GenomeNet

Database: PDB
Entry: 3L3T
LinkDB: 3L3T
Original site: 3L3T 
HEADER    HYDROLASE/CELL ADHESION                 17-DEC-09   3L3T              
TITLE     HUMAN MESOTRYPSIN COMPLEXED WITH AMYLOID PRECURSOR PROTEIN INHIBITOR  
TITLE    2 VARIANT (APPIR15K)                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PRSS3 PROTEIN;                                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 28-251;                                       
COMPND   5 SYNONYM: MESOTRYPSIN;                                                
COMPND   6 EC: 3.4.21.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PROTEIN APP;                                               
COMPND  11 CHAIN: E, F, G, H;                                                   
COMPND  12 FRAGMENT: UNP RESIDUES 211-267;                                      
COMPND  13 SYNONYM: ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR;                 
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 STRAIN: BL21(DE3);                                                   
SOURCE   6 GENE: PRSS3;                                                         
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: APP;                                                           
SOURCE  14 EXPRESSION_SYSTEM: PICHIA PASTORIS;                                  
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    HUMAN MESOTRYPSIN, CANONICAL INHIBITOR, ALZHEIMER'S AMYLOID PRECURSOR 
KEYWDS   2 PROTEIN INHIBITOR,APPI, APPI-R15K, HYDROLASE-CELL ADHESION COMPLEX   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.SALAMEH,A.S.SOARES,E.S.RADISKY                                    
REVDAT   2   12-JAN-11 3L3T    1       JRNL                                     
REVDAT   1   22-SEP-10 3L3T    0                                                
JRNL        AUTH   M.A.SALAMEH,A.S.SOARES,D.NAVANEETHAM,D.SINHA,P.N.WALSH,      
JRNL        AUTH 2 E.S.RADISKY                                                  
JRNL        TITL   DETERMINANTS OF AFFINITY AND PROTEOLYTIC STABILITY IN        
JRNL        TITL 2 INTERACTIONS OF KUNITZ FAMILY PROTEASE INHIBITORS WITH       
JRNL        TITL 3 MESOTRYPSIN.                                                 
JRNL        REF    J.BIOL.CHEM.                  V. 285 36884 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20861008                                                     
JRNL        DOI    10.1074/JBC.M110.171348                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.38 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.38                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.52                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 63638                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6115                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 24.5160 - 13.6950    0.96      520     0  0.3380 0.0000        
REMARK   3     2 13.6950 - 11.2050    0.94      504     0  0.2440 0.0000        
REMARK   3     3 11.2050 -  9.8950    0.92      487     0  0.1740 0.0000        
REMARK   3     4  9.8950 -  9.0400    0.95      512     0  0.1750 0.0000        
REMARK   3     5  9.0400 -  8.4200    0.95      506     0  0.1920 0.0000        
REMARK   3     6  8.4200 -  7.9420    0.95      520     0  0.1770 0.0000        
REMARK   3     7  7.9420 -  7.5560    0.96      524     0  0.1680 0.0000        
REMARK   3     8  7.5560 -  7.2360    0.92      495     0  0.1720 0.0000        
REMARK   3     9  7.2360 -  6.9640    0.94      498     0  0.1760 0.0000        
REMARK   3    10  6.9640 -  6.7290    0.96      518     0  0.1800 0.0000        
REMARK   3    11  6.7290 -  6.5220    0.95      515     0  0.1690 0.0000        
REMARK   3    12  6.5220 -  6.3390    0.94      519     0  0.1520 0.0000        
REMARK   3    13  6.3390 -  6.1750    0.95      494     0  0.1520 0.0000        
REMARK   3    14  6.1750 -  6.0270    0.95      525     0  0.1570 0.0000        
REMARK   3    15  6.0270 -  5.8920    0.95      517     0  0.1700 0.0000        
REMARK   3    16  5.8920 -  5.7680    0.97      499     0  0.1520 0.0000        
REMARK   3    17  5.7680 -  5.6540    0.95      537     0  0.1480 0.0000        
REMARK   3    18  5.6540 -  5.5490    0.94      512     0  0.1470 0.0000        
REMARK   3    19  5.5490 -  5.4510    0.96      489     0  0.1450 0.0000        
REMARK   3    20  5.4510 -  5.3590    0.94      531     0  0.1410 0.0000        
REMARK   3    21  5.3590 -  5.2730    0.96      503     0  0.1380 0.0000        
REMARK   3    22  5.2730 -  5.1930    0.95      489     0  0.1330 0.0000        
REMARK   3    23  5.1930 -  5.1170    0.94      528     0  0.1290 0.0000        
REMARK   3    24  5.1170 -  5.0460    0.96      499     0  0.1290 0.0000        
REMARK   3    25  5.0460 -  4.9780    0.96      531     0  0.1280 0.0000        
REMARK   3    26  4.9780 -  4.9140    0.94      494     0  0.1230 0.0000        
REMARK   3    27  4.9140 -  4.8530    0.93      494     0  0.1260 0.0000        
REMARK   3    28  4.8530 -  4.7950    0.94      530     0  0.1140 0.0000        
REMARK   3    29  4.7950 -  4.7400    0.97      499     0  0.1170 0.0000        
REMARK   3    30  4.7400 -  4.6870    0.94      494     0  0.1240 0.0000        
REMARK   3    31  4.6870 -  4.6360    0.94      512     0  0.1150 0.0000        
REMARK   3    32  4.6360 -  4.5880    0.95      523     0  0.1120 0.0000        
REMARK   3    33  4.5880 -  4.5420    0.97      525     0  0.1070 0.0000        
REMARK   3    34  4.5420 -  4.4970    0.95      520     0  0.1130 0.0000        
REMARK   3    35  4.4970 -  4.4540    0.95      497     0  0.1070 0.0000        
REMARK   3    36  4.4540 -  4.4120    0.96      492     0  0.1110 0.0000        
REMARK   3    37  4.4120 -  4.3720    0.94      525     0  0.1120 0.0000        
REMARK   3    38  4.3720 -  4.3340    0.95      515     0  0.1070 0.0000        
REMARK   3    39  4.3340 -  4.2970    0.93      482     0  0.1090 0.0000        
REMARK   3    40  4.2970 -  4.2610    0.95      528     0  0.0980 0.0000        
REMARK   3    41  4.2610 -  4.2260    0.95      491     0  0.1070 0.0000        
REMARK   3    42  4.2260 -  4.1930    0.93      503     0  0.1160 0.0000        
REMARK   3    43  4.1930 -  4.1600    0.95      527     0  0.1060 0.0000        
REMARK   3    44  4.1600 -  4.1280    0.97      524     0  0.1070 0.0000        
REMARK   3    45  4.1280 -  4.0980    0.96      517     0  0.1140 0.0000        
REMARK   3    46  4.0980 -  4.0680    0.95      492     0  0.1070 0.0000        
REMARK   3    47  4.0680 -  4.0390    0.96      505     0  0.1070 0.0000        
REMARK   3    48  4.0390 -  4.0110    0.95      528     0  0.1190 0.0000        
REMARK   3    49  4.0110 -  3.9840    0.93      496     0  0.1210 0.0000        
REMARK   3    50  3.9840 -  3.9570    0.94      530     0  0.1180 0.0000        
REMARK   3    51  3.9570 -  3.9310    0.93      461     0  0.1280 0.0000        
REMARK   3    52  3.9310 -  3.9060    0.94      519     0  0.1180 0.0000        
REMARK   3    53  3.9060 -  3.8810    0.96      515     0  0.1180 0.0000        
REMARK   3    54  3.8810 -  3.8570    0.96      511     0  0.1240 0.0000        
REMARK   3    55  3.8570 -  3.8340    0.94      513     0  0.1220 0.0000        
REMARK   3    56  3.8340 -  3.8110    0.97      526     0  0.1170 0.0000        
REMARK   3    57  3.8110 -  3.7890    0.96      504     0  0.1440 0.0000        
REMARK   3    58  3.7890 -  3.7670    0.95      532     0  0.1270 0.0000        
REMARK   3    59  3.7670 -  3.7450    0.94      503     0  0.1240 0.0000        
REMARK   3    60  3.7450 -  3.7240    0.94      495     0  0.1220 0.0000        
REMARK   3    61  3.7240 -  3.7040    0.94      494     0  0.1350 0.0000        
REMARK   3    62  3.7040 -  3.6840    0.95      520     0  0.1400 0.0000        
REMARK   3    63  3.6840 -  3.6650    0.95      536     0  0.1330 0.0000        
REMARK   3    64  3.6650 -  3.6450    0.96      475     0  0.1350 0.0000        
REMARK   3    65  3.6450 -  3.6270    0.95      546     0  0.1280 0.0000        
REMARK   3    66  3.6270 -  3.6080    0.97      517     0  0.1350 0.0000        
REMARK   3    67  3.6080 -  3.5900    0.94      489     0  0.1500 0.0000        
REMARK   3    68  3.5900 -  3.5730    0.97      525     0  0.1430 0.0000        
REMARK   3    69  3.5730 -  3.5560    0.95      508     0  0.1490 0.0000        
REMARK   3    70  3.5560 -  3.5390    0.94      526     0  0.1400 0.0000        
REMARK   3    71  3.5390 -  3.5220    0.94      495     0  0.1370 0.0000        
REMARK   3    72  3.5220 -  3.5060    0.94      509     0  0.1570 0.0000        
REMARK   3    73  3.5060 -  3.4900    0.96      497     0  0.1480 0.0000        
REMARK   3    74  3.4900 -  3.4740    0.94      523     0  0.1400 0.0000        
REMARK   3    75  3.4740 -  3.4580    0.97      506     0  0.1380 0.0000        
REMARK   3    76  3.4580 -  3.4430    0.94      507     0  0.1440 0.0000        
REMARK   3    77  3.4430 -  3.4280    0.94      510     0  0.1430 0.0000        
REMARK   3    78  3.4280 -  3.4140    0.96      510     0  0.1350 0.0000        
REMARK   3    79  3.4140 -  3.3990    0.96      492     0  0.1410 0.0000        
REMARK   3    80  3.3990 -  3.3850    0.96      553     0  0.1430 0.0000        
REMARK   3    81  3.3850 -  3.3710    0.92      491     0  0.1490 0.0000        
REMARK   3    82  3.3710 -  3.3570    0.97      520     0  0.1380 0.0000        
REMARK   3    83  3.3570 -  3.3440    0.96      507     0  0.1450 0.0000        
REMARK   3    84  3.3440 -  3.3300    0.97      509     0  0.1740 0.0000        
REMARK   3    85  3.3300 -  3.3170    0.95      485     0  0.1680 0.0000        
REMARK   3    86  3.3170 -  3.3050    0.97      567     0  0.1510 0.0000        
REMARK   3    87  3.3050 -  3.2920    0.95      494     0  0.1570 0.0000        
REMARK   3    88  3.2920 -  3.2790    0.96      536     0  0.1660 0.0000        
REMARK   3    89  3.2790 -  3.2670    0.96      520     0  0.1770 0.0000        
REMARK   3    90  3.2670 -  3.2550    0.95      495     0  0.1640 0.0000        
REMARK   3    91  3.2550 -  3.2430    0.95      486     0  0.1560 0.0000        
REMARK   3    92  3.2430 -  3.2310    0.95      556     0  0.1910 0.0000        
REMARK   3    93  3.2310 -  3.2200    0.96      514     0  0.1790 0.0000        
REMARK   3    94  3.2200 -  3.2080    0.97      504     0  0.1870 0.0000        
REMARK   3    95  3.2080 -  3.1970    0.94      470     0  0.1880 0.0000        
REMARK   3    96  3.1970 -  3.1860    0.96      550     0  0.1800 0.0000        
REMARK   3    97  3.1860 -  3.1750    0.95      514     0  0.2150 0.0000        
REMARK   3    98  3.1750 -  3.1640    0.93      501     0  0.1840 0.0000        
REMARK   3    99  3.1640 -  3.1530    0.95      520     0  0.1990 0.0000        
REMARK   3   100  3.1530 -  3.1430    0.94      470     0  0.2040 0.0000        
REMARK   3   101  3.1430 -  3.1320    0.95      560     0  0.1910 0.0000        
REMARK   3   102  3.1320 -  3.1220    0.94      467     0  0.1880 0.0000        
REMARK   3   103  3.1220 -  3.1120    0.94      540     0  0.1920 0.0000        
REMARK   3   104  3.1120 -  3.1020    0.93      464     0  0.2080 0.0000        
REMARK   3   105  3.1020 -  3.0920    0.95      483     0  0.1850 0.0000        
REMARK   3   106  3.0920 -  3.0820    0.94      543     0  0.2050 0.0000        
REMARK   3   107  3.0820 -  3.0730    0.96      530     0  0.2120 0.0000        
REMARK   3   108  3.0730 -  3.0630    0.95      509     0  0.2070 0.0000        
REMARK   3   109  3.0630 -  3.0540    0.98      529     0  0.1900 0.0000        
REMARK   3   110  3.0540 -  3.0450    0.95      518     0  0.1930 0.0000        
REMARK   3   111  3.0450 -  3.0360    0.96      491     0  0.2060 0.0000        
REMARK   3   112  3.0360 -  3.0260    0.94      523     0  0.2110 0.0000        
REMARK   3   113  3.0260 -  3.0180    0.94      506     0  0.1970 0.0000        
REMARK   3   114  3.0180 -  3.0090    0.93      464     0  0.2160 0.0000        
REMARK   3   115  3.0090 -  3.0000    0.98      546     0  0.2120 0.0000        
REMARK   3   116  3.0000 -  2.9910    0.97      540     0  0.2240 0.0000        
REMARK   3   117  2.9910 -  2.9830    0.95      504     0  0.2230 0.0000        
REMARK   3   118  2.9830 -  2.9740    0.95      499     0  0.2200 0.0000        
REMARK   3   119  2.9740 -  2.9660    0.95      536     0  0.2220 0.0000        
REMARK   3   120  2.9660 -  2.9580    0.93      487     0  0.2190 0.0000        
REMARK   3   121  2.9580 -  2.9500    0.96      496     0  0.2190 0.0000        
REMARK   3   122  2.9500 -  2.9420    0.95      499     0  0.2310 0.0000        
REMARK   3   123  2.9420 -  2.9340    0.95      547     0  0.2140 0.0000        
REMARK   3   124  2.9340 -  2.9260    0.96      505     0  0.2140 0.0000        
REMARK   3   125  2.9260 -  2.9180    0.96      509     0  0.2090 0.0000        
REMARK   3   126  2.9180 -  2.9100    0.94      506     0  0.2110 0.0000        
REMARK   3   127  2.9100 -  2.9030    0.98      516     0  0.2080 0.0000        
REMARK   3   128  2.9030 -  2.8950    0.95      488     0  0.2330 0.0000        
REMARK   3   129  2.8950 -  2.8880    0.96      519     0  0.2140 0.0000        
REMARK   3   130  2.8880 -  2.8800    0.94      505     0  0.2160 0.0000        
REMARK   3   131  2.8800 -  2.8730    0.95      555     0  0.2230 0.0000        
REMARK   3   132  2.8730 -  2.8650    0.94      505     0  0.2360 0.0000        
REMARK   3   133  2.8650 -  2.8580    0.96      491     0  0.2280 0.0000        
REMARK   3   134  2.8580 -  2.8510    0.97      523     0  0.2250 0.0000        
REMARK   3   135  2.8510 -  2.8440    0.95      520     0  0.2410 0.0000        
REMARK   3   136  2.8440 -  2.8370    0.96      486     0  0.2370 0.0000        
REMARK   3   137  2.8370 -  2.8300    0.98      556     0  0.2370 0.0000        
REMARK   3   138  2.8300 -  2.8230    0.95      501     0  0.2370 0.0000        
REMARK   3   139  2.8230 -  2.8170    0.95      516     0  0.2230 0.0000        
REMARK   3   140  2.8170 -  2.8100    0.97      472     0  0.2230 0.0000        
REMARK   3   141  2.8100 -  2.8030    0.97      534     0  0.2330 0.0000        
REMARK   3   142  2.8030 -  2.7970    0.95      546     0  0.2160 0.0000        
REMARK   3   143  2.7970 -  2.7900    0.97      525     0  0.2120 0.0000        
REMARK   3   144  2.7900 -  2.7840    0.95      518     0  0.2290 0.0000        
REMARK   3   145  2.7840 -  2.7770    0.93      494     0  0.2350 0.0000        
REMARK   3   146  2.7770 -  2.7710    0.95      524     0  0.2330 0.0000        
REMARK   3   147  2.7710 -  2.7650    0.98      472     0  0.2200 0.0000        
REMARK   3   148  2.7650 -  2.7580    0.96      545     0  0.2290 0.0000        
REMARK   3   149  2.7580 -  2.7520    0.95      519     0  0.2360 0.0000        
REMARK   3   150  2.7520 -  2.7460    0.94      501     0  0.2240 0.0000        
REMARK   3   151  2.7460 -  2.7400    0.94      492     0  0.2260 0.0000        
REMARK   3   152  2.7400 -  2.7340    0.94      499     0  0.2440 0.0000        
REMARK   3   153  2.7340 -  2.7280    0.94      488     0  0.2360 0.0000        
REMARK   3   154  2.7280 -  2.7220    0.96      536     0  0.2310 0.0000        
REMARK   3   155  2.7220 -  2.7160    0.96      566     0  0.2230 0.0000        
REMARK   3   156  2.7160 -  2.7110    0.94      422     0  0.2360 0.0000        
REMARK   3   157  2.7110 -  2.7050    0.92      529     0  0.2470 0.0000        
REMARK   3   158  2.7050 -  2.6990    0.92      480     0  0.2320 0.0000        
REMARK   3   159  2.6990 -  2.6930    0.95      522     0  0.2360 0.0000        
REMARK   3   160  2.6930 -  2.6880    0.95      539     0  0.2250 0.0000        
REMARK   3   161  2.6880 -  2.6820    0.95      500     0  0.2380 0.0000        
REMARK   3   162  2.6820 -  2.6770    0.95      544     0  0.2300 0.0000        
REMARK   3   163  2.6770 -  2.6710    0.92      473     0  0.2470 0.0000        
REMARK   3   164  2.6710 -  2.6660    0.95      494     0  0.2240 0.0000        
REMARK   3   165  2.6660 -  2.6600    0.96      483     0  0.2250 0.0000        
REMARK   3   166  2.6600 -  2.6550    0.94      486     0  0.2600 0.0000        
REMARK   3   167  2.6550 -  2.6500    0.96      539     0  0.2420 0.0000        
REMARK   3   168  2.6500 -  2.6450    0.94      528     0  0.2500 0.0000        
REMARK   3   169  2.6450 -  2.6390    0.96      524     0  0.2510 0.0000        
REMARK   3   170  2.6390 -  2.6340    0.96      539     0  0.2490 0.0000        
REMARK   3   171  2.6340 -  2.6290    0.97      510     0  0.2540 0.0000        
REMARK   3   172  2.6290 -  2.6240    0.93      496     0  0.2650 0.0000        
REMARK   3   173  2.6240 -  2.6190    0.96      485     0  0.2190 0.0000        
REMARK   3   174  2.6190 -  2.6140    0.94      537     0  0.2270 0.0000        
REMARK   3   175  2.6140 -  2.6090    0.96      513     0  0.2280 0.0000        
REMARK   3   176  2.6090 -  2.6040    0.95      487     0  0.2420 0.0000        
REMARK   3   177  2.6040 -  2.5990    0.91      506     0  0.2420 0.0000        
REMARK   3   178  2.5990 -  2.5940    0.97      498     0  0.2500 0.0000        
REMARK   3   179  2.5940 -  2.5890    0.95      530     0  0.2540 0.0000        
REMARK   3   180  2.5890 -  2.5840    0.96      519     0  0.2560 0.0000        
REMARK   3   181  2.5840 -  2.5800    0.96      482     0  0.2460 0.0000        
REMARK   3   182  2.5800 -  2.5750    0.96      520     0  0.2870 0.0000        
REMARK   3   183  2.5750 -  2.5700    0.92      515     0  0.2270 0.0000        
REMARK   3   184  2.5700 -  2.5660    0.95      530     0  0.2490 0.0000        
REMARK   3   185  2.5660 -  2.5610    0.96      481     0  0.2790 0.0000        
REMARK   3   186  2.5610 -  2.5560    0.97      547     0  0.2790 0.0000        
REMARK   3   187  2.5560 -  2.5520    0.97      531     0  0.2820 0.0000        
REMARK   3   188  2.5520 -  2.5470    0.94      485     0  0.2500 0.0000        
REMARK   3   189  2.5470 -  2.5430    0.95      500     0  0.2520 0.0000        
REMARK   3   190  2.5430 -  2.5380    0.94      523     0  0.2660 0.0000        
REMARK   3   191  2.5380 -  2.5340    0.96      486     0  0.2980 0.0000        
REMARK   3   192  2.5340 -  2.5300    0.93      527     0  0.2900 0.0000        
REMARK   3   193  2.5300 -  2.5250    0.95      482     0  0.2920 0.0000        
REMARK   3   194  2.5250 -  2.5210    0.93      532     0  0.2760 0.0000        
REMARK   3   195  2.5210 -  2.5160    0.97      517     0  0.2800 0.0000        
REMARK   3   196  2.5160 -  2.5120    0.95      516     0  0.2870 0.0000        
REMARK   3   197  2.5120 -  2.5080    0.95      464     0  0.3020 0.0000        
REMARK   3   198  2.5080 -  2.5040    0.97      537     0  0.2770 0.0000        
REMARK   3   199  2.5040 -  2.5000    0.96      479     0  0.2690 0.0000        
REMARK   3   200  2.5000 -  2.4950    0.95      549     0  0.3060 0.0000        
REMARK   3   201  2.4950 -  2.4910    0.95      529     0  0.3060 0.0000        
REMARK   3   202  2.4910 -  2.4870    0.94      498     0  0.2860 0.0000        
REMARK   3   203  2.4870 -  2.4830    0.94      516     0  0.3050 0.0000        
REMARK   3   204  2.4830 -  2.4790    0.96      542     0  0.3080 0.0000        
REMARK   3   205  2.4790 -  2.4750    0.96      494     0  0.2930 0.0000        
REMARK   3   206  2.4750 -  2.4710    0.95      485     0  0.2770 0.0000        
REMARK   3   207  2.4710 -  2.4670    0.95      555     0  0.2940 0.0000        
REMARK   3   208  2.4670 -  2.4630    0.93      512     0  0.3060 0.0000        
REMARK   3   209  2.4630 -  2.4590    0.93      439     0  0.2810 0.0000        
REMARK   3   210  2.4590 -  2.4550    0.96      497     0  0.3010 0.0000        
REMARK   3   211  2.4550 -  2.4510    0.93      502     0  0.3080 0.0000        
REMARK   3   212  2.4510 -  2.4470    0.96      529     0  0.3140 0.0000        
REMARK   3   213  2.4470 -  2.4440    0.94      482     0  0.3120 0.0000        
REMARK   3   214  2.4440 -  2.4400    0.95      520     0  0.3050 0.0000        
REMARK   3   215  2.4400 -  2.4360    0.95      562     0  0.2870 0.0000        
REMARK   3   216  2.4360 -  2.4320    0.91      473     0  0.3120 0.0000        
REMARK   3   217  2.4320 -  2.4280    0.93      509     0  0.3300 0.0000        
REMARK   3   218  2.4280 -  2.4250    0.95      522     0  0.3120 0.0000        
REMARK   3   219  2.4250 -  2.4210    0.94      496     0  0.3140 0.0000        
REMARK   3   220  2.4210 -  2.4170    0.92      482     0  0.2780 0.0000        
REMARK   3   221  2.4170 -  2.4140    0.93      439     0  0.3300 0.0000        
REMARK   3   222  2.4140 -  2.4100    0.91      540     0  0.3130 0.0000        
REMARK   3   223  2.4100 -  2.4070    0.91      493     0  0.3160 0.0000        
REMARK   3   224  2.4070 -  2.4030    0.82      432     0  0.3220 0.0000        
REMARK   3   225  2.4030 -  2.3990    0.75      422     0  0.3230 0.0000        
REMARK   3   226  2.3990 -  2.3960    0.57      321     0  0.2780 0.0000        
REMARK   3   227  2.3960 -  2.3920    0.38      199     0  0.3010 0.0000        
REMARK   3   228  2.3920 -  2.3890    0.32      157     0  0.2860 0.0000        
REMARK   3   229  2.3890 -  2.3850    0.25      127     0  0.2930 0.0000        
REMARK   3   230  2.3850 -  2.3820    0.16       81     0  0.2800 0.0000        
REMARK   3   231  2.3820 -  2.3780    0.08       42     0  0.3250 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : 0.41                                          
REMARK   3   B_SOL              : 56.07                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.06900                                             
REMARK   3    B22 (A**2) : -2.39700                                             
REMARK   3    B33 (A**2) : 5.46600                                              
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           NULL                                  
REMARK   3   ANGLE     :  0.698           NULL                                  
REMARK   3   CHIRALITY :  0.055           NULL                                  
REMARK   3   PLANARITY :  0.003           NULL                                  
REMARK   3   DIHEDRAL  : 11.535           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -30.0694  -3.6906  26.3361              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1788 T22:   0.2084                                     
REMARK   3      T33:   0.1504 T12:   0.0373                                     
REMARK   3      T13:   0.0100 T23:   0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2010 L22:   1.1587                                     
REMARK   3      L33:   0.6891 L12:  -0.1352                                     
REMARK   3      L13:  -0.0570 L23:   0.0276                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0436 S12:   0.0173 S13:  -0.0099                       
REMARK   3      S21:  -0.0213 S22:   0.0279 S23:   0.0192                       
REMARK   3      S31:  -0.0370 S32:  -0.0462 S33:   0.0099                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2949  -1.0544  26.6910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1152 T22:   0.1584                                     
REMARK   3      T33:   0.1288 T12:   0.0216                                     
REMARK   3      T13:   0.0063 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4464 L22:   1.1361                                     
REMARK   3      L33:   1.0521 L12:   0.1146                                     
REMARK   3      L13:  -0.0819 L23:  -0.2247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0151 S12:  -0.1210 S13:   0.0740                       
REMARK   3      S21:   0.0175 S22:   0.0036 S23:  -0.0112                       
REMARK   3      S31:   0.0375 S32:   0.0521 S33:   0.0083                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -24.9495 -25.3519  48.6636              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1754 T22:   0.0911                                     
REMARK   3      T33:   0.1922 T12:  -0.0124                                     
REMARK   3      T13:  -0.0606 T23:   0.1024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6152 L22:   1.6621                                     
REMARK   3      L33:   1.1867 L12:   0.1777                                     
REMARK   3      L13:  -0.5213 L23:   0.5151                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1106 S12:   0.0930 S13:   0.2360                       
REMARK   3      S21:   0.2642 S22:   0.0460 S23:  -0.1326                       
REMARK   3      S31:   0.0931 S32:   0.0438 S33:   0.0574                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -41.2100 -42.5081   9.0719              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4073 T22:   0.0733                                     
REMARK   3      T33:   0.3541 T12:  -0.0312                                     
REMARK   3      T13:  -0.0700 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1843 L22:   1.3182                                     
REMARK   3      L33:   1.3388 L12:   1.1671                                     
REMARK   3      L13:   1.0868 L23:   1.1331                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2542 S12:  -0.1235 S13:  -0.6314                       
REMARK   3      S21:   0.0865 S22:  -0.0593 S23:  -0.4675                       
REMARK   3      S31:   0.4114 S32:  -0.0350 S33:  -0.2007                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN E                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -28.7752  10.9352   4.5137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2753 T22:   0.3441                                     
REMARK   3      T33:   0.1846 T12:   0.0351                                     
REMARK   3      T13:   0.0364 T23:   0.0795                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0428 L22:   0.6600                                     
REMARK   3      L33:  -0.4804 L12:   0.7022                                     
REMARK   3      L13:   1.6268 L23:   0.2846                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0117 S12:   0.3086 S13:  -0.0338                       
REMARK   3      S21:   0.0226 S22:  -0.0010 S23:  -0.1529                       
REMARK   3      S31:  -0.0624 S32:   0.2594 S33:  -0.0496                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN F                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  12.0316 -11.6647   2.4936              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1237 T22:   0.5031                                     
REMARK   3      T33:   0.1277 T12:  -0.0200                                     
REMARK   3      T13:  -0.0112 T23:  -0.1112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.2007 L22:   0.5649                                     
REMARK   3      L33:   3.0679 L12:   0.2304                                     
REMARK   3      L13:  -1.1112 L23:  -1.1518                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0514 S12:   0.2152 S13:  -0.0334                       
REMARK   3      S21:   0.0137 S22:   0.1210 S23:   0.2044                       
REMARK   3      S31:  -0.3073 S32:  -0.7061 S33:  -0.0236                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN G                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -28.7875 -42.4682  67.7881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2841 T22:   0.3202                                     
REMARK   3      T33:   0.1870 T12:  -0.0289                                     
REMARK   3      T13:  -0.0506 T23:   0.1685                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0410 L22:   0.1859                                     
REMARK   3      L33:   6.9850 L12:   0.5649                                     
REMARK   3      L13:   0.3992 L23:  -0.0947                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1535 S12:  -0.3814 S13:  -0.1157                       
REMARK   3      S21:   0.2318 S22:  -0.4358 S23:  -0.3430                       
REMARK   3      S31:  -0.6643 S32:  -0.1350 S33:   0.2336                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN H                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -45.5267 -21.4843  -5.4044              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4136 T22:   0.2496                                     
REMARK   3      T33:   0.2588 T12:  -0.0812                                     
REMARK   3      T13:  -0.0202 T23:   0.1191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3115 L22:   0.0222                                     
REMARK   3      L33:   0.4802 L12:   0.0969                                     
REMARK   3      L13:   0.1912 L23:   1.0910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0501 S12:   0.0398 S13:  -0.0895                       
REMARK   3      S21:  -0.0488 S22:   0.2659 S23:   0.1166                       
REMARK   3      S31:   0.4445 S32:  -0.2649 S33:  -0.0703                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3L3T COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB056797.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63709                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.378                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.516                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 13.200                             
REMARK 200  R MERGE                    (I) : 0.16200                            
REMARK 200  R SYM                      (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.38                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.01277                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4M SODIUM FORMATE SOLUTION, VAPOR        
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   X,-Y,-Z                                                 
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   -X,-Y+1/2,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.03350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.16900            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       65.03350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       66.16900            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   62   CZ   NH1  NH2                                       
REMARK 480     LYS A   74   NZ                                                  
REMARK 480     ARG A   96   CZ   NH1  NH2                                       
REMARK 480     LYS A  175   NZ                                                  
REMARK 480     ASN B   25   CG   OD1  ND2                                       
REMARK 480     LEU B   76   CD2                                                 
REMARK 480     ARG B   96   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     SER B  246   C    O    OXT                                       
REMARK 480     LYS C   74   CE   NZ                                             
REMARK 480     ALA D   86   CB                                                  
REMARK 480     LYS D   87   CD   CE   NZ                                        
REMARK 480     LYS D   93   CE   NZ                                             
REMARK 480     LYS D  222   NZ                                                  
REMARK 480     LYS D  239   NZ                                                  
REMARK 480     ARG H   42   CD                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  25      -92.18    -59.90                                   
REMARK 500    SER A  26      -82.97     57.76                                   
REMARK 500    LEU A  27       71.71   -116.87                                   
REMARK 500    SER A  37      -99.30   -100.78                                   
REMARK 500    GLU A  49      -36.06    -30.86                                   
REMARK 500    HIS A  71      -54.72   -123.93                                   
REMARK 500    ASN A 115     -155.28   -147.64                                   
REMARK 500    ASP A 150       89.93   -150.92                                   
REMARK 500    ARG A 193       -3.11     81.29                                   
REMARK 500    SER A 214      -76.08   -123.07                                   
REMARK 500    SER B  37      -85.45    -93.53                                   
REMARK 500    ASN B 115     -154.86   -158.02                                   
REMARK 500    ARG B 193       -2.12     86.06                                   
REMARK 500    SER B 214      -78.70   -119.18                                   
REMARK 500    LEU C  27       74.22   -118.96                                   
REMARK 500    SER C  37      -58.17   -134.99                                   
REMARK 500    SER C  39      123.53     91.90                                   
REMARK 500    HIS C  71      -57.95   -124.74                                   
REMARK 500    ARG C 193       -8.59     96.96                                   
REMARK 500    SER C 214      -75.97   -119.81                                   
REMARK 500    ASN C 223       19.82     58.15                                   
REMARK 500    ASN D  25       35.98   -160.94                                   
REMARK 500    SER D  37      -84.30   -106.72                                   
REMARK 500    HIS D  71      -47.86   -130.29                                   
REMARK 500    LEU D  76     -152.50    -71.69                                   
REMARK 500    ASN D  79      -32.57     80.92                                   
REMARK 500    ASN D 115     -155.46   -160.84                                   
REMARK 500    ASP D 150       81.85   -154.26                                   
REMARK 500    ARG D 193       -5.19     84.48                                   
REMARK 500    SER D 214      -76.47   -121.64                                   
REMARK 500    ALA D 244        4.22    -67.94                                   
REMARK 500    ASN E  44      101.07   -162.24                                   
REMARK 500    SER E  57     -129.03     76.95                                   
REMARK 500    ALA E  58       58.39   -159.76                                   
REMARK 500    VAL G   4      -71.91     39.56                                   
REMARK 500    GLU H  49     -176.87    -68.24                                   
REMARK 500    TYR H  50      -60.31     59.44                                   
REMARK 500    SER H  57      -10.89    -41.75                                   
REMARK 500    ALA H  58       98.85    -49.05                                   
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    ASN D  79        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 250  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 VAL A  75   O   158.8                                              
REMARK 620 3 ASN A  72   O    91.8  74.6                                        
REMARK 620 4 GLU A  77   OE1  97.6  97.6  86.2                                  
REMARK 620 5 GLU A  80   OE2 104.3  91.9 162.0  83.9                            
REMARK 620 6 HOH A 269   O    78.9  89.4 106.6 166.7  84.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  72   O                                                      
REMARK 620 2 VAL B  75   O    72.3                                              
REMARK 620 3 GLU B  70   OE2 133.0 137.4                                        
REMARK 620 4 GLU B  77   OE1  93.7 100.8 109.0                                  
REMARK 620 5 GLU B  80   OE2 158.9  86.7  62.8  92.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D   4  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  80   OE2                                                    
REMARK 620 2 HOH D 267   O   124.9                                              
REMARK 620 3 ASN D  72   O   101.6 127.8                                        
REMARK 620 4 GLU D  70   OE1 124.9  64.6 109.3                                  
REMARK 620 5 VAL D  75   O    67.7 115.4  58.6 165.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C   3  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 289   O                                                      
REMARK 620 2 ASN C  72   O   118.9                                              
REMARK 620 3 GLU C  77   OE1 153.9  53.9                                        
REMARK 620 4 GLU C  80   OE2 116.2 103.1  52.6                                  
REMARK 620 5 VAL C  75   O   100.6  60.5  53.3  60.3                            
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 FMT A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 250                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 4                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R9P   RELATED DB: PDB                                   
REMARK 900 HUMAN MESOTRYPSIN                                                    
REMARK 900 RELATED ID: 1ZJD   RELATED DB: PDB                                   
REMARK 900 KUNITZ PROTEASE INHIBITOR DOMAIN                                     
DBREF  3L3T A   16   246  UNP    Q8N2U3   Q8N2U3_HUMAN    28    251             
DBREF  3L3T B   16   246  UNP    Q8N2U3   Q8N2U3_HUMAN    28    251             
DBREF  3L3T C   16   246  UNP    Q8N2U3   Q8N2U3_HUMAN    28    251             
DBREF  3L3T D   16   246  UNP    Q8N2U3   Q8N2U3_HUMAN    28    251             
DBREF  3L3T E    3    59  UNP    C9JHU0   C9JHU0_HUMAN   211    267             
DBREF  3L3T F    3    59  UNP    C9JHU0   C9JHU0_HUMAN   211    267             
DBREF  3L3T G    3    59  UNP    C9JHU0   C9JHU0_HUMAN   211    267             
DBREF  3L3T H    3    59  UNP    C9JHU0   C9JHU0_HUMAN   211    267             
SEQADV 3L3T ALA A  195  UNP  Q8N2U3    SER   204 ENGINEERED MUTATION            
SEQADV 3L3T ALA B  195  UNP  Q8N2U3    SER   204 ENGINEERED MUTATION            
SEQADV 3L3T ALA C  195  UNP  Q8N2U3    SER   204 ENGINEERED MUTATION            
SEQADV 3L3T ALA D  195  UNP  Q8N2U3    SER   204 ENGINEERED MUTATION            
SEQADV 3L3T LYS E   15  UNP  C9JHU0    ARG   223 ENGINEERED MUTATION            
SEQADV 3L3T LYS F   15  UNP  C9JHU0    ARG   223 ENGINEERED MUTATION            
SEQADV 3L3T LYS G   15  UNP  C9JHU0    ARG   223 ENGINEERED MUTATION            
SEQADV 3L3T LYS H   15  UNP  C9JHU0    ARG   223 ENGINEERED MUTATION            
SEQRES   1 A  224  ILE VAL GLY GLY TYR THR CYS GLU GLU ASN SER LEU PRO          
SEQRES   2 A  224  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  224  GLY SER LEU ILE SER GLU GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  224  HIS CYS TYR LYS THR ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  224  HIS ASN ILE LYS VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO LYS TYR ASN ARG          
SEQRES   7 A  224  ASP THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  224  SER PRO ALA VAL ILE ASN ALA ARG VAL SER THR ILE SER          
SEQRES   9 A  224  LEU PRO THR ALA PRO PRO ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  224  ILE SER GLY TRP GLY ASN THR LEU SER PHE GLY ALA ASP          
SEQRES  11 A  224  TYR PRO ASP GLU LEU LYS CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 A  224  THR GLN ALA GLU CYS LYS ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 A  224  THR ASN SER MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  224  LYS ASP SER CYS GLN ARG ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 A  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY HIS          
SEQRES  16 A  224  GLY CYS ALA TRP LYS ASN ARG PRO GLY VAL TYR THR LYS          
SEQRES  17 A  224  VAL TYR ASN TYR VAL ASP TRP ILE LYS ASP THR ILE ALA          
SEQRES  18 A  224  ALA ASN SER                                                  
SEQRES   1 B  224  ILE VAL GLY GLY TYR THR CYS GLU GLU ASN SER LEU PRO          
SEQRES   2 B  224  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 B  224  GLY SER LEU ILE SER GLU GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  224  HIS CYS TYR LYS THR ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  224  HIS ASN ILE LYS VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO LYS TYR ASN ARG          
SEQRES   7 B  224  ASP THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  224  SER PRO ALA VAL ILE ASN ALA ARG VAL SER THR ILE SER          
SEQRES   9 B  224  LEU PRO THR ALA PRO PRO ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 B  224  ILE SER GLY TRP GLY ASN THR LEU SER PHE GLY ALA ASP          
SEQRES  11 B  224  TYR PRO ASP GLU LEU LYS CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 B  224  THR GLN ALA GLU CYS LYS ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 B  224  THR ASN SER MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  224  LYS ASP SER CYS GLN ARG ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 B  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY HIS          
SEQRES  16 B  224  GLY CYS ALA TRP LYS ASN ARG PRO GLY VAL TYR THR LYS          
SEQRES  17 B  224  VAL TYR ASN TYR VAL ASP TRP ILE LYS ASP THR ILE ALA          
SEQRES  18 B  224  ALA ASN SER                                                  
SEQRES   1 C  224  ILE VAL GLY GLY TYR THR CYS GLU GLU ASN SER LEU PRO          
SEQRES   2 C  224  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 C  224  GLY SER LEU ILE SER GLU GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 C  224  HIS CYS TYR LYS THR ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 C  224  HIS ASN ILE LYS VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 C  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO LYS TYR ASN ARG          
SEQRES   7 C  224  ASP THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 C  224  SER PRO ALA VAL ILE ASN ALA ARG VAL SER THR ILE SER          
SEQRES   9 C  224  LEU PRO THR ALA PRO PRO ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 C  224  ILE SER GLY TRP GLY ASN THR LEU SER PHE GLY ALA ASP          
SEQRES  11 C  224  TYR PRO ASP GLU LEU LYS CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 C  224  THR GLN ALA GLU CYS LYS ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 C  224  THR ASN SER MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 C  224  LYS ASP SER CYS GLN ARG ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 C  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY HIS          
SEQRES  16 C  224  GLY CYS ALA TRP LYS ASN ARG PRO GLY VAL TYR THR LYS          
SEQRES  17 C  224  VAL TYR ASN TYR VAL ASP TRP ILE LYS ASP THR ILE ALA          
SEQRES  18 C  224  ALA ASN SER                                                  
SEQRES   1 D  224  ILE VAL GLY GLY TYR THR CYS GLU GLU ASN SER LEU PRO          
SEQRES   2 D  224  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 D  224  GLY SER LEU ILE SER GLU GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 D  224  HIS CYS TYR LYS THR ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 D  224  HIS ASN ILE LYS VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 D  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO LYS TYR ASN ARG          
SEQRES   7 D  224  ASP THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 D  224  SER PRO ALA VAL ILE ASN ALA ARG VAL SER THR ILE SER          
SEQRES   9 D  224  LEU PRO THR ALA PRO PRO ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 D  224  ILE SER GLY TRP GLY ASN THR LEU SER PHE GLY ALA ASP          
SEQRES  11 D  224  TYR PRO ASP GLU LEU LYS CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 D  224  THR GLN ALA GLU CYS LYS ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 D  224  THR ASN SER MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 D  224  LYS ASP SER CYS GLN ARG ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 D  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY HIS          
SEQRES  16 D  224  GLY CYS ALA TRP LYS ASN ARG PRO GLY VAL TYR THR LYS          
SEQRES  17 D  224  VAL TYR ASN TYR VAL ASP TRP ILE LYS ASP THR ILE ALA          
SEQRES  18 D  224  ALA ASN SER                                                  
SEQRES   1 E   57  GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO CYS LYS          
SEQRES   2 E   57  ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR GLU GLY          
SEQRES   3 E   57  LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY GLY ASN          
SEQRES   4 E   57  ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET ALA VAL          
SEQRES   5 E   57  CYS GLY SER ALA ILE                                          
SEQRES   1 F   57  GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO CYS LYS          
SEQRES   2 F   57  ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR GLU GLY          
SEQRES   3 F   57  LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY GLY ASN          
SEQRES   4 F   57  ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET ALA VAL          
SEQRES   5 F   57  CYS GLY SER ALA ILE                                          
SEQRES   1 G   57  GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO CYS LYS          
SEQRES   2 G   57  ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR GLU GLY          
SEQRES   3 G   57  LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY GLY ASN          
SEQRES   4 G   57  ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET ALA VAL          
SEQRES   5 G   57  CYS GLY SER ALA ILE                                          
SEQRES   1 H   57  GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO CYS LYS          
SEQRES   2 H   57  ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR GLU GLY          
SEQRES   3 H   57  LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY GLY ASN          
SEQRES   4 H   57  ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET ALA VAL          
SEQRES   5 H   57  CYS GLY SER ALA ILE                                          
HET    FMT  A   1       3                                                       
HET    FMT  A   2       3                                                       
HET    FMT  A   4       3                                                       
HET    FMT  A 247       3                                                       
HET    FMT  A 248       3                                                       
HET    FMT  A 249       3                                                       
HET    FMT  A  13       3                                                       
HET     CA  A 250       1                                                       
HET    FMT  B   3       3                                                       
HET    FMT  B   6       3                                                       
HET    FMT  B  10       3                                                       
HET    FMT  B  11       3                                                       
HET    FMT  B  12       3                                                       
HET     CA  B   1       1                                                       
HET    FMT  C 247       3                                                       
HET     CA  C   3       1                                                       
HET     CA  D   4       1                                                       
HETNAM     FMT FORMIC ACID                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   9  FMT    13(C H2 O2)                                                  
FORMUL  16   CA    4(CA 2+)                                                     
FORMUL  26  HOH   *345(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 THR A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
HELIX    4   4 ALA B   55  TYR B   59  5                                   5    
HELIX    5   5 THR B  164  TYR B  172  1                                   9    
HELIX    6   6 TYR B  234  ASN B  245  1                                  12    
HELIX    7   7 ALA C   55  TYR C   59  5                                   5    
HELIX    8   8 THR C  164  TYR C  172  1                                   9    
HELIX    9   9 TYR C  234  ASN C  245  1                                  12    
HELIX   10  10 ALA D   55  TYR D   59  5                                   5    
HELIX   11  11 THR D  164  TYR D  172  1                                   9    
HELIX   12  12 TYR D  234  ALA D  244  1                                  11    
HELIX   13  13 ASN D  245  SER D  246  5                                   2    
HELIX   14  14 GLU E    3  GLU E    7  5                                   5    
HELIX   15  15 THR E   47  CYS E   55  1                                   9    
HELIX   16  16 THR F   47  GLY F   56  1                                  10    
HELIX   17  17 GLU G    3  GLU G    7  5                                   5    
HELIX   18  18 THR G   47  GLY G   56  1                                  10    
HELIX   19  19 THR H   47  GLY H   56  1                                  10    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 LYS A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLU A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  TRP A 215 -1  O  GLN A 210   N  VAL A 199           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  PHE A 181   O  TYR A 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  SER A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   B 7 GLN A  81  ARG A  90 -1                                        
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  VAL A  65   O  ILE A  83           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    1   C 7 TYR B  20  THR B  21  0                                        
SHEET    2   C 7 LYS B 156  PRO B 161 -1  O  CYS B 157   N  TYR B  20           
SHEET    3   C 7 GLU B 135  GLY B 140 -1  N  CYS B 136   O  ALA B 160           
SHEET    4   C 7 PRO B 198  VAL B 200 -1  O  VAL B 200   N  LEU B 137           
SHEET    5   C 7 LEU B 209  TRP B 215 -1  O  GLN B 210   N  VAL B 199           
SHEET    6   C 7 GLY B 226  LYS B 230 -1  O  VAL B 227   N  TRP B 215           
SHEET    7   C 7 MET B 180  VAL B 183 -1  N  PHE B 181   O  TYR B 228           
SHEET    1   D 7 GLN B  30  ASN B  34  0                                        
SHEET    2   D 7 HIS B  40  SER B  48 -1  O  CYS B  42   N  LEU B  33           
SHEET    3   D 7 TRP B  51  SER B  54 -1  O  VAL B  53   N  SER B  45           
SHEET    4   D 7 MET B 104  LEU B 108 -1  O  ILE B 106   N  VAL B  52           
SHEET    5   D 7 GLN B  81  ARG B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    6   D 7 GLN B  64  LEU B  67 -1  N  VAL B  65   O  ILE B  83           
SHEET    7   D 7 GLN B  30  ASN B  34 -1  N  SER B  32   O  ARG B  66           
SHEET    1   E 7 TYR C  20  THR C  21  0                                        
SHEET    2   E 7 LYS C 156  PRO C 161 -1  O  CYS C 157   N  TYR C  20           
SHEET    3   E 7 GLU C 135  GLY C 140 -1  N  ILE C 138   O  LEU C 158           
SHEET    4   E 7 PRO C 198  CYS C 201 -1  O  VAL C 200   N  LEU C 137           
SHEET    5   E 7 GLN C 204  TRP C 215 -1  O  GLN C 210   N  VAL C 199           
SHEET    6   E 7 GLY C 226  LYS C 230 -1  O  VAL C 227   N  TRP C 215           
SHEET    7   E 7 MET C 180  VAL C 183 -1  N  PHE C 181   O  TYR C 228           
SHEET    1   F 7 GLN C  30  ASN C  34  0                                        
SHEET    2   F 7 HIS C  40  LEU C  46 -1  O  GLY C  44   N  VAL C  31           
SHEET    3   F 7 TRP C  51  SER C  54 -1  O  VAL C  53   N  SER C  45           
SHEET    4   F 7 MET C 104  LEU C 108 -1  O  MET C 104   N  SER C  54           
SHEET    5   F 7 GLN C  81  ARG C  90 -1  N  ILE C  89   O  LEU C 105           
SHEET    6   F 7 GLN C  64  LEU C  67 -1  N  VAL C  65   O  ILE C  83           
SHEET    7   F 7 GLN C  30  ASN C  34 -1  N  ASN C  34   O  GLN C  64           
SHEET    1   G 7 TYR D  20  THR D  21  0                                        
SHEET    2   G 7 LYS D 156  PRO D 161 -1  O  CYS D 157   N  TYR D  20           
SHEET    3   G 7 GLU D 135  GLY D 140 -1  N  ILE D 138   O  LEU D 158           
SHEET    4   G 7 PRO D 198  CYS D 201 -1  O  VAL D 200   N  LEU D 137           
SHEET    5   G 7 GLN D 204  TRP D 215 -1  O  GLN D 204   N  CYS D 201           
SHEET    6   G 7 GLY D 226  LYS D 230 -1  O  VAL D 227   N  TRP D 215           
SHEET    7   G 7 MET D 180  VAL D 183 -1  N  PHE D 181   O  TYR D 228           
SHEET    1   H 7 GLN D  30  ASN D  34  0                                        
SHEET    2   H 7 HIS D  40  LEU D  46 -1  O  CYS D  42   N  LEU D  33           
SHEET    3   H 7 TRP D  51  SER D  54 -1  O  VAL D  53   N  SER D  45           
SHEET    4   H 7 MET D 104  LEU D 108 -1  O  MET D 104   N  SER D  54           
SHEET    5   H 7 GLN D  81  ARG D  90 -1  N  ILE D  89   O  LEU D 105           
SHEET    6   H 7 GLN D  64  LEU D  67 -1  N  VAL D  65   O  ILE D  83           
SHEET    7   H 7 GLN D  30  ASN D  34 -1  N  SER D  32   O  ARG D  66           
SHEET    1   I 2 ILE E  18  ASP E  24  0                                        
SHEET    2   I 2 LYS E  29  TYR E  35 -1  O  TYR E  35   N  ILE E  18           
SHEET    1   J 2 ILE F  18  ASP F  24  0                                        
SHEET    2   J 2 LYS F  29  TYR F  35 -1  O  TYR F  35   N  ILE F  18           
SHEET    1   K 2 ILE G  18  ASP G  24  0                                        
SHEET    2   K 2 LYS G  29  TYR G  35 -1  O  ALA G  31   N  TYR G  22           
SHEET    1   L 2 ILE H  18  ASP H  24  0                                        
SHEET    2   L 2 LYS H  29  TYR H  35 -1  O  TYR H  35   N  ILE H  18           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.04  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.05  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.06  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.07  
SSBOND   6 CYS B   22    CYS B  157                          1555   1555  2.05  
SSBOND   7 CYS B   42    CYS B   58                          1555   1555  2.04  
SSBOND   8 CYS B  136    CYS B  201                          1555   1555  2.04  
SSBOND   9 CYS B  168    CYS B  182                          1555   1555  2.06  
SSBOND  10 CYS B  191    CYS B  220                          1555   1555  2.06  
SSBOND  11 CYS C   22    CYS C  157                          1555   1555  2.04  
SSBOND  12 CYS C   42    CYS C   58                          1555   1555  2.04  
SSBOND  13 CYS C  136    CYS C  201                          1555   1555  2.04  
SSBOND  14 CYS C  168    CYS C  182                          1555   1555  2.05  
SSBOND  15 CYS C  191    CYS C  220                          1555   1555  2.05  
SSBOND  16 CYS D   22    CYS D  157                          1555   1555  2.03  
SSBOND  17 CYS D   42    CYS D   58                          1555   1555  2.03  
SSBOND  18 CYS D  136    CYS D  201                          1555   1555  2.04  
SSBOND  19 CYS D  168    CYS D  182                          1555   1555  2.04  
SSBOND  20 CYS D  191    CYS D  220                          1555   1555  2.05  
SSBOND  21 CYS E    5    CYS E   55                          1555   1555  2.04  
SSBOND  22 CYS E   14    CYS E   38                          1555   1555  2.03  
SSBOND  23 CYS E   30    CYS E   51                          1555   1555  2.04  
SSBOND  24 CYS F    5    CYS F   55                          1555   1555  2.03  
SSBOND  25 CYS F   14    CYS F   38                          1555   1555  2.04  
SSBOND  26 CYS F   30    CYS F   51                          1555   1555  2.03  
SSBOND  27 CYS G    5    CYS G   55                          1555   1555  2.04  
SSBOND  28 CYS G   14    CYS G   38                          1555   1555  2.05  
SSBOND  29 CYS G   30    CYS G   51                          1555   1555  2.04  
SSBOND  30 CYS H    5    CYS H   55                          1555   1555  2.04  
SSBOND  31 CYS H   14    CYS H   38                          1555   1555  2.06  
SSBOND  32 CYS H   30    CYS H   51                          1555   1555  2.04  
LINK         OE1 GLU A  70                CA    CA A 250     1555   1555  2.46  
LINK         O   VAL A  75                CA    CA A 250     1555   1555  2.46  
LINK         O   ASN B  72                CA    CA B   1     1555   1555  2.66  
LINK         O   VAL B  75                CA    CA B   1     1555   1555  2.66  
LINK         O   ASN A  72                CA    CA A 250     1555   1555  2.69  
LINK         OE1 GLU A  77                CA    CA A 250     1555   1555  2.72  
LINK         OE2 GLU D  80                CA    CA D   4     1555   1555  2.73  
LINK         OE2 GLU A  80                CA    CA A 250     1555   1555  2.75  
LINK        CA    CA D   4                 O   HOH D 267     1555   1555  2.76  
LINK        CA    CA C   3                 O   HOH C 289     1555   1555  2.80  
LINK         OE2 GLU B  70                CA    CA B   1     1555   1555  2.87  
LINK         OE1 GLU B  77                CA    CA B   1     1555   1555  2.87  
LINK         O   ASN D  72                CA    CA D   4     1555   1555  2.88  
LINK         OE1 GLU D  70                CA    CA D   4     1555   1555  2.88  
LINK        CA    CA A 250                 O   HOH A 269     1555   1555  2.94  
LINK         OE2 GLU B  80                CA    CA B   1     1555   1555  2.94  
LINK         O   VAL D  75                CA    CA D   4     1555   1555  2.95  
LINK         O   ASN C  72                CA    CA C   3     1555   1555  3.06  
LINK         OE1 GLU C  77                CA    CA C   3     1555   1555  3.11  
LINK         OE2 GLU C  80                CA    CA C   3     1555   1555  3.16  
LINK         O   VAL C  75                CA    CA C   3     1555   1555  3.19  
CISPEP   1 GLY C   38    SER C   39          0         0.55                     
CISPEP   2 LEU D   76    GLU D   77          0        -4.53                     
CISPEP   3 GLY D   78    ASN D   79          0        -1.79                     
CISPEP   4 ALA F   58    ILE F   59          0        -2.56                     
SITE     1 AC1  2 LEU A 163  HOH A 300                                          
SITE     1 AC2  4 ARG A  66  ILE A  73  HOH A 269  HOH A 341                    
SITE     1 AC3  2 PRO B 129  LEU B 163                                          
SITE     1 AC4  5 ASN A 233  TYR A 234  VAL A 235  ASP A 236                    
SITE     2 AC4  5 TRP A 237                                                     
SITE     1 AC5  4 ALA A 221  TRP A 221A LYS A 222  HOH A 327                    
SITE     1 AC6  6 SER A 119  THR A 120  HOH A 205  HOH A 301                    
SITE     2 AC6  6 SER C 122  GLY C 203                                          
SITE     1 AC7  2 PRO C 129  LYS C 230                                          
SITE     1 AC8  2 SER B 171  ASN B 223                                          
SITE     1 AC9  3 HIS B  91  LYS B  93  GLY C 174                               
SITE     1 BC1  2 THR A 164  THR B 164                                          
SITE     1 BC2  1 GLY A 219                                                     
SITE     1 BC3  5 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 BC3  5 GLU B  80                                                     
SITE     1 BC4  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 BC4  6 GLU A  80  HOH A 269                                          
SITE     1 BC5  6 GLU C  70  ASN C  72  VAL C  75  GLU C  77                    
SITE     2 BC5  6 GLU C  80  HOH C 289                                          
SITE     1 BC6  5 GLU D  70  ASN D  72  VAL D  75  GLU D  80                    
SITE     2 BC6  5 HOH D 267                                                     
CRYST1   92.793  130.067  132.338  90.00  90.00  90.00 P 2 21 21    16          
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      0.010777  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007688  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007556        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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