GenomeNet

Database: PDB
Entry: 1SPJ
LinkDB: 1SPJ
Original site: 1SPJ 
HEADER    HYDROLASE                               16-MAR-04   1SPJ              
TITLE     STRUCTURE OF MATURE HUMAN TISSUE KALLIKREIN (HUMAN KALLIKREIN 1 OR    
TITLE    2 KLK1) AT 1.70 ANGSTROM RESOLUTION WITH VACANT ACTIVE SITE            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: KALLIKREIN 1;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TISSUE KALLIKREIN, KIDNEY/PANCREAS/SALIVARY GLAND           
COMPND   5 KALLIKREIN;                                                          
COMPND   6 EC: 3.4.21.35;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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: KLK1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBAC3                                     
KEYWDS    SERINE PROTEASE, KLK1, HK1, HUMAN KALLIKREIN 1, HUMAN TISSUE          
KEYWDS   2 KALLIKREIN 1, TISSUE KALLIKREIN, HYDROLASE                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.LAXMIKANTHAN,S.I.BLABER,M.J.BERNETT,M.BLABER                        
REVDAT   5   29-JUL-20 1SPJ    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE                                     
REVDAT   4   13-JUL-11 1SPJ    1       VERSN                                    
REVDAT   3   24-FEB-09 1SPJ    1       VERSN                                    
REVDAT   2   08-MAR-05 1SPJ    1       JRNL                                     
REVDAT   1   25-JAN-05 1SPJ    0                                                
JRNL        AUTH   G.LAXMIKANTHAN,S.I.BLABER,M.J.BERNETT,I.A.SCARISBRICK,       
JRNL        AUTH 2 M.A.JULIANO,M.BLABER                                         
JRNL        TITL   1.70 A X-RAY STRUCTURE OF HUMAN APO KALLIKREIN 1: STRUCTURAL 
JRNL        TITL 2 CHANGES UPON PEPTIDE INHIBITOR/SUBSTRATE BINDING             
JRNL        REF    PROTEINS                      V.  58   802 2005              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   15651049                                                     
JRNL        DOI    10.1002/PROT.20368                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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) : 38.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 324246.890                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 27474                          
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) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1336                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) (%) : 87.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4042                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2390                       
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 219                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1820                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 354                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.08000                                             
REMARK   3    B22 (A**2) : 1.45000                                              
REMARK   3    B33 (A**2) : -1.37000                                             
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) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
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) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.10                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.600                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.910                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 47.65                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  5  : ACETATE.PARAM                                  
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  5   : ACETATE.TOP                                    
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SPJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000021896.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 103.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC BLUE CONFOCAL MIRRORS        
REMARK 200  OPTICS                         : OSMIC BLUE CONFOCAL MIRRORS        
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27997                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.868                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% POLY ETHYLENE GLYCOL 3350, 100 MM    
REMARK 280  TRIS 6.5,150 MM CALCIUM ACETATE,, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 277.15K, PH 6.5                                         
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       22.35950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.31300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.20200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.31300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.35950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.20200            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     HIS A    95G                                                     
REMARK 465     THR A    95H                                                     
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     ASN A  95F   CG   OD1  ND2                                       
REMARK 470     ARG A  95I   CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  95J   CG   CD   OE1  NE2                                  
REMARK 470     GLU A 129    CG   CD   OE1  OE2                                  
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    GLN A  65   N   -  CA  -  C   ANGL. DEV. = -17.4 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 A  36     -126.76     56.05                                   
REMARK 500    HIS A  71      -54.06   -131.86                                   
REMARK 500    SER A 214      -62.41   -121.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 300  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 169   O                                                      
REMARK 620 2 HIS A 172   O    91.2                                              
REMARK 620 3 HOH A 619   O    90.1  73.4                                        
REMARK 620 4 HOH A 937   O   174.5  91.7  86.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 245   OD1                                                    
REMARK 620 2 HOH A 684   O    94.9                                              
REMARK 620 3 HOH A 767   O    98.0  76.7                                        
REMARK 620 4 HOH A 776   O    81.8 150.8 132.5                                  
REMARK 620 5 HOH A 882   O    78.4  82.7 158.8  68.1                            
REMARK 620 6 HOH A 912   O    92.4 138.8  62.1  70.4 138.3                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  1SPJ A   16   246  UNP    P06870   KLK1_HUMAN      25    262             
SEQADV 1SPJ GLU A  128  UNP  P06870    GLN   145 ENGINEERED                     
SEQADV 1SPJ LYS A  169  UNP  P06870    GLU   186 ENGINEERED                     
SEQRES   1 A  238  ILE VAL GLY GLY TRP GLU CYS GLU GLN HIS SER GLN PRO          
SEQRES   2 A  238  TRP GLN ALA ALA LEU TYR HIS PHE SER THR PHE GLN CYS          
SEQRES   3 A  238  GLY GLY ILE LEU VAL HIS ARG GLN TRP VAL LEU THR ALA          
SEQRES   4 A  238  ALA HIS CYS ILE SER ASP ASN TYR GLN LEU TRP LEU GLY          
SEQRES   5 A  238  ARG HIS ASN LEU PHE ASP ASP GLU ASN THR ALA GLN PHE          
SEQRES   6 A  238  VAL HIS VAL SER GLU SER PHE PRO HIS PRO GLY PHE ASN          
SEQRES   7 A  238  MET SER LEU LEU GLU ASN HIS THR ARG GLN ALA ASP GLU          
SEQRES   8 A  238  ASP TYR SER HIS ASP LEU MET LEU LEU ARG LEU THR GLU          
SEQRES   9 A  238  PRO ALA ASP THR ILE THR ASP ALA VAL LYS VAL VAL GLU          
SEQRES  10 A  238  LEU PRO THR GLU GLU PRO GLU VAL GLY SER THR CYS LEU          
SEQRES  11 A  238  ALA SER GLY TRP GLY SER ILE GLU PRO GLU ASN PHE SER          
SEQRES  12 A  238  PHE PRO ASP ASP LEU GLN CYS VAL ASP LEU LYS ILE LEU          
SEQRES  13 A  238  PRO ASN ASP GLU CYS LYS LYS ALA HIS VAL GLN LYS VAL          
SEQRES  14 A  238  THR ASP PHE MET LEU CYS VAL GLY HIS LEU GLU GLY GLY          
SEQRES  15 A  238  LYS ASP THR CYS VAL GLY ASP SER GLY GLY PRO LEU MET          
SEQRES  16 A  238  CYS ASP GLY VAL LEU GLN GLY VAL THR SER TRP GLY TYR          
SEQRES  17 A  238  VAL PRO CYS GLY THR PRO ASN LYS PRO SER VAL ALA VAL          
SEQRES  18 A  238  ARG VAL LEU SER TYR VAL LYS TRP ILE GLU ASP THR ILE          
SEQRES  19 A  238  ALA GLU ASN SER                                              
MODRES 1SPJ ASN A   95  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 401      14                                                       
HET     CA  A 300       1                                                       
HET     CA  A 301       1                                                       
HET    ACY  A 501       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  ACY    C2 H4 O2                                                     
FORMUL   6  HOH   *354(H2 O)                                                    
HELIX    1   1 ALA A   55  ILE A   59  5                                   5    
HELIX    2   2 ASN A   95  GLU A   95E 5                                   6    
HELIX    3   3 PRO A  164  HIS A  172  1                                   9    
HELIX    4   4 TYR A  234  ASN A  245  1                                  12    
SHEET    1   A 8 TRP A  20  GLU A  21  0                                        
SHEET    2   A 8 GLN A 156  LEU A 163 -1  O  CYS A 157   N  TRP A  20           
SHEET    3   A 8 MET A 180  GLY A 184 -1  O  CYS A 182   N  LEU A 163           
SHEET    4   A 8 SER A 226  ARG A 230 -1  O  SER A 226   N  VAL A 183           
SHEET    5   A 8 VAL A 208  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    6   A 8 PRO A 198  CYS A 201 -1  N  CYS A 201   O  VAL A 208           
SHEET    7   A 8 THR A 135  GLY A 140 -1  N  LEU A 137   O  MET A 200           
SHEET    8   A 8 GLN A 156  LEU A 163 -1  O  LEU A 160   N  CYS A 136           
SHEET    1   B 7 GLN A  81  VAL A  83  0                                        
SHEET    2   B 7 TYR A  64  LEU A  68 -1  N  LEU A  68   O  GLN A  81           
SHEET    3   B 7 GLN A  30  HIS A  35 -1  N  TYR A  34   O  GLN A  65           
SHEET    4   B 7 THR A  39  HIS A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    5   B 7 TRP A  51  THR A  54 -1  O  LEU A  53   N  ILE A  45           
SHEET    6   B 7 MET A 104  LEU A 108 -1  O  LEU A 106   N  VAL A  52           
SHEET    7   B 7 VAL A  85  PRO A  90 -1  N  PHE A  89   O  LEU A 105           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.05  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.04  
LINK         ND2 ASN A  95                 C1  NAG A 401     1555   1555  1.45  
LINK         O   LYS A 169                CA    CA A 300     1555   1555  2.33  
LINK         O   HIS A 172                CA    CA A 300     1555   1555  2.34  
LINK         OD1 ASN A 245                CA    CA A 301     1555   1555  2.30  
LINK        CA    CA A 300                 O   HOH A 619     1555   1555  2.42  
LINK        CA    CA A 300                 O   HOH A 937     1555   1555  2.39  
LINK        CA    CA A 301                 O   HOH A 684     1555   1555  2.48  
LINK        CA    CA A 301                 O   HOH A 767     1555   1555  2.36  
LINK        CA    CA A 301                 O   HOH A 776     1555   1555  2.59  
LINK        CA    CA A 301                 O   HOH A 882     1555   1555  2.53  
LINK        CA    CA A 301                 O   HOH A 912     1555   1555  2.46  
CISPEP   1 VAL A  218    PRO A  219          0         0.32                     
CRYST1   44.719   76.404   76.626  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      0.022362  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013088  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013050        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system