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    HEADER    HYDROLASE/HYDROLASE INHIBITOR           11-DEC-00   1HOV              
    TITLE     SOLUTION STRUCTURE OF A CATALYTIC DOMAIN OF MMP-2 COMPLEXED           
    TITLE    2 WITH SC-74020                                                        
    COMPND    MOL_ID: 1;                                                            
    COMPND   2 MOLECULE: MATRIX METALLOPROTEINASE-2;                                
    COMPND   3 CHAIN: A;                                                            
    COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
    COMPND   5 EC: 3.4.24.24;                                                       
    COMPND   6 ENGINEERED: YES                                                      
    SOURCE    MOL_ID: 1;                                                            
    SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
    SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
    SOURCE   4 ORGANISM_TAXID: 9606;                                                
    SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
    SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
    SOURCE   7 EXPRESSION_SYSTEM_STRAIN: W3110-II5;                                 
    SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: RECA                                  
    KEYWDS    ENZYME-INHIBITOR COMPLEX, HYDROLASE/HYDROLASE INHIBITOR               
    KEYWDS   2 COMPLEX                                                              
    EXPDTA    SOLUTION NMR                                                          
    NUMMDL    11                                                                    
    AUTHOR    Y.FENG,J.J.LIKOS,L.ZHU,H.WOODWARD,G.MUNIE,J.J.MCDONALD,               
    AUTHOR   2 A.M.STEVENS,C.P.HOWARD,G.A.DE CRESCENZO,D.WELSCH,H.-S.SHIEH,         
    AUTHOR   3 W.C.STALLINGS                                                        
    REVDAT   3   24-FEB-09 1HOV    1       VERSN                                    
    REVDAT   2   20-DEC-02 1HOV    1       AUTHOR JRNL   REMARK                     
    REVDAT   1   12-DEC-01 1HOV    0                                                
    JRNL        AUTH   Y.FENG,J.J.LIKOS,L.ZHU,H.WOODWARD,G.MUNIE,                   
    JRNL        AUTH 2 J.J.MCDONALD,A.M.STEVENS,C.P.HOWARD,                         
    JRNL        AUTH 3 G.A.DE CRESCENZO,D.WELSCH,H.-S.SHIEH,W.C.STALLINGS           
    JRNL        TITL   SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE              
    JRNL        TITL 2 CATALYTIC DOMAIN OF MATRIX METALLOPROTEINASE-2               
    JRNL        TITL 3 COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR                   
    JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1598    10 2002              
    JRNL        REFN                   ISSN 0006-3002                               
    JRNL        PMID   12147339                                                     
    JRNL        DOI    10.1016/S0167-4838(02)00307-2                                
    REMARK   1                                                                      
    REMARK   1 REFERENCE 1                                                          
    REMARK   1  TITL   1H, 13C AND 15N RESONANCE ASSIGNMENTS FOR A                  
    REMARK   1  TITL 2 TRUNCATED AND INHIBITED CATALYTIC DOMAIN OF MATRIX           
    REMARK   1  TITL 3 METALLOPROTEINASE-2                                          
    REMARK   1  REF    J.BIOMOL.NMR                  V.  17    85 2000              
    REMARK   1  REFN                   ISSN 0925-2738                               
    REMARK   2                                                                      
    REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
    REMARK   3                                                                      
    REMARK   3 REFINEMENT.                                                          
    REMARK   3   PROGRAM     : X-PLOR 98.1                                          
    REMARK   3   AUTHORS     : MSI                                                  
    REMARK   3                                                                      
    REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
    REMARK   4                                                                      
    REMARK   4 1HOV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
    REMARK 100                                                                      
    REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-00.                  
    REMARK 100 THE RCSB ID CODE IS RCSB012486.                                      
    REMARK 210                                                                      
    REMARK 210 EXPERIMENTAL DETAILS                                                 
    REMARK 210  EXPERIMENT TYPE                : NMR                                
    REMARK 210  TEMPERATURE           (KELVIN) : 303                                
    REMARK 210  PH                             : 7.4                                
    REMARK 210  IONIC STRENGTH                 : 50                                 
    REMARK 210  PRESSURE                       : 1 ATM                              
    REMARK 210  SAMPLE CONTENTS                : 0.3-0.4MM U-15N, 13C MMP-2C:       
    REMARK 210                                   UNLABELED SC-74020 IN 20MM         
    REMARK 210                                   TRIS-D11-HCL, 5MM CACL2, 10UM      
    REMARK 210                                   ZNCL2, 20UM UNLABELED SC-74020     
    REMARK 210                                                                      
    REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
    REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 500 MHZ                   
    REMARK 210  SPECTROMETER MODEL             : INOVA, UNITY                       
    REMARK 210  SPECTROMETER MANUFACTURER      : VARIAN                             
    REMARK 210                                                                      
    REMARK 210  STRUCTURE DETERMINATION.                                            
    REMARK 210   SOFTWARE USED                 : VNMR 6.1B, FELIX 97                
    REMARK 210   METHOD USED                   : DISTANCE GEOMETRY,  SIMULATED      
    REMARK 210                                   ANNEALING, MOLECULAR DYNAMICS,     
    REMARK 210                                   TORSION ANGLE DYNAMICS             
    REMARK 210                                                                      
    REMARK 210 CONFORMERS, NUMBER CALCULATED   : 14                                 
    REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 11                                 
    REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LEAST          
    REMARK 210                                   RESTRAINT VIOLATIONS               
    REMARK 210                                                                      
    REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3                   
    REMARK 210                                                                      
    REMARK 210 REMARK: NULL                                                         
    REMARK 215                                                                      
    REMARK 215 NMR STUDY                                                            
    REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
    REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
    REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
    REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
    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  1 TYR A   2      -89.33     53.48                                   
    REMARK 500  1 PRO A   6       41.86    -76.03                                   
    REMARK 500  1 ARG A   7      -49.23     71.79                                   
    REMARK 500  1 LYS A  10      134.05    -30.88                                   
    REMARK 500  1 ASP A  12       74.65   -175.87                                   
    REMARK 500  1 ASN A  14     -173.81    -53.98                                   
    REMARK 500  1 GLN A  15       98.49     47.67                                   
    REMARK 500  1 THR A  47      148.15   -178.13                                   
    REMARK 500  1 ILE A  54     -168.73   -124.38                                   
    REMARK 500  1 HIS A  55       30.23   -176.15                                   
    REMARK 500  1 ASP A  56      -32.83   -163.31                                   
    REMARK 500  1 GLU A  58      170.42     58.04                                   
    REMARK 500  1 ASN A  64     -138.71    178.85                                   
    REMARK 500  1 ARG A  67      170.49     60.75                                   
    REMARK 500  1 GLU A  69      -96.23    -75.85                                   
    REMARK 500  1 HIS A  70      -80.06     78.17                                   
    REMARK 500  1 ASP A  72      -90.10    -37.72                                   
    REMARK 500  1 TYR A  74       74.32   -179.67                                   
    REMARK 500  1 PHE A  76      158.96     50.53                                   
    REMARK 500  1 ASP A  77      -29.39    178.56                                   
    REMARK 500  1 LYS A  79     -173.56     43.56                                   
    REMARK 500  1 ASP A  80      -95.85    -67.15                                   
    REMARK 500  1 ALA A  84     -178.07    169.40                                   
    REMARK 500  1 HIS A  85      175.86    179.05                                   
    REMARK 500  1 ALA A  88      172.78    -48.55                                   
    REMARK 500  1 ASP A 101      -78.56    -76.29                                   
    REMARK 500  1 ASP A 102       91.16    -66.04                                   
    REMARK 500  1 THR A 108     -145.28    -91.89                                   
    REMARK 500  1 SER A 109       37.99    -89.90                                   
    REMARK 500  1 ALA A 110      -97.30    -64.14                                   
    REMARK 500  1 ASN A 111      -46.45   -178.31                                   
    REMARK 500  1 SER A 113      110.12     62.20                                   
    REMARK 500  1 MET A 126      -96.37    -78.99                                   
    REMARK 500  1 GLN A 132      -24.80     82.48                                   
    REMARK 500  1 PRO A 140       21.66    -78.97                                   
    REMARK 500  1 ASN A 147       20.61   -160.00                                   
    REMARK 500  1 PHE A 148       94.05     36.24                                   
    REMARK 500  1 TYR A 162      -93.30   -140.11                                   
    REMARK 500  2 TYR A   2      -94.28    -58.49                                   
    REMARK 500  2 ASN A   3       98.06     60.21                                   
    REMARK 500  2 PRO A   6     -161.09    -74.18                                   
    REMARK 500  2 ARG A   7       54.44     77.44                                   
    REMARK 500  2 LYS A   8      144.59     60.52                                   
    REMARK 500  2 LYS A  10     -137.11    -62.34                                   
    REMARK 500  2 TRP A  11       44.18   -163.00                                   
    REMARK 500  2 ASN A  14      -85.71    -34.18                                   
    REMARK 500  2 GLN A  15      106.97    -51.88                                   
    REMARK 500  2 TYR A  23     -114.33    -58.07                                   
    REMARK 500  2 ASP A  26       81.73   -158.64                                   
    REMARK 500  2 THR A  47      149.32   -179.33                                   
    REMARK 500  2 HIS A  55     -147.56    -60.32                                   
    REMARK 500  2 ASP A  60      -70.19    -77.88                                   
    REMARK 500  2 ARG A  67     -135.15    -96.90                                   
    REMARK 500  2 ASP A  72       28.04   -151.47                                   
    REMARK 500  2 TYR A  74      164.36     55.14                                   
    REMARK 500  2 PRO A  75     -159.10    -76.45                                   
    REMARK 500  2 PHE A  76      168.86    177.54                                   
    REMARK 500  2 ASP A  80     -111.21     39.55                                   
    REMARK 500  2 LEU A  82      123.99    -26.94                                   
    REMARK 500  2 ALA A  84      146.54    172.51                                   
    REMARK 500  2 THR A  91       78.51   -162.59                                   
    REMARK 500  2 ASP A 101      -86.42    -44.58                                   
    REMARK 500  2 ASP A 102     -128.43    -77.22                                   
    REMARK 500  2 GLU A 103      -29.86     83.92                                   
    REMARK 500  2 LEU A 104       74.56     68.81                                   
    REMARK 500  2 THR A 106     -173.82    171.48                                   
    REMARK 500  2 THR A 108     -110.89     73.31                                   
    REMARK 500  2 ALA A 110      -45.26   -135.78                                   
    REMARK 500  2 ASN A 111      -86.89   -158.39                                   
    REMARK 500  2 LEU A 128      146.12    -37.00                                   
    REMARK 500  2 ALA A 136     -177.85    -67.77                                   
    REMARK 500  2 LYS A 146     -106.75     52.60                                   
    REMARK 500  2 PHE A 148      125.81     68.01                                   
    REMARK 500  2 ARG A 149      -70.30   -100.77                                   
    REMARK 500  2 LEU A 150      172.15    169.29                                   
    REMARK 500  2 TYR A 162      -91.28   -122.38                                   
    REMARK 500  3 TYR A   2      123.00     75.17                                   
    REMARK 500  3 PHE A   5      -54.46    171.11                                   
    REMARK 500  3 ARG A   7       44.37   -105.01                                   
    REMARK 500  3 LYS A  10     -162.03     40.45                                   
    REMARK 500  3 ASN A  14      -89.21    -79.44                                   
    REMARK 500  3 TYR A  23     -163.30    -66.29                                   
    REMARK 500  3 ASP A  26      -35.43    -35.23                                   
    REMARK 500  3 PRO A  48       45.65    -74.91                                   
    REMARK 500  3 ASP A  56      -67.24   -130.21                                   
    REMARK 500  3 GLU A  58      162.72     68.09                                   
    REMARK 500  3 ASN A  64     -148.67   -154.49                                   
    REMARK 500  3 TRP A  68     -162.15    177.46                                   
    REMARK 500  3 HIS A  70     -172.77    -49.74                                   
    REMARK 500  3 ASP A  72     -169.99    -54.89                                   
    REMARK 500  3 LYS A  79      167.60    -43.16                                   
    REMARK 500  3 ASP A  80     -162.01     41.15                                   
    REMARK 500  3 LEU A  82      107.10    -47.77                                   
    REMARK 500  3 ALA A  84      158.95    169.50                                   
    REMARK 500  3 ASP A  96      117.02   -160.80                                   
    REMARK 500  3 ASP A 100      167.01    -44.70                                   
    REMARK 500  3 ASP A 102     -144.88    -99.42                                   
    REMARK 500  3 GLU A 103      136.95     75.24                                   
    REMARK 500  3 SER A 109       81.34     45.62                                   
    REMARK 500  3 ALA A 110      -42.11   -136.13                                   
    REMARK 500  3 ASN A 111      -77.31   -137.48                                   
    REMARK 500  3 TYR A 112     -102.00   -107.98                                   
    REMARK 500  3 SER A 113       98.05    165.43                                   
    REMARK 500  3 LEU A 128      176.04    -49.35                                   
    REMARK 500  3 SER A 131      -77.53    -84.86                                   
    REMARK 500  3 GLN A 132      -29.80    161.03                                   
    REMARK 500  3 ILE A 141     -157.06   -159.53                                   
    REMARK 500  3 TYR A 142      119.03   -165.69                                   
    REMARK 500  3 TYR A 144      158.32    -45.39                                   
    REMARK 500  3 ASN A 147      -95.34     58.96                                   
    REMARK 500  3 PHE A 148      142.88    177.72                                   
    REMARK 500  3 LEU A 150      139.34     66.57                                   
    REMARK 500  4 ASN A   3       93.13     49.59                                   
    REMARK 500  4 PHE A   5      -55.96    178.83                                   
    REMARK 500  4 ARG A   7      -71.40    -74.07                                   
    REMARK 500  4 LYS A  10      175.60    -51.99                                   
    REMARK 500  4 ASN A  14      141.30     61.96                                   
    REMARK 500  4 GLN A  15       76.14     45.04                                   
    REMARK 500  4 ASP A  60      -57.03   -134.22                                   
    REMARK 500  4 ASN A  64     -174.69    175.30                                   
    REMARK 500  4 ARG A  67     -170.44    -56.05                                   
    REMARK 500  4 HIS A  70      -70.93   -175.09                                   
    REMARK 500  4 ASP A  72     -177.05    -46.33                                   
    REMARK 500  4 PHE A  76      159.89     60.24                                   
    REMARK 500  4 ASP A  77      -31.21   -178.90                                   
    REMARK 500  4 ASP A  80     -150.41     41.42                                   
    REMARK 500  4 LEU A  82       98.34    -50.68                                   
    REMARK 500  4 ASP A 101      -95.31    -57.37                                   
    REMARK 500  4 ASP A 102      -93.23     21.67                                   
    REMARK 500  4 GLU A 103      161.15    -41.95                                   
    REMARK 500  4 THR A 106     -159.68   -159.02                                   
    REMARK 500  4 THR A 108      -99.06   -168.20                                   
    REMARK 500  4 SER A 109       59.82   -142.67                                   
    REMARK 500  4 ALA A 110      -24.13   -140.93                                   
    REMARK 500  4 ASN A 111     -153.66   -169.57                                   
    REMARK 500  4 TYR A 112     -167.16    -67.74                                   
    REMARK 500  4 LEU A 128      145.25    -32.44                                   
    REMARK 500  4 SER A 131     -152.16    -93.35                                   
    REMARK 500  4 THR A 143       84.77   -150.06                                   
    REMARK 500  4 TYR A 144      164.19    -42.37                                   
    REMARK 500  4 LYS A 146      104.27    -44.83                                   
    REMARK 500  4 ASN A 147      -79.15     68.81                                   
    REMARK 500  4 PHE A 148      113.88    171.14                                   
    REMARK 500  4 LEU A 150     -160.53     71.98                                   
    REMARK 500  4 LEU A 161      -64.50    -98.96                                   
    REMARK 500  4 TYR A 162       85.27   -151.64                                   
    REMARK 500  5 TYR A   2       83.16   -153.27                                   
    REMARK 500  5 LYS A   8      144.14     62.43                                   
    REMARK 500  5 ASP A  12       99.41    167.92                                   
    REMARK 500  5 LYS A  13       32.00   -161.64                                   
    REMARK 500  5 ASN A  14      -62.97     72.28                                   
    REMARK 500  5 TYR A  23      179.02    -55.31                                   
    REMARK 500  5 ASP A  26      -27.16    -39.48                                   
    REMARK 500  5 THR A  47      147.56   -173.04                                   
    REMARK 500  5 PRO A  48       46.78    -78.52                                   
    REMARK 500  5 ASP A  56     -175.37    -62.04                                   
    REMARK 500  5 GLU A  58      153.91    177.35                                   
    REMARK 500  5 ALA A  59      143.66    176.45                                   
    REMARK 500  5 ASN A  64     -167.14   -164.19                                   
    REMARK 500  5 ARG A  67     -150.38     47.91                                   
    REMARK 500  5 TRP A  68      -72.57    -91.12                                   
    REMARK 500  5 GLU A  69       99.95    -62.42                                   
    REMARK 500  5 HIS A  70     -160.28   -127.29                                   
    REMARK 500  5 TYR A  74      -52.46    163.33                                   
    REMARK 500  5 LYS A  79      172.51    -41.65                                   
    REMARK 500  5 ASP A  80      -93.17    -25.18                                   
    REMARK 500  5 LEU A  82      109.37    -54.51                                   
    REMARK 500  5 ALA A  84      155.93    171.77                                   
    REMARK 500  5 THR A  91       92.56     67.78                                   
    REMARK 500  5 THR A 108      -60.50   -123.08                                   
    REMARK 500  5 SER A 109      -91.41   -165.26                                   
    REMARK 500  5 ALA A 110      -95.12     43.60                                   
    REMARK 500  5 ASN A 111     -104.63   -110.55                                   
    REMARK 500  5 TYR A 112     -124.17    -90.95                                   
    REMARK 500  5 SER A 113      117.24   -171.99                                   
    REMARK 500  5 ALA A 125      -32.36    -37.56                                   
    REMARK 500  5 MET A 126      -82.15    -69.89                                   
    REMARK 500  5 LEU A 128      153.82    -49.90                                   
    REMARK 500  5 HIS A 130      172.58    -44.72                                   
    REMARK 500  5 SER A 131     -152.23   -123.58                                   
    REMARK 500  5 ALA A 139      153.72    -43.15                                   
    REMARK 500  5 TYR A 144      147.71     68.42                                   
    REMARK 500  5 LYS A 146      -83.11    -83.69                                   
    REMARK 500  5 PHE A 148       99.80     60.14                                   
    REMARK 500  5 LEU A 150     -144.74     59.32                                   
    REMARK 500  5 SER A 151      129.05   -178.41                                   
    REMARK 500  5 TYR A 162      -75.05   -140.30                                   
    REMARK 500  6 ARG A   7     -109.09     72.68                                   
    REMARK 500  6 LYS A  10      -94.25     22.17                                   
    REMARK 500  6 TRP A  11     -160.25    176.00                                   
    REMARK 500  6 ASP A  12      158.39    -44.57                                   
    REMARK 500  6 ASN A  14      -82.84     43.26                                   
    REMARK 500  6 TYR A  23     -153.34    -68.74                                   
    REMARK 500  6 ASP A  56      -76.00     55.36                                   
    REMARK 500  6 ASN A  64     -147.10   -153.95                                   
    REMARK 500  6 PHE A  65     -178.55   -177.85                                   
    REMARK 500  6 TRP A  68      -89.03     57.04                                   
    REMARK 500  6 HIS A  70      -57.00    173.45                                   
    REMARK 500  6 PHE A  76      170.87     61.08                                   
    REMARK 500  6 ASP A  77      -34.86    172.63                                   
    REMARK 500  6 ASP A  80     -138.78     27.96                                   
    REMARK 500  6 LEU A  82       97.53    -42.68                                   
    REMARK 500  6 THR A  91      115.29     56.25                                   
    REMARK 500  6 VAL A  93      160.07    -45.65                                   
    REMARK 500  6 ASP A 102       79.33   -170.12                                   
    REMARK 500  6 LEU A 104      141.50     76.66                                   
    REMARK 500  6 TRP A 105      -50.44   -149.01                                   
    REMARK 500  6 THR A 106      -89.21   -138.13                                   
    REMARK 500  6 ASN A 107       19.26     52.92                                   
    REMARK 500  6 SER A 109       31.91   -168.07                                   
    REMARK 500  6 SER A 113       93.24     81.01                                   
    REMARK 500  6 HIS A 130      167.06    -44.24                                   
    REMARK 500  6 SER A 131      -80.53   -115.60                                   
    REMARK 500  6 GLN A 132      -35.64    177.11                                   
    REMARK 500  6 TYR A 144      170.84    -44.39                                   
    REMARK 500  6 THR A 145      113.30    179.64                                   
    REMARK 500  6 ASN A 147      -54.83     71.30                                   
    REMARK 500  6 PHE A 148      143.55     68.74                                   
    REMARK 500  6 ARG A 149      -86.63   -134.11                                   
    REMARK 500  6 LEU A 150      152.65    160.29                                   
    REMARK 500  7 TYR A   2       38.28    -98.46                                   
    REMARK 500  7 ARG A   7     -166.74    -54.58                                   
    REMARK 500  7 LYS A  10     -171.04    -64.61                                   
    REMARK 500  7 TRP A  11     -105.58   -107.60                                   
    REMARK 500  7 ASN A  14      -88.16    -82.54                                   
    REMARK 500  7 GLN A  15       95.35    -52.45                                   
    REMARK 500  7 ASP A  26      -28.27    -38.88                                   
    REMARK 500  7 THR A  47      149.79   -173.74                                   
    REMARK 500  7 PRO A  48       47.12    -81.03                                   
    REMARK 500  7 HIS A  55      -33.22   -159.08                                   
    REMARK 500  7 GLU A  58      158.83     65.16                                   
    REMARK 500  7 ASN A  64     -172.15    179.30                                   
    REMARK 500  7 ARG A  67     -149.78    -55.14                                   
    REMARK 500  7 HIS A  70      -73.40     73.32                                   
    REMARK 500  7 ASP A  72       68.50   -170.66                                   
    REMARK 500  7 TYR A  74       76.29   -118.81                                   
    REMARK 500  7 PRO A  75      -84.16    -74.78                                   
    REMARK 500  7 PHE A  76     -100.12     59.52                                   
    REMARK 500  7 ASP A  77      -53.96     75.69                                   
    REMARK 500  7 ASP A  80     -147.41     39.05                                   
    REMARK 500  7 ALA A  84      163.17    163.98                                   
    REMARK 500  7 THR A  91      142.04     71.30                                   
    REMARK 500  7 ASP A 101     -112.27    -89.64                                   
    REMARK 500  7 ASP A 102     -160.05     36.03                                   
    REMARK 500  7 GLU A 103     -124.11     34.97                                   
    REMARK 500  7 LEU A 104      134.33   -177.62                                   
    REMARK 500  7 SER A 109      -86.17   -178.68                                   
    REMARK 500  7 ALA A 110      -94.21     36.26                                   
    REMARK 500  7 ASN A 111      -80.98    -85.23                                   
    REMARK 500  7 TYR A 112       40.44   -157.42                                   
    REMARK 500  7 SER A 113      108.70     61.92                                   
    REMARK 500  7 MET A 126      -80.65    -72.97                                   
    REMARK 500  7 GLN A 132     -156.17     54.07                                   
    REMARK 500  7 ASP A 133      134.99     66.37                                   
    REMARK 500  7 ILE A 141      -99.06   -122.75                                   
    REMARK 500  7 TYR A 142      144.45    179.46                                   
    REMARK 500  7 THR A 145      137.62    176.82                                   
    REMARK 500  7 LYS A 146      -69.82    -93.80                                   
    REMARK 500  7 PHE A 148      134.46     59.45                                   
    REMARK 500  7 LEU A 150      -24.84     84.13                                   
    REMARK 500  7 SER A 151      132.64     55.99                                   
    REMARK 500  7 TYR A 162      -77.38    -77.90                                   
    REMARK 500  8 TYR A   2     -177.36     75.71                                   
    REMARK 500  8 PHE A   4     -124.29     55.41                                   
    REMARK 500  8 PHE A   5      -58.57    179.76                                   
    REMARK 500  8 LYS A  13     -163.55   -124.63                                   
    REMARK 500  8 TYR A  23      177.56    -46.73                                   
    REMARK 500  8 ASP A  26      -27.52    -39.83                                   
    REMARK 500  8 PRO A  48       29.96    -78.52                                   
    REMARK 500  8 HIS A  55       38.64   -145.97                                   
    REMARK 500  8 ASP A  56      166.80    169.04                                   
    REMARK 500  8 GLU A  58      166.24    178.33                                   
    REMARK 500  8 ASN A  64     -171.47   -174.64                                   
    REMARK 500  8 GLU A  69     -105.68    -76.55                                   
    REMARK 500  8 HIS A  70     -158.34     56.28                                   
    REMARK 500  8 ASP A  80     -170.21     53.72                                   
    REMARK 500  8 LEU A  82      127.02    -38.25                                   
    REMARK 500  8 ASP A 100      163.58    -46.91                                   
    REMARK 500  8 ASN A 107       68.59   -111.78                                   
    REMARK 500  8 THR A 108       77.16   -172.63                                   
    REMARK 500  8 SER A 109       75.57     45.67                                   
    REMARK 500  8 ALA A 110     -158.19   -155.77                                   
    REMARK 500  8 ASN A 111     -114.20    -73.47                                   
    REMARK 500  8 LEU A 116      -72.12    -62.65                                   
    REMARK 500  8 LEU A 128      151.36    -44.73                                   
    REMARK 500  8 GLN A 132      -21.72     82.99                                   
    REMARK 500  8 TYR A 144      165.87     60.93                                   
    REMARK 500  8 ASN A 147      -91.98   -126.53                                   
    REMARK 500  8 PHE A 148      149.36    156.93                                   
    REMARK 500  8 ARG A 149      -40.53   -150.95                                   
    REMARK 500  8 LEU A 150      144.91     65.60                                   
    REMARK 500  8 TYR A 162      -69.05   -120.30                                   
    REMARK 500  9 ASN A   3     -167.04   -102.16                                   
    REMARK 500  9 PHE A   5       81.85     51.59                                   
    REMARK 500  9 PRO A   6       41.58    -77.92                                   
    REMARK 500  9 ARG A   7     -154.50   -142.32                                   
    REMARK 500  9 LYS A  10      -93.07    -41.70                                   
    REMARK 500  9 TRP A  11       45.99    174.86                                   
    REMARK 500  9 ASN A  14      -69.63     65.34                                   
    REMARK 500  9 TYR A  23     -161.60    -61.63                                   
    REMARK 500  9 THR A  31      -71.48    -66.27                                   
    REMARK 500  9 ALA A  35      -39.40    -36.77                                   
    REMARK 500  9 PRO A  48       49.59    -79.11                                   
    REMARK 500  9 HIS A  55     -145.14    -72.44                                   
    REMARK 500  9 GLU A  58      160.05     64.43                                   
    REMARK 500  9 ASN A  64     -168.79    174.99                                   
    REMARK 500  9 ARG A  67     -145.99    -71.87                                   
    REMARK 500  9 TRP A  68     -147.11    -63.22                                   
    REMARK 500  9 GLU A  69     -143.54     47.79                                   
    REMARK 500  9 HIS A  70      156.47     68.02                                   
    REMARK 500  9 ASP A  72       74.95    -66.30                                   
    REMARK 500  9 PHE A  76      -87.49     62.64                                   
    REMARK 500  9 ASP A  77      -46.17     80.95                                   
    REMARK 500  9 ASP A  80     -165.89     43.69                                   
    REMARK 500  9 LEU A  82      106.83    -40.08                                   
    REMARK 500  9 ALA A  84      152.93    165.05                                   
    REMARK 500  9 ASP A 101      -70.27    -94.14                                   
    REMARK 500  9 ASP A 102       86.66    -60.70                                   
    REMARK 500  9 THR A 106      162.65    179.62                                   
    REMARK 500  9 SER A 109       69.06    -66.69                                   
    REMARK 500  9 ALA A 110      115.96   -160.41                                   
    REMARK 500  9 ASN A 111     -150.30     64.96                                   
    REMARK 500  9 TYR A 112     -147.73    -67.88                                   
    REMARK 500  9 ALA A 139      156.75    -41.69                                   
    REMARK 500  9 TYR A 142      -82.28    -56.52                                   
    REMARK 500  9 THR A 143      -33.56     81.59                                   
    REMARK 500  9 TYR A 144      175.23     71.59                                   
    REMARK 500  9 ASN A 147       21.04     89.16                                   
    REMARK 500  9 PHE A 148      164.82     52.34                                   
    REMARK 500  9 ARG A 149      -22.78    165.20                                   
    REMARK 500  9 LEU A 150      123.71     69.01                                   
    REMARK 500 10 TYR A   2      132.35     67.16                                   
    REMARK 500 10 PHE A   5       84.31     42.86                                   
    REMARK 500 10 PRO A   6      -85.98    -77.33                                   
    REMARK 500 10 ARG A   7     -165.33     44.35                                   
    REMARK 500 10 LYS A   8      161.86    -44.74                                   
    REMARK 500 10 LYS A  10      128.25     60.35                                   
    REMARK 500 10 TRP A  11      110.64    -37.50                                   
    REMARK 500 10 LYS A  13     -167.59   -108.84                                   
    REMARK 500 10 TYR A  23      172.41    -45.74                                   
    REMARK 500 10 ARG A  50       66.64   -116.60                                   
    REMARK 500 10 HIS A  55       70.76   -154.01                                   
    REMARK 500 10 GLU A  58      158.35    172.18                                   
    REMARK 500 10 ALA A  59      143.04    178.95                                   
    REMARK 500 10 ASN A  64     -156.25    176.44                                   
    REMARK 500 10 ARG A  67     -160.00    -78.26                                   
    REMARK 500 10 TRP A  68      -86.71    -42.95                                   
    REMARK 500 10 GLU A  69       95.23    -36.74                                   
    REMARK 500 10 HIS A  70      -61.58   -168.57                                   
    REMARK 500 10 ASP A  72       83.03    -56.10                                   
    REMARK 500 10 PRO A  75     -157.99    -78.15                                   
    REMARK 500 10 LYS A  79      154.60    -47.25                                   
    REMARK 500 10 ASP A  80     -177.79     49.50                                   
    REMARK 500 10 ALA A  84      147.98    176.47                                   
    REMARK 500 10 THR A 108     -152.53   -139.22                                   
    REMARK 500 10 ALA A 110      -97.95   -159.80                                   
    REMARK 500 10 ASN A 111      -78.05   -120.79                                   
    REMARK 500 10 TYR A 112     -156.15   -100.92                                   
    REMARK 500 10 SER A 113      114.63   -164.61                                   
    REMARK 500 10 LEU A 114      -70.24    -50.16                                   
    REMARK 500 10 PHE A 115      -27.87    -39.50                                   
    REMARK 500 10 LEU A 116      -71.60    -78.57                                   
    REMARK 500 10 MET A 126      -98.92    -71.90                                   
    REMARK 500 10 SER A 131      -80.51    -88.76                                   
    REMARK 500 10 GLN A 132      -34.53    177.03                                   
    REMARK 500 10 PHE A 148      104.29     49.20                                   
    REMARK 500 10 LEU A 150      147.46     66.47                                   
    REMARK 500 11 PHE A   5      106.47     62.55                                   
    REMARK 500 11 ARG A   7     -163.74   -165.74                                   
    REMARK 500 11 LYS A  10      -81.24    -55.60                                   
    REMARK 500 11 TRP A  11       42.91    172.05                                   
    REMARK 500 11 ASN A  14      -76.10     60.90                                   
    REMARK 500 11 TYR A  23     -163.52    -69.88                                   
    REMARK 500 11 PRO A  48       49.15    -77.84                                   
    REMARK 500 11 ASN A  64      159.79    177.93                                   
    REMARK 500 11 ARG A  67      -77.85     62.70                                   
    REMARK 500 11 TRP A  68      -56.08   -165.35                                   
    REMARK 500 11 GLU A  69       74.16    -62.55                                   
    REMARK 500 11 HIS A  70      -66.39   -106.86                                   
    REMARK 500 11 ASP A  72       73.40    -62.65                                   
    REMARK 500 11 LYS A  79      173.69    -45.75                                   
    REMARK 500 11 ASP A  80      -98.02    -25.69                                   
    REMARK 500 11 LEU A  82      118.67    -37.18                                   
    REMARK 500 11 ALA A  84      175.94    170.50                                   
    REMARK 500 11 HIS A  85      149.08   -177.62                                   
    REMARK 500 11 ALA A  88     -178.98    -57.09                                   
    REMARK 500 11 THR A  91      -96.00    -67.13                                   
    REMARK 500 11 ASP A 101      -81.71    -55.48                                   
    REMARK 500 11 ASP A 102       96.61    -40.03                                   
    REMARK 500 11 GLU A 103      156.90    175.09                                   
    REMARK 500 11 THR A 108       25.89   -142.05                                   
    REMARK 500 11 SER A 109       89.30     70.68                                   
    REMARK 500 11 ALA A 110      137.04    174.87                                   
    REMARK 500 11 ASN A 111     -149.04     64.59                                   
    REMARK 500 11 SER A 113      124.73     75.38                                   
    REMARK 500 11 SER A 131     -115.22    -90.25                                   
    REMARK 500 11 GLN A 132      -48.64   -159.41                                   
    REMARK 500 11 PRO A 140       21.11    -77.27                                   
    REMARK 500 11 THR A 143      -33.46   -161.97                                   
    REMARK 500 11 TYR A 144      166.06     59.24                                   
    REMARK 500 11 PHE A 148      139.28     75.45                                   
    REMARK 500 11 ARG A 149      -25.06   -155.65                                   
    REMARK 500 11 LEU A 150       83.36     65.66                                   
    REMARK 500 11 TYR A 162      -51.47   -131.24                                   
    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                           1  ZN A 165  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS A  85   NE2                                                    
    REMARK 620 2 HIS A  98   ND1  92.1                                              
    REMARK 620 3 HIS A  70   NE2 134.6  72.8                                        
    REMARK 620 4 ASP A  72   OD2  90.5 150.0  84.2                                  
    REMARK 620 N                    1     2     3                                   
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                           1  CA A 167  CA                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 ASP A  77   OD2                                                    
    REMARK 620 2 ASP A 100   OD1  92.3                                              
    REMARK 620 3 ASP A 100   OD2 104.0  45.6                                        
    REMARK 620 4 GLU A 103   OE1 141.9  92.2  56.0                                  
    REMARK 620 5 GLU A 103   OE2 173.8  90.8  81.9  43.2                            
    REMARK 620 6 ASP A  77   OD1  45.5  67.3  59.2 103.0 140.7                      
    REMARK 620 7 GLY A  78   O    66.6 144.5 109.8  88.8 113.2  77.9                
    REMARK 620 8 LYS A  79   O   108.7 158.8 127.8  73.5  68.1 130.4  52.9          
    REMARK 620 9 ASP A  80   O    82.2 119.0 162.8 127.2  91.6 127.3  87.4  62.7    
    REMARK 620 10 LEU A  82   O    83.3  50.5  95.9 127.0  94.6  95.3 143.9         
    REMARK 620  127.0  68.6                                                         
    REMARK 620 N                    1     2     3     4     5     6     7     8     
    REMARK 620     9                                                                
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                           1  CA A 168  CA                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 ASP A  60   O                                                      
    REMARK 620 2 GLY A  92   O   100.0                                              
    REMARK 620 3 GLY A  94   O    82.5 112.6                                        
    REMARK 620 4 GLY A  95   N   115.7 132.2  48.0                                  
    REMARK 620 5 ASP A  96   N   124.4 125.4 103.8  56.7                            
    REMARK 620 6 ASP A  96   OD1 104.2  68.7 173.0 125.7  70.8                      
    REMARK 620 N                    1     2     3     4     5                       
    REMARK 620                                                                      
    REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
    REMARK 620                           1  ZN A 166  ZN                            
    REMARK 620 N RES CSSEQI ATOM                                                    
    REMARK 620 1 HIS A 120   NE2                                                    
    REMARK 620 2 HIS A 124   NE2 100.3                                              
    REMARK 620 3 HIS A 130   NE2 111.5  71.9                                        
    REMARK 620 4 I52 A 800   O26 145.1 106.8  97.8                                  
    REMARK 620 5 I52 A 800   O1   85.8  81.2 149.9  77.2                            
    REMARK 620 N                    1     2     3     4                             
    REMARK 800                                                                      
    REMARK 800 SITE                                                                 
    REMARK 800 SITE_IDENTIFIER: AC1                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 165                  
    REMARK 800 SITE_IDENTIFIER: AC2                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 166                  
    REMARK 800 SITE_IDENTIFIER: AC3                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 167                  
    REMARK 800 SITE_IDENTIFIER: AC4                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 168                  
    REMARK 800 SITE_IDENTIFIER: AC5                                                 
    REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
    REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE I52 A 800                 
    DBREF  1HOV A    2   148  UNP    P08253   MMP2_HUMAN     110    256             
    SEQRES   1 A  163  MET TYR ASN PHE PHE PRO ARG LYS PRO LYS TRP ASP LYS          
    SEQRES   2 A  163  ASN GLN ILE THR TYR ARG ILE ILE GLY TYR THR PRO ASP          
    SEQRES   3 A  163  LEU ASP PRO GLU THR VAL ASP ASP ALA PHE ALA ARG ALA          
    SEQRES   4 A  163  PHE GLN VAL TRP SER ASP VAL THR PRO LEU ARG PHE SER          
    SEQRES   5 A  163  ARG ILE HIS ASP GLY GLU ALA ASP ILE MET ILE ASN PHE          
    SEQRES   6 A  163  GLY ARG TRP GLU HIS GLY ASP GLY TYR PRO PHE ASP GLY          
    SEQRES   7 A  163  LYS ASP GLY LEU LEU ALA HIS ALA PHE ALA PRO GLY THR          
    SEQRES   8 A  163  GLY VAL GLY GLY ASP SER HIS PHE ASP ASP ASP GLU LEU          
    SEQRES   9 A  163  TRP THR ASN THR SER ALA ASN TYR SER LEU PHE LEU VAL          
    SEQRES  10 A  163  ALA ALA HIS GLU PHE GLY HIS ALA MET GLY LEU GLU HIS          
    SEQRES  11 A  163  SER GLN ASP PRO GLY ALA LEU MET ALA PRO ILE TYR THR          
    SEQRES  12 A  163  TYR THR LYS ASN PHE ARG LEU SER GLN ASP ASP ILE LYS          
    SEQRES  13 A  163  GLY ILE GLN GLU LEU TYR GLY                                  
    HET     ZN  A 165       1                                                       
    HET     ZN  A 166       1                                                       
    HET     CA  A 167       1                                                       
    HET     CA  A 168       1                                                       
    HET    I52  A 800      82                                                       
    HETNAM      ZN ZINC ION                                                         
    HETNAM      CA CALCIUM ION                                                      
    HETNAM     I52 N-{4-[(1-HYDROXYCARBAMOYL-2-METHYL-PROPYL)-(2-                   
    HETNAM   2 I52  MORPHOLIN-4-YL-ETHYL)-SULFAMOYL]-4-PENTYL-BENZAMIDE             
    HETSYN     I52 SC-74020                                                         
    FORMUL   2   ZN    2(ZN 2+)                                                     
    FORMUL   4   CA    2(CA 2+)                                                     
    FORMUL   6  I52    C29 H42 N4 O6 S                                              
    HELIX    1   1 ASP A   28  ASP A   45  1                                  18    
    HELIX    2   2 SER A  113  ALA A  125  1                                  13    
    HELIX    3   3 SER A  151  TYR A  162  1                                  12    
    SHEET    1   A 5 PHE A  51  ARG A  53  0                                        
    SHEET    2   A 5 ILE A  16  ILE A  20  1  O  ILE A  16   N  SER A  52           
    SHEET    3   A 5 ILE A  61  PHE A  65  1  N  ILE A  61   O  THR A  17           
    SHEET    4   A 5 SER A  97  PHE A  99  1  N  SER A  97   O  MET A  62           
    SHEET    5   A 5 ALA A  84  ALA A  86 -1  O  HIS A  85   N  HIS A  98           
    LINK        ZN    ZN A 165                 NE2 HIS A  85     1555   1555  2.07  
    LINK        ZN    ZN A 165                 ND1 HIS A  98     1555   1555  2.26  
    LINK        ZN    ZN A 165                 NE2 HIS A  70     1555   1555  2.13  
    LINK        ZN    ZN A 165                 OD2 ASP A  72     1555   1555  2.29  
    LINK        CA    CA A 167                 OD2 ASP A  77     1555   1555  2.64  
    LINK        CA    CA A 167                 OD1 ASP A 100     1555   1555  2.87  
    LINK        CA    CA A 167                 OD2 ASP A 100     1555   1555  2.67  
    LINK        CA    CA A 167                 OE1 GLU A 103     1555   1555  3.13  
    LINK        CA    CA A 167                 OE2 GLU A 103     1555   1555  2.48  
    LINK        CA    CA A 167                 OD1 ASP A  77     1555   1555  2.90  
    LINK        CA    CA A 167                 O   GLY A  78     1555   1555  2.59  
    LINK        CA    CA A 167                 O   LYS A  79     1555   1555  2.50  
    LINK        CA    CA A 167                 O   ASP A  80     1555   1555  2.57  
    LINK        CA    CA A 167                 O   LEU A  82     1555   1555  2.57  
    LINK         O   ASP A  60                CA    CA A 168     1555   1555  2.45  
    LINK         O   GLY A  92                CA    CA A 168     1555   1555  2.47  
    LINK         O   GLY A  94                CA    CA A 168     1555   1555  2.54  
    LINK         N   GLY A  95                CA    CA A 168     1555   1555  2.83  
    LINK         N   ASP A  96                CA    CA A 168     1555   1555  2.84  
    LINK         OD1 ASP A  96                CA    CA A 168     1555   1555  2.44  
    LINK         NE2 HIS A 120                ZN    ZN A 166     1555   1555  2.16  
    LINK         NE2 HIS A 124                ZN    ZN A 166     1555   1555  2.30  
    LINK         NE2 HIS A 130                ZN    ZN A 166     1555   1555  2.06  
    LINK        ZN    ZN A 166                 O26 I52 A 800     1555   1555  2.13  
    LINK        ZN    ZN A 166                 O1  I52 A 800     1555   1555  2.08  
    SITE     1 AC1  4 HIS A  70  ASP A  72  HIS A  85  HIS A  98                    
    SITE     1 AC2  4 HIS A 120  HIS A 124  HIS A 130  I52 A 800                    
    SITE     1 AC3  7 ASP A  77  GLY A  78  LYS A  79  ASP A  80                    
    SITE     2 AC3  7 LEU A  82  ASP A 100  GLU A 103                               
    SITE     1 AC4  6 ASP A  60  GLY A  92  VAL A  93  GLY A  94                    
    SITE     2 AC4  6 GLY A  95  ASP A  96                                          
    SITE     1 AC5 19 GLY A  81  LEU A  82  LEU A  83  ALA A  84                    
    SITE     2 AC5 19 HIS A  85  HIS A 120  GLU A 121  HIS A 124                    
    SITE     3 AC5 19 HIS A 130  ALA A 136  LEU A 137  ALA A 139                    
    SITE     4 AC5 19 ILE A 141  TYR A 142  THR A 143  THR A 145                    
    SITE     5 AC5 19 PHE A 148  ARG A 149   ZN A 166                               
    CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
    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      1.000000  0.000000  0.000000        0.00000                         
    SCALE2      0.000000  1.000000  0.000000        0.00000                         
    SCALE3      0.000000  0.000000  1.000000        0.00000                         
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    ENDMDL                                                                          
    CONECT  977 2520                                                                
    CONECT 1154 2517                                                                
    CONECT 1176 2517                                                                
    CONECT 1249 2519                                                                
    CONECT 1250 2519                                                                
    CONECT 1258 2519                                                                
    CONECT 1265 2519                                                                
    CONECT 1287 2519                                                                
    CONECT 1306 2519                                                                
    CONECT 1360 2517                                                                
    CONECT 1446 2520                                                                
    CONECT 1469 2520                                                                
    CONECT 1473 2520                                                                
    CONECT 1480 2520                                                                
    CONECT 1486 2520                                                                
    CONECT 1509 2517                                                                
    CONECT 1546 2519                                                                
    CONECT 1547 2519                                                                
    CONECT 1583 2519                                                                
    CONECT 1584 2519                                                                
    CONECT 1846 2518                                                                
    CONECT 1905 2518                                                                
    CONECT 1990 2518                                                                
    CONECT 2517 1154 1176 1360 1509                                                 
    CONECT 2518 1846 1905 1990 2537                                                 
    CONECT 2518 2543                                                                
    CONECT 2519 1249 1250 1258 1265                                                 
    CONECT 2519 1287 1306 1546 1547                                                 
    CONECT 2519 1583 1584                                                           
    CONECT 2520  977 1446 1469 1473                                                 
    CONECT 2520 1480 1486                                                           
    CONECT 2521 2522 2523 2561 2562                                                 
    CONECT 2522 2521 2563 2564 2565                                                 
    CONECT 2523 2521 2525 2566 2567                                                 
    CONECT 2524 2525 2553 2568 2569                                                 
    CONECT 2525 2523 2524 2570 2571                                                 
    CONECT 2526 2536 2572 2573 2574                                                 
    CONECT 2527 2536 2575 2576 2577                                                 
    CONECT 2528 2529 2530 2531                                                      
    CONECT 2529 2528 2539 2578 2579                                                 
    CONECT 2530 2528 2534 2580 2581                                                 
    CONECT 2531 2528 2533 2582 2583                                                 
    CONECT 2532 2533 2534                                                           
    CONECT 2533 2531 2532 2584 2585                                                 
    CONECT 2534 2530 2532 2586 2587                                                 
    CONECT 2535 2552 2553 2588                                                      
    CONECT 2536 2526 2527 2538 2589                                                 
    CONECT 2537 2518 2542                                                           
    CONECT 2538 2536 2541 2542 2590                                                 
    CONECT 2539 2529 2541 2591 2592                                                 
    CONECT 2540 2541 2545 2556 2557                                                 
    CONECT 2541 2538 2539 2540                                                      
    CONECT 2542 2537 2538 2544                                                      
    CONECT 2543 2518 2544 2593                                                      
    CONECT 2544 2542 2543 2594                                                      
    CONECT 2545 2540                                                                
    CONECT 2546 2547                                                                
    CONECT 2547 2546 2548 2549                                                      
    CONECT 2548 2547 2555 2595                                                      
    CONECT 2549 2547 2551 2552                                                      
    CONECT 2550 2551 2553 2596                                                      
    CONECT 2551 2549 2550 2597                                                      
    CONECT 2552 2535 2549 2598                                                      
    CONECT 2553 2524 2535 2550                                                      
    CONECT 2554 2556 2559 2599                                                      
    CONECT 2555 2548 2559 2560                                                      
    CONECT 2556 2540 2554 2558                                                      
    CONECT 2557 2540                                                                
    CONECT 2558 2556 2560 2600                                                      
    CONECT 2559 2554 2555 2601                                                      
    CONECT 2560 2555 2558 2602                                                      
    CONECT 2561 2521                                                                
    CONECT 2562 2521                                                                
    CONECT 2563 2522                                                                
    CONECT 2564 2522                                                                
    CONECT 2565 2522                                                                
    CONECT 2566 2523                                                                
    CONECT 2567 2523                                                                
    CONECT 2568 2524                                                                
    CONECT 2569 2524                                                                
    CONECT 2570 2525                                                                
    CONECT 2571 2525                                                                
    CONECT 2572 2526                                                                
    CONECT 2573 2526                                                                
    CONECT 2574 2526                                                                
    CONECT 2575 2527                                                                
    CONECT 2576 2527                                                                
    CONECT 2577 2527                                                                
    CONECT 2578 2529                                                                
    CONECT 2579 2529                                                                
    CONECT 2580 2530                                                                
    CONECT 2581 2530                                                                
    CONECT 2582 2531                                                                
    CONECT 2583 2531                                                                
    CONECT 2584 2533                                                                
    CONECT 2585 2533                                                                
    CONECT 2586 2534                                                                
    CONECT 2587 2534                                                                
    CONECT 2588 2535                                                                
    CONECT 2589 2536                                                                
    CONECT 2590 2538                                                                
    CONECT 2591 2539                                                                
    CONECT 2592 2539                                                                
    CONECT 2593 2543                                                                
    CONECT 2594 2544                                                                
    CONECT 2595 2548                                                                
    CONECT 2596 2550                                                                
    CONECT 2597 2551                                                                
    CONECT 2598 2552                                                                
    CONECT 2599 2554                                                                
    CONECT 2600 2558                                                                
    CONECT 2601 2559                                                                
    CONECT 2602 2560                                                                
    MASTER      546    0    5    3    5    0   11    628611   11  113   13          
    END                                                                             

    3D molecular view of vibration

    Displacement vectors
    Display
    Animation
    Display

    Still image of displacement vectors and GIF animation


    Mode 1

    Time-average properties and properties of the 10 lowest-frequency modes

    Fluctuation of atoms:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of dihedral angles:
    Time average and for the 3 lowest-frequency modes.
    Fluctuation of atomsFluctuation of dihedral angles

    Correlations between fluctuations of atoms

    Mode 1
    Correlations between fluctuations of atoms - Mode 1
    Time Average
    Time Average
    Distance map
    Distance map

    Calculation note

    PDB file name : pdb1hov.ent

    Chains and HETATMs selected: 
      ATOM        A

    The following atoms are removed from PDB data on concern that they may have 
    abnormally large fluctuations, because they interact with few atoms.
      ATOM      6  CG  MET A   1      -1.080  44.177   0.894  1.00  0.00           C  
      ATOM      7  SD  MET A   1      -0.914  42.422   1.304  1.00  0.00           S  
      ATOM      8  CE  MET A   1       0.481  42.589   2.444  1.00  0.00           C  
      ATOM     63  CG  ARG A   7       7.834  44.792   9.473  1.00  0.00           C  
      ATOM     64  CD  ARG A   7       9.216  44.555   8.862  1.00  0.00           C  
      ATOM     65  NE  ARG A   7       9.108  44.558   7.375  1.00  0.00           N  
      ATOM     66  CZ  ARG A   7       8.779  45.651   6.741  1.00  0.00           C  
      ATOM     67  NH1 ARG A   7       8.535  46.747   7.407  1.00  0.00           N  
      ATOM     68  NH2 ARG A   7       8.689  45.646   5.438  1.00  0.00           N  
      ATOM    560  CG  ARG A  67      24.786  23.518  18.535  1.00  0.00           C  
      ATOM    561  CD  ARG A  67      24.985  24.714  17.606  1.00  0.00           C  
      ATOM    562  NE  ARG A  67      26.126  24.433  16.691  1.00  0.00           N  
      ATOM    563  CZ  ARG A  67      26.409  25.258  15.719  1.00  0.00           C  
      ATOM    564  NH1 ARG A  67      25.696  26.338  15.544  1.00  0.00           N  
      ATOM    565  NH2 ARG A  67      27.411  25.005  14.924  1.00  0.00           N  
      ATOM    662  CG  LYS A  79      17.800  13.184  31.516  1.00  0.00           C  
      ATOM    663  CD  LYS A  79      18.332  13.959  32.719  1.00  0.00           C  
      ATOM    664  CE  LYS A  79      19.503  13.196  33.330  1.00  0.00           C  
      ATOM    665  NZ  LYS A  79      20.783  13.828  32.901  1.00  0.00           N  
      ATOM   1166  CG  LYS A 146       2.679   1.809  21.576  1.00  0.00           C  
      ATOM   1167  CD  LYS A 146       2.947   2.232  23.021  1.00  0.00           C  
      ATOM   1168  CE  LYS A 146       1.926   1.564  23.946  1.00  0.00           C  
      ATOM   1169  NZ  LYS A 146       0.927   2.572  24.391  1.00  0.00           N  
      ATOM   1194  CG  ARG A 149      -2.889   8.470  18.101  1.00  0.00           C  
      ATOM   1195  CD  ARG A 149      -3.673   9.047  19.278  1.00  0.00           C  
      ATOM   1196  NE  ARG A 149      -4.026   7.956  20.232  1.00  0.00           N  
      ATOM   1197  CZ  ARG A 149      -5.016   8.117  21.072  1.00  0.00           C  
      ATOM   1198  NH1 ARG A 149      -5.689   9.235  21.082  1.00  0.00           N  
      ATOM   1199  NH2 ARG A 149      -5.333   7.159  21.905  1.00  0.00           N  
      ATOM   1252  CG  LYS A 156     -10.621  23.453  12.586  1.00  0.00           C  
      ATOM   1253  CD  LYS A 156     -10.248  24.360  13.759  1.00  0.00           C  
      ATOM   1254  CE  LYS A 156     -11.511  24.742  14.525  1.00  0.00           C  
      ATOM   1255  NZ  LYS A 156     -12.104  23.519  15.134  1.00  0.00           N  

    = Normal mode analysis calculation =

    No. of modes used in the calculation : All modes.

    Parameters of potential energies:
      1-4 and 1-5 non-bonded interactions: E(d) = A*exp(-d(PDB)**2/B**2)(d-d(PDB))**2.
      Loop-closing potential:              E(d) = A*(d-d(PDB))**2.
        for a disulfide bond and one of the bonds in the DNA and RNA sugar ring.
      where d and d(PDB) are distances between atoms in calculation and in PDB data, 
      respectively.

      Interaction type   A       B      Cutoff distance (A)
        1-4             1.00    5.00      100.00
        1-5             1.00    5.00      100.00
        Loop-closing  100.00

    Temperature adjustment by magnitude of fluctuation:
      Set to mean displacements of atoms       0.500 A

    Animation
      No. of frames: 11
      Mean displacements (A):    0.50

    Displacement vector
      Mean length of vectors (A):    3.00