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Database: PDB
Entry: 1JAQ
LinkDB: 1JAQ
Original site: 1JAQ 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-MAR-96   1JAQ              
TITLE     COMPLEX OF 1-HYDROXYLAMINE-2-ISOBUTYLMALONYL-ALA-GLY-NH2 WITH THE     
TITLE    2 CATALYTIC DOMAIN OF MATRIX METALLO PROTEINASE-8 (MET80 FORM)         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATRIX METALLO PROTEINASE-8 (MET80 FORM);                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 80 - 242;                       
COMPND   5 SYNONYM: MMP-8-MET80 FORM;                                           
COMPND   6 EC: 3.4.24.34;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: MMP-8 IS IDENTICAL TO THE HUMAN NEUTROPHIL COLLAGENASE
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL: NEUTROPHILS;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    METALLOPROTEASE, ZINC-ENDOPEPTIDASE, METZINCINS, HYDROLASE-HYDROLASE  
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GRAMS,P.REINEMER,J.C.POWERS,T.KLEINE,M.PIPER,H.TSCHESCHE,R.HUBER,   
AUTHOR   2 W.BODE                                                               
REVDAT   3   13-JUL-11 1JAQ    1       VERSN                                    
REVDAT   2   24-FEB-09 1JAQ    1       VERSN                                    
REVDAT   1   11-JUL-96 1JAQ    0                                                
JRNL        AUTH   F.GRAMS,P.REINEMER,J.C.POWERS,T.KLEINE,M.PIEPER,H.TSCHESCHE, 
JRNL        AUTH 2 R.HUBER,W.BODE                                               
JRNL        TITL   X-RAY STRUCTURES OF HUMAN NEUTROPHIL COLLAGENASE COMPLEXED   
JRNL        TITL 2 WITH PEPTIDE HYDROXAMATE AND PEPTIDE THIOL INHIBITORS.       
JRNL        TITL 3 IMPLICATIONS FOR SUBSTRATE BINDING AND RATIONAL DRUG DESIGN. 
JRNL        REF    EUR.J.BIOCHEM.                V. 228   830 1995              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   7737183                                                      
JRNL        DOI    10.1111/J.1432-1033.1995.TB20329.X                           
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BODE,P.REINEMER,R.HUBER,T.KLEINE,S.SCHNIERER,H.TSCHESCHE   
REMARK   1  TITL   THE X-RAY CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN 
REMARK   1  TITL 2 NEUTROPHIL COLLAGENASE INHIBITED BY A SUBSTRATE ANALOGUE     
REMARK   1  TITL 3 REVEALS THE ESSENTIALS FOR CATALYSIS AND SPECIFICITY         
REMARK   1  REF    EMBO J.                       V.  13  1263 1994              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.REINEMER,F.GRAMS,R.HUBER,T.KLEINE,S.SCHNIERER,M.PIPER,     
REMARK   1  AUTH 2 H.TSCHESCHE,W.BODE                                           
REMARK   1  TITL   STRUCTURAL IMPLICATIONS FOR THE ROLE OF THE N TERMINUS IN    
REMARK   1  TITL 2 THE 'SUPERACTIVATION' OF COLLAGENASES. A CRYSTALLOGRAPHIC    
REMARK   1  TITL 3 STUDY                                                        
REMARK   1  REF    FEBS LETT.                    V. 338   227 1994              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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             : 7202                           
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) : 0.198                           
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            : 1249                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 25                                      
REMARK   3   SOLVENT ATOMS            : 89                                      
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) : 0.022                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.10                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  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 1JAQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
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) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, CCP4                       
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) : 0.12100                            
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       16.56500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.15500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.68500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.15500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       16.56500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.68500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    80                                                      
REMARK 465     LEU A    81                                                      
REMARK 465     THR A    82                                                      
REMARK 465     PRO A    83                                                      
REMARK 465     GLY A    84                                                      
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   O    HOH A  1019     H1   HOH A  1035              1.51            
REMARK 500   O    HOH A  1008     H2   HOH A  1087              1.59            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    ASN A   188     O    HOH A  1049     4566     1.12            
REMARK 500   O    ASN A   188     H2   HOH A  1049     4566     1.27            
REMARK 500   HG1  THR A   129    HD21  ASN A   218     1455     1.33            
REMARK 500   O    HOH A  1009     H1   HOH A  1088     4466     1.54            
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    PRO A 102   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  89       33.90    -99.30                                   
REMARK 500    ARG A 145     -114.40     41.20                                   
REMARK 500    PRO A 156      152.47    -47.80                                   
REMARK 500    ASN A 157     -154.97     49.56                                   
REMARK 500    THR A 185     -163.16   -106.28                                   
REMARK 500    ALA A 206     -169.79   -104.41                                   
REMARK 500    TYR A 241     -122.80   -110.07                                   
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    ASP A 149        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1047        DISTANCE =  5.65 ANGSTROMS                       
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 996  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 137   O                                                      
REMARK 620 2 GLY A 169   O   160.2                                              
REMARK 620 3 GLY A 171   O   104.9  94.8                                        
REMARK 620 4 ASP A 173   OD1  88.7  92.4  90.8                                  
REMARK 620 5 HOH A1026   O    78.9  81.2 174.7  92.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 997  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 154   OD1                                                    
REMARK 620 2 GLY A 155   O    86.5                                              
REMARK 620 3 ASN A 157   O    91.9  85.7                                        
REMARK 620 4 ILE A 159   O    89.6 176.1  94.3                                  
REMARK 620 5 GLU A 180   OE2 178.5  93.0  86.7  90.9                            
REMARK 620 6 ASP A 177   OD2  89.6  91.9 177.0  88.3  91.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 998  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 147   NE2                                                    
REMARK 620 2 ASP A 149   OD2 109.8                                              
REMARK 620 3 HIS A 162   NE2 114.7 105.4                                        
REMARK 620 4 HIS A 175   ND1 118.7  97.3 108.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 999  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 197   NE2                                                    
REMARK 620 2 HIS A 201   NE2 100.9                                              
REMARK 620 3 HIS A 207   NE2  98.8  93.5                                        
REMARK 620 4 01S A   1   OH  111.9  88.5 148.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: N-[(2R)-2-(HYDROXYCARBAMOYL)-4-METHYLPENTANOYL]-L-    
REMARK 630 ALANYLGLYCINAMIDE                                                    
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     01S A     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    HMI ALA GLY NH2                                          
REMARK 630 DETAILS: NULL                                                        
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 996                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 01S A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 997                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 998                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 999                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JAO   RELATED DB: PDB                                   
DBREF  1JAQ A   80   242  UNP    P22894   MM08_HUMAN     100    262             
SEQRES   1 A  163  MET LEU THR PRO GLY ASN PRO LYS TRP GLU ARG THR ASN          
SEQRES   2 A  163  LEU THR TYR ARG ILE ARG ASN TYR THR PRO GLN LEU SER          
SEQRES   3 A  163  GLU ALA GLU VAL GLU ARG ALA ILE LYS ASP ALA PHE GLU          
SEQRES   4 A  163  LEU TRP SER VAL ALA SER PRO LEU ILE PHE THR ARG ILE          
SEQRES   5 A  163  SER GLN GLY GLU ALA ASP ILE ASN ILE ALA PHE TYR GLN          
SEQRES   6 A  163  ARG ASP HIS GLY ASP ASN SER PRO PHE ASP GLY PRO ASN          
SEQRES   7 A  163  GLY ILE LEU ALA HIS ALA PHE GLN PRO GLY GLN GLY ILE          
SEQRES   8 A  163  GLY GLY ASP ALA HIS PHE ASP ALA GLU GLU THR TRP THR          
SEQRES   9 A  163  ASN THR SER ALA ASN TYR ASN LEU PHE LEU VAL ALA ALA          
SEQRES  10 A  163  HIS GLU PHE GLY HIS SER LEU GLY LEU ALA HIS SER SER          
SEQRES  11 A  163  ASP PRO GLY ALA LEU MET TYR PRO ASN TYR ALA PHE ARG          
SEQRES  12 A  163  GLU THR SER ASN TYR SER LEU PRO GLN ASP ASP ILE ASP          
SEQRES  13 A  163  GLY ILE GLN ALA ILE TYR GLY                                  
HET     CA  A 996       1                                                       
HET    01S  A   1      27                                                       
HET     CA  A 997       1                                                       
HET     ZN  A 998       1                                                       
HET     ZN  A 999       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     01S N-[(2R)-2-(HYDROXYCARBAMOYL)-4-METHYLPENTANOYL]-L-               
HETNAM   2 01S  ALANYLGLYCINAMIDE                                               
HETNAM      ZN ZINC ION                                                         
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   3  01S    C12 H22 N4 O5                                                
FORMUL   5   ZN    2(ZN 2+)                                                     
FORMUL   7  HOH   *89(H2 O)                                                     
HELIX    1   1 GLU A  106  ALA A  123  1                                  18    
HELIX    2   2 LEU A  191  SER A  202  1                                  12    
HELIX    3   3 GLN A  231  ILE A  240  1                                  10    
SHEET    1   A 5 ILE A 127  ARG A 130  0                                        
SHEET    2   A 5 ASN A  92  ILE A  97  1  N  LEU A  93   O  ILE A 127           
SHEET    3   A 5 ILE A 138  TYR A 143  1  N  ILE A 138   O  ARG A  96           
SHEET    4   A 5 ALA A 174  ASP A 177  1  N  ALA A 174   O  ALA A 141           
SHEET    5   A 5 ALA A 161  ALA A 163 -1  N  HIS A 162   O  HIS A 175           
LINK        CA    CA A 996                 O   ASP A 137     1555   1555  2.21  
LINK        CA    CA A 996                 O   GLY A 169     1555   1555  2.30  
LINK        CA    CA A 996                 O   GLY A 171     1555   1555  2.34  
LINK        CA    CA A 997                 OD1 ASP A 154     1555   1555  2.20  
LINK        CA    CA A 997                 O   GLY A 155     1555   1555  2.36  
LINK        CA    CA A 997                 O   ASN A 157     1555   1555  2.32  
LINK        CA    CA A 997                 O   ILE A 159     1555   1555  2.32  
LINK        CA    CA A 997                 OE2 GLU A 180     1555   1555  2.16  
LINK        ZN    ZN A 998                 NE2 HIS A 147     1555   1555  1.96  
LINK        ZN    ZN A 998                 OD2 ASP A 149     1555   1555  1.82  
LINK        ZN    ZN A 998                 NE2 HIS A 162     1555   1555  2.19  
LINK        ZN    ZN A 998                 ND1 HIS A 175     1555   1555  2.26  
LINK        ZN    ZN A 999                 NE2 HIS A 197     1555   1555  1.87  
LINK        ZN    ZN A 999                 NE2 HIS A 201     1555   1555  2.27  
LINK        ZN    ZN A 999                 NE2 HIS A 207     1555   1555  2.05  
LINK         OD1 ASP A 173                CA    CA A 996     1555   1555  2.60  
LINK         OD2 ASP A 177                CA    CA A 997     1555   1555  2.65  
LINK        CA    CA A 996                 O   HOH A1026     1555   1555  2.41  
LINK        ZN    ZN A 999                 OH  01S A   1     1555   1555  2.10  
CISPEP   1 ASN A  188    TYR A  189          0        -0.42                     
SITE     1 AC1  5 ASP A 137  GLY A 169  GLY A 171  ASP A 173                    
SITE     2 AC1  5 HOH A1026                                                     
SITE     1 AC2 15 ILE A 159  LEU A 160  ALA A 161  HIS A 197                    
SITE     2 AC2 15 GLU A 198  HIS A 201  HIS A 207  TYR A 216                    
SITE     3 AC2 15 PRO A 217  ASN A 218  TYR A 219   ZN A 999                    
SITE     4 AC2 15 HOH A1020  HOH A1038  HOH A1076                               
SITE     1 AC3  6 ASP A 154  GLY A 155  ASN A 157  ILE A 159                    
SITE     2 AC3  6 ASP A 177  GLU A 180                                          
SITE     1 AC4  4 HIS A 147  ASP A 149  HIS A 162  HIS A 175                    
SITE     1 AC5  4 01S A   1  HIS A 197  HIS A 201  HIS A 207                    
CRYST1   33.130   69.370   72.310  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.030184  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014415  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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