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Database: PDB
Entry: 1Z7K
LinkDB: 1Z7K
Original site: 1Z7K 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           25-MAR-05   1Z7K              
TITLE     CRYSTAL STRUCTURE OF TRYPSIN- OVOMUCOID TURKEY EGG WHITE INHIBITOR    
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: OVOMUCOID;                                                 
COMPND   7 CHAIN: B;                                                            
COMPND   8 FRAGMENT: SECOND DOMAIN, RESIDUES 2-63;                              
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: OVOMUCOID;                                                 
COMPND  11 CHAIN: C;                                                            
COMPND  12 FRAGMENT: FIRST DOMAIN, RESIDUES 1-4                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 TISSUE: PANCREAS;                                                    
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MELEAGRIS GALLOPAVO;                            
SOURCE   8 ORGANISM_COMMON: TURKEY;                                             
SOURCE   9 ORGANISM_TAXID: 9103;                                                
SOURCE  10 TISSUE: EGG WHITE;                                                   
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MELEAGRIS GALLOPAVO;                            
SOURCE  13 ORGANISM_COMMON: TURKEY;                                             
SOURCE  14 ORGANISM_TAXID: 9103;                                                
SOURCE  15 TISSUE: EGG WHITE                                                    
KEYWDS    SERINE PROTEASE, HYDROLASE, PROTEASE INHIBITOR, DI-NAG, HYDROLASE-    
KEYWDS   2 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.SYED IBRAHIM,V.PATTABHI                                             
REVDAT   3   13-JUL-11 1Z7K    1       VERSN                                    
REVDAT   2   24-FEB-09 1Z7K    1       VERSN                                    
REVDAT   1   05-APR-05 1Z7K    0                                                
SPRSDE     05-APR-05 1Z7K      1R0T                                             
JRNL        AUTH   B.SYED IBRAHIM,V.PATTABHI                                    
JRNL        TITL   CRYSTAL STRUCTURE OF TRYPSIN-TURKEY EGG WHITE INHIBITOR      
JRNL        TITL 2 COMPLEX                                                      
JRNL        REF    BIOCHEM.BIOPHYS.RES.COMMUN.   V. 313     8 2004              
JRNL        REFN                   ISSN 0006-291X                               
JRNL        PMID   14672690                                                     
JRNL        DOI    10.1016/J.BBRC.2003.11.082                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 29711                          
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                     : 0.188                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1480                            
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           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1720                       
REMARK   3   BIN FREE R VALUE                    : 0.1880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1480                         
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            : 2136                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 126                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.77000                                              
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -1.55000                                             
REMARK   3    B12 (A**2) : 0.99000                                              
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
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) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.031                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.75                            
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        : 0.35                                                 
REMARK   3   BSOL        : 46.55                                                
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  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1Z7K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032397.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 5.30                               
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 RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : COSMIC MIRRORS                     
REMARK 200  OPTICS                         : COSMIC MIRRORS                     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARXDS, DENZO                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29711                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07800                            
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) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.07800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
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: TRYPSIN                                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5M AMMONIUM SULPHATE, 10MM ZINC        
REMARK 280  ACETATE, 50MM ACETATE BUFFER, PH 5.30, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.14933            
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       24.57467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       36.86200            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       12.28733            
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       61.43667            
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 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN B    11     C2   NAG B    64              2.17            
REMARK 500   O    ALA A    23     OG   SER A    26              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A  30   CG    GLN A  30   CD     -0.162                       
REMARK 500    PHE A  41   CZ    PHE A  41   CE2     0.117                       
REMARK 500    SER A  49   CA    SER A  49   CB      0.101                       
REMARK 500    SER A  49   CB    SER A  49   OG     -0.149                       
REMARK 500    GLN A  50   CB    GLN A  50   CG     -0.187                       
REMARK 500    GLU A  80   CD    GLU A  80   OE1    -0.111                       
REMARK 500    GLU A  80   CD    GLU A  80   OE2     0.084                       
REMARK 500    TYR A 151   CE1   TYR A 151   CZ     -0.081                       
REMARK 500    LYS A 159   CE    LYS A 159   NZ     -0.153                       
REMARK 500    TYR A 234   CZ    TYR A 234   CE2    -0.129                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  74   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    GLU A  80   CG  -  CD  -  OE1 ANGL. DEV. = -16.8 DEGREES          
REMARK 500    GLU A  80   CG  -  CD  -  OE2 ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    LYS A 159   CD  -  CE  -  NZ  ANGL. DEV. =  16.0 DEGREES          
REMARK 500    ASP B  39   CB  -  CG  -  OD1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    GLY B  61   C   -  N   -  CA  ANGL. DEV. = -14.6 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    HIS A  71      -63.37   -107.42                                   
REMARK 500    SER A 150       99.99   -167.64                                   
REMARK 500    SER A 214      -67.47   -127.16                                   
REMARK 500    PRO B   3     -124.59    -71.91                                   
REMARK 500    SER B  14     -168.71    -79.23                                   
REMARK 500    ASN C   2     -140.81    -46.73                                   
REMARK 500    GLU C   3       49.59     91.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLN A  50        25.0      L          L   OUTSIDE RANGE           
REMARK 500    HIS A  71        45.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 64                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 65                  
DBREF  1Z7K A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1Z7K B    2    63  UNP    P68390   IOVO_MELGA      65    126             
DBREF  1Z7K C    1     4  UNP    P68390   IOVO_MELGA      12     15             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
SEQRES   1 B   62  VAL PRO MET ASP CYS SER ARG TYR PRO ASN THR THR SER          
SEQRES   2 B   62  GLU GLU GLY LYS VAL MET ILE LEU CYS ASN LYS ALA LEU          
SEQRES   3 B   62  ASN PRO VAL CYS GLY THR ASP GLY VAL THR TYR ASP ASN          
SEQRES   4 B   62  GLU CYS VAL LEU CYS ALA HIS ASN LEU GLU GLN GLY THR          
SEQRES   5 B   62  SER VAL GLY LYS LYS HIS ASP GLY GLU CYS                      
SEQRES   1 C    4  THR ASN GLU GLU                                              
MODRES 1Z7K ASN B   11  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B  64      15                                                       
HET    NAG  B  65      15                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   4  NAG    2(C8 H15 N O6)                                               
FORMUL   5  HOH   *126(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ALA A  244  1                                  11    
HELIX    4   4 ASP B    5  TYR B    9  5                                   5    
HELIX    5   5 ASN B   40  GLY B   52  1                                  13    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  ILE A 181   O  TYR A 228           
SHEET    1   B 6 TYR A  20  THR A  21  0                                        
SHEET    2   B 6 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   B 6 GLU A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4   B 6 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   B 6 GLN A 204  GLY A 216 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   B 6 CYS B  23  ASN B  24 -1  O  CYS B  23   N  GLY A 216           
SHEET    1   C 7 GLN A  30  ASN A  34  0                                        
SHEET    2   C 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   C 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   C 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   C 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   C 7 GLN A  64  LEU A  67 -1  N  VAL A  65   O  ILE A  83           
SHEET    7   C 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SHEET    1   D 2 ASN B  11  THR B  13  0                                        
SHEET    2   D 2 VAL B  19  ILE B  21 -1  O  MET B  20   N  THR B  12           
SHEET    1   E 3 THR B  37  TYR B  38  0                                        
SHEET    2   E 3 VAL B  30  GLY B  32 -1  N  VAL B  30   O  TYR B  38           
SHEET    3   E 3 LYS B  57  HIS B  59 -1  O  HIS B  59   N  CYS B  31           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  1.96  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.10  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.00  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   7 CYS B    6    CYS B   45                          1555   1555  2.05  
SSBOND   8 CYS B   23    CYS B   42                          1555   1555  1.94  
SSBOND   9 CYS B   31    CYS B   63                          1555   1555  1.94  
LINK         ND2 ASN B  11                 C1  NAG B  64     1555   1555  1.43  
LINK         O4  NAG B  64                 C1  NAG B  65     1555   1555  1.50  
SITE     1 AC1  4 SER B   7  ASN B  11  NAG B  65  HOH B  89                    
SITE     1 AC2  4 SER B   7  NAG B  64  THR C   1  ASN C   2                    
CRYST1   98.575   98.575   73.724  90.00  90.00 120.00 P 65          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      0.010145  0.005857  0.000000        0.00000                         
SCALE2      0.000000  0.011714  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013564        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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