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Database: PDB
Entry: 1MCT
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Original site: 1MCT 
HEADER    COMPLEX(PROTEINASE/INHIBITOR)           24-OCT-92   1MCT              
TITLE     THE REFINED 1.6 ANGSTROMS RESOLUTION CRYSTAL STRUCTURE OF             
TITLE    2 THE COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND MCTI-A,          
TITLE    3 A TRYPSIN INHIBITOR OF SQUASH FAMILY                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-TRYPSIN;                                              
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRYPSIN INHIBITOR A;                                       
COMPND   8 CHAIN: I;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: SEED;                                                         
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MOMORDICA CHARANTIA;                            
SOURCE   8 ORGANISM_COMMON: BALSAM PEAR;                                        
SOURCE   9 ORGANISM_TAXID: 3673;                                                
SOURCE  10 ORGAN: SEED                                                          
KEYWDS    COMPLEX(PROTEINASE/INHIBITOR)                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.HUANG,S.LIU,Y.TANG                                                  
REVDAT   4   24-FEB-09 1MCT    1       VERSN                                    
REVDAT   3   01-APR-03 1MCT    1       JRNL                                     
REVDAT   2   15-JAN-94 1MCT    3       CRYST1 SCALE                             
REVDAT   1   31-JAN-94 1MCT    0                                                
JRNL        AUTH   Q.HUANG,S.LIU,Y.TANG                                         
JRNL        TITL   REFINED 1.6 A RESOLUTION CRYSTAL STRUCTURE OF THE            
JRNL        TITL 2 COMPLEX FORMED BETWEEN PORCINE BETA-TRYPSIN AND              
JRNL        TITL 3 MCTI-A, A TRYPSIN INHIBITOR OF THE SQUASH FAMILY.            
JRNL        TITL 4 DETAILED COMPARISON WITH BOVINE BETA-TRYPSIN AND             
JRNL        TITL 5 ITS COMPLEX.                                                 
JRNL        REF    J.MOL.BIOL.                   V. 229  1022 1993              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8445634                                                      
JRNL        DOI    10.1006/JMBI.1993.1102                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Q.HUANG,S.LIU,Y.TANG,F.ZENG,R.QIAN                           
REMARK   1  TITL   AMINO ACID SEQUENCING OF A TRYPSIN INHIBITOR BY              
REMARK   1  TITL 2 REFINED 1.6 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF             
REMARK   1  TITL 3 ITS COMPLEX WITH PORCINE BETA-TRYPSIN                        
REMARK   1  REF    FEBS LETT.                    V. 297   143 1992              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
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            : 2294                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 405                                     
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) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 14.80                           
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  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 1MCT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SQUASH, X-PLOR                                        
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 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+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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       82.87333            
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       41.43667            
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       41.43667            
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       82.87333            
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: 1590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9970 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   62   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     ASN A   79   CB    CG    OD1   ND2                               
REMARK 480     ARG A  125   CG    CD    NE    CZ    NH1   NH2                   
REMARK 480     LYS A  145   CE    NZ                                            
REMARK 480     SER A  147   O     OG                                            
REMARK 480     SER A  149   OG                                                  
REMARK 480     GLN A  221   CD    OE1                                           
REMARK 480     LYS A  222   CG    CD    CE    NZ                                
REMARK 480     ASN A  236   OD1   ND2                                           
REMARK 480     GLN A  239   CD                                                  
REMARK 480     GLN A  240   CG    CD    OE1   NE2                               
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    ARG A  66   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG A 117   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG I   1   NE  -  CZ  -  NH1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG I   1   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 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    ASN A  25      -12.90     81.17                                   
REMARK 500    HIS A  71      -58.25   -132.56                                   
REMARK 500    ASN A 115     -150.82   -149.65                                   
REMARK 500    SER A 214      -66.53   -125.70                                   
REMARK 500    ARG I   5       34.71    -91.12                                   
REMARK 500    ALA I  18     -128.09     42.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 217         0.07    SIDE_CHAIN                              
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 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  77   OE1                                                    
REMARK 620 2 GLU A  80   OE2  86.4                                              
REMARK 620 3 ASN A  72   O    84.9 167.1                                        
REMARK 620 4 VAL A  75   O   104.2  93.4  79.6                                  
REMARK 620 5 GLU A  70   OE1 100.1 101.6  89.3 152.1                            
REMARK 620 6 HOH A 254   O   173.0  89.3 100.2  81.6  75.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 246                  
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: TRYP_PIG                                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        ASP    145            ASN   A      145                        
REMARK 999        GLU    167            GLN   A      167                        
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: ITR2_MOMCH                               
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999        NAME   NUMBER         NAME  CHAIN  SEQ/INSERT CODE            
REMARK 999        LYS     11            THR   I       11                        
REMARK 999        GLN     19            LYS   I       19                        
REMARK 999        ASP     24            ALA   I       24                        
REMARK 999                                                                      
REMARK 999 THE SEQUENCE USED IN THIS ENTRY WAS DETERMINED BY X-RAY              
REMARK 999 CRYSTALLOGRAPHY.  THERE ARE SEVERAL UNCERTAIN ASSIGNMENTS            
REMARK 999 WHICH DIFFER FROM THE CHEMICALLY DETERMINED SEQUENCES.               
DBREF  1MCT A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1MCT I    1    28  UNP    P30709   ITRA_MOMCH       1     28             
SEQADV 1MCT ASN A  165  UNP  P00761    ASP   153 CONFLICT                       
SEQADV 1MCT GLN A  186  UNP  P00761    GLU   175 CONFLICT                       
SEQADV 1MCT ILE I    2  UNP  P30709    SER     2 CONFLICT                       
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 ASN 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 GLN 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 I   28  ARG ILE CYS PRO ARG ILE TRP MET GLU CYS THR ARG ASP          
SEQRES   2 I   28  SER ASP CYS MET ALA LYS CYS ILE CYS VAL ALA GLY HIS          
SEQRES   3 I   28  CYS GLY                                                      
HET     CA  A 246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *135(H2 O)                                                    
HELIX    1  H1 SER A  164  PRO A  173  1                                  10    
HELIX    2  H2 TYR A  234  ASN A  245  1                                  12    
SHEET    1   A 7 MET A 180  VAL A 183  0                                        
SHEET    2   A 7 GLY A 226  LYS A 230 -1  O  GLY A 226   N  VAL A 183           
SHEET    3   A 7 GLN A 204  GLY A 216 -1  O  ILE A 212   N  THR A 229           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 199   N  GLN A 210           
SHEET    5   A 7 GLU A 135  GLY A 140 -1  O  LEU A 137   N  VAL A 200           
SHEET    6   A 7 GLN A 156  PRO A 161 -1  N  GLN A 156   O  GLY A 140           
SHEET    7   A 7 TYR A  20  THR A  21 -1  O  TYR A  20   N  CYS A 157           
SHEET    1   B 4 MET A 180  VAL A 183  0                                        
SHEET    2   B 4 GLY A 226  LYS A 230 -1  O  GLY A 226   N  VAL A 183           
SHEET    3   B 4 GLN A 204  GLY A 216 -1  O  ILE A 212   N  THR A 229           
SHEET    1   C 7 GLN A  30  ASN A  34  0                                        
SHEET    2   C 7 HIS A  40  ASN A  48 -1  N  PHE A  41   O  LEU A  33           
SHEET    3   C 7 TRP A  51  SER A  54 -1  O  TRP A  51   N  ILE A  47           
SHEET    4   C 7 MET A 104  LEU A 108 -1  O  MET A 104   N  SER A  54           
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  O  SER A  32   N  ARG A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.01  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.02  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.02  
SSBOND   7 CYS I    3    CYS I   20                          1555   1555  2.01  
SSBOND   8 CYS I   10    CYS I   22                          1555   1555  2.03  
SSBOND   9 CYS I   16    CYS I   27                          1555   1555  2.03  
LINK        CA    CA A 246                 OE1 GLU A  77     1555   1555  2.80  
LINK        CA    CA A 246                 OE2 GLU A  80     1555   1555  2.34  
LINK        CA    CA A 246                 O   ASN A  72     1555   1555  2.43  
LINK        CA    CA A 246                 O   VAL A  75     1555   1555  2.31  
LINK        CA    CA A 246                 OE1 GLU A  70     1555   1555  2.36  
LINK        CA    CA A 246                 O   HOH A 254     1555   1555  2.64  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  6 GLU A  80  HOH A 254                                          
CRYST1   62.650   62.650  124.310  90.00  90.00 120.00 P 32 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      0.015962  0.009215  0.000000        0.00000                         
SCALE2      0.000000  0.018431  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008044        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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