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Database: PDB
Entry: 5HD6
LinkDB: 5HD6
Original site: 5HD6 
HEADER    LYASE                                   04-JAN-16   5HD6              
TITLE     HIGH RESOLUTION STRUCTURE OF 3-HYDROXYDECANOYL-(ACYL CARRIER PROTEIN) 
TITLE    2 DEHYDRATASE FROM YERSINIA PESTIS AT 1.35 A                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 3-HYDROXYDECANOYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE;      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: 3-HYDROXYACYL-[ACYL-CARRIER-PROTEIN] DEHYDRATASE FABA,BETA- 
COMPND   5 HYDROXYDECANOYL THIOESTER DEHYDRASE,TRANS-2-DECENOYL-[ACYL-CARRIER-  
COMPND   6 PROTEIN] ISOMERASE;                                                  
COMPND   7 EC: 4.2.1.59;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS CO92;                           
SOURCE   3 ORGANISM_TAXID: 214092;                                              
SOURCE   4 GENE: FABA, AK38_1122;                                               
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, MIDWEST CENTER FOR STRUCTURAL       
KEYWDS   2 GENOMICS, MCSG, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS         
KEYWDS   3 DISEASES, CSGID, LYASE                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHANG,N.MALTSEVA,Y.KIM,R.MULLIGAN,K.KWON,W.F.ANDERSON,A.JOACHIMIAK, 
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)        
REVDAT   1   20-JAN-16 5HD6    0                                                
JRNL        AUTH   C.CHANG,N.MALTSEVA,Y.KIM,R.MULLIGAN,K.KWON,W.F.ANDERSON,     
JRNL        AUTH 2 A.JOACHIMIAK,                                                
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   HIGH RESOLUTION STRUCTURE OF 3-HYDROXYDECANOYL-(ACYL CARRIER 
JRNL        TITL 2 PROTEIN) DEHYDRATASE FROM YERSINIA PESTIS AT 1.35 A          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.35 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10_2155                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.970                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 241904                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.138                           
REMARK   3   R VALUE            (WORKING SET) : 0.136                           
REMARK   3   FREE R VALUE                     : 0.170                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 21576                           
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 26.9200 -  4.1900    0.94    15402   725  0.1482 0.1509        
REMARK   3     2  4.1900 -  3.3277    0.95    15490   683  0.1238 0.1434        
REMARK   3     3  3.3277 -  2.9076    0.93    15127   772  0.1416 0.1707        
REMARK   3     4  2.9076 -  2.6420    0.93    15095   818  0.1554 0.2003        
REMARK   3     5  2.6420 -  2.4528    0.93    15079   741  0.1535 0.1743        
REMARK   3     6  2.4528 -  2.3083    0.92    14939   720  0.1356 0.1622        
REMARK   3     7  2.3083 -  2.1927    0.92    14875   871  0.1241 0.1604        
REMARK   3     8  2.1927 -  2.0973    0.91    14856   773  0.1217 0.1505        
REMARK   3     9  2.0973 -  2.0166    0.91    14606   728  0.1250 0.1570        
REMARK   3    10  2.0166 -  1.9470    0.90    14574   731  0.1241 0.1632        
REMARK   3    11  1.9470 -  1.8862    0.90    14692   797  0.1180 0.1566        
REMARK   3    12  1.8862 -  1.8323    0.89    14458   702  0.1177 0.1468        
REMARK   3    13  1.8323 -  1.7840    0.89    14569   695  0.1262 0.1698        
REMARK   3    14  1.7840 -  1.7405    0.88    14304   752  0.1198 0.1631        
REMARK   3    15  1.7405 -  1.7010    0.88    13984   887  0.1201 0.1754        
REMARK   3    16  1.7010 -  1.6648    0.88    14512   749  0.1214 0.1715        
REMARK   3    17  1.6648 -  1.6315    0.87    13923   802  0.1302 0.1882        
REMARK   3    18  1.6315 -  1.6007    0.87    14140   793  0.1353 0.1788        
REMARK   3    19  1.6007 -  1.5721    0.87    13873   839  0.1324 0.1765        
REMARK   3    20  1.5721 -  1.5455    0.86    14216   626  0.1254 0.1738        
REMARK   3    21  1.5455 -  1.5205    0.86    13981   687  0.1322 0.1845        
REMARK   3    22  1.5205 -  1.4971    0.86    13810   741  0.1370 0.1811        
REMARK   3    23  1.4971 -  1.4751    0.85    13884   635  0.1459 0.2067        
REMARK   3    24  1.4751 -  1.4543    0.85    13941   614  0.1539 0.2210        
REMARK   3    25  1.4543 -  1.4347    0.85    13746   756  0.1618 0.2114        
REMARK   3    26  1.4347 -  1.4161    0.84    13617   647  0.1644 0.2124        
REMARK   3    27  1.4161 -  1.3984    0.78    12805   661  0.1703 0.2337        
REMARK   3    28  1.3984 -  1.3815    0.74    11793   646  0.1798 0.2367        
REMARK   3    29  1.3815 -  1.3655    0.67    10943   512  0.1867 0.2507        
REMARK   3    30  1.3655 -  1.3501    0.55     8959   473  0.2008 0.2581        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.72                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.007          11401                                  
REMARK   3   ANGLE     :  0.877          15370                                  
REMARK   3   CHIRALITY :  0.084           1600                                  
REMARK   3   PLANARITY :  0.005           2006                                  
REMARK   3   DIHEDRAL  : 19.619           4266                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5HD6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216593.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 241931                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.350                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.04200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 3Q62                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.16 M MAGNESIUM CHLORIDE, 0.08 M TRIS   
REMARK 280  -HCL, 24 % PEG 4000, 20 % GLYCEROL, PH 8.5, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 297K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 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: 4140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: 4380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 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: 4570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER E    -2                                                      
REMARK 465     ASN E    -1                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     ASN F    -1                                                      
REMARK 465     ALA F     0                                                      
REMARK 465     MSE F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     ASN F   170                                                      
REMARK 465     ALA F   171                                                      
REMARK 465     SER G    -2                                                      
REMARK 465     ASN G    -1                                                      
REMARK 465     ALA G     0                                                      
REMARK 465     MSE G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     ASN G   170                                                      
REMARK 465     ALA G   171                                                      
REMARK 465     SER H    -2                                                      
REMARK 465     ASN H    -1                                                      
REMARK 465     ALA H   171                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     VAL H   2    CG1  CG2                                            
REMARK 470     ASN H 170    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OH   TYR C   156     O    HOH C   301              1.98            
REMARK 500   O    HOH B   337     O    HOH B   455              2.12            
REMARK 500   O    PHE G    22     O    HOH G   301              2.13            
REMARK 500   O    PHE E    22     O    HOH E   301              2.14            
REMARK 500   OG1  THR G   169     O    HOH G   302              2.15            
REMARK 500   OD2  ASP D   168     O    HOH D   301              2.16            
REMARK 500   O    HOH G   349     O    HOH G   386              2.19            
REMARK 500   OE2  GLU C    20     O    HOH C   302              2.19            
REMARK 500   O    HOH G   397     O    HOH G   420              2.19            
REMARK 500   O    HOH G   322     O    HOH G   445              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU H    11     C3   GOL D   201     1655     1.37            
REMARK 500   OE2  GLU H    11     O3   GOL D   201     1655     1.89            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  75       67.97   -161.58                                   
REMARK 500    ARG A 137     -142.53   -130.21                                   
REMARK 500    ARG A 137     -142.03   -130.21                                   
REMARK 500    ASP B  75       68.61   -161.59                                   
REMARK 500    ARG B 137     -141.63   -130.82                                   
REMARK 500    ASP C  75       68.87   -160.30                                   
REMARK 500    ARG C 137     -141.43   -129.88                                   
REMARK 500    ASP D  75       69.17   -161.20                                   
REMARK 500    ARG D 137     -138.77   -128.96                                   
REMARK 500    PHE E  22     -158.59    -92.04                                   
REMARK 500    ASP E  75       67.27   -159.51                                   
REMARK 500    ARG E 137     -165.87   -121.30                                   
REMARK 500    ASN E 170       -2.85   -156.66                                   
REMARK 500    ASP F  75       68.05   -158.99                                   
REMARK 500    ARG F 137     -165.97   -121.86                                   
REMARK 500    PHE G  22     -159.96    -91.06                                   
REMARK 500    ASP G  75       67.76   -160.89                                   
REMARK 500    ARG G 137     -165.16   -122.79                                   
REMARK 500    ASP H  75       68.00   -159.20                                   
REMARK 500    ARG H 137     -165.77   -119.89                                   
REMARK 500    ARG H 137     -165.77   -122.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 497        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH H 488        DISTANCE =  5.90 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 203                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP90513   RELATED DB: TARGETTRACK                 
DBREF1 5HD6 A    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 A     A0A0B6NZG1                          1         172             
DBREF1 5HD6 B    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 B     A0A0B6NZG1                          1         172             
DBREF1 5HD6 C    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 C     A0A0B6NZG1                          1         172             
DBREF1 5HD6 D    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 D     A0A0B6NZG1                          1         172             
DBREF1 5HD6 E    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 E     A0A0B6NZG1                          1         172             
DBREF1 5HD6 F    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 F     A0A0B6NZG1                          1         172             
DBREF1 5HD6 G    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 G     A0A0B6NZG1                          1         172             
DBREF1 5HD6 H    1   172  UNP                  A0A0B6NZG1_YERPE                 
DBREF2 5HD6 H     A0A0B6NZG1                          1         172             
SEQADV 5HD6 SER A   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN A   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA A    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER B   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN B   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA B    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER C   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN C   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA C    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER D   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN D   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA D    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER E   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN E   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA E    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER F   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN F   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA F    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER G   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN G   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA G    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 SER H   -2  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ASN H   -1  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQADV 5HD6 ALA H    0  UNP  A0A0B6NZG           EXPRESSION TAG                 
SEQRES   1 A  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 A  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 A  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 A  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 A  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 A  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 A  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 A  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 A  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 A  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 A  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 A  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 A  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 A  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 B  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 B  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 B  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 B  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 B  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 B  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 B  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 B  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 B  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 B  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 B  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 B  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 B  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 B  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 C  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 C  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 C  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 C  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 C  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 C  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 C  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 C  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 C  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 C  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 C  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 C  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 C  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 C  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 D  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 D  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 D  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 D  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 D  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 D  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 D  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 D  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 D  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 D  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 D  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 D  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 D  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 D  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 E  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 E  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 E  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 E  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 E  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 E  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 E  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 E  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 E  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 E  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 E  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 E  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 E  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 E  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 F  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 F  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 F  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 F  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 F  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 F  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 F  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 F  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 F  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 F  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 F  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 F  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 F  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 F  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 G  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 G  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 G  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 G  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 G  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 G  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 G  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 G  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 G  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 G  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 G  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 G  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 G  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 G  175  LYS ASP THR ASN ALA PHE                                      
SEQRES   1 H  175  SER ASN ALA MSE VAL ASP LYS ARG GLU SER TYR THR LYS          
SEQRES   2 H  175  GLU ASP LEU GLU ALA SER GLY ARG GLY GLU LEU PHE GLY          
SEQRES   3 H  175  ALA GLY GLY PRO PRO LEU PRO ALA GLY ASN MSE LEU MSE          
SEQRES   4 H  175  MSE ASP ARG ILE VAL LYS MSE ILE GLU ASP GLY GLY SER          
SEQRES   5 H  175  HIS ASN LYS GLY TYR VAL GLU ALA GLU LEU ASP ILE ASN          
SEQRES   6 H  175  PRO ASP LEU TRP PHE PHE GLY CYS HIS PHE ILE GLY ASP          
SEQRES   7 H  175  PRO VAL MSE PRO GLY CYS LEU GLY LEU ASP ALA MSE TRP          
SEQRES   8 H  175  GLN LEU VAL GLY PHE TYR LEU GLY TRP LEU GLY GLY GLU          
SEQRES   9 H  175  GLY LYS GLY ARG ALA LEU GLY VAL GLY GLU VAL LYS PHE          
SEQRES  10 H  175  THR GLY GLN VAL LEU PRO ASP ALA LYS LYS VAL THR TYR          
SEQRES  11 H  175  ARG ILE ASN PHE LYS ARG VAL ILE MSE ARG LYS LEU ILE          
SEQRES  12 H  175  MSE GLY VAL ALA ASP GLY GLU VAL LEU VAL ASP GLY LYS          
SEQRES  13 H  175  VAL ILE TYR THR ALA THR ASP LEU LYS VAL GLY LEU PHE          
SEQRES  14 H  175  LYS ASP THR ASN ALA PHE                                      
MODRES 5HD6 MSE A    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE A  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE B  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE C  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE D  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE E  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE F  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE G  141  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H    1  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   34  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   36  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   37  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   43  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   78  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H   87  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H  136  MET  MODIFIED RESIDUE                                   
MODRES 5HD6 MSE H  141  MET  MODIFIED RESIDUE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  34       8                                                       
HET    MSE  A  36       8                                                       
HET    MSE  A  37      16                                                       
HET    MSE  A  43       8                                                       
HET    MSE  A  78       8                                                       
HET    MSE  A  87       8                                                       
HET    MSE  A 136       8                                                       
HET    MSE  A 141       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  34       8                                                       
HET    MSE  B  36       8                                                       
HET    MSE  B  37      16                                                       
HET    MSE  B  43       8                                                       
HET    MSE  B  78       8                                                       
HET    MSE  B  87       8                                                       
HET    MSE  B 136       8                                                       
HET    MSE  B 141       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  34       8                                                       
HET    MSE  C  36       8                                                       
HET    MSE  C  37      16                                                       
HET    MSE  C  43       8                                                       
HET    MSE  C  78       8                                                       
HET    MSE  C  87       8                                                       
HET    MSE  C 136       8                                                       
HET    MSE  C 141       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D  34       8                                                       
HET    MSE  D  36       8                                                       
HET    MSE  D  37      16                                                       
HET    MSE  D  43       8                                                       
HET    MSE  D  78       8                                                       
HET    MSE  D  87       8                                                       
HET    MSE  D 136       8                                                       
HET    MSE  D 141       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E  34       8                                                       
HET    MSE  E  36       8                                                       
HET    MSE  E  37      16                                                       
HET    MSE  E  43       8                                                       
HET    MSE  E  78       8                                                       
HET    MSE  E  87       8                                                       
HET    MSE  E 136       8                                                       
HET    MSE  E 141       8                                                       
HET    MSE  F  34       8                                                       
HET    MSE  F  36       8                                                       
HET    MSE  F  37      16                                                       
HET    MSE  F  43       8                                                       
HET    MSE  F  78       8                                                       
HET    MSE  F  87       8                                                       
HET    MSE  F 136       8                                                       
HET    MSE  F 141       8                                                       
HET    MSE  G  34       8                                                       
HET    MSE  G  36       8                                                       
HET    MSE  G  37      16                                                       
HET    MSE  G  43      16                                                       
HET    MSE  G  78       8                                                       
HET    MSE  G  87       8                                                       
HET    MSE  G 136       8                                                       
HET    MSE  G 141       8                                                       
HET    MSE  H   1       8                                                       
HET    MSE  H  34       8                                                       
HET    MSE  H  36       8                                                       
HET    MSE  H  37      16                                                       
HET    MSE  H  43      16                                                       
HET    MSE  H  78       8                                                       
HET    MSE  H  87       8                                                       
HET    MSE  H 136      16                                                       
HET    MSE  H 141       8                                                       
HET    GOL  A 201       6                                                       
HET    GOL  B 201       6                                                       
HET    GOL  C 201       6                                                       
HET    GOL  C 202       6                                                       
HET    GOL  C 203       6                                                       
HET    GOL  D 201       6                                                       
HET    GOL  D 202       6                                                       
HET    GOL  E 201       6                                                       
HET    GOL  F 201       6                                                       
HET    GOL  F 202       6                                                       
HET    GOL  G 201       6                                                       
HET    GOL  G 202      12                                                       
HET    GOL  H 201       6                                                       
HET    GOL  H 202       6                                                       
HET    GOL  H 203       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    70(C5 H11 N O2 SE)                                           
FORMUL   9  GOL    15(C3 H8 O3)                                                 
FORMUL  24  HOH   *1634(H2 O)                                                   
HELIX    1 AA1 THR A    9  ARG A   18  1                                  10    
HELIX    2 AA2 ALA A   31  LEU A   35  5                                   5    
HELIX    3 AA3 LEU A   65  HIS A   71  1                                   7    
HELIX    4 AA4 PRO A   79  LEU A   98  1                                  20    
HELIX    5 AA5 THR B    9  ARG B   18  1                                  10    
HELIX    6 AA6 ALA B   31  LEU B   35  5                                   5    
HELIX    7 AA7 LEU B   65  HIS B   71  1                                   7    
HELIX    8 AA8 PRO B   79  LEU B   98  1                                  20    
HELIX    9 AA9 THR C    9  ARG C   18  1                                  10    
HELIX   10 AB1 ALA C   31  LEU C   35  5                                   5    
HELIX   11 AB2 LEU C   65  HIS C   71  1                                   7    
HELIX   12 AB3 PRO C   79  LEU C   98  1                                  20    
HELIX   13 AB4 THR D    9  ARG D   18  1                                  10    
HELIX   14 AB5 ALA D   31  LEU D   35  5                                   5    
HELIX   15 AB6 LEU D   65  HIS D   71  1                                   7    
HELIX   16 AB7 PRO D   79  LEU D   98  1                                  20    
HELIX   17 AB8 THR E    9  ARG E   18  1                                  10    
HELIX   18 AB9 ALA E   31  LEU E   35  5                                   5    
HELIX   19 AC1 LEU E   65  HIS E   71  1                                   7    
HELIX   20 AC2 PRO E   79  LEU E   98  1                                  20    
HELIX   21 AC3 THR F    9  ARG F   18  1                                  10    
HELIX   22 AC4 ALA F   31  LEU F   35  5                                   5    
HELIX   23 AC5 LEU F   65  HIS F   71  1                                   7    
HELIX   24 AC6 PRO F   79  LEU F   98  1                                  20    
HELIX   25 AC7 THR G    9  ARG G   18  1                                  10    
HELIX   26 AC8 ALA G   31  LEU G   35  5                                   5    
HELIX   27 AC9 LEU G   65  HIS G   71  1                                   7    
HELIX   28 AD1 PRO G   79  LEU G   98  1                                  20    
HELIX   29 AD2 THR H    9  ARG H   18  1                                  10    
HELIX   30 AD3 ALA H   31  LEU H   35  5                                   5    
HELIX   31 AD4 LEU H   65  HIS H   71  1                                   7    
HELIX   32 AD5 PRO H   79  LEU H   98  1                                  20    
SHEET    1 AA112 ARG A  39  ILE A  44  0                                        
SHEET    2 AA112 TYR A  54  ASP A  60 -1  O  TYR A  54   N  ILE A  44           
SHEET    3 AA112 LYS A 124  MSE A 136 -1  O  ILE A 129   N  VAL A  55           
SHEET    4 AA112 ILE A 140  VAL A 150 -1  O  VAL A 143   N  LYS A 132           
SHEET    5 AA112 LYS A 153  PHE A 166 -1  O  ALA A 158   N  GLY A 146           
SHEET    6 AA112 LYS A 103  VAL A 109 -1  N  LYS A 103   O  PHE A 166           
SHEET    7 AA112 VAL G 112  PHE G 114 -1  O  VAL G 112   N  VAL A 109           
SHEET    8 AA112 LYS G 153  PHE G 166 -1  O  THR G 157   N  LYS G 113           
SHEET    9 AA112 ILE G 140  VAL G 150 -1  N  VAL G 148   O  ILE G 155           
SHEET   10 AA112 LYS G 124  MSE G 136 -1  N  LYS G 132   O  VAL G 143           
SHEET   11 AA112 TYR G  54  ASP G  60 -1  N  LEU G  59   O  VAL G 125           
SHEET   12 AA112 ARG G  39  ILE G  44 -1  N  LYS G  42   O  GLU G  56           
SHEET    1 AA212 ARG A  39  ILE A  44  0                                        
SHEET    2 AA212 TYR A  54  ASP A  60 -1  O  TYR A  54   N  ILE A  44           
SHEET    3 AA212 LYS A 124  MSE A 136 -1  O  ILE A 129   N  VAL A  55           
SHEET    4 AA212 ILE A 140  VAL A 150 -1  O  VAL A 143   N  LYS A 132           
SHEET    5 AA212 LYS A 153  PHE A 166 -1  O  ALA A 158   N  GLY A 146           
SHEET    6 AA212 GLU A 111  PHE A 114 -1  N  GLU A 111   O  THR A 159           
SHEET    7 AA212 LYS G 103  VAL G 109 -1  O  VAL G 109   N  VAL A 112           
SHEET    8 AA212 LYS G 153  PHE G 166 -1  O  PHE G 166   N  LYS G 103           
SHEET    9 AA212 ILE G 140  VAL G 150 -1  N  VAL G 148   O  ILE G 155           
SHEET   10 AA212 LYS G 124  MSE G 136 -1  N  LYS G 132   O  VAL G 143           
SHEET   11 AA212 TYR G  54  ASP G  60 -1  N  LEU G  59   O  VAL G 125           
SHEET   12 AA212 ARG G  39  ILE G  44 -1  N  LYS G  42   O  GLU G  56           
SHEET    1 AA312 ARG B  39  ILE B  44  0                                        
SHEET    2 AA312 TYR B  54  ASP B  60 -1  O  TYR B  54   N  ILE B  44           
SHEET    3 AA312 LYS B 124  MSE B 136 -1  O  ILE B 129   N  VAL B  55           
SHEET    4 AA312 ILE B 140  VAL B 150 -1  O  VAL B 143   N  LYS B 132           
SHEET    5 AA312 LYS B 153  PHE B 166 -1  O  ALA B 158   N  GLY B 146           
SHEET    6 AA312 LYS B 103  VAL B 109 -1  N  LYS B 103   O  PHE B 166           
SHEET    7 AA312 VAL F 112  PHE F 114 -1  O  VAL F 112   N  VAL B 109           
SHEET    8 AA312 LYS F 153  PHE F 166 -1  O  THR F 157   N  LYS F 113           
SHEET    9 AA312 ILE F 140  VAL F 150 -1  N  VAL F 148   O  ILE F 155           
SHEET   10 AA312 LYS F 124  MSE F 136 -1  N  LYS F 132   O  VAL F 143           
SHEET   11 AA312 TYR F  54  ASP F  60 -1  N  LEU F  59   O  VAL F 125           
SHEET   12 AA312 ARG F  39  ILE F  44 -1  N  LYS F  42   O  GLU F  56           
SHEET    1 AA412 ARG B  39  ILE B  44  0                                        
SHEET    2 AA412 TYR B  54  ASP B  60 -1  O  TYR B  54   N  ILE B  44           
SHEET    3 AA412 LYS B 124  MSE B 136 -1  O  ILE B 129   N  VAL B  55           
SHEET    4 AA412 ILE B 140  VAL B 150 -1  O  VAL B 143   N  LYS B 132           
SHEET    5 AA412 LYS B 153  PHE B 166 -1  O  ALA B 158   N  GLY B 146           
SHEET    6 AA412 GLU B 111  PHE B 114 -1  N  GLU B 111   O  THR B 159           
SHEET    7 AA412 LYS F 103  VAL F 109 -1  O  VAL F 109   N  VAL B 112           
SHEET    8 AA412 LYS F 153  PHE F 166 -1  O  LYS F 162   N  LEU F 107           
SHEET    9 AA412 ILE F 140  VAL F 150 -1  N  VAL F 148   O  ILE F 155           
SHEET   10 AA412 LYS F 124  MSE F 136 -1  N  LYS F 132   O  VAL F 143           
SHEET   11 AA412 TYR F  54  ASP F  60 -1  N  LEU F  59   O  VAL F 125           
SHEET   12 AA412 ARG F  39  ILE F  44 -1  N  LYS F  42   O  GLU F  56           
SHEET    1 AA512 ARG C  39  ILE C  44  0                                        
SHEET    2 AA512 TYR C  54  ASP C  60 -1  O  TYR C  54   N  ILE C  44           
SHEET    3 AA512 LYS C 124  MSE C 136 -1  O  ILE C 129   N  VAL C  55           
SHEET    4 AA512 ILE C 140  VAL C 150 -1  O  VAL C 143   N  LYS C 132           
SHEET    5 AA512 LYS C 153  PHE C 166 -1  O  ALA C 158   N  GLY C 146           
SHEET    6 AA512 LYS C 103  VAL C 109 -1  N  LYS C 103   O  PHE C 166           
SHEET    7 AA512 VAL E 112  PHE E 114 -1  O  VAL E 112   N  VAL C 109           
SHEET    8 AA512 LYS E 153  PHE E 166 -1  O  THR E 157   N  LYS E 113           
SHEET    9 AA512 ILE E 140  VAL E 150 -1  N  VAL E 148   O  ILE E 155           
SHEET   10 AA512 LYS E 124  MSE E 136 -1  N  LYS E 132   O  VAL E 143           
SHEET   11 AA512 TYR E  54  ASP E  60 -1  N  LEU E  59   O  VAL E 125           
SHEET   12 AA512 ARG E  39  ILE E  44 -1  N  LYS E  42   O  GLU E  56           
SHEET    1 AA612 ARG C  39  ILE C  44  0                                        
SHEET    2 AA612 TYR C  54  ASP C  60 -1  O  TYR C  54   N  ILE C  44           
SHEET    3 AA612 LYS C 124  MSE C 136 -1  O  ILE C 129   N  VAL C  55           
SHEET    4 AA612 ILE C 140  VAL C 150 -1  O  VAL C 143   N  LYS C 132           
SHEET    5 AA612 LYS C 153  PHE C 166 -1  O  ALA C 158   N  GLY C 146           
SHEET    6 AA612 GLU C 111  PHE C 114 -1  N  GLU C 111   O  THR C 159           
SHEET    7 AA612 LYS E 103  VAL E 109 -1  O  VAL E 109   N  VAL C 112           
SHEET    8 AA612 LYS E 153  PHE E 166 -1  O  PHE E 166   N  LYS E 103           
SHEET    9 AA612 ILE E 140  VAL E 150 -1  N  VAL E 148   O  ILE E 155           
SHEET   10 AA612 LYS E 124  MSE E 136 -1  N  LYS E 132   O  VAL E 143           
SHEET   11 AA612 TYR E  54  ASP E  60 -1  N  LEU E  59   O  VAL E 125           
SHEET   12 AA612 ARG E  39  ILE E  44 -1  N  LYS E  42   O  GLU E  56           
SHEET    1 AA712 ARG D  39  ILE D  44  0                                        
SHEET    2 AA712 TYR D  54  ASP D  60 -1  O  TYR D  54   N  ILE D  44           
SHEET    3 AA712 LYS D 124  MSE D 136 -1  O  ILE D 129   N  VAL D  55           
SHEET    4 AA712 ILE D 140  VAL D 150 -1  O  VAL D 143   N  LYS D 132           
SHEET    5 AA712 LYS D 153  PHE D 166 -1  O  ALA D 158   N  GLY D 146           
SHEET    6 AA712 LYS D 103  VAL D 109 -1  N  LYS D 103   O  PHE D 166           
SHEET    7 AA712 VAL H 112  PHE H 114 -1  O  VAL H 112   N  VAL D 109           
SHEET    8 AA712 LYS H 153  PHE H 166 -1  O  THR H 157   N  LYS H 113           
SHEET    9 AA712 ILE H 140  VAL H 150 -1  N  VAL H 148   O  ILE H 155           
SHEET   10 AA712 LYS H 124  MSE H 136 -1  N  LYS H 132   O  VAL H 143           
SHEET   11 AA712 TYR H  54  ASP H  60 -1  N  LEU H  59   O  VAL H 125           
SHEET   12 AA712 ARG H  39  ILE H  44 -1  N  LYS H  42   O  GLU H  56           
SHEET    1 AA812 ARG D  39  ILE D  44  0                                        
SHEET    2 AA812 TYR D  54  ASP D  60 -1  O  TYR D  54   N  ILE D  44           
SHEET    3 AA812 LYS D 124  MSE D 136 -1  O  ILE D 129   N  VAL D  55           
SHEET    4 AA812 ILE D 140  VAL D 150 -1  O  VAL D 143   N  LYS D 132           
SHEET    5 AA812 LYS D 153  PHE D 166 -1  O  ALA D 158   N  GLY D 146           
SHEET    6 AA812 GLU D 111  PHE D 114 -1  N  GLU D 111   O  THR D 159           
SHEET    7 AA812 LYS H 103  VAL H 109 -1  O  VAL H 109   N  VAL D 112           
SHEET    8 AA812 LYS H 153  PHE H 166 -1  O  LYS H 162   N  LEU H 107           
SHEET    9 AA812 ILE H 140  VAL H 150 -1  N  VAL H 148   O  ILE H 155           
SHEET   10 AA812 LYS H 124  MSE H 136 -1  N  LYS H 132   O  VAL H 143           
SHEET   11 AA812 TYR H  54  ASP H  60 -1  N  LEU H  59   O  VAL H 125           
SHEET   12 AA812 ARG H  39  ILE H  44 -1  N  LYS H  42   O  GLU H  56           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   VAL A   2     1555   1555  1.33  
LINK         C   ASN A  33                 N   MSE A  34     1555   1555  1.33  
LINK         C   MSE A  34                 N   LEU A  35     1555   1555  1.33  
LINK         C   LEU A  35                 N   MSE A  36     1555   1555  1.33  
LINK         C   MSE A  36                 N  AMSE A  37     1555   1555  1.32  
LINK         C   MSE A  36                 N  BMSE A  37     1555   1555  1.34  
LINK         C  AMSE A  37                 N   ASP A  38     1555   1555  1.33  
LINK         C  BMSE A  37                 N   ASP A  38     1555   1555  1.34  
LINK         C   LYS A  42                 N   MSE A  43     1555   1555  1.33  
LINK         C   MSE A  43                 N   ILE A  44     1555   1555  1.33  
LINK         C   VAL A  77                 N   MSE A  78     1555   1555  1.32  
LINK         C   MSE A  78                 N   PRO A  79     1555   1555  1.33  
LINK         C   ALA A  86                 N   MSE A  87     1555   1555  1.33  
LINK         C   MSE A  87                 N   TRP A  88     1555   1555  1.34  
LINK         C   ILE A 135                 N   MSE A 136     1555   1555  1.33  
LINK         C   MSE A 136                 N   ARG A 137     1555   1555  1.33  
LINK         C   ILE A 140                 N   MSE A 141     1555   1555  1.33  
LINK         C   MSE A 141                 N   GLY A 142     1555   1555  1.32  
LINK         C   ALA B   0                 N   MSE B   1     1555   1555  1.33  
LINK         C   MSE B   1                 N   VAL B   2     1555   1555  1.34  
LINK         C   ASN B  33                 N   MSE B  34     1555   1555  1.33  
LINK         C   MSE B  34                 N   LEU B  35     1555   1555  1.33  
LINK         C   LEU B  35                 N   MSE B  36     1555   1555  1.33  
LINK         C   MSE B  36                 N  AMSE B  37     1555   1555  1.32  
LINK         C   MSE B  36                 N  BMSE B  37     1555   1555  1.34  
LINK         C  AMSE B  37                 N   ASP B  38     1555   1555  1.33  
LINK         C  BMSE B  37                 N   ASP B  38     1555   1555  1.34  
LINK         C   LYS B  42                 N   MSE B  43     1555   1555  1.33  
LINK         C   MSE B  43                 N   ILE B  44     1555   1555  1.33  
LINK         C   VAL B  77                 N   MSE B  78     1555   1555  1.33  
LINK         C   MSE B  78                 N   PRO B  79     1555   1555  1.34  
LINK         C   ALA B  86                 N   MSE B  87     1555   1555  1.33  
LINK         C   MSE B  87                 N   TRP B  88     1555   1555  1.34  
LINK         C   ILE B 135                 N   MSE B 136     1555   1555  1.33  
LINK         C   MSE B 136                 N   ARG B 137     1555   1555  1.33  
LINK         C   ILE B 140                 N   MSE B 141     1555   1555  1.32  
LINK         C   MSE B 141                 N   GLY B 142     1555   1555  1.32  
LINK         C   ALA C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   VAL C   2     1555   1555  1.33  
LINK         C   ASN C  33                 N   MSE C  34     1555   1555  1.33  
LINK         C   MSE C  34                 N   LEU C  35     1555   1555  1.33  
LINK         C   LEU C  35                 N   MSE C  36     1555   1555  1.33  
LINK         C   MSE C  36                 N  AMSE C  37     1555   1555  1.32  
LINK         C   MSE C  36                 N  BMSE C  37     1555   1555  1.33  
LINK         C  AMSE C  37                 N   ASP C  38     1555   1555  1.33  
LINK         C  BMSE C  37                 N   ASP C  38     1555   1555  1.34  
LINK         C   LYS C  42                 N   MSE C  43     1555   1555  1.33  
LINK         C   MSE C  43                 N   ILE C  44     1555   1555  1.33  
LINK         C   VAL C  77                 N   MSE C  78     1555   1555  1.33  
LINK         C   MSE C  78                 N   PRO C  79     1555   1555  1.33  
LINK         C   ALA C  86                 N   MSE C  87     1555   1555  1.33  
LINK         C   MSE C  87                 N   TRP C  88     1555   1555  1.34  
LINK         C   ILE C 135                 N   MSE C 136     1555   1555  1.33  
LINK         C   MSE C 136                 N   ARG C 137     1555   1555  1.33  
LINK         C   ILE C 140                 N   MSE C 141     1555   1555  1.33  
LINK         C   MSE C 141                 N   GLY C 142     1555   1555  1.32  
LINK         C   ALA D   0                 N   MSE D   1     1555   1555  1.33  
LINK         C   MSE D   1                 N   VAL D   2     1555   1555  1.33  
LINK         C   ASN D  33                 N   MSE D  34     1555   1555  1.33  
LINK         C   MSE D  34                 N   LEU D  35     1555   1555  1.33  
LINK         C   LEU D  35                 N   MSE D  36     1555   1555  1.33  
LINK         C   MSE D  36                 N  AMSE D  37     1555   1555  1.32  
LINK         C   MSE D  36                 N  BMSE D  37     1555   1555  1.34  
LINK         C  AMSE D  37                 N   ASP D  38     1555   1555  1.33  
LINK         C  BMSE D  37                 N   ASP D  38     1555   1555  1.34  
LINK         C   LYS D  42                 N   MSE D  43     1555   1555  1.33  
LINK         C   MSE D  43                 N   ILE D  44     1555   1555  1.33  
LINK         C   VAL D  77                 N   MSE D  78     1555   1555  1.33  
LINK         C   MSE D  78                 N   PRO D  79     1555   1555  1.33  
LINK         C   ALA D  86                 N   MSE D  87     1555   1555  1.33  
LINK         C   MSE D  87                 N   TRP D  88     1555   1555  1.34  
LINK         C   ILE D 135                 N   MSE D 136     1555   1555  1.33  
LINK         C   MSE D 136                 N   ARG D 137     1555   1555  1.33  
LINK         C   ILE D 140                 N   MSE D 141     1555   1555  1.32  
LINK         C   MSE D 141                 N   GLY D 142     1555   1555  1.32  
LINK         C   ALA E   0                 N   MSE E   1     1555   1555  1.33  
LINK         C   MSE E   1                 N   VAL E   2     1555   1555  1.33  
LINK         C   ASN E  33                 N   MSE E  34     1555   1555  1.33  
LINK         C   MSE E  34                 N   LEU E  35     1555   1555  1.33  
LINK         C   LEU E  35                 N   MSE E  36     1555   1555  1.33  
LINK         C   MSE E  36                 N  AMSE E  37     1555   1555  1.32  
LINK         C   MSE E  36                 N  BMSE E  37     1555   1555  1.34  
LINK         C  AMSE E  37                 N   ASP E  38     1555   1555  1.32  
LINK         C  BMSE E  37                 N   ASP E  38     1555   1555  1.34  
LINK         C   LYS E  42                 N   MSE E  43     1555   1555  1.33  
LINK         C   MSE E  43                 N   ILE E  44     1555   1555  1.33  
LINK         C   VAL E  77                 N   MSE E  78     1555   1555  1.33  
LINK         C   MSE E  78                 N   PRO E  79     1555   1555  1.34  
LINK         C   ALA E  86                 N   MSE E  87     1555   1555  1.33  
LINK         C   MSE E  87                 N   TRP E  88     1555   1555  1.34  
LINK         C   ILE E 135                 N   MSE E 136     1555   1555  1.33  
LINK         C   MSE E 136                 N   ARG E 137     1555   1555  1.33  
LINK         C   ILE E 140                 N   MSE E 141     1555   1555  1.33  
LINK         C   MSE E 141                 N   GLY E 142     1555   1555  1.33  
LINK         C   ASN F  33                 N   MSE F  34     1555   1555  1.33  
LINK         C   MSE F  34                 N   LEU F  35     1555   1555  1.34  
LINK         C   LEU F  35                 N   MSE F  36     1555   1555  1.33  
LINK         C   MSE F  36                 N  AMSE F  37     1555   1555  1.33  
LINK         C   MSE F  36                 N  BMSE F  37     1555   1555  1.33  
LINK         C  AMSE F  37                 N   ASP F  38     1555   1555  1.33  
LINK         C  BMSE F  37                 N   ASP F  38     1555   1555  1.33  
LINK         C   LYS F  42                 N   MSE F  43     1555   1555  1.33  
LINK         C   MSE F  43                 N   ILE F  44     1555   1555  1.33  
LINK         C   VAL F  77                 N   MSE F  78     1555   1555  1.33  
LINK         C   MSE F  78                 N   PRO F  79     1555   1555  1.34  
LINK         C   ALA F  86                 N   MSE F  87     1555   1555  1.33  
LINK         C   MSE F  87                 N   TRP F  88     1555   1555  1.34  
LINK         C  AILE F 135                 N   MSE F 136     1555   1555  1.33  
LINK         C  BILE F 135                 N   MSE F 136     1555   1555  1.33  
LINK         C   MSE F 136                 N   ARG F 137     1555   1555  1.33  
LINK         C   ILE F 140                 N   MSE F 141     1555   1555  1.33  
LINK         C   MSE F 141                 N   GLY F 142     1555   1555  1.32  
LINK         C   ASN G  33                 N   MSE G  34     1555   1555  1.33  
LINK         C   MSE G  34                 N   LEU G  35     1555   1555  1.33  
LINK         C   LEU G  35                 N   MSE G  36     1555   1555  1.33  
LINK         C   MSE G  36                 N  AMSE G  37     1555   1555  1.33  
LINK         C   MSE G  36                 N  BMSE G  37     1555   1555  1.33  
LINK         C  AMSE G  37                 N   ASP G  38     1555   1555  1.34  
LINK         C  BMSE G  37                 N   ASP G  38     1555   1555  1.33  
LINK         C   LYS G  42                 N  AMSE G  43     1555   1555  1.33  
LINK         C   LYS G  42                 N  BMSE G  43     1555   1555  1.33  
LINK         C  AMSE G  43                 N   ILE G  44     1555   1555  1.33  
LINK         C  BMSE G  43                 N   ILE G  44     1555   1555  1.33  
LINK         C   VAL G  77                 N   MSE G  78     1555   1555  1.33  
LINK         C   MSE G  78                 N   PRO G  79     1555   1555  1.33  
LINK         C   ALA G  86                 N   MSE G  87     1555   1555  1.33  
LINK         C   MSE G  87                 N   TRP G  88     1555   1555  1.34  
LINK         C   ILE G 135                 N   MSE G 136     1555   1555  1.33  
LINK         C   MSE G 136                 N   ARG G 137     1555   1555  1.33  
LINK         C   ILE G 140                 N   MSE G 141     1555   1555  1.32  
LINK         C   MSE G 141                 N   GLY G 142     1555   1555  1.32  
LINK         C   ALA H   0                 N   MSE H   1     1555   1555  1.33  
LINK         C   MSE H   1                 N   VAL H   2     1555   1555  1.33  
LINK         C   ASN H  33                 N   MSE H  34     1555   1555  1.33  
LINK         C   MSE H  34                 N   LEU H  35     1555   1555  1.34  
LINK         C   LEU H  35                 N   MSE H  36     1555   1555  1.33  
LINK         C   MSE H  36                 N  AMSE H  37     1555   1555  1.32  
LINK         C   MSE H  36                 N  BMSE H  37     1555   1555  1.34  
LINK         C  AMSE H  37                 N   ASP H  38     1555   1555  1.32  
LINK         C  BMSE H  37                 N   ASP H  38     1555   1555  1.34  
LINK         C   LYS H  42                 N  AMSE H  43     1555   1555  1.33  
LINK         C   LYS H  42                 N  BMSE H  43     1555   1555  1.33  
LINK         C  AMSE H  43                 N   ILE H  44     1555   1555  1.33  
LINK         C  BMSE H  43                 N   ILE H  44     1555   1555  1.33  
LINK         C   VAL H  77                 N   MSE H  78     1555   1555  1.33  
LINK         C   MSE H  78                 N   PRO H  79     1555   1555  1.34  
LINK         C   ALA H  86                 N   MSE H  87     1555   1555  1.33  
LINK         C   MSE H  87                 N   TRP H  88     1555   1555  1.34  
LINK         C   ILE H 135                 N  AMSE H 136     1555   1555  1.33  
LINK         C   ILE H 135                 N  BMSE H 136     1555   1555  1.33  
LINK         C  AMSE H 136                 N   ARG H 137     1555   1555  1.33  
LINK         C  BMSE H 136                 N   ARG H 137     1555   1555  1.33  
LINK         C   ILE H 140                 N   MSE H 141     1555   1555  1.33  
LINK         C   MSE H 141                 N   GLY H 142     1555   1555  1.32  
CISPEP   1 HIS A   71    PHE A   72          0        -1.08                     
CISPEP   2 HIS B   71    PHE B   72          0        -3.21                     
CISPEP   3 HIS C   71    PHE C   72          0        -2.55                     
CISPEP   4 HIS D   71    PHE D   72          0        -2.59                     
CISPEP   5 HIS E   71    PHE E   72          0        -4.08                     
CISPEP   6 HIS F   71    PHE F   72          0        -3.03                     
CISPEP   7 HIS G   71    PHE G   72          0        -2.37                     
CISPEP   8 HIS H   71    PHE H   72          0        -4.32                     
SITE     1 AC1 10 MSE A  78  GLY A  80  GLY A 116  GLN A 117                    
SITE     2 AC1 10 TYR A 156  HOH A 322  ARG G 105  ALA G 106                    
SITE     3 AC1 10 PHE G 172  GOL G 202                                          
SITE     1 AC2 10 MSE B  78  GLY B  80  GLY B 116  GLN B 117                    
SITE     2 AC2 10 TYR B 156  HOH B 315  HOH B 322  ARG F 105                    
SITE     3 AC2 10 ALA F 106  PHE F 172                                          
SITE     1 AC3 10 MSE C  78  GLY C  80  GLY C 116  GLN C 117                    
SITE     2 AC3 10 TYR C 156  HOH C 319  ARG E 105  ALA E 106                    
SITE     3 AC3 10 PHE E 172  HOH E 303                                          
SITE     1 AC4  6 LYS C 138  LEU C 165  LYS C 167  ASP C 168                    
SITE     2 AC4  6 HOH C 303  HOH C 361                                          
SITE     1 AC5  9 ARG C 105  ALA C 106  MSE E  78  PRO E  79                    
SITE     2 AC5  9 GLY E  80  GLY E 116  GLN E 117  TYR E 156                    
SITE     3 AC5  9 HOH E 328                                                     
SITE     1 AC6  6 ARG D 133  ASP D 160  LYS D 162  HOH D 305                    
SITE     2 AC6  6 LYS H  10  GLU H  11                                          
SITE     1 AC7 10 MSE D  78  GLY D  80  GLY D 116  GLN D 117                    
SITE     2 AC7 10 TYR D 156  HOH D 318  ARG H 105  ALA H 106                    
SITE     3 AC7 10 PHE H 172  GOL H 202                                          
SITE     1 AC8  8 PHE C  72  PRO E  30  TRP E  88  GLN E  89                    
SITE     2 AC8  8 GLY E 104  HOH E 303  HOH E 318  HOH E 337                    
SITE     1 AC9  9 ARG B 105  ALA B 106  HOH B 448  MSE F  78                    
SITE     2 AC9  9 GLY F  80  GLY F 116  GLN F 117  TYR F 156                    
SITE     3 AC9  9 HOH F 329                                                     
SITE     1 AD1  7 PHE B  72  HOH B 315  TRP F  88  GLN F  89                    
SITE     2 AD1  7 VAL F 163  HOH F 334  HOH F 356                               
SITE     1 AD2  8 ARG A 105  ALA A 106  MSE G  78  GLY G  80                    
SITE     2 AD2  8 GLY G 116  GLN G 117  TYR G 156  HOH G 338                    
SITE     1 AD3 11 PHE A  72  GOL A 201  PRO G  30  ASP G  85                    
SITE     2 AD3 11 TRP G  88  GLN G  89  GLY G 104  ARG G 105                    
SITE     3 AD3 11 ALA G 106  HOH G 307  HOH G 311                               
SITE     1 AD4  9 ARG D 105  ALA D 106  MSE H  78  GLY H  80                    
SITE     2 AD4  9 GLY H 116  GLN H 117  TYR H 156  HOH H 329                    
SITE     3 AD4  9 HOH H 412                                                     
SITE     1 AD5  6 PHE D  72  GOL D 202  TRP H  88  ALA H 106                    
SITE     2 AD5  6 HOH H 321  HOH H 345                                          
SITE     1 AD6  9 LYS H  10  GLY H  32  LEU H  35  ASP H  38                    
SITE     2 AD6  9 LEU H  59  LEU H  65  HOH H 333  HOH H 359                    
SITE     3 AD6  9 HOH H 368                                                     
CRYST1   42.665   50.816  138.780  90.02  90.02  90.10 P 1           8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023438  0.000042  0.000006        0.00000                         
SCALE2      0.000000  0.019679  0.000005        0.00000                         
SCALE3      0.000000  0.000000  0.007206        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system