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Database: PDB
Entry: 3CMS
LinkDB: 3CMS
Original site: 3CMS 
HEADER    HYDROLASE                               26-FEB-90   3CMS              
TITLE     ENGINEERING ENZYME SUB-SITE SPECIFICITY: PREPARATION, KINETIC         
TITLE    2 CHARACTERIZATION AND X-RAY ANALYSIS AT 2.0-ANGSTROMS RESOLUTION OF   
TITLE    3 VAL111PHE SITE-MUTATED CALF CHYMOSIN                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHYMOSIN B;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.23.4;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913                                                 
KEYWDS    HYDROLASE, ACID PROTEINASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.NEWMAN,C.FRAZAO,A.SHEARER,I.J.TICKLE,T.L.BLUNDELL                   
REVDAT   5   29-NOV-17 3CMS    1       HELIX                                    
REVDAT   4   29-FEB-12 3CMS    1       VERSN                                    
REVDAT   3   24-FEB-09 3CMS    1       VERSN                                    
REVDAT   2   01-APR-03 3CMS    1       JRNL                                     
REVDAT   1   15-OCT-92 3CMS    0                                                
JRNL        AUTH   P.STROP,J.SEDLACEK,J.STYS,Z.KADERABKOVA,I.BLAHA,             
JRNL        AUTH 2 L.PAVLICKOVA,J.POHL,M.FABRY,V.KOSTKA,M.NEWMAN                
JRNL        TITL   ENGINEERING ENZYME SUBSITE SPECIFICITY: PREPARATION, KINETIC 
JRNL        TITL 2 CHARACTERIZATION, AND X-RAY ANALYSIS AT 2.0-A RESOLUTION OF  
JRNL        TITL 3 VAL111PHE SITE-MUTATED CALF CHYMOSIN.                        
JRNL        REF    BIOCHEMISTRY                  V.  29  9863 1990              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   2271625                                                      
JRNL        DOI    10.1021/BI00494A016                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.NEWMAN,M.SAFRO,C.FRAZAO,G.KAHN,A.ZDANOV,I.J.TICKLE,        
REMARK   1  AUTH 2 T.L.BLUNDELL,N.ANDREEVA                                      
REMARK   1  TITL   X-RAY ANALYSES OF ASPARTIC PROTEINASES IV: STRUCTURE AND     
REMARK   1  TITL 2 REFINEMENT AT 2.2 ANGSTROMS RESOLUTION OF BOVINE CHYMOSIN    
REMARK   1  REF    J.MOL.BIOL.                   V. 221  1295 1991              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : RESTRAIN                                             
REMARK   3   AUTHORS     : MOSS,DRIESSEN,HANEEF,HOWLIN,HARRIS                   
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21710                          
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 + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2490                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 145                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.022 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.050 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS:                                           
REMARK   3  THE QUANTITY PRESENTED IN THE TEMPERATURE FACTOR FIELD IS           
REMARK   3  U.                                                                  
REMARK   3                                                                      
REMARK   3  RESIDUES 72 TO 79 HAVE BEEN REFINED IN TWO ALTERNATE                
REMARK   3  CONFORMATIONS.  TURN 5 WITH THE A CONFORMATION IS                   
REMARK   3  CLASSIFED TYPE II' 2:2 DISTORTED.  TURN 5 WITH THE B                
REMARK   3  CONFORMATION IS UNCLASSIFIED 2:2.                                   
REMARK   3                                                                      
REMARK   3  INVARIANT RESIDUE TYR 14 HAS BEEN BUILT INTO A CONFORMATION         
REMARK   3  THAT DIFFERS FROM THE WILD-TYPE CHYMOSIN STRUCTURE.                 
REMARK   3  HOWEVER, THIS RESIDUE BELONGS TO THE POORLY DEFINED SURFACE         
REMARK   3  REGION BETWEEN STRANDS AN AND BN, AND THUS THE ASSIGNMENT           
REMARK   3  OF ITS POSITION MUST BE REGARDED AS TENTATIVE.                      
REMARK   4                                                                      
REMARK   4 3CMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000178915.                                   
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       40.10500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.28000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       36.21500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.10500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.28000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       36.21500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       40.10500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.28000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       36.21500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       40.10500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.28000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       36.21500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 THE SPECIFIC GENE MUTATION V111F IS SITUATED BETWEEN THE             
REMARK 400 PRIMARY SPECIFICITY BINDING POCKET S1 AND THE SECONDARY              
REMARK 400 SPECIFICITY POCKET S3, EFFECTING THE BINDING OF LARGE                
REMARK 400 HYDROPHOBIC RESIDUES IN BOTH THESE POCKETS.  THIS MUTATION           
REMARK 400 IS RESPONSIBLE FOR THE REARRANGEMENT OF RESIDUES 72 TO 79            
REMARK 400 KNOWN AS THE ACTIVE SITE FLAP, A FLEXIBLE BETA-HAIRPIN TURN          
REMARK 400 ABOVE THE ACTIVE SITE.                                               
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     ASN A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     SER A   296                                                      
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    LEU A   6   C     THR A   7   N      -0.188                       
REMARK 500    ASP A  11   C     SER A  12   N       0.174                       
REMARK 500    SER A  12   N     SER A  12   CA      0.137                       
REMARK 500    PHE A  15   C     GLY A  16   N       0.175                       
REMARK 500    ASN A  66   C     LEU A  67   N      -0.203                       
REMARK 500    VAL A 202   C     VAL A 203   N      -0.213                       
REMARK 500    GLY A 243   C     GLU A 244   N      -0.142                       
REMARK 500    VAL A 258   C     VAL A 259   N       0.237                       
REMARK 500    ALA A 273   C     TYR A 274   N       0.228                       
REMARK 500    PHE A 305   C     ILE A 306   N       0.243                       
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    TYR A   9   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ASP A  11   O   -  C   -  N   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    TYR A  19   CB  -  CG  -  CD1 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    GLU A  26   CB  -  CG  -  CD  ANGL. DEV. = -16.7 DEGREES          
REMARK 500    GLU A  26   OE1 -  CD  -  OE2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    GLU A  26   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ASP A  32   CB  -  CG  -  OD2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A  37   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    VAL A  40   CA  -  CB  -  CG2 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A  55   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A  59   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A  96   C   -  N   -  CA  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LEU A 103   CB  -  CG  -  CD2 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    GLY A 122   C   -  N   -  CA  ANGL. DEV. =  19.6 DEGREES          
REMARK 500    MET A 123   CG  -  SD  -  CE  ANGL. DEV. =  18.2 DEGREES          
REMARK 500    MET A 140   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    MET A 141   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A 143   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP A 149   CB  -  CG  -  OD1 ANGL. DEV. =  10.9 DEGREES          
REMARK 500    MET A 155   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A 157   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    MET A 164   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    TYR A 189   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    TYR A 189   CG  -  CD1 -  CE1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    SER A 200   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    CYS A 206   CB  -  CA  -  C   ANGL. DEV. =   7.5 DEGREES          
REMARK 500    GLU A 207   O   -  C   -  N   ANGL. DEV. = -10.7 DEGREES          
REMARK 500    GLY A 208   C   -  N   -  CA  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    GLN A 232   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    MET A 255   CG  -  SD  -  CE  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    VAL A 259   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    MET A 266   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    VAL A 304   CA  -  CB  -  CG2 ANGL. DEV. =  10.8 DEGREES          
REMARK 500    ILE A 306   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    ARG A 307   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    TYR A 310   O   -  C   -  N   ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ASP A 314   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 315   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A 315   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    VAL A 320   O   -  C   -  N   ANGL. DEV. = -11.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  10       60.63     30.32                                   
REMARK 500    ASP A  11       -1.95     68.75                                   
REMARK 500    ILE A  43      -19.68    -45.72                                   
REMARK 500    THR A  77      -66.67    -29.65                                   
REMARK 500    SER A  92     -125.39     57.84                                   
REMARK 500    GLN A  98       57.77     37.02                                   
REMARK 500    TYR A 132       -0.01     76.63                                   
REMARK 500    GLN A 161      -15.08   -153.98                                   
REMARK 500    GLN A 188      -72.24   -150.13                                   
REMARK 500    GLN A 279     -152.25     44.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    MET A  80         10.42                                           
REMARK 500    LEU A 128         11.29                                           
REMARK 500    GLU A 261         14.64                                           
REMARK 500    ASP A 278         12.21                                           
REMARK 500    TYR A 310         16.02                                           
REMARK 500    ALA A 323         11.90                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: active site                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: active site                                        
DBREF  3CMS A   -2   326  UNP    P00794   CHYM_BOVIN      59    381             
SEQADV 3CMS PHE A  111  UNP  P00794    VAL   171 CONFLICT                       
SEQRES   1 A  323  GLY GLU VAL ALA SER VAL PRO LEU THR ASN TYR LEU ASP          
SEQRES   2 A  323  SER GLN TYR PHE GLY LYS ILE TYR LEU GLY THR PRO PRO          
SEQRES   3 A  323  GLN GLU PHE THR VAL LEU PHE ASP THR GLY SER SER ASP          
SEQRES   4 A  323  PHE TRP VAL PRO SER ILE TYR CYS LYS SER ASN ALA CYS          
SEQRES   5 A  323  LYS ASN HIS GLN ARG PHE ASP PRO ARG LYS SER SER THR          
SEQRES   6 A  323  PHE GLN ASN LEU GLY LYS PRO LEU SER ILE HIS TYR GLY          
SEQRES   7 A  323  THR GLY SER MET GLN GLY ILE LEU GLY TYR ASP THR VAL          
SEQRES   8 A  323  THR VAL SER ASN ILE VAL ASP ILE GLN GLN THR VAL GLY          
SEQRES   9 A  323  LEU SER THR GLN GLU PRO GLY ASP PHE PHE THR TYR ALA          
SEQRES  10 A  323  GLU PHE ASP GLY ILE LEU GLY MET ALA TYR PRO SER LEU          
SEQRES  11 A  323  ALA SER GLU TYR SER ILE PRO VAL PHE ASP ASN MET MET          
SEQRES  12 A  323  ASN ARG HIS LEU VAL ALA GLN ASP LEU PHE SER VAL TYR          
SEQRES  13 A  323  MET ASP ARG ASN GLY GLN GLU SER MET LEU THR LEU GLY          
SEQRES  14 A  323  ALA ILE ASP PRO SER TYR TYR THR GLY SER LEU HIS TRP          
SEQRES  15 A  323  VAL PRO VAL THR VAL GLN GLN TYR TRP GLN PHE THR VAL          
SEQRES  16 A  323  ASP SER VAL THR ILE SER GLY VAL VAL VAL ALA CYS GLU          
SEQRES  17 A  323  GLY GLY CYS GLN ALA ILE LEU ASP THR GLY THR SER LYS          
SEQRES  18 A  323  LEU VAL GLY PRO SER SER ASP ILE LEU ASN ILE GLN GLN          
SEQRES  19 A  323  ALA ILE GLY ALA THR GLN ASN GLN TYR GLY GLU PHE ASP          
SEQRES  20 A  323  ILE ASP CYS ASP ASN LEU SER TYR MET PRO THR VAL VAL          
SEQRES  21 A  323  PHE GLU ILE ASN GLY LYS MET TYR PRO LEU THR PRO SER          
SEQRES  22 A  323  ALA TYR THR SER GLN ASP GLN GLY PHE CYS THR SER GLY          
SEQRES  23 A  323  PHE GLN SER GLU ASN HIS SER GLN LYS TRP ILE LEU GLY          
SEQRES  24 A  323  ASP VAL PHE ILE ARG GLU TYR TYR SER VAL PHE ASP ARG          
SEQRES  25 A  323  ALA ASN ASN LEU VAL GLY LEU ALA LYS ALA ILE                  
FORMUL   2  HOH   *145(H2 O)                                                    
HELIX    1  HN ASN A   48  LYS A   51  1                                   4    
HELIX    2 HN1 PRO A   58  LYS A   60  5                                   3    
HELIX    3 HN2 ASP A  110  TYR A  114  1DISTORTED                          5    
HELIX    4 HN3 PRO A  126  LEU A  128  5                                   3    
HELIX    5 HNP VAL A  136  ASN A  142  1                                   7    
HELIX    6 HC1 PRO A  172  TYR A  174  5                                   3    
HELIX    7  HC SER A  225  ILE A  235  1                                  11    
HELIX    8 HC2 LEU A  252  TYR A  254  5                                   3    
HELIX    9 HC3 PRO A  271  TYR A  274  1                                   4    
HELIX   10 HCP ASP A  303  ILE A  306  1                                   4    
SHEET    1  1N 8 THR A   7  TYR A   9  0                                        
SHEET    2  1N 8 GLN A  13  GLY A  16 -1  N  THR A   7   O  PHE A  15           
SHEET    3  1N 8 THR A  28  ASP A  32 -1  N  VAL A  29   O  GLY A  16           
SHEET    4  1N 8 GLY A 119  GLY A 122  1  N  GLY A 119   O  THR A  28           
SHEET    5  1N 8 PHE A  38  PRO A  41 -1  N  TRP A  39   O  ILE A 120           
SHEET    6  1N 8 GLN A  99  SER A 104  1  N  GLY A 102   O  PHE A  38           
SHEET    7  1N 8 ILE A  83  ASP A  87 -1  N  ILE A  83   O  LEU A 103           
SHEET    8  1N 8 GLN A  65  ASN A  66 -1  N  GLN A  65   O  TYR A  86           
SHEET    1 1NP 3 THR A 105  GLN A 106  0                                        
SHEET    2 1NP 3 GLY A  78  GLY A  82 -1  N  GLN A  81   O  GLN A 106           
SHEET    3 1NP 3 PRO A  70  TYR A  75 -1  N  TYR A  75   O  GLY A  78           
SHEET    1  1C 5 TRP A 190  VAL A 194  0                                        
SHEET    2  1C 5 CYS A 210  LEU A 214 -1  N  CYS A 210   O  VAL A 194           
SHEET    3  1C 5 TRP A 299  LEU A 301  1  N  TRP A 299   O  GLN A 211           
SHEET    4  1C 5 LEU A 221  PRO A 224 -1  O  VAL A 222   N  ILE A 300           
SHEET    5  1C 5 PHE A 286  GLU A 289  1  N  GLN A 287   O  LEU A 221           
SHEET    1 1CP 4 THR A 275  ASP A 278  0                                        
SHEET    2 1CP 4 PHE A 281  SER A 284 -1  N  PHE A 281   O  ASP A 278           
SHEET    3 1CP 4 PHE A 245  ILE A 247 -1  N  ILE A 247   O  CYS A 282           
SHEET    4 1CP 4 THR A 238  GLN A 239 -1  N  THR A 238   O  ASP A 246           
SHEET    1  2N 4 GLN A  25  PHE A  27  0                                        
SHEET    2  2N 4 LYS A  17  LEU A  20 -1  N  ILE A  18   O  PHE A  27           
SHEET    3  2N 4 THR A  88  VAL A  91 -1  N  THR A  90   O  TYR A  19           
SHEET    4  2N 4 ILE A  94  GLN A  98 -1  N  ILE A  94   O  VAL A  91           
SHEET    1  2C 4 VAL A 202  ALA A 205  0                                        
SHEET    2  2C 4 ASP A 195  ILE A 199 -1  N  VAL A 197   O  ALA A 205           
SHEET    3  2C 4 VAL A 258  ILE A 262 -1  N  VAL A 259   O  THR A 198           
SHEET    4  2C 4 LYS A 265  LEU A 269 -1  N  LYS A 265   O  ILE A 262           
SHEET    1   3 6 ALA A   2  PRO A   5  0                                        
SHEET    2   3 6 MET A 164  LEU A 167 -1  N  LEU A 165   O  VAL A   4           
SHEET    3   3 6 LEU A 150  TYR A 154 -1  N  SER A 152   O  THR A 166           
SHEET    4   3 6 TYR A 309  ASP A 314 -1  N  SER A 311   O  VAL A 153           
SHEET    5   3 6 LEU A 319  ALA A 325 -1  N  LEU A 319   O  ASP A 314           
SHEET    6   3 6 TYR A 175  PRO A 183 -1  N  THR A 176   O  LYS A 324           
SSBOND   1 CYS A   45    CYS A   50                          1555   1555  2.10  
SSBOND   2 CYS A  206    CYS A  210                          1555   1555  2.13  
SSBOND   3 CYS A  249    CYS A  282                          1555   1555  2.07  
CISPEP   1 THR A   22    PRO A   23          0        -3.84                     
SITE     1 AC1  1 ASP A  32                                                     
SITE     1 AC2  1 ASP A 215                                                     
CRYST1   80.210  114.560   72.430  90.00  90.00  90.00 I 2 2 2       8          
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      0.012467  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008729  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013806        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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