GenomeNet

Database: PDB
Entry: 1OQ1
LinkDB: 1OQ1
Original site: 1OQ1 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   06-MAR-03   1OQ1              
TITLE     CRYSTAL STRUCTURE OF PROTEIN OF UNKNOWN FUNCTION WITH GALECTIN-LIKE   
TITLE    2 FOLD FROM BACILLUS SUBTILIS                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN YESU;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HYPOTHETICAL PROTEIN APC1120;                               
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, SINGLETON, PSI, PROTEIN STRUCTURE INITIATIVE,    
KEYWDS   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.KIM,L.LEZONDRA,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS  
AUTHOR   2 (MCSG)                                                               
REVDAT   4   13-JUL-11 1OQ1    1       VERSN                                    
REVDAT   3   24-FEB-09 1OQ1    1       VERSN                                    
REVDAT   2   18-JAN-05 1OQ1    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   23-SEP-03 1OQ1    0                                                
JRNL        AUTH   Y.KIM,L.LEZONDRA,A.JOACHIMIAK                                
JRNL        TITL   CRYSTAL STRUCTURE OF THE BACILLUS SUBTILIS HYPOTHETICAL      
JRNL        TITL 2 PROTEIN APC1120                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.21                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 403841.080                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 87402                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8765                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.78                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 0.50                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7483                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2160                       
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.70                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1142                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.009                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7151                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 999                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 11.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.55000                                             
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 1.96000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.79000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.09                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.13                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.80                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.230 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.870 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.500 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.810 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 46.03                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ACY.PARAM                                      
REMARK   3  PARAMETER FILE  4  : GOL.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ACY.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : GOL.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OQ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018549.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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) : 0.97945                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK, HKL-2000                   
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88537                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 51.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BISTRIS, PEG10000,     
REMARK 280  PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       22.30800            
REMARK 290   SMTRY3   2  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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 4 CHAINS. THE BIOLOGICAL MOLECULE                  
REMARK 300 MAY BE A DIMER OR TETRAMER.                                          
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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 B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  1081     O    HOH B  1205              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  1205     O    HOH D  1148     2647     2.17            
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    ALA A 111      155.95    178.88                                   
REMARK 500    LYS A 166     -123.37     56.91                                   
REMARK 500    THR A 193      -90.66   -118.91                                   
REMARK 500    PRO A 204       36.35    -93.90                                   
REMARK 500    ASP B  21       -2.06     78.90                                   
REMARK 500    ALA B 111      157.51    178.78                                   
REMARK 500    LYS B 166     -126.77     56.56                                   
REMARK 500    THR B 193      -88.07   -119.10                                   
REMARK 500    PRO B 204       36.04    -93.77                                   
REMARK 500    SER C 106       35.94   -143.76                                   
REMARK 500    ALA C 111      157.64    179.50                                   
REMARK 500    SER C 156     -169.70     49.17                                   
REMARK 500    LYS C 166     -126.41     56.67                                   
REMARK 500    THR C 193      -89.34   -121.35                                   
REMARK 500    PRO C 204       33.60    -91.68                                   
REMARK 500    LYS D 166     -126.14     56.64                                   
REMARK 500    THR D 193      -87.79   -122.19                                   
REMARK 500    PRO D 204       39.24    -92.75                                   
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 A1247        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH A1249        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A1281        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH C1126        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH D1258        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH D1260        DISTANCE =  5.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY D 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 1006                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC1120   RELATED DB: TARGETDB                           
DBREF  1OQ1 A    1   220  UNP    O31524   YESU_BACSU       1    220             
DBREF  1OQ1 B    1   220  UNP    O31524   YESU_BACSU       1    220             
DBREF  1OQ1 C    1   220  UNP    O31524   YESU_BACSU       1    220             
DBREF  1OQ1 D    1   220  UNP    O31524   YESU_BACSU       1    220             
SEQADV 1OQ1 SER A   -2  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ASN A   -1  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ALA A    0  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 MSE A    1  UNP  O31524    MET     1 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A   24  UNP  O31524    MET    24 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A   76  UNP  O31524    MET    76 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A  143  UNP  O31524    MET   143 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A  160  UNP  O31524    MET   160 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A  182  UNP  O31524    MET   182 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A  202  UNP  O31524    MET   202 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE A  205  UNP  O31524    MET   205 MODIFIED RESIDUE               
SEQADV 1OQ1 SER B   -2  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ASN B   -1  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ALA B    0  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 MSE B    1  UNP  O31524    MET     1 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B   24  UNP  O31524    MET    24 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B   76  UNP  O31524    MET    76 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B  143  UNP  O31524    MET   143 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B  160  UNP  O31524    MET   160 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B  182  UNP  O31524    MET   182 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B  202  UNP  O31524    MET   202 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE B  205  UNP  O31524    MET   205 MODIFIED RESIDUE               
SEQADV 1OQ1 SER C   -2  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ASN C   -1  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ALA C    0  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 MSE C    1  UNP  O31524    MET     1 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C   24  UNP  O31524    MET    24 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C   76  UNP  O31524    MET    76 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C  143  UNP  O31524    MET   143 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C  160  UNP  O31524    MET   160 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C  182  UNP  O31524    MET   182 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C  202  UNP  O31524    MET   202 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE C  205  UNP  O31524    MET   205 MODIFIED RESIDUE               
SEQADV 1OQ1 SER D   -2  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ASN D   -1  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 ALA D    0  UNP  O31524              CLONING ARTIFACT               
SEQADV 1OQ1 MSE D    1  UNP  O31524    MET     1 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D   24  UNP  O31524    MET    24 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D   76  UNP  O31524    MET    76 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D  143  UNP  O31524    MET   143 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D  160  UNP  O31524    MET   160 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D  182  UNP  O31524    MET   182 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D  202  UNP  O31524    MET   202 MODIFIED RESIDUE               
SEQADV 1OQ1 MSE D  205  UNP  O31524    MET   205 MODIFIED RESIDUE               
SEQRES   1 A  223  SER ASN ALA MSE TYR LYS GLU GLY ALA CYS LEU TYR ARG          
SEQRES   2 A  223  ASN PRO LEU ARG SER LYS SER ASP VAL LYS ASP TRP ARG          
SEQRES   3 A  223  MSE GLU GLY GLY GLY GLN ILE SER PHE ASP ASP HIS SER          
SEQRES   4 A  223  LEU HIS LEU SER HIS VAL GLN ASP GLU ALA HIS PHE VAL          
SEQRES   5 A  223  PHE TRP CYS PRO GLU THR PHE PRO ASP GLY ILE ILE VAL          
SEQRES   6 A  223  THR TRP ASP PHE SER PRO ILE GLU GLN PRO GLY LEU CYS          
SEQRES   7 A  223  MSE LEU PHE PHE ALA ALA ALA GLY ILE ARG GLY GLU ASP          
SEQRES   8 A  223  LEU PHE ASP PRO SER LEU ARG LYS ARG THR GLY THR TYR          
SEQRES   9 A  223  PRO GLU TYR HIS SER GLY ASP ILE ASN ALA LEU HIS LEU          
SEQRES  10 A  223  SER TYR PHE ARG ARG LYS TYR ALA GLU GLU ARG ALA PHE          
SEQRES  11 A  223  ARG THR CYS ASN LEU ARG LYS SER ARG GLY PHE HIS LEU          
SEQRES  12 A  223  ALA ALA MSE GLY ALA ASP PRO LEU PRO SER PRO ASP ASP          
SEQRES  13 A  223  ALA ASP SER PRO TYR ARG MSE LYS LEU ILE LYS ASP LYS          
SEQRES  14 A  223  GLY TYR VAL HIS PHE SER ILE ASN GLY LEU PRO ILE LEU          
SEQRES  15 A  223  GLU TRP MSE ASP ASP GLY SER THR TYR GLY PRO VAL LEU          
SEQRES  16 A  223  THR LYS GLY LYS ILE GLY PHE ARG GLN MSE ALA PRO MSE          
SEQRES  17 A  223  LYS ALA VAL TYR ARG ASP PHE ALA VAL HIS GLN ALA VAL          
SEQRES  18 A  223  ARG ARG                                                      
SEQRES   1 B  223  SER ASN ALA MSE TYR LYS GLU GLY ALA CYS LEU TYR ARG          
SEQRES   2 B  223  ASN PRO LEU ARG SER LYS SER ASP VAL LYS ASP TRP ARG          
SEQRES   3 B  223  MSE GLU GLY GLY GLY GLN ILE SER PHE ASP ASP HIS SER          
SEQRES   4 B  223  LEU HIS LEU SER HIS VAL GLN ASP GLU ALA HIS PHE VAL          
SEQRES   5 B  223  PHE TRP CYS PRO GLU THR PHE PRO ASP GLY ILE ILE VAL          
SEQRES   6 B  223  THR TRP ASP PHE SER PRO ILE GLU GLN PRO GLY LEU CYS          
SEQRES   7 B  223  MSE LEU PHE PHE ALA ALA ALA GLY ILE ARG GLY GLU ASP          
SEQRES   8 B  223  LEU PHE ASP PRO SER LEU ARG LYS ARG THR GLY THR TYR          
SEQRES   9 B  223  PRO GLU TYR HIS SER GLY ASP ILE ASN ALA LEU HIS LEU          
SEQRES  10 B  223  SER TYR PHE ARG ARG LYS TYR ALA GLU GLU ARG ALA PHE          
SEQRES  11 B  223  ARG THR CYS ASN LEU ARG LYS SER ARG GLY PHE HIS LEU          
SEQRES  12 B  223  ALA ALA MSE GLY ALA ASP PRO LEU PRO SER PRO ASP ASP          
SEQRES  13 B  223  ALA ASP SER PRO TYR ARG MSE LYS LEU ILE LYS ASP LYS          
SEQRES  14 B  223  GLY TYR VAL HIS PHE SER ILE ASN GLY LEU PRO ILE LEU          
SEQRES  15 B  223  GLU TRP MSE ASP ASP GLY SER THR TYR GLY PRO VAL LEU          
SEQRES  16 B  223  THR LYS GLY LYS ILE GLY PHE ARG GLN MSE ALA PRO MSE          
SEQRES  17 B  223  LYS ALA VAL TYR ARG ASP PHE ALA VAL HIS GLN ALA VAL          
SEQRES  18 B  223  ARG ARG                                                      
SEQRES   1 C  223  SER ASN ALA MSE TYR LYS GLU GLY ALA CYS LEU TYR ARG          
SEQRES   2 C  223  ASN PRO LEU ARG SER LYS SER ASP VAL LYS ASP TRP ARG          
SEQRES   3 C  223  MSE GLU GLY GLY GLY GLN ILE SER PHE ASP ASP HIS SER          
SEQRES   4 C  223  LEU HIS LEU SER HIS VAL GLN ASP GLU ALA HIS PHE VAL          
SEQRES   5 C  223  PHE TRP CYS PRO GLU THR PHE PRO ASP GLY ILE ILE VAL          
SEQRES   6 C  223  THR TRP ASP PHE SER PRO ILE GLU GLN PRO GLY LEU CYS          
SEQRES   7 C  223  MSE LEU PHE PHE ALA ALA ALA GLY ILE ARG GLY GLU ASP          
SEQRES   8 C  223  LEU PHE ASP PRO SER LEU ARG LYS ARG THR GLY THR TYR          
SEQRES   9 C  223  PRO GLU TYR HIS SER GLY ASP ILE ASN ALA LEU HIS LEU          
SEQRES  10 C  223  SER TYR PHE ARG ARG LYS TYR ALA GLU GLU ARG ALA PHE          
SEQRES  11 C  223  ARG THR CYS ASN LEU ARG LYS SER ARG GLY PHE HIS LEU          
SEQRES  12 C  223  ALA ALA MSE GLY ALA ASP PRO LEU PRO SER PRO ASP ASP          
SEQRES  13 C  223  ALA ASP SER PRO TYR ARG MSE LYS LEU ILE LYS ASP LYS          
SEQRES  14 C  223  GLY TYR VAL HIS PHE SER ILE ASN GLY LEU PRO ILE LEU          
SEQRES  15 C  223  GLU TRP MSE ASP ASP GLY SER THR TYR GLY PRO VAL LEU          
SEQRES  16 C  223  THR LYS GLY LYS ILE GLY PHE ARG GLN MSE ALA PRO MSE          
SEQRES  17 C  223  LYS ALA VAL TYR ARG ASP PHE ALA VAL HIS GLN ALA VAL          
SEQRES  18 C  223  ARG ARG                                                      
SEQRES   1 D  223  SER ASN ALA MSE TYR LYS GLU GLY ALA CYS LEU TYR ARG          
SEQRES   2 D  223  ASN PRO LEU ARG SER LYS SER ASP VAL LYS ASP TRP ARG          
SEQRES   3 D  223  MSE GLU GLY GLY GLY GLN ILE SER PHE ASP ASP HIS SER          
SEQRES   4 D  223  LEU HIS LEU SER HIS VAL GLN ASP GLU ALA HIS PHE VAL          
SEQRES   5 D  223  PHE TRP CYS PRO GLU THR PHE PRO ASP GLY ILE ILE VAL          
SEQRES   6 D  223  THR TRP ASP PHE SER PRO ILE GLU GLN PRO GLY LEU CYS          
SEQRES   7 D  223  MSE LEU PHE PHE ALA ALA ALA GLY ILE ARG GLY GLU ASP          
SEQRES   8 D  223  LEU PHE ASP PRO SER LEU ARG LYS ARG THR GLY THR TYR          
SEQRES   9 D  223  PRO GLU TYR HIS SER GLY ASP ILE ASN ALA LEU HIS LEU          
SEQRES  10 D  223  SER TYR PHE ARG ARG LYS TYR ALA GLU GLU ARG ALA PHE          
SEQRES  11 D  223  ARG THR CYS ASN LEU ARG LYS SER ARG GLY PHE HIS LEU          
SEQRES  12 D  223  ALA ALA MSE GLY ALA ASP PRO LEU PRO SER PRO ASP ASP          
SEQRES  13 D  223  ALA ASP SER PRO TYR ARG MSE LYS LEU ILE LYS ASP LYS          
SEQRES  14 D  223  GLY TYR VAL HIS PHE SER ILE ASN GLY LEU PRO ILE LEU          
SEQRES  15 D  223  GLU TRP MSE ASP ASP GLY SER THR TYR GLY PRO VAL LEU          
SEQRES  16 D  223  THR LYS GLY LYS ILE GLY PHE ARG GLN MSE ALA PRO MSE          
SEQRES  17 D  223  LYS ALA VAL TYR ARG ASP PHE ALA VAL HIS GLN ALA VAL          
SEQRES  18 D  223  ARG ARG                                                      
MODRES 1OQ1 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A   24  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A   76  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A  143  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A  160  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A  182  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A  202  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE A  205  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B   24  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B   76  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B  143  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B  160  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B  182  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B  202  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE B  205  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C    1  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C   24  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C   76  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C  143  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C  160  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C  182  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C  202  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE C  205  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D    1  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D   24  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D   76  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D  143  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D  160  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D  182  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D  202  MET  SELENOMETHIONINE                                   
MODRES 1OQ1 MSE D  205  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  24       8                                                       
HET    MSE  A  76       8                                                       
HET    MSE  A 143       8                                                       
HET    MSE  A 160       8                                                       
HET    MSE  A 182       8                                                       
HET    MSE  A 202       8                                                       
HET    MSE  A 205       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  24       8                                                       
HET    MSE  B  76       8                                                       
HET    MSE  B 143       8                                                       
HET    MSE  B 160       8                                                       
HET    MSE  B 182       8                                                       
HET    MSE  B 202       8                                                       
HET    MSE  B 205       8                                                       
HET    MSE  C   1       8                                                       
HET    MSE  C  24       8                                                       
HET    MSE  C  76       8                                                       
HET    MSE  C 143       8                                                       
HET    MSE  C 160       8                                                       
HET    MSE  C 182       8                                                       
HET    MSE  C 202       8                                                       
HET    MSE  C 205       8                                                       
HET    MSE  D   1       8                                                       
HET    MSE  D  24       8                                                       
HET    MSE  D  76       8                                                       
HET    MSE  D 143       8                                                       
HET    MSE  D 160       8                                                       
HET    MSE  D 182       8                                                       
HET    MSE  D 202       8                                                       
HET    MSE  D 205       8                                                       
HET    ACY  A1001       4                                                       
HET    ACY  B1002       4                                                       
HET    ACY  C1003       4                                                       
HET    ACY  D1004       4                                                       
HET    GOL  A1005       6                                                       
HET    GOL  D1006       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ACY ACETIC ACID                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    32(C5 H11 N O2 SE)                                           
FORMUL   5  ACY    4(C2 H4 O2)                                                  
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  11  HOH   *999(H2 O)                                                    
HELIX    1   1 SER A   15  LYS A   20  5                                   6    
HELIX    2   2 PHE A   32  SER A   36  5                                   5    
HELIX    3   3 TYR A  101  SER A  106  1                                   6    
HELIX    4   4 TYR A  121  ALA A  126  1                                   6    
HELIX    5   5 SER A  150  ALA A  154  5                                   5    
HELIX    6   6 SER B   15  LYS B   20  5                                   6    
HELIX    7   7 TYR B  101  SER B  106  1                                   6    
HELIX    8   8 TYR B  121  ALA B  126  1                                   6    
HELIX    9   9 SER B  150  ALA B  154  5                                   5    
HELIX   10  10 SER C   15  LYS C   20  5                                   6    
HELIX   11  11 PHE C   32  SER C   36  5                                   5    
HELIX   12  12 TYR C  101  SER C  106  1                                   6    
HELIX   13  13 TYR C  121  ALA C  126  1                                   6    
HELIX   14  14 SER C  150  ALA C  154  5                                   5    
HELIX   15  15 SER D   15  LYS D   20  5                                   6    
HELIX   16  16 PHE D   32  SER D   36  5                                   5    
HELIX   17  17 TYR D  101  SER D  106  1                                   6    
HELIX   18  18 TYR D  121  ALA D  126  1                                   6    
HELIX   19  19 SER D  150  ALA D  154  5                                   5    
SHEET    1   A 6 LEU A 176  MSE A 182  0                                        
SHEET    2   A 6 TYR A 168  ILE A 173 -1  N  PHE A 171   O  ILE A 178           
SHEET    3   A 6 TYR A 158  ASP A 165 -1  N  ILE A 163   O  HIS A 170           
SHEET    4   A 6 ILE A  60  GLU A  70 -1  N  VAL A  62   O  LEU A 162           
SHEET    5   A 6 LYS A 206  ARG A 219 -1  O  ARG A 210   N  ASP A  65           
SHEET    6   A 6 TYR A   2  ASN A  11 -1  N  ASN A  11   O  PHE A 212           
SHEET    1   B 7 LEU A 176  MSE A 182  0                                        
SHEET    2   B 7 TYR A 168  ILE A 173 -1  N  PHE A 171   O  ILE A 178           
SHEET    3   B 7 TYR A 158  ASP A 165 -1  N  ILE A 163   O  HIS A 170           
SHEET    4   B 7 ILE A  60  GLU A  70 -1  N  VAL A  62   O  LEU A 162           
SHEET    5   B 7 LYS A 206  ARG A 219 -1  O  ARG A 210   N  ASP A  65           
SHEET    6   B 7 LEU A  37  HIS A  41 -1  N  LEU A  39   O  ALA A 207           
SHEET    7   B 7 GLY A  28  SER A  31 -1  N  SER A  31   O  HIS A  38           
SHEET    1   C 7 ARG A  23  GLY A  26  0                                        
SHEET    2   C 7 PHE A  48  TRP A  51 -1  O  TRP A  51   N  ARG A  23           
SHEET    3   C 7 LYS A 196  MSE A 202 -1  O  PHE A 199   N  PHE A  50           
SHEET    4   C 7 GLY A  73  GLY A  83 -1  N  MSE A  76   O  ARG A 200           
SHEET    5   C 7 ILE A 109  ARG A 119 -1  O  ASN A 110   N  ALA A  82           
SHEET    6   C 7 THR A 129  SER A 135 -1  O  SER A 135   N  ALA A 111           
SHEET    7   C 7 HIS A 139  ALA A 145 -1  O  GLY A 144   N  CYS A 130           
SHEET    1   D 6 LEU B 176  MSE B 182  0                                        
SHEET    2   D 6 TYR B 168  ILE B 173 -1  N  PHE B 171   O  ILE B 178           
SHEET    3   D 6 TYR B 158  ASP B 165 -1  N  ILE B 163   O  HIS B 170           
SHEET    4   D 6 ILE B  60  GLU B  70 -1  N  VAL B  62   O  LEU B 162           
SHEET    5   D 6 LYS B 206  ARG B 219 -1  O  ARG B 210   N  ASP B  65           
SHEET    6   D 6 TYR B   2  ASN B  11 -1  N  ASN B  11   O  PHE B 212           
SHEET    1   E 7 LEU B 176  MSE B 182  0                                        
SHEET    2   E 7 TYR B 168  ILE B 173 -1  N  PHE B 171   O  ILE B 178           
SHEET    3   E 7 TYR B 158  ASP B 165 -1  N  ILE B 163   O  HIS B 170           
SHEET    4   E 7 ILE B  60  GLU B  70 -1  N  VAL B  62   O  LEU B 162           
SHEET    5   E 7 LYS B 206  ARG B 219 -1  O  ARG B 210   N  ASP B  65           
SHEET    6   E 7 LEU B  37  HIS B  41 -1  N  LEU B  39   O  ALA B 207           
SHEET    7   E 7 GLY B  28  SER B  31 -1  N  GLN B  29   O  SER B  40           
SHEET    1   F 7 ARG B  23  GLY B  26  0                                        
SHEET    2   F 7 PHE B  48  TRP B  51 -1  O  TRP B  51   N  ARG B  23           
SHEET    3   F 7 LYS B 196  MSE B 202 -1  O  PHE B 199   N  PHE B  50           
SHEET    4   F 7 GLY B  73  GLY B  83 -1  N  MSE B  76   O  ARG B 200           
SHEET    5   F 7 ILE B 109  ARG B 119 -1  O  ASN B 110   N  ALA B  82           
SHEET    6   F 7 THR B 129  SER B 135 -1  O  SER B 135   N  ALA B 111           
SHEET    7   F 7 HIS B 139  ALA B 145 -1  O  GLY B 144   N  CYS B 130           
SHEET    1   G 6 LEU C 176  MSE C 182  0                                        
SHEET    2   G 6 TYR C 168  ILE C 173 -1  N  PHE C 171   O  ILE C 178           
SHEET    3   G 6 TYR C 158  ASP C 165 -1  N  ILE C 163   O  HIS C 170           
SHEET    4   G 6 ILE C  60  GLU C  70 -1  N  VAL C  62   O  LEU C 162           
SHEET    5   G 6 LYS C 206  ARG C 219 -1  O  ARG C 210   N  ASP C  65           
SHEET    6   G 6 TYR C   2  ASN C  11 -1  N  ASN C  11   O  PHE C 212           
SHEET    1   H 7 LEU C 176  MSE C 182  0                                        
SHEET    2   H 7 TYR C 168  ILE C 173 -1  N  PHE C 171   O  ILE C 178           
SHEET    3   H 7 TYR C 158  ASP C 165 -1  N  ILE C 163   O  HIS C 170           
SHEET    4   H 7 ILE C  60  GLU C  70 -1  N  VAL C  62   O  LEU C 162           
SHEET    5   H 7 LYS C 206  ARG C 219 -1  O  ARG C 210   N  ASP C  65           
SHEET    6   H 7 LEU C  37  HIS C  41 -1  N  LEU C  39   O  ALA C 207           
SHEET    7   H 7 GLY C  28  SER C  31 -1  N  SER C  31   O  HIS C  38           
SHEET    1   I 7 ARG C  23  GLY C  26  0                                        
SHEET    2   I 7 PHE C  48  TRP C  51 -1  O  TRP C  51   N  ARG C  23           
SHEET    3   I 7 LYS C 196  MSE C 202 -1  O  PHE C 199   N  PHE C  50           
SHEET    4   I 7 GLY C  73  GLY C  83 -1  N  MSE C  76   O  ARG C 200           
SHEET    5   I 7 ILE C 109  ARG C 119 -1  O  ASN C 110   N  ALA C  82           
SHEET    6   I 7 THR C 129  SER C 135 -1  O  SER C 135   N  ALA C 111           
SHEET    7   I 7 HIS C 139  ALA C 145 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   J 6 LEU D 176  MSE D 182  0                                        
SHEET    2   J 6 TYR D 168  ILE D 173 -1  N  PHE D 171   O  ILE D 178           
SHEET    3   J 6 TYR D 158  ASP D 165 -1  N  ILE D 163   O  HIS D 170           
SHEET    4   J 6 ILE D  60  GLU D  70 -1  N  VAL D  62   O  LEU D 162           
SHEET    5   J 6 LYS D 206  ARG D 219 -1  O  ARG D 210   N  ASP D  65           
SHEET    6   J 6 TYR D   2  ASN D  11 -1  N  ASN D  11   O  PHE D 212           
SHEET    1   K 7 LEU D 176  MSE D 182  0                                        
SHEET    2   K 7 TYR D 168  ILE D 173 -1  N  PHE D 171   O  ILE D 178           
SHEET    3   K 7 TYR D 158  ASP D 165 -1  N  ILE D 163   O  HIS D 170           
SHEET    4   K 7 ILE D  60  GLU D  70 -1  N  VAL D  62   O  LEU D 162           
SHEET    5   K 7 LYS D 206  ARG D 219 -1  O  ARG D 210   N  ASP D  65           
SHEET    6   K 7 LEU D  37  HIS D  41 -1  N  LEU D  39   O  ALA D 207           
SHEET    7   K 7 GLY D  28  SER D  31 -1  N  SER D  31   O  HIS D  38           
SHEET    1   L 7 ARG D  23  GLY D  26  0                                        
SHEET    2   L 7 PHE D  48  TRP D  51 -1  O  TRP D  51   N  ARG D  23           
SHEET    3   L 7 LYS D 196  MSE D 202 -1  O  PHE D 199   N  PHE D  50           
SHEET    4   L 7 GLY D  73  GLY D  83 -1  N  MSE D  76   O  ARG D 200           
SHEET    5   L 7 ILE D 109  ARG D 119 -1  O  ASN D 110   N  ALA D  82           
SHEET    6   L 7 THR D 129  SER D 135 -1  O  ARG D 133   N  HIS D 113           
SHEET    7   L 7 HIS D 139  ALA D 145 -1  O  GLY D 144   N  CYS D 130           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   TYR A   2     1555   1555  1.33  
LINK         C   ARG A  23                 N   MSE A  24     1555   1555  1.33  
LINK         C   MSE A  24                 N   GLU A  25     1555   1555  1.33  
LINK         C   CYS A  75                 N   MSE A  76     1555   1555  1.33  
LINK         C   MSE A  76                 N   LEU A  77     1555   1555  1.33  
LINK         C   ALA A 142                 N   MSE A 143     1555   1555  1.33  
LINK         C   MSE A 143                 N   GLY A 144     1555   1555  1.33  
LINK         C   ARG A 159                 N   MSE A 160     1555   1555  1.33  
LINK         C   MSE A 160                 N   LYS A 161     1555   1555  1.33  
LINK         C   TRP A 181                 N   MSE A 182     1555   1555  1.33  
LINK         C   MSE A 182                 N   ASP A 183     1555   1555  1.33  
LINK         C   GLN A 201                 N   MSE A 202     1555   1555  1.33  
LINK         C   MSE A 202                 N   ALA A 203     1555   1555  1.33  
LINK         C   PRO A 204                 N   MSE A 205     1555   1555  1.33  
LINK         C   MSE A 205                 N   LYS A 206     1555   1555  1.33  
LINK         C   MSE B   1                 N   TYR B   2     1555   1555  1.33  
LINK         C   ARG B  23                 N   MSE B  24     1555   1555  1.33  
LINK         C   MSE B  24                 N   GLU B  25     1555   1555  1.33  
LINK         C   CYS B  75                 N   MSE B  76     1555   1555  1.32  
LINK         C   MSE B  76                 N   LEU B  77     1555   1555  1.33  
LINK         C   ALA B 142                 N   MSE B 143     1555   1555  1.33  
LINK         C   MSE B 143                 N   GLY B 144     1555   1555  1.33  
LINK         C   ARG B 159                 N   MSE B 160     1555   1555  1.33  
LINK         C   MSE B 160                 N   LYS B 161     1555   1555  1.33  
LINK         C   TRP B 181                 N   MSE B 182     1555   1555  1.33  
LINK         C   MSE B 182                 N   ASP B 183     1555   1555  1.33  
LINK         C   GLN B 201                 N   MSE B 202     1555   1555  1.33  
LINK         C   MSE B 202                 N   ALA B 203     1555   1555  1.33  
LINK         C   PRO B 204                 N   MSE B 205     1555   1555  1.33  
LINK         C   MSE B 205                 N   LYS B 206     1555   1555  1.33  
LINK         C   ALA C   0                 N   MSE C   1     1555   1555  1.33  
LINK         C   MSE C   1                 N   TYR C   2     1555   1555  1.33  
LINK         C   ARG C  23                 N   MSE C  24     1555   1555  1.33  
LINK         C   MSE C  24                 N   GLU C  25     1555   1555  1.33  
LINK         C   CYS C  75                 N   MSE C  76     1555   1555  1.32  
LINK         C   MSE C  76                 N   LEU C  77     1555   1555  1.33  
LINK         C   ALA C 142                 N   MSE C 143     1555   1555  1.33  
LINK         C   MSE C 143                 N   GLY C 144     1555   1555  1.33  
LINK         C   ARG C 159                 N   MSE C 160     1555   1555  1.33  
LINK         C   MSE C 160                 N   LYS C 161     1555   1555  1.33  
LINK         C   TRP C 181                 N   MSE C 182     1555   1555  1.33  
LINK         C   MSE C 182                 N   ASP C 183     1555   1555  1.33  
LINK         C   GLN C 201                 N   MSE C 202     1555   1555  1.33  
LINK         C   MSE C 202                 N   ALA C 203     1555   1555  1.33  
LINK         C   PRO C 204                 N   MSE C 205     1555   1555  1.33  
LINK         C   MSE C 205                 N   LYS C 206     1555   1555  1.33  
LINK         C   ALA D   0                 N   MSE D   1     1555   1555  1.33  
LINK         C   MSE D   1                 N   TYR D   2     1555   1555  1.33  
LINK         C   ARG D  23                 N   MSE D  24     1555   1555  1.33  
LINK         C   MSE D  24                 N   GLU D  25     1555   1555  1.33  
LINK         C   CYS D  75                 N   MSE D  76     1555   1555  1.33  
LINK         C   MSE D  76                 N   LEU D  77     1555   1555  1.33  
LINK         C   ALA D 142                 N   MSE D 143     1555   1555  1.33  
LINK         C   MSE D 143                 N   GLY D 144     1555   1555  1.33  
LINK         C   ARG D 159                 N   MSE D 160     1555   1555  1.33  
LINK         C   MSE D 160                 N   LYS D 161     1555   1555  1.33  
LINK         C   TRP D 181                 N   MSE D 182     1555   1555  1.33  
LINK         C   MSE D 182                 N   ASP D 183     1555   1555  1.33  
LINK         C   GLN D 201                 N   MSE D 202     1555   1555  1.33  
LINK         C   MSE D 202                 N   ALA D 203     1555   1555  1.33  
LINK         C   PRO D 204                 N   MSE D 205     1555   1555  1.33  
LINK         C   MSE D 205                 N   LYS D 206     1555   1555  1.33  
CISPEP   1 GLN A   71    PRO A   72          0        -0.04                     
CISPEP   2 SER A  135    ARG A  136          0         0.33                     
CISPEP   3 SER A  156    PRO A  157          0         0.11                     
CISPEP   4 ALA A  203    PRO A  204          0         0.17                     
CISPEP   5 GLN B   71    PRO B   72          0        -0.05                     
CISPEP   6 SER B  135    ARG B  136          0        -0.21                     
CISPEP   7 SER B  156    PRO B  157          0         0.20                     
CISPEP   8 ALA B  203    PRO B  204          0         0.20                     
CISPEP   9 GLN C   71    PRO C   72          0        -0.22                     
CISPEP  10 SER C  135    ARG C  136          0         0.48                     
CISPEP  11 SER C  156    PRO C  157          0        -0.18                     
CISPEP  12 ALA C  203    PRO C  204          0         0.09                     
CISPEP  13 GLN D   71    PRO D   72          0        -0.22                     
CISPEP  14 SER D  135    ARG D  136          0         0.43                     
CISPEP  15 SER D  156    PRO D  157          0         0.17                     
CISPEP  16 ALA D  203    PRO D  204          0         0.21                     
SITE     1 AC1  6 MSE A  76  TYR A 101  ARG A 200  MSE A 202                    
SITE     2 AC1  6 HOH A1078  HOH A1150                                          
SITE     1 AC2  5 MSE B  76  TYR B 101  ARG B 200  MSE B 202                    
SITE     2 AC2  5 HOH B1109                                                     
SITE     1 AC3  5 MSE C  76  TYR C 101  ARG C 200  MSE C 202                    
SITE     2 AC3  5 HOH C1090                                                     
SITE     1 AC4  6 MSE D  76  TYR D 101  ARG D 200  MSE D 202                    
SITE     2 AC4  6 HOH D1099  HOH D1169                                          
SITE     1 AC5  5 HIS A  41  GLN A  43  ASP A  44  HOH A1042                    
SITE     2 AC5  5 HOH A1187                                                     
SITE     1 AC6  5 HIS D  41  GLN D  43  ASP D  44  HOH D1055                    
SITE     2 AC6  5 HOH D1104                                                     
CRYST1   74.839   44.616  139.391  90.00 100.34  90.00 P 1 21 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      0.013362  0.000000  0.002438        0.00000                         
SCALE2      0.000000  0.022413  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007292        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system