON                        
JRNL        TITL   MOLECULAR BASIS OF FACTOR IXA RECOGNITION BY                 
JRNL        TITL 2 HEPARIN-ACTIVATED ANTITHROMBIN REVEALED BY A 1.7-A STRUCTURE 
JRNL        TITL 3 OF THE TERNARY COMPLEX.                                      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107   645 2010              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   20080729                                                     
JRNL        DOI    10.1073/PNAS.0910144107                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.05                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2168682.340                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 112546                         
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                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5670                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.81                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 17733                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3160                       
REMARK   3   BIN FREE R VALUE                    : 0.3430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 951                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5492                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 204                                     
REMARK   3   SOLVENT ATOMS            : 667                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.52000                                              
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : 0.30000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
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) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.790                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.290 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.090 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.900 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.940 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 52.45                                                
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 3KCG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055817.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-MAY-09                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9796                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 112588                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 58.830                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.58000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1E03, 1RFN                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.25M AMMONIUM SULFATE, 19.5% PEG        
REMARK 280  3350, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       39.39000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.61500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       44.22000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.61500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.39000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       44.22000            
REMARK 290   SMTRY3   4  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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, I, A, B, C, D                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER L   138                                                      
REMARK 465     GLN L   139                                                      
REMARK 465     THR L   140                                                      
REMARK 465     SER L   141                                                      
REMARK 465     LYS L   142                                                      
REMARK 465     HIS I     1                                                      
REMARK 465     GLY I     2                                                      
REMARK 465     LYS I    28                                                      
REMARK 465     LYS I    29                                                      
REMARK 465     ALA I    30                                                      
REMARK 465     THR I    31                                                      
REMARK 465     GLU I    32                                                      
REMARK 465     ASP I    33                                                      
REMARK 465     GLU I    34                                                      
REMARK 465     GLY I    35                                                      
REMARK 465     SER I    36                                                      
REMARK 465     GLU I    37                                                      
REMARK 465     LYS I   432                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET L  84    CG   SD   CE                                        
REMARK 470     THR L  87    OG1  CG2                                            
REMARK 470     LYS L 100    CD   CE   NZ                                        
REMARK 470     SER L 102    OG                                                  
REMARK 470     ASP L 104    CG   OD1  OD2                                       
REMARK 470     LYS L 106    CE   NZ                                             
REMARK 470     GLU L 113    OE1  OE2                                            
REMARK 470     ARG L 116    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU L 119    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 125    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  23    CE   NZ                                             
REMARK 470     LYS H  82    CD   CE   NZ                                        
REMARK 470     LYS H 173    CD   CE   NZ                                        
REMARK 470     SER I   3    OG                                                  
REMARK 470     LYS I  11    CE   NZ                                             
REMARK 470     ILE I  15    CG1  CG2  CD1                                       
REMARK 470     GLU I  27    CG   CD   OE1  OE2                                  
REMARK 470     GLN I  38    CG   CD   OE1  NE2                                  
REMARK 470     LYS I  39    CG   CD   CE   NZ                                   
REMARK 470     GLU I  42    CD   OE1  OE2                                       
REMARK 470     ARG I 132    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS I 136    CD   CE   NZ                                        
REMARK 470     LYS I 188    CD   CE   NZ                                        
REMARK 470     LYS I 222    CE   NZ                                             
REMARK 470     LYS I 257    CG   CD   CE   NZ                                   
REMARK 470     GLU I 289    CG   CD   OE1  OE2                                  
REMARK 470     LYS I 294    CG   CD   CE   NZ                                   
REMARK 470     LYS I 297    CD   CE   NZ                                        
REMARK 470     THR I 300    OG1  CG2                                            
REMARK 470     GLU I 302    CG   CD   OE1  OE2                                  
REMARK 470     VAL I 303    CG1  CG2                                            
REMARK 470     GLU I 306    CD   OE1  OE2                                       
REMARK 470     GLU I 312    CD   OE1  OE2                                       
REMARK 470     GLU I 313    CD   OE1  OE2                                       
REMARK 470     VAL I 431    CG1  CG2                                            
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    CYS H 182   CA  -  CB  -  SG  ANGL. DEV. =   8.8 DEGREES          
REMARK 500    CYS H 220   CA  -  CB  -  SG  ANGL. DEV. =   7.1 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    ASP L  85      -62.55    170.75                                   
REMARK 500    GLN L  97      -87.26   -116.07                                   
REMARK 500    ASP L 104       62.17     68.06                                   
REMARK 500    GLN L 121       14.17     59.40                                   
REMARK 500    HIS H  71      -63.57   -134.31                                   
REMARK 500    ASN H  97      118.23    124.60                                   
REMARK 500    ASN H  97      121.63    123.54                                   
REMARK 500    ASN H 115     -168.47   -160.60                                   
REMARK 500    SER H 214      -73.49   -124.97                                   
REMARK 500    GLU H 219     -154.05     64.26                                   
REMARK 500    MET I  17       44.81   -143.75                                   
REMARK 500    ASN I  96     -139.87     51.67                                   
REMARK 500    ASN I  96     -139.87     51.37                                   
REMARK 500    SER I 138     -179.56   -175.43                                   
REMARK 500    ASN I 178       50.09   -141.59                                   
REMARK 500    GLU I 205       -0.05     70.85                                   
REMARK 500    ASP I 277      -18.72     66.26                                   
REMARK 500    ASP I 277      -16.16     66.26                                   
REMARK 500    GLU I 289      -23.89     91.56                                   
REMARK 500    LEU I 299      110.02   -168.92                                   
REMARK 500    ASN I 396       85.08     82.27                                   
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 H 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU H  70   OE2                                                    
REMARK 620 2 ASN H  72   O    86.5                                              
REMARK 620 3 GLU H  75   O   164.5  83.6                                        
REMARK 620 4 GLU H  77   OE1  81.2  89.1 110.5                                  
REMARK 620 5 GLU H  80   OE2 101.2 170.5  90.0  86.6                            
REMARK 620 6 HOH H 267   O    84.1  95.8  85.0 164.2  90.6                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  3KCG L   85   142  UNP    P00740   FA9_HUMAN      131    188             
DBREF  3KCG H   16   245  UNP    P00740   FA9_HUMAN      227    461             
DBREF  3KCG I    1   432  UNP    P01008   ANT3_HUMAN      33    464             
SEQADV 3KCG MET L   84  UNP  P00740              INITIATING METHIONINE          
SEQADV 3KCG ALA H  195  UNP  P00740    SER   411 ENGINEERED MUTATION            
SEQADV 3KCG ALA I  137  UNP  P01008    SER   169 ENGINEERED MUTATION            
SEQRES   1 L   59  MET ASP VAL THR CYS ASN ILE LYS ASN GLY ARG CYS GLU          
SEQRES   2 L   59  GLN PHE CYS LYS ASN SER ALA ASP ASN LYS VAL VAL CYS          
SEQRES   3 L   59  SER CYS THR GLU GLY TYR ARG LEU ALA GLU ASN GLN LYS          
SEQRES   4 L   59  SER CYS GLU PRO ALA VAL PRO PHE PRO CYS GLY ARG VAL          
SEQRES   5 L   59  SER VAL SER GLN THR SER LYS                                  
SEQRES   1 H  235  VAL VAL GLY GLY GLU ASP ALA LYS PRO GLY GLN PHE PRO          
SEQRES   2 H  235  TRP GLN VAL VAL LEU ASN GLY LYS VAL ASP ALA PHE CYS          
SEQRES   3 H  235  GLY GLY SER ILE VAL ASN GLU LYS TRP ILE VAL THR ALA          
SEQRES   4 H  235  ALA HIS CYS VAL GLU THR GLY VAL LYS ILE THR VAL VAL          
SEQRES   5 H  235  ALA GLY GLU HIS ASN ILE GLU GLU THR GLU HIS THR GLU          
SEQRES   6 H  235  GLN LYS ARG ASN VAL ILE ARG ILE ILE PRO HIS HIS ASN          
SEQRES   7 H  235  TYR ASN ALA ALA ILE ASN LYS TYR ASN HIS ASP ILE ALA          
SEQRES   8 H  235  LEU LEU GLU LEU ASP GLU PRO LEU VAL LEU ASN SER TYR          
SEQRES   9 H  235  VAL THR PRO ILE CYS ILE ALA ASP LYS GLU TYR THR ASN          
SEQRES  10 H  235  ILE PHE LEU LYS PHE GLY SER GLY TYR VAL SER GLY TRP          
SEQRES  11 H  235  GLY ARG VAL PHE HIS LYS GLY ARG SER ALA LEU VAL LEU          
SEQRES  12 H  235  GLN TYR LEU ARG VAL PRO LEU VAL ASP ARG ALA THR CYS          
SEQRES  13 H  235  LEU ARG SER THR LYS PHE THR ILE TYR ASN ASN MET PHE          
SEQRES  14 H  235  CYS ALA GLY PHE HIS GLU GLY GLY ARG ASP SER CYS GLN          
SEQRES  15 H  235  GLY ASP ALA GLY GLY PRO HIS VAL THR GLU VAL GLU GLY          
SEQRES  16 H  235  THR SER PHE LEU THR GLY ILE ILE SER TRP GLY GLU GLU          
SEQRES  17 H  235  CYS ALA MET LYS GLY LYS TYR GLY ILE TYR THR LYS VAL          
SEQRES  18 H  235  SER ARG TYR VAL ASN TRP ILE LYS GLU LYS THR LYS LEU          
SEQRES  19 H  235  THR                                                          
SEQRES   1 I  432  HIS GLY SER PRO VAL ASP ILE CYS THR ALA LYS PRO ARG          
SEQRES   2 I  432  ASP ILE PRO MET ASN PRO MET CYS ILE TYR ARG SER PRO          
SEQRES   3 I  432  GLU LYS LYS ALA THR GLU ASP GLU GLY SER GLU GLN LYS          
SEQRES   4 I  432  ILE PRO GLU ALA THR ASN ARG ARG VAL TRP GLU LEU SER          
SEQRES   5 I  432  LYS ALA ASN SER ARG PHE ALA THR THR PHE TYR GLN HIS          
SEQRES   6 I  432  LEU ALA ASP SER LYS ASN ASP ASN ASP ASN ILE PHE LEU          
SEQRES   7 I  432  SER PRO LEU SER ILE SER THR ALA PHE ALA MET THR LYS          
SEQRES   8 I  432  LEU GLY ALA CYS ASN ASP THR LEU GLN GLN LEU MET GLU          
SEQRES   9 I  432  VAL PHE LYS PHE ASP THR ILE SER GLU LYS THR SER ASP          
SEQRES  10 I  432  GLN ILE HIS PHE PHE PHE ALA LYS LEU ASN CYS ARG LEU          
SEQRES  11 I  432  TYR ARG LYS ALA ASN LYS ALA SER LYS LEU VAL SER ALA          
SEQRES  12 I  432  ASN ARG LEU PHE GLY ASP LYS SER LEU THR PHE ASN GLU          
SEQRES  13 I  432  THR TYR GLN ASP ILE SER GLU LEU VAL TYR GLY ALA LYS          
SEQRES  14 I  432  LEU GLN PRO LEU ASP PHE LYS GLU ASN ALA GLU GLN SER          
SEQRES  15 I  432  ARG ALA ALA ILE ASN LYS TRP VAL SER ASN LYS THR GLU          
SEQRES  16 I  432  GLY ARG ILE THR ASP VAL ILE PRO SER GLU ALA ILE ASN          
SEQRES  17 I  432  GLU LEU THR VAL LEU VAL LEU VAL ASN THR ILE TYR PHE          
SEQRES  18 I  432  LYS GLY LEU TRP LYS SER LYS PHE SER PRO GLU ASN THR          
SEQRES  19 I  432  ARG LYS GLU LEU PHE TYR LYS ALA ASP GLY GLU SER CYS          
SEQRES  20 I  432  SER ALA SER MET MET TYR GLN GLU GLY LYS PHE ARG TYR          
SEQRES  21 I  432  ARG ARG VAL ALA GLU GLY THR GLN VAL LEU GLU LEU PRO          
SEQRES  22 I  432  PHE LYS GLY ASP ASP ILE THR MET VAL LEU ILE LEU PRO          
SEQRES  23 I  432  LYS PRO GLU LYS SER LEU ALA LYS VAL GLU LYS GLU LEU          
SEQRES  24 I  432  THR PRO GLU VAL LEU GLN GLU TRP LEU ASP GLU LEU GLU          
SEQRES  25 I  432  GLU MET MET LEU VAL VAL HIS MET PRO ARG PHE ARG ILE          
SEQRES  26 I  432  GLU ASP GLY PHE SER LEU LYS GLU GLN LEU GLN ASP MET          
SEQRES  27 I  432  GLY LEU VAL ASP LEU PHE SER PRO GLU LYS SER LYS LEU          
SEQRES  28 I  432  PRO GLY ILE VAL ALA GLU GLY ARG ASP ASP LEU TYR VAL          
SEQRES  29 I  432  SER ASP ALA PHE HIS LYS ALA PHE LEU GLU VAL ASN GLU          
SEQRES  30 I  432  GLU GLY SER GLU ALA ALA ALA SER THR ALA VAL VAL ILE          
SEQRES  31 I  432  ALA GLY ARG SER LEU ASN PRO ASN ARG VAL THR PHE LYS          
SEQRES  32 I  432  ALA ASN ARG PRO PHE LEU VAL PHE ILE ARG GLU VAL PRO          
SEQRES  33 I  432  LEU ASN THR ILE ILE PHE MET GLY ARG VAL ALA ASN PRO          
SEQRES  34 I  432  CYS VAL LYS                                                  
MODRES 3KCG ASN I   96  ASN  GLYCOSYLATION SITE                                 
MODRES 3KCG ASN I  155  ASN  GLYCOSYLATION SITE                                 
MODRES 3KCG ASN I  192  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A   1      14                                                       
HET    FUC  A   2      10                                                       
HET    NAG  B   1      14                                                       
HET    NAG  B   2      14                                                       
HET    MAN  B   3      11                                                       
HET    NAG  C   1      14                                                       
HET    FUC  C   2      10                                                       
HET    Z9L  D   1      25                                                       
HET    Z9K  D   2      17                                                       
HET    GU6  D   3      23                                                       
HET    GU1  D   4      14                                                       
HET    Z9H  D   5      21                                                       
HET     CA  H 500       1                                                       
HET    MPD  I5276       8                                                       
HET    MPD  I5277       8                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     Z9L METHYL 2,3,6-TRI-O-SULFO-ALPHA-D-GLUCOPYRANOSIDE                 
HETNAM     Z9K 3-O-METHYL-2-O-SULFO-ALPHA-L-IDOPYRANURONIC ACID                 
HETNAM     GU6 2,3,6-TRI-O-SULFO-ALPHA-D-GLUCOPYRANOSE                          
HETNAM     GU1 2,3-DI-O-METHYL-BETA-D-GLUCOPYRANURONIC ACID                     
HETNAM     Z9H 3,4-DI-O-METHYL-2,6-DI-O-SULFO-ALPHA-D-GLUCOPYRANOSE             
HETNAM      CA CALCIUM 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                         
HETSYN     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
HETSYN     GU6 2,3,6-TRI-O-SULFONATO-ALPHA-D-GLUCOPYRANOSE; 2,3,6-TRI-          
HETSYN   2 GU6  O-SULFO-ALPHA-D-GLUCOSE; 2,3,6-TRI-O-SULFO-D-GLUCOSE;           
HETSYN   3 GU6  2,3,6-TRI-O-SULFO-GLUCOSE                                       
HETSYN     GU1 2,3-DI-O-METHYL-BETA-D-GLUCURONIC ACID; 2,3-DI-O-                
HETSYN   2 GU1  METHYL-D-GLUCURONIC ACID; 2,3-DI-O-METHYL-GLUCURONIC            
HETSYN   3 GU1  ACID                                                            
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   7  Z9L    C7 H14 O15 S3                                                
FORMUL   7  Z9K    C7 H12 O10 S                                                 
FORMUL   7  GU6    C6 H12 O15 S3                                                
FORMUL   7  GU1    C8 H14 O7                                                    
FORMUL   7  Z9H    C8 H16 O12 S2                                                
FORMUL   8   CA    CA 2+                                                        
FORMUL   9  MPD    2(C6 H14 O2)                                                 
FORMUL  11  HOH   *667(H2 O)                                                    
HELIX    1   1 ILE L   90  CYS L   95  5                                   6    
HELIX    2   2 ALA H   55  VAL H   59  5                                   5    
HELIX    3   3 ASN H   95  ASN H   97  5                                   5    
HELIX    4   4 ASP H  125  LYS H  132  1                                  10    
HELIX    5   5 ASP H  164  ARG H  170  1                                   7    
HELIX    6   6 TYR H  234  LYS H  243  1                                  10    
HELIX    7   7 ASP I    6  ALA I   10  5                                   5    
HELIX    8   8 ASN I   45  LYS I   70  1                                  26    
HELIX    9   9 SER I   79  LEU I   92  1                                  14    
HELIX   10  10 CYS I   95  PHE I  106  1                                  12    
HELIX   11  11 SER I  112  GLN I  118  1                                   7    
HELIX   12  12 GLN I  118  ASN I  135  1                                  18    
HELIX   13  13 ASN I  155  GLY I  167  1                                  13    
HELIX   14  14 ASP I  174  THR I  194  1                                  21    
HELIX   15  15 SER I  230  THR I  234  5                                   5    
HELIX   16  16 ALA I  264  GLY I  266  5                                   3    
HELIX   17  17 SER I  291  GLU I  298  1                                   8    
HELIX   18  18 THR I  300  LEU I  311  1                                  12    
HELIX   19  19 LEU I  331  MET I  338  1                                   8    
HELIX   20  20 VAL I  341  SER I  345  5                                   5    
SHEET    1   A 2 PHE L  98  ASN L 101  0                                        
SHEET    2   A 2 VAL L 107  SER L 110 -1  O  VAL L 108   N  LYS L 100           
SHEET    1   B 2 TYR L 115  LEU L 117  0                                        
SHEET    2   B 2 CYS L 124  PRO L 126 -1  O  GLU L 125   N  ARG L 116           
SHEET    1   C 6 GLU H  20  ASP H  21  0                                        
SHEET    2   C 6 GLN H 156  VAL H 163 -1  O  TYR H 157   N  GLU H  20           
SHEET    3   C 6 SER H 135  GLY H 140 -1  N  GLY H 136   O  VAL H 160           
SHEET    4   C 6 PRO H 198  VAL H 203 -1  O  VAL H 200   N  TYR H 137           
SHEET    5   C 6 THR H 206  GLY H 216 -1  O  THR H 206   N  VAL H 203           
SHEET    6   C 6 ALA I 391  GLY I 392 -1  O  ALA I 391   N  GLY H 216           
SHEET    1   D 6 GLU H  20  ASP H  21  0                                        
SHEET    2   D 6 GLN H 156  VAL H 163 -1  O  TYR H 157   N  GLU H  20           
SHEET    3   D 6 MET H 180  ALA H 183 -1  O  CYS H 182   N  VAL H 163           
SHEET    4   D 6 GLY H 226  LYS H 230 -1  O  TYR H 228   N  PHE H 181           
SHEET    5   D 6 THR H 206  GLY H 216 -1  N  TRP H 215   O  ILE H 227           
SHEET    6   D 6 ALA I 391  GLY I 392 -1  O  ALA I 391   N  GLY H 216           
SHEET    1   E 7 GLN H  30  ASN H  34  0                                        
SHEET    2   E 7 CYS H  42  ASN H  48 -1  O  CYS H  42   N  LEU H  33           
SHEET    3   E 7 TRP H  51  THR H  54 -1  O  TRP H  51   N  VAL H  47           
SHEET    4   E 7 ALA H 104  LEU H 108 -1  O  LEU H 106   N  ILE H  52           
SHEET    5   E 7 GLN H  81  PRO H  90 -1  N  ILE H  89   O  LEU H 105           
SHEET    6   E 7 THR H  65  ALA H  68 -1  N  VAL H  66   O  ARG H  83           
SHEET    7   E 7 GLN H  30  ASN H  34 -1  N  ASN H  34   O  THR H  65           
SHEET    1   F 7 ILE I  76  LEU I  78  0                                        
SHEET    2   F 7 THR I 419  VAL I 426 -1  O  ARG I 425   N  ILE I  76           
SHEET    3   F 7 PHE I 408  GLU I 414 -1  N  PHE I 408   O  VAL I 426           
SHEET    4   F 7 ILE I 279  LEU I 285 -1  N  VAL I 282   O  PHE I 411           
SHEET    5   F 7 GLN I 268  PRO I 273 -1  N  LEU I 270   O  LEU I 283           
SHEET    6   F 7 SER I 246  ARG I 262 -1  N  ARG I 261   O  VAL I 269           
SHEET    7   F 7 ARG I 235  TYR I 240 -1  N  PHE I 239   O  CYS I 247           
SHEET    1   G 8 ILE I  76  LEU I  78  0                                        
SHEET    2   G 8 THR I 419  VAL I 426 -1  O  ARG I 425   N  ILE I  76           
SHEET    3   G 8 PHE I 408  GLU I 414 -1  N  PHE I 408   O  VAL I 426           
SHEET    4   G 8 ILE I 279  LEU I 285 -1  N  VAL I 282   O  PHE I 411           
SHEET    5   G 8 GLN I 268  PRO I 273 -1  N  LEU I 270   O  LEU I 283           
SHEET    6   G 8 SER I 246  ARG I 262 -1  N  ARG I 261   O  VAL I 269           
SHEET    7   G 8 GLU I 312  PRO I 321 -1  O  MET I 320   N  MET I 252           
SHEET    8   G 8 VAL I 400  LYS I 403  1  O  PHE I 402   N  HIS I 319           
SHEET    1   H 5 GLN I 171  LEU I 173  0                                        
SHEET    2   H 5 SER I 138  ASP I 149  1  N  GLY I 148   O  LEU I 173           
SHEET    3   H 5 LEU I 213  GLY I 223 -1  O  TYR I 220   N  VAL I 141           
SHEET    4   H 5 ASP I 366  VAL I 375  1  O  PHE I 368   N  LEU I 215           
SHEET    5   H 5 PHE I 323  SER I 330 -1  N  PHE I 323   O  VAL I 375           
SSBOND   1 CYS L   88    CYS L   99                          1555   1555  2.03  
SSBOND   2 CYS L   95    CYS L  109                          1555   1555  2.03  
SSBOND   3 CYS L  111    CYS L  124                          1555   1555  2.03  
SSBOND   4 CYS L  132    CYS H  122                          1555   1555  2.04  
SSBOND   5 CYS H   42    CYS H   58                          1555   1555  2.04  
SSBOND   6 CYS H  168    CYS H  182                          1555   1555  2.02  
SSBOND   7 CYS H  191    CYS H  220                          1555   1555  2.04  
SSBOND   8 CYS I    8    CYS I  128                          1555   1555  2.04  
SSBOND   9 CYS I   21    CYS I   95                          1555   1555  2.03  
SSBOND  10 CYS I  247    CYS I  430                          1555   1555  2.03  
LINK         ND2 ASN I  96                 C1  NAG A   1     1555   1555  1.45  
LINK         ND2 ASN I 155                 C1  NAG B   1     1555   1555  1.45  
LINK         ND2 ASN I 192                 C1  NAG C   1     1555   1555  1.45  
LINK         O6  NAG A   1                 C1  FUC A   2     1555   1555  1.40  
LINK         O4  NAG B   1                 C1  NAG B   2     1555   1555  1.43  
LINK         O4  NAG B   2                 C1  MAN B   3     1555   1555  1.39  
LINK         O6  NAG C   1                 C1  FUC C   2     1555   1555  1.40  
LINK         O4  Z9L D   1                 C1  Z9K D   2     1555   1555  1.44  
LINK         O4  Z9K D   2                 C1  GU6 D   3     1555   1555  1.44  
LINK         O4  GU6 D   3                 C1  GU1 D   4     1555   1555  1.44  
LINK         O4  GU1 D   4                 C1  Z9H D   5     1555   1555  1.44  
LINK         OE2 GLU H  70                CA    CA H 500     1555   1555  2.26  
LINK         O   ASN H  72                CA    CA H 500     1555   1555  2.36  
LINK         O   GLU H  75                CA    CA H 500     1555   1555  2.20  
LINK         OE1 GLU H  77                CA    CA H 500     1555   1555  2.45  
LINK         OE2 GLU H  80                CA    CA H 500     1555   1555  2.33  
LINK         O   HOH H 267                CA    CA H 500     1555   1555  2.22  
CRYST1   78.780   88.440  147.230  90.00  90.00  90.00 P 21 21 21    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      0.012694  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011307  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006792        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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