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Database: PDB
Entry: 1K9O
LinkDB: 1K9O
Original site: 1K9O 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           29-OCT-01   1K9O              
TITLE     CRYSTAL STRUCTURE OF MICHAELIS SERPIN-TRYPSIN COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALASERPIN;                                                 
COMPND   3 CHAIN: I;                                                            
COMPND   4 SYNONYM: SERPIN 1;                                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TRYPSIN II ANIONIC;                                        
COMPND   9 CHAIN: E;                                                            
COMPND  10 SYNONYM: PRETRYPSINOGEN II;                                          
COMPND  11 EC: 3.4.21.4;                                                        
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MANDUCA SEXTA;                                  
SOURCE   3 ORGANISM_COMMON: TOBACCO HORNWORM;                                   
SOURCE   4 ORGANISM_TAXID: 7130;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: XL1-BLUE;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: H6PQE-60;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  12 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  13 ORGANISM_TAXID: 10116;                                               
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PYT                                       
KEYWDS    MICHAELIS SERPIN-PROTEASE COMPLEX INHIBITORY TRIAD,                   
KEYWDS   2 HYDROLASE/HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.YE,A.L.CECH,R.BELMARES,R.C.BERGSTROM,Y.TONG,D.R.COREY,              
AUTHOR   2 M.R.KANOST,E.J.GOLDSMITH                                             
REVDAT   2   24-FEB-09 1K9O    1       VERSN                                    
REVDAT   1   21-NOV-01 1K9O    0                                                
SPRSDE     21-NOV-01 1K9O      1I99                                             
JRNL        AUTH   S.YE,A.L.CECH,R.BELMARES,R.C.BERGSTROM,Y.TONG,               
JRNL        AUTH 2 D.R.COREY,M.R.KANOST,E.J.GOLDSMITH                           
JRNL        TITL   THE STRUCTURE OF A MICHAELIS SERPIN-PROTEASE                 
JRNL        TITL 2 COMPLEX.                                                     
JRNL        REF    NAT.STRUCT.BIOL.              V.   8   979 2001              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11685246                                                     
JRNL        DOI    10.1038/NSB1101-979                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26545                          
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) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2566                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4604                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 182                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1K9O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-NOV-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014734.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-DEC-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03320                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30999                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRIES 1SEK AND 1DPO                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, DTT, POTASSIUM PHOSPHATE,      
REMARK 280  SODIUM PHOSPHATE, 2-PROPANOL, AMMONIUM CHLORIDE, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       31.98500            
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       63.97000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       63.97000            
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       31.98500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, E                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH I 388  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH I 390  LIES ON A SPECIAL POSITION.                          
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     MET I     9                                                      
REMARK 465     ALA I    10                                                      
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    THR I 169   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ASN I 346   N   -  CA  -  C   ANGL. DEV. =  20.5 DEGREES          
REMARK 500    ILE I 350   N   -  CA  -  C   ANGL. DEV. = -19.6 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    GLU I  12        1.19    -68.49                                   
REMARK 500    ALA I  60      -35.37   -130.10                                   
REMARK 500    ARG I  93      -94.67    -97.28                                   
REMARK 500    ALA I  94      -80.05   -124.44                                   
REMARK 500    VAL I  95     -176.70     72.89                                   
REMARK 500    VAL I 125      -34.27   -153.60                                   
REMARK 500    LYS I 137       77.57   -100.03                                   
REMARK 500    GLU I 168       44.68    -90.38                                   
REMARK 500    GLN I 238      -30.16   -132.50                                   
REMARK 500    ASN I 300       50.27     77.94                                   
REMARK 500    PHE I 305       32.65    -96.68                                   
REMARK 500    GLU I 341       54.30     71.52                                   
REMARK 500    ALA I 342     -129.19     65.72                                   
REMARK 500    ALA I 343      -22.09   -149.61                                   
REMARK 500    ALA I 344      -74.50   -135.39                                   
REMARK 500    ALA I 345       43.22    -97.84                                   
REMARK 500    ASN I 346        4.29    -44.85                                   
REMARK 500    ALA I 347     -105.26    -32.31                                   
REMARK 500    PHE I 348     -152.63   -119.44                                   
REMARK 500    GLU I 370      138.83   -177.34                                   
REMARK 500    ASP I 374       82.36     63.31                                   
REMARK 500    GLU I 385      107.78   -167.58                                   
REMARK 500    ASN E  25       -1.47     92.45                                   
REMARK 500    SER E  37       50.56   -149.52                                   
REMARK 500    TYR E  39      146.51   -176.73                                   
REMARK 500    ASP E  49       -0.59    -54.44                                   
REMARK 500    GLN E  50       11.99   -146.50                                   
REMARK 500    HIS E  71      -66.02   -125.84                                   
REMARK 500    ASN E  74       40.11    -85.63                                   
REMARK 500    VAL E  75      148.86   -177.38                                   
REMARK 500    ASN E 115     -152.50    -94.15                                   
REMARK 500    CYS E 191     -157.58   -141.99                                   
REMARK 500    LEU E 209       90.44    -69.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH I 388        DISTANCE = 10.17 ANGSTROMS                       
REMARK 525    HOH I 390        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH I 395        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH E1236        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH E1239        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH I 408        DISTANCE =  9.53 ANGSTROMS                       
REMARK 525    HOH I 414        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH I 415        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH E1253        DISTANCE = 11.59 ANGSTROMS                       
REMARK 525    HOH I 418        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH E1258        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH E1259        DISTANCE = 11.43 ANGSTROMS                       
REMARK 525    HOH E1265        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH I 434        DISTANCE =  7.80 ANGSTROMS                       
REMARK 525    HOH E1271        DISTANCE =  9.12 ANGSTROMS                       
REMARK 525    HOH E1275        DISTANCE = 12.91 ANGSTROMS                       
REMARK 525    HOH E1280        DISTANCE = 10.25 ANGSTROMS                       
REMARK 525    HOH I 445        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH E1281        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH E1283        DISTANCE =  7.84 ANGSTROMS                       
REMARK 525    HOH I 450        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH E1293        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH I 459        DISTANCE =  8.84 ANGSTROMS                       
REMARK 525    HOH E1297        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH I 463        DISTANCE =  7.52 ANGSTROMS                       
REMARK 525    HOH E1300        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH E1303        DISTANCE =  8.35 ANGSTROMS                       
REMARK 525    HOH I 474        DISTANCE = 10.41 ANGSTROMS                       
REMARK 525    HOH I 476        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH I 477        DISTANCE = 13.23 ANGSTROMS                       
REMARK 525    HOH I 480        DISTANCE =  7.53 ANGSTROMS                       
DBREF  1K9O I    9   386  UNP    P14754   SERA_MANSE      15    392             
DBREF  1K9O E   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1K9O THR I  280  UNP  P14754    TYR   286 SEE REMARK 999                 
SEQADV 1K9O THR I  323  UNP  P14754    TYR   329 SEE REMARK 999                 
SEQADV 1K9O LYS I  353  UNP  P14754    ALA   359 ENGINEERED                     
SEQADV 1K9O ALA E  195  UNP  P00763    SER   200 ENGINEERED                     
SEQRES   1 I  378  MET ALA GLY GLU THR ASP LEU GLN LYS ILE LEU ARG GLU          
SEQRES   2 I  378  SER ASN ASP GLN PHE THR ALA GLN MET PHE SER GLU VAL          
SEQRES   3 I  378  VAL LYS ALA ASN PRO GLY GLN ASN VAL VAL LEU SER ALA          
SEQRES   4 I  378  PHE SER VAL LEU PRO PRO LEU GLY GLN LEU ALA LEU ALA          
SEQRES   5 I  378  SER VAL GLY GLU SER HIS ASP GLU LEU LEU ARG ALA LEU          
SEQRES   6 I  378  ALA LEU PRO ASN ASP ASN VAL THR LYS ASP VAL PHE ALA          
SEQRES   7 I  378  ASP LEU ASN ARG GLY VAL ARG ALA VAL LYS GLY VAL ASP          
SEQRES   8 I  378  LEU LYS MET ALA SER LYS ILE TYR VAL ALA LYS GLY LEU          
SEQRES   9 I  378  GLU LEU ASN ASP ASP PHE ALA ALA VAL SER ARG ASP VAL          
SEQRES  10 I  378  PHE GLY SER GLU VAL GLN ASN VAL ASP PHE VAL LYS SER          
SEQRES  11 I  378  VAL GLU ALA ALA GLY ALA ILE ASN LYS TRP VAL GLU ASP          
SEQRES  12 I  378  GLN THR ASN ASN ARG ILE LYS ASN LEU VAL ASP PRO ASP          
SEQRES  13 I  378  ALA LEU ASP GLU THR THR ARG SER VAL LEU VAL ASN ALA          
SEQRES  14 I  378  ILE TYR PHE LYS GLY SER TRP LYS ASP LYS PHE VAL LYS          
SEQRES  15 I  378  GLU ARG THR MET ASP ARG ASP PHE HIS VAL SER LYS ASP          
SEQRES  16 I  378  LYS THR ILE LYS VAL PRO THR MET ILE GLY LYS LYS ASP          
SEQRES  17 I  378  VAL ARG TYR ALA ASP VAL PRO GLU LEU ASP ALA LYS MET          
SEQRES  18 I  378  ILE GLU MET SER TYR GLU GLY ASP GLN ALA SER MET ILE          
SEQRES  19 I  378  ILE ILE LEU PRO ASN GLN VAL ASP GLY ILE THR ALA LEU          
SEQRES  20 I  378  GLU GLN LYS LEU LYS ASP PRO LYS ALA LEU SER ARG ALA          
SEQRES  21 I  378  GLU GLU ARG LEU TYR ASN THR GLU VAL GLU ILE THR LEU          
SEQRES  22 I  378  PRO LYS PHE LYS ILE GLU THR THR THR ASP LEU LYS GLU          
SEQRES  23 I  378  VAL LEU SER ASN MET ASN ILE LYS LYS LEU PHE THR PRO          
SEQRES  24 I  378  GLY ALA ALA ARG LEU GLU ASN LEU LEU LYS THR LYS GLU          
SEQRES  25 I  378  SER LEU THR VAL ASP ALA ALA ILE GLN LYS ALA PHE ILE          
SEQRES  26 I  378  GLU VAL ASN GLU GLU GLY ALA GLU ALA ALA ALA ALA ASN          
SEQRES  27 I  378  ALA PHE GLY ILE VAL PRO LYS SER LEU ILE LEU TYR PRO          
SEQRES  28 I  378  GLU VAL HIS ILE ASP ARG PRO PHE TYR PHE GLU LEU LYS          
SEQRES  29 I  378  ILE ASP GLY ILE PRO MET PHE ASN GLY LYS VAL ILE GLU          
SEQRES  30 I  378  PRO                                                          
SEQRES   1 E  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 E  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 E  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 E  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 E  223  HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 E  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 E  223  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 E  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 E  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 E  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 E  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 E  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 E  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 E  223  LYS ASP SER CYS GLN GLY ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 E  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 E  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 E  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 E  223  ALA ASN                                                      
FORMUL   3  HOH   *182(H2 O)                                                    
HELIX    1   1 GLU I   12  LYS I   17  1                                   6    
HELIX    2   2 ILE I   18  LYS I   36  1                                  19    
HELIX    3   3 ALA I   47  SER I   49  5                                   3    
HELIX    4   4 VAL I   50  ALA I   58  1                                   9    
HELIX    5   5 GLY I   63  LEU I   73  1                                  11    
HELIX    6   6 ASN I   79  ASN I   89  1                                  11    
HELIX    7   7 ASP I  116  ALA I  120  5                                   5    
HELIX    8   8 LYS I  137  THR I  153  1                                  17    
HELIX    9   9 ASP I  162  LEU I  166  5                                   5    
HELIX   10  10 VAL I  189  THR I  193  5                                   5    
HELIX   11  11 GLU I  235  ASP I  237  5                                   3    
HELIX   12  12 GLY I  251  LEU I  259  1                                   9    
HELIX   13  13 LEU I  292  ASN I  298  1                                   7    
HELIX   14  14 ALA E   55  TYR E   59  5                                   5    
HELIX   15  15 PRO E  164  TYR E  172  1                                   9    
HELIX   16  16 TYR E  234  ASN E  245  1                                  12    
SHEET    1   A 4 GLU I 360  HIS I 362  0                                        
SHEET    2   A 4 TYR I 273  PRO I 282  1  N  THR I 280   O  VAL I 361           
SHEET    3   A 4 ILE I 206  VAL I 222 -1  N  TYR I 219   O  TYR I 273           
SHEET    4   A 4 MET I 194  PHE I 198 -1  N  MET I 194   O  THR I 210           
SHEET    1   B 8 GLU I 360  HIS I 362  0                                        
SHEET    2   B 8 TYR I 273  PRO I 282  1  N  THR I 280   O  VAL I 361           
SHEET    3   B 8 ILE I 206  VAL I 222 -1  N  TYR I 219   O  TYR I 273           
SHEET    4   B 8 ALA I 227  SER I 233 -1  O  MET I 229   N  ALA I 220           
SHEET    5   B 8 ALA I 239  PRO I 246 -1  O  MET I 241   N  MET I 232           
SHEET    6   B 8 PHE I 367  ILE I 373 -1  O  GLU I 370   N  ILE I 242           
SHEET    7   B 8 PRO I 377  VAL I 383 -1  O  VAL I 383   N  PHE I 367           
SHEET    8   B 8 VAL I  43  LEU I  45 -1  N  LEU I  45   O  ASN I 380           
SHEET    1   C 5 VAL I 130  VAL I 133  0                                        
SHEET    2   C 5 LYS I 101  ALA I 109  1  N  ILE I 106   O  GLN I 131           
SHEET    3   C 5 SER I 172  LYS I 181 -1  O  ALA I 177   N  ALA I 103           
SHEET    4   C 5 ALA I 326  VAL I 335  1  O  PHE I 332   N  PHE I 180           
SHEET    5   C 5 PHE I 284  ASP I 291 -1  N  THR I 290   O  GLN I 329           
SHEET    1   D 4 MET E 180  VAL E 183  0                                        
SHEET    2   D 4 GLY E 226  LYS E 230 -1  O  TYR E 228   N  VAL E 181           
SHEET    3   D 4 GLU E 204  GLY E 216 -1  N  TRP E 215   O  VAL E 227           
SHEET    4   D 4 VAL I 351  PRO I 352 -1  N  VAL I 351   O  GLY E 216           
SHEET    1   E 7 MET E 180  VAL E 183  0                                        
SHEET    2   E 7 GLY E 226  LYS E 230 -1  O  TYR E 228   N  VAL E 181           
SHEET    3   E 7 GLU E 204  GLY E 216 -1  N  TRP E 215   O  VAL E 227           
SHEET    4   E 7 PRO E 198  CYS E 201 -1  N  CYS E 201   O  GLU E 204           
SHEET    5   E 7 GLN E 135  GLY E 140 -1  N  LEU E 137   O  VAL E 200           
SHEET    6   E 7 GLN E 156  PRO E 161 -1  O  LEU E 158   N  ILE E 138           
SHEET    7   E 7 TYR E  20  THR E  21 -1  N  TYR E  20   O  CYS E 157           
SHEET    1   F 7 GLN E  30  ASN E  34  0                                        
SHEET    2   F 7 HIS E  40  ASN E  48 -1  O  CYS E  42   N  LEU E  33           
SHEET    3   F 7 TRP E  51  SER E  54 -1  O  VAL E  53   N  SER E  45           
SHEET    4   F 7 MET E 104  LEU E 108 -1  O  MET E 104   N  SER E  54           
SHEET    5   F 7 GLN E  81  LYS E  90 -1  N  ILE E  89   O  LEU E 105           
SHEET    6   F 7 GLN E  64  LEU E  67 -1  N  VAL E  65   O  VAL E  83           
SHEET    7   F 7 GLN E  30  ASN E  34 -1  N  SER E  32   O  ARG E  66           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.03  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.03  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.04  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.03  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  2.03  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.03  
CRYST1  112.572  112.572   95.955  90.00  90.00 120.00 P 31 2 1      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      0.008880  0.005130  0.000000        0.00000                         
SCALE2      0.000000  0.010260  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010420        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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