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Database: PDB
Entry: 2AP9
LinkDB: 2AP9
Original site: 2AP9 
HEADER    SIGNALING PROTEIN,TRANSFERASE           15-AUG-05   2AP9              
TITLE     CRYSTAL STRUCTURE OF ACETYLGLUTAMATE KINASE FROM MYCOBACTERIUM        
TITLE    2 TUBERCULOSIS CDC1551                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLGLUTAMATE KINASE;                                    
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: ACETYLGLUTAMATE KINASE;                                    
COMPND   5 SYNONYM: NAG KINASE; AGK; N-ACETYL-L-GLUTAMATE 5-PHOSPHOTRANSFERASE; 
COMPND   6 EC: 2.7.2.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83331;                                               
SOURCE   4 STRAIN: CDC1551;                                                     
SOURCE   5 GENE: ARGB, RV1654, MT1692;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: B834, DE3;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET T7                                    
KEYWDS    STRUCTURAL GENOMICS; PROTEIN STRUCTURE INITIATIVE; NYSGXRC; T1702;    
KEYWDS   2 ACETYLGLUTAMATE KINASE; PSI; NEW YORK SGX RESEARCH CENTER FOR        
KEYWDS   3 STRUCTURAL GENOMICS, SIGNALING PROTEIN, TRANSFERASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.RAJASHANKAR,R.KNIEWEL,K.LEE,C.D.LIMA,S.K.BURLEY,NEW YORK SGX      
AUTHOR   2 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                    
REVDAT   4   03-FEB-21 2AP9    1       AUTHOR REMARK SEQADV LINK                
REVDAT   3   13-JUL-11 2AP9    1       VERSN                                    
REVDAT   2   24-FEB-09 2AP9    1       VERSN                                    
REVDAT   1   30-AUG-05 2AP9    0                                                
JRNL        AUTH   K.R.RAJASHANKAR,R.KNIEWEL,K.LEE,C.D.LIMA                     
JRNL        TITL   CRYSTAL STRUCTURE OF ACETYLGLUTAMATE KINASE FROM             
JRNL        TITL 2 MYCOBACTERIUM TUBERCULOSIS CDC1551                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 178264.750                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 88420                          
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) : 0.258                           
REMARK   3   FREE R VALUE                     : 0.284                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4316                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.98                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 56.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8966                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4640                       
REMARK   3   BIN FREE R VALUE                    : 0.4490                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 423                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 13025                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 113                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 81.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.89000                                              
REMARK   3    B22 (A**2) : 22.62000                                             
REMARK   3    B33 (A**2) : -27.50000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.50                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.95                            
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) : 0.53                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.82                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.850                           
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) : 1.300 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.350 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.680 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.650 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.30                                                 
REMARK   3   BSOL        : 31.49                                                
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: CERTAIN REGIONS OF THE MODEL DO NOT       
REMARK   3  HAVE WELL DEFINED ELECTRON DENSITY. THESE ARE RESIDUES 143-152      
REMARK   3  AND 222-231. TWO SOLVENT PEAKS HAVE BEEN REFINED AS MAGNESIUM       
REMARK   3  IONS, AND ONE SOLVENT PEAK HAS BE REFINED AS A NICKLE ION (AS IT    
REMARK   3  IS BOUND TO HIS6 RAG).                                              
REMARK   4                                                                      
REMARK   4 2AP9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000034157.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-APR-05                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.975                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : VERTICAL FOCUSSING MIRROR DOWN     
REMARK 200                                   STREAM OF MONOCHROMATOR            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 94360                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -1.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 3.170                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 63.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.49700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.030                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: MODEL BUILT BASED ON THE EXPERIMENTAL ELECTRON       
REMARK 200  DENSITY MAP                                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 3% PEG 6000, 0.1M TRIS PH 8.5, 0.1M      
REMARK 280  POTASSIUM CHLORIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       44.01200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       97.29050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.49800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       97.29050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.01200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.49800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: POLYPEPTIDE CHAIN A, B, C, D, E AND F TOGETHER FORM A        
REMARK 300 BIOLOGICAL ASSEMBLY                                                  
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16730 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 67680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, 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 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     GLY B   298                                                      
REMARK 465     HIS B   299                                                      
REMARK 465     HIS B   300                                                      
REMARK 465     HIS B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     HIS B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     GLY C   298                                                      
REMARK 465     HIS C   299                                                      
REMARK 465     HIS C   300                                                      
REMARK 465     HIS C   301                                                      
REMARK 465     HIS C   302                                                      
REMARK 465     HIS C   303                                                      
REMARK 465     HIS C   304                                                      
REMARK 465     GLY D   298                                                      
REMARK 465     HIS D   299                                                      
REMARK 465     HIS D   300                                                      
REMARK 465     HIS D   301                                                      
REMARK 465     HIS D   302                                                      
REMARK 465     HIS D   303                                                      
REMARK 465     HIS D   304                                                      
REMARK 465     HIS E   301                                                      
REMARK 465     HIS E   302                                                      
REMARK 465     HIS E   303                                                      
REMARK 465     HIS E   304                                                      
REMARK 465     GLY F   298                                                      
REMARK 465     HIS F   299                                                      
REMARK 465     HIS F   300                                                      
REMARK 465     HIS F   301                                                      
REMARK 465     HIS F   302                                                      
REMARK 465     HIS F   303                                                      
REMARK 465     HIS F   304                                                      
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   C    TRP C   224     CD   PRO C   225              1.78            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 146   N   -  CA  -  C   ANGL. DEV. = -23.8 DEGREES          
REMARK 500    TRP B 224   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    PRO C 225   C   -  N   -  CA  ANGL. DEV. =  60.4 DEGREES          
REMARK 500    PRO C 225   C   -  N   -  CD  ANGL. DEV. = -50.6 DEGREES          
REMARK 500    PRO C 225   CA  -  N   -  CD  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    PRO D 225   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    PRO D 225   N   -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    GLY D 288   N   -  CA  -  C   ANGL. DEV. =  15.6 DEGREES          
REMARK 500    TRP E 224   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ASP E 226   N   -  CA  -  C   ANGL. DEV. =  20.7 DEGREES          
REMARK 500    ASP E 228   N   -  CA  -  C   ANGL. DEV. =  21.8 DEGREES          
REMARK 500    PHE F  88   N   -  CA  -  C   ANGL. DEV. =  17.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A   8       30.09    -84.89                                   
REMARK 500    THR A  43      -70.12    -57.02                                   
REMARK 500    VAL A  94       98.12     62.26                                   
REMARK 500    GLN A 110      -67.19   -135.52                                   
REMARK 500    ASN A 120        8.88    -65.86                                   
REMARK 500    TYR A 125      -68.79   -104.70                                   
REMARK 500    ALA A 134       18.58     53.20                                   
REMARK 500    VAL A 146      -91.56    161.61                                   
REMARK 500    ASP A 147      -21.68   -144.38                                   
REMARK 500    VAL A 149      -14.49     65.43                                   
REMARK 500    ALA A 150       29.59    -71.31                                   
REMARK 500    ASP A 160      -74.06    -88.25                                   
REMARK 500    THR A 181       79.24    -48.04                                   
REMARK 500    ASP A 216       32.45    -94.00                                   
REMARK 500    ARG A 223       80.03   -157.94                                   
REMARK 500    TRP A 224      -68.61    -11.88                                   
REMARK 500    PRO A 244       12.93    -69.32                                   
REMARK 500    THR A 245       41.20   -144.58                                   
REMARK 500    VAL A 265      109.65    -58.63                                   
REMARK 500    ASP A 286       31.77    -85.66                                   
REMARK 500    GLU B  20       -6.05    -55.57                                   
REMARK 500    THR B  43      -70.12    -57.62                                   
REMARK 500    VAL B  94       83.39     55.12                                   
REMARK 500    THR B  95       91.97    -65.97                                   
REMARK 500    GLN B 110      -67.72   -136.93                                   
REMARK 500    ASN B 120        8.63    -65.53                                   
REMARK 500    TYR B 125      -68.14   -104.61                                   
REMARK 500    ALA B 134       18.42     53.80                                   
REMARK 500    VAL B 146       59.42   -118.78                                   
REMARK 500    VAL B 149      -31.02    -35.41                                   
REMARK 500    ALA B 150       75.85    -57.20                                   
REMARK 500    ILE B 153       31.87    -68.71                                   
REMARK 500    ASP B 160      -74.90    -87.57                                   
REMARK 500    THR B 181       77.55    -47.84                                   
REMARK 500    ASP B 216       31.72    -93.55                                   
REMARK 500    TYR B 221       99.11    -69.37                                   
REMARK 500    ARG B 223      111.57     60.39                                   
REMARK 500    TRP B 224      130.62      9.77                                   
REMARK 500    PRO B 225      101.41     -1.01                                   
REMARK 500    ASP B 226      104.91   -171.35                                   
REMARK 500    ARG B 227        1.23    -67.68                                   
REMARK 500    SER B 229       48.37    -79.02                                   
REMARK 500    VAL B 231      174.58    -58.75                                   
REMARK 500    GLU B 233       75.81   -163.07                                   
REMARK 500    GLN B 241       38.74    -81.84                                   
REMARK 500    ASP B 286       44.61    -77.02                                   
REMARK 500    THR C  43      -70.19    -58.12                                   
REMARK 500    GLN C 110      -67.03   -136.64                                   
REMARK 500    ASN C 120        8.85    -65.60                                   
REMARK 500    TYR C 125      -69.32   -103.88                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     126 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 235   OD2                                                    
REMARK 620 2 HIS A 301   O    74.1                                              
REMARK 620 3 HIS A 304   O   142.3  70.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1003                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T1702   RELATED DB: TARGETDB                     
DBREF  2AP9 A    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
DBREF  2AP9 B    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
DBREF  2AP9 C    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
DBREF  2AP9 D    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
DBREF  2AP9 E    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
DBREF  2AP9 F    6   296  UNP    P0A4Y6   ARGB_MYCTU       4    294             
SEQADV 2AP9 MSE A   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE A   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE A   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE A  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE A  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE A  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU A  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE A  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU A  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY A  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS A  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 MSE B   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE B   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE B   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE B  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE B  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE B  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU B  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE B  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU B  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY B  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS B  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 MSE C   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE C   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE C   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE C  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE C  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE C  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU C  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE C  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU C  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY C  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS C  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 MSE D   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE D   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE D   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE D  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE D  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE D  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU D  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE D  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU D  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY D  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS D  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 MSE E   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE E   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE E   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE E  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE E  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE E  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU E  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE E  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU E  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY E  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS E  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 MSE F   42  UNP  P0A4Y6    MET    40 MODIFIED RESIDUE               
SEQADV 2AP9 MSE F   55  UNP  P0A4Y6    MET    53 MODIFIED RESIDUE               
SEQADV 2AP9 MSE F   78  UNP  P0A4Y6    MET    76 MODIFIED RESIDUE               
SEQADV 2AP9 MSE F  105  UNP  P0A4Y6    MET   103 MODIFIED RESIDUE               
SEQADV 2AP9 MSE F  167  UNP  P0A4Y6    MET   165 MODIFIED RESIDUE               
SEQADV 2AP9 MSE F  213  UNP  P0A4Y6    MET   211 MODIFIED RESIDUE               
SEQADV 2AP9 LEU F  248  UNP  P0A4Y6    SER   246 CONFLICT                       
SEQADV 2AP9 MSE F  250  UNP  P0A4Y6    MET   248 MODIFIED RESIDUE               
SEQADV 2AP9 GLU F  297  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 GLY F  298  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  299  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  300  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  301  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  302  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  303  UNP  P0A4Y6              EXPRESSION TAG                 
SEQADV 2AP9 HIS F  304  UNP  P0A4Y6              EXPRESSION TAG                 
SEQRES   1 A  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 A  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 A  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 A  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 A  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 A  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 A  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 A  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 A  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 A  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 A  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 A  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 A  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 A  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 A  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 A  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 A  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 A  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 A  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 A  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 A  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 A  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 A  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 B  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 B  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 B  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 B  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 B  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 B  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 B  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 B  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 B  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 B  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 B  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 B  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 B  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 B  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 B  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 B  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 B  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 B  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 B  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 B  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 B  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 B  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 C  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 C  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 C  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 C  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 C  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 C  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 C  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 C  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 C  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 C  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 C  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 C  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 C  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 C  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 C  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 C  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 C  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 C  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 C  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 C  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 C  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 C  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 D  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 D  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 D  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 D  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 D  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 D  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 D  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 D  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 D  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 D  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 D  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 D  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 D  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 D  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 D  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 D  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 D  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 D  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 D  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 D  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 D  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 D  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 E  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 E  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 E  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 E  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 E  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 E  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 E  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 E  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 E  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 E  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 E  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 E  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 E  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 E  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 E  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 E  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 E  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 E  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 E  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 E  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 E  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 E  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 E  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 F  299  ILE GLU ALA LEU PRO THR HIS ILE LYS ALA GLN VAL LEU          
SEQRES   2 F  299  ALA GLU ALA LEU PRO TRP LEU LYS GLN LEU HIS GLY LYS          
SEQRES   3 F  299  VAL VAL VAL VAL LYS TYR GLY GLY ASN ALA MSE THR ASP          
SEQRES   4 F  299  ASP THR LEU ARG ARG ALA PHE ALA ALA ASP MSE ALA PHE          
SEQRES   5 F  299  LEU ARG ASN CYS GLY ILE HIS PRO VAL VAL VAL HIS GLY          
SEQRES   6 F  299  GLY GLY PRO GLN ILE THR ALA MSE LEU ARG ARG LEU GLY          
SEQRES   7 F  299  ILE GLU GLY ASP PHE LYS GLY GLY PHE ARG VAL THR THR          
SEQRES   8 F  299  PRO GLU VAL LEU ASP VAL ALA ARG MSE VAL LEU PHE GLY          
SEQRES   9 F  299  GLN VAL GLY ARG GLU LEU VAL ASN LEU ILE ASN ALA HIS          
SEQRES  10 F  299  GLY PRO TYR ALA VAL GLY ILE THR GLY GLU ASP ALA GLN          
SEQRES  11 F  299  LEU PHE THR ALA VAL ARG ARG SER VAL THR VAL ASP GLY          
SEQRES  12 F  299  VAL ALA THR ASP ILE GLY LEU VAL GLY ASP VAL ASP GLN          
SEQRES  13 F  299  VAL ASN THR ALA ALA MSE LEU ASP LEU VAL ALA ALA GLY          
SEQRES  14 F  299  ARG ILE PRO VAL VAL SER THR LEU ALA PRO ASP ALA ASP          
SEQRES  15 F  299  GLY VAL VAL HIS ASN ILE ASN ALA ASP THR ALA ALA ALA          
SEQRES  16 F  299  ALA VAL ALA GLU ALA LEU GLY ALA GLU LYS LEU LEU MSE          
SEQRES  17 F  299  LEU THR ASP ILE ASP GLY LEU TYR THR ARG TRP PRO ASP          
SEQRES  18 F  299  ARG ASP SER LEU VAL SER GLU ILE ASP THR GLY THR LEU          
SEQRES  19 F  299  ALA GLN LEU LEU PRO THR LEU GLU LEU GLY MSE VAL PRO          
SEQRES  20 F  299  LYS VAL GLU ALA CYS LEU ARG ALA VAL ILE GLY GLY VAL          
SEQRES  21 F  299  PRO SER ALA HIS ILE ILE ASP GLY ARG VAL THR HIS CYS          
SEQRES  22 F  299  VAL LEU VAL GLU LEU PHE THR ASP ALA GLY THR GLY THR          
SEQRES  23 F  299  LYS VAL VAL ARG GLY GLU GLY HIS HIS HIS HIS HIS HIS          
MODRES 2AP9 MSE A   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE A  250  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE B  250  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE C  250  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE D  250  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE E  250  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F   42  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F   55  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F   78  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F  105  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F  167  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F  213  MET  SELENOMETHIONINE                                   
MODRES 2AP9 MSE F  250  MET  SELENOMETHIONINE                                   
HET    MSE  A  42       8                                                       
HET    MSE  A  55       8                                                       
HET    MSE  A  78       8                                                       
HET    MSE  A 105       8                                                       
HET    MSE  A 167       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 250       8                                                       
HET    MSE  B  42       8                                                       
HET    MSE  B  55       8                                                       
HET    MSE  B  78       8                                                       
HET    MSE  B 105       8                                                       
HET    MSE  B 167       8                                                       
HET    MSE  B 213       8                                                       
HET    MSE  B 250       8                                                       
HET    MSE  C  42       8                                                       
HET    MSE  C  55       8                                                       
HET    MSE  C  78       8                                                       
HET    MSE  C 105       8                                                       
HET    MSE  C 167       8                                                       
HET    MSE  C 213       8                                                       
HET    MSE  C 250       8                                                       
HET    MSE  D  42       8                                                       
HET    MSE  D  55       8                                                       
HET    MSE  D  78       8                                                       
HET    MSE  D 105       8                                                       
HET    MSE  D 167       8                                                       
HET    MSE  D 213       8                                                       
HET    MSE  D 250       8                                                       
HET    MSE  E  42       8                                                       
HET    MSE  E  55       8                                                       
HET    MSE  E  78       8                                                       
HET    MSE  E 105       8                                                       
HET    MSE  E 167       8                                                       
HET    MSE  E 213       8                                                       
HET    MSE  E 250       8                                                       
HET    MSE  F  42       8                                                       
HET    MSE  F  55       8                                                       
HET    MSE  F  78       8                                                       
HET    MSE  F 105       8                                                       
HET    MSE  F 167       8                                                       
HET    MSE  F 213       8                                                       
HET    MSE  F 250       8                                                       
HET     MG  A1002       1                                                       
HET     NI  A1003       1                                                       
HET     MG  D1001       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   1  MSE    42(C5 H11 N O2 SE)                                           
FORMUL   7   MG    2(MG 2+)                                                     
FORMUL   8   NI    NI 2+                                                        
FORMUL  10  HOH   *113(H2 O)                                                    
HELIX    1   1 PRO A   10  HIS A   29  1                                  20    
HELIX    2   2 GLY A   39  ASP A   44  1                                   6    
HELIX    3   3 ASP A   44  ASN A   60  1                                  17    
HELIX    4   4 GLY A   72  GLY A   83  1                                  12    
HELIX    5   5 THR A   96  GLN A  110  1                                  15    
HELIX    6   6 GLN A  110  ASN A  120  1                                  11    
HELIX    7   7 GLU A  132  GLN A  135  5                                   4    
HELIX    8   8 ASN A  163  ALA A  173  1                                  11    
HELIX    9   9 ASN A  194  LEU A  206  1                                  13    
HELIX   10  10 THR A  236  LEU A  243  1                                   8    
HELIX   11  11 PRO A  244  LEU A  246  5                                   3    
HELIX   12  12 MSE A  250  GLY A  264  1                                  15    
HELIX   13  13 HIS A  277  THR A  285  1                                   9    
HELIX   14  14 GLY A  298  HIS A  304  1                                   7    
HELIX   15  15 PRO B   10  GLU B   20  1                                  11    
HELIX   16  16 ALA B   21  HIS B   29  1                                   9    
HELIX   17  17 GLY B   39  ASP B   44  1                                   6    
HELIX   18  18 ASP B   44  ASN B   60  1                                  17    
HELIX   19  19 GLY B   72  LEU B   82  1                                  11    
HELIX   20  20 THR B   96  GLN B  110  1                                  15    
HELIX   21  21 GLN B  110  ASN B  120  1                                  11    
HELIX   22  22 GLU B  132  GLN B  135  5                                   4    
HELIX   23  23 ASN B  163  ALA B  173  1                                  11    
HELIX   24  24 ASN B  194  LEU B  206  1                                  13    
HELIX   25  25 LEU B  239  LEU B  246  5                                   8    
HELIX   26  26 MSE B  250  ILE B  262  1                                  13    
HELIX   27  27 HIS B  277  THR B  285  1                                   9    
HELIX   28  28 PRO C   10  GLU C   20  1                                  11    
HELIX   29  29 ALA C   21  HIS C   29  1                                   9    
HELIX   30  30 GLY C   39  ASP C   44  1                                   6    
HELIX   31  31 ASP C   44  ASN C   60  1                                  17    
HELIX   32  32 GLY C   72  LEU C   82  1                                  11    
HELIX   33  33 THR C   96  GLN C  110  1                                  15    
HELIX   34  34 GLN C  110  ASN C  120  1                                  11    
HELIX   35  35 GLU C  132  GLN C  135  5                                   4    
HELIX   36  36 ASN C  163  ALA C  173  1                                  11    
HELIX   37  37 ASN C  194  LEU C  206  1                                  13    
HELIX   38  38 THR C  236  LEU C  242  1                                   7    
HELIX   39  39 GLU C  247  GLY C  249  5                                   3    
HELIX   40  40 MSE C  250  ILE C  262  1                                  13    
HELIX   41  41 HIS C  277  THR C  285  1                                   9    
HELIX   42  42 PRO D   10  GLU D   20  1                                  11    
HELIX   43  43 ALA D   21  HIS D   29  1                                   9    
HELIX   44  44 GLY D   39  ASP D   44  1                                   6    
HELIX   45  45 ASP D   44  ASN D   60  1                                  17    
HELIX   46  46 GLY D   72  GLY D   83  1                                  12    
HELIX   47  47 THR D   96  GLN D  110  1                                  15    
HELIX   48  48 GLN D  110  ASN D  120  1                                  11    
HELIX   49  49 GLU D  132  GLN D  135  5                                   4    
HELIX   50  50 ASN D  163  ALA D  173  1                                  11    
HELIX   51  51 ASN D  194  LEU D  206  1                                  13    
HELIX   52  52 LEU D  242  LEU D  246  5                                   5    
HELIX   53  53 MSE D  250  GLY D  264  1                                  15    
HELIX   54  54 HIS D  277  PHE D  284  1                                   8    
HELIX   55  55 PRO E   10  GLU E   20  1                                  11    
HELIX   56  56 ALA E   21  HIS E   29  1                                   9    
HELIX   57  57 GLY E   39  ASP E   44  1                                   6    
HELIX   58  58 ASP E   44  ASN E   60  1                                  17    
HELIX   59  59 GLY E   72  LEU E   82  1                                  11    
HELIX   60  60 THR E   96  GLN E  110  1                                  15    
HELIX   61  61 GLN E  110  ASN E  120  1                                  11    
HELIX   62  62 GLU E  132  GLN E  135  5                                   4    
HELIX   63  63 ASN E  163  ALA E  173  1                                  11    
HELIX   64  64 ASN E  194  LEU E  206  1                                  13    
HELIX   65  65 GLU E  247  GLY E  249  5                                   3    
HELIX   66  66 MSE E  250  ILE E  262  1                                  13    
HELIX   67  67 HIS E  277  THR E  285  1                                   9    
HELIX   68  68 PRO F   10  GLU F   20  1                                  11    
HELIX   69  69 ALA F   21  HIS F   29  1                                   9    
HELIX   70  70 GLY F   39  ASP F   44  1                                   6    
HELIX   71  71 ASP F   44  ASN F   60  1                                  17    
HELIX   72  72 GLY F   72  GLY F   83  1                                  12    
HELIX   73  73 THR F   96  GLN F  110  1                                  15    
HELIX   74  74 GLN F  110  ASN F  120  1                                  11    
HELIX   75  75 GLU F  132  GLN F  135  5                                   4    
HELIX   76  76 ASN F  163  ALA F  173  1                                  11    
HELIX   77  77 ASN F  194  LEU F  206  1                                  13    
HELIX   78  78 GLY F  237  LEU F  242  1                                   6    
HELIX   79  79 MSE F  250  GLY F  263  1                                  14    
HELIX   80  80 HIS F  277  THR F  285  1                                   9    
SHEET    1   A 8 ALA A 126  THR A 130  0                                        
SHEET    2   A 8 ILE A 176  SER A 180  1  O  VAL A 178   N  VAL A 127           
SHEET    3   A 8 HIS A  64  HIS A  69  1  N  VAL A  67   O  VAL A 179           
SHEET    4   A 8 VAL A  32  TYR A  37  1  N  VAL A  35   O  VAL A  68           
SHEET    5   A 8 LYS A 210  THR A 215  1  O  LEU A 212   N  VAL A  34           
SHEET    6   A 8 SER A 267  ASP A 272  1  O  HIS A 269   N  LEU A 211           
SHEET    7   A 8 THR A 291  VAL A 294 -1  O  VAL A 293   N  ALA A 268           
SHEET    8   A 8 GLU A 233  ASP A 235  1  N  ILE A 234   O  LYS A 292           
SHEET    1   B 4 PHE A 137  ARG A 141  0                                        
SHEET    2   B 4 VAL A 156  VAL A 162 -1  O  ASP A 160   N  THR A 138           
SHEET    3   B 4 VAL A 190  ILE A 193  1  O  ASN A 192   N  GLY A 157           
SHEET    4   B 4 LEU A 182  PRO A 184 -1  N  ALA A 183   O  HIS A 191           
SHEET    1   C 2 LEU A 220  TYR A 221  0                                        
SHEET    2   C 2 LEU A 230  VAL A 231 -1  O  VAL A 231   N  LEU A 220           
SHEET    1   D 8 ALA B 126  THR B 130  0                                        
SHEET    2   D 8 ILE B 176  SER B 180  1  O  VAL B 178   N  VAL B 127           
SHEET    3   D 8 HIS B  64  HIS B  69  1  N  VAL B  67   O  VAL B 179           
SHEET    4   D 8 VAL B  32  TYR B  37  1  N  VAL B  35   O  VAL B  68           
SHEET    5   D 8 LYS B 210  THR B 215  1  O  LEU B 212   N  VAL B  34           
SHEET    6   D 8 SER B 267  ASP B 272  1  O  HIS B 269   N  LEU B 211           
SHEET    7   D 8 THR B 291  VAL B 294 -1  O  THR B 291   N  ILE B 270           
SHEET    8   D 8 GLU B 233  ASP B 235  1  N  ILE B 234   O  LYS B 292           
SHEET    1   E 4 PHE B 137  ARG B 141  0                                        
SHEET    2   E 4 VAL B 156  VAL B 162 -1  O  ASP B 160   N  THR B 138           
SHEET    3   E 4 HIS B 191  ILE B 193  1  O  ASN B 192   N  GLY B 157           
SHEET    4   E 4 LEU B 182  ALA B 183 -1  N  ALA B 183   O  HIS B 191           
SHEET    1   F 8 ALA C 126  THR C 130  0                                        
SHEET    2   F 8 ILE C 176  SER C 180  1  O  VAL C 178   N  VAL C 127           
SHEET    3   F 8 HIS C  64  HIS C  69  1  N  VAL C  67   O  VAL C 179           
SHEET    4   F 8 VAL C  32  TYR C  37  1  N  VAL C  35   O  VAL C  68           
SHEET    5   F 8 LYS C 210  THR C 215  1  O  LEU C 212   N  VAL C  34           
SHEET    6   F 8 SER C 267  ASP C 272  1  O  HIS C 269   N  LEU C 211           
SHEET    7   F 8 LYS C 292  VAL C 294 -1  O  VAL C 293   N  ALA C 268           
SHEET    8   F 8 GLU C 233  ASP C 235  1  N  ILE C 234   O  LYS C 292           
SHEET    1   G 4 PHE C 137  ARG C 141  0                                        
SHEET    2   G 4 VAL C 156  VAL C 162 -1  O  ASP C 160   N  THR C 138           
SHEET    3   G 4 HIS C 191  ILE C 193  1  O  ASN C 192   N  GLY C 157           
SHEET    4   G 4 LEU C 182  ALA C 183 -1  N  ALA C 183   O  HIS C 191           
SHEET    1   H 8 ALA D 126  ILE D 129  0                                        
SHEET    2   H 8 ILE D 176  SER D 180  1  O  VAL D 178   N  VAL D 127           
SHEET    3   H 8 HIS D  64  HIS D  69  1  N  VAL D  67   O  VAL D 179           
SHEET    4   H 8 VAL D  32  TYR D  37  1  N  VAL D  33   O  HIS D  64           
SHEET    5   H 8 LYS D 210  THR D 215  1  O  LEU D 212   N  LYS D  36           
SHEET    6   H 8 SER D 267  ASP D 272  1  O  HIS D 269   N  MSE D 213           
SHEET    7   H 8 THR D 291  VAL D 294 -1  O  VAL D 293   N  ALA D 268           
SHEET    8   H 8 ILE D 234  ASP D 235  1  N  ILE D 234   O  VAL D 294           
SHEET    1   I 2 PHE D  88  LYS D  89  0                                        
SHEET    2   I 2 PHE D  92  ARG D  93 -1  O  PHE D  92   N  LYS D  89           
SHEET    1   J 4 PHE D 137  THR D 145  0                                        
SHEET    2   J 4 ALA D 150  VAL D 162 -1  O  ASP D 158   N  VAL D 140           
SHEET    3   J 4 VAL D 190  ILE D 193  1  O  ASN D 192   N  LEU D 155           
SHEET    4   J 4 LEU D 182  PRO D 184 -1  N  ALA D 183   O  HIS D 191           
SHEET    1   K 7 ALA E 126  THR E 130  0                                        
SHEET    2   K 7 ILE E 176  SER E 180  1  O  VAL E 178   N  VAL E 127           
SHEET    3   K 7 HIS E  64  HIS E  69  1  N  VAL E  67   O  VAL E 179           
SHEET    4   K 7 VAL E  32  TYR E  37  1  N  VAL E  35   O  VAL E  68           
SHEET    5   K 7 LYS E 210  THR E 215  1  O  LEU E 212   N  VAL E  34           
SHEET    6   K 7 SER E 267  ASP E 272  1  O  HIS E 269   N  LEU E 211           
SHEET    7   K 7 THR E 291  VAL E 293 -1  O  THR E 291   N  ILE E 270           
SHEET    1   L 4 PHE E 137  ARG E 141  0                                        
SHEET    2   L 4 VAL E 156  VAL E 162 -1  O  ASP E 160   N  THR E 138           
SHEET    3   L 4 HIS E 191  ILE E 193  1  O  ASN E 192   N  GLY E 157           
SHEET    4   L 4 LEU E 182  ALA E 183 -1  N  ALA E 183   O  HIS E 191           
SHEET    1   M 8 ALA F 126  THR F 130  0                                        
SHEET    2   M 8 ILE F 176  SER F 180  1  O  VAL F 178   N  VAL F 127           
SHEET    3   M 8 HIS F  64  HIS F  69  1  N  VAL F  67   O  VAL F 179           
SHEET    4   M 8 VAL F  32  TYR F  37  1  N  VAL F  35   O  VAL F  68           
SHEET    5   M 8 LYS F 210  THR F 215  1  O  LEU F 212   N  VAL F  34           
SHEET    6   M 8 SER F 267  ASP F 272  1  O  HIS F 269   N  LEU F 211           
SHEET    7   M 8 GLY F 290  VAL F 294 -1  O  VAL F 293   N  ALA F 268           
SHEET    8   M 8 GLU F 233  ASP F 235  1  N  ILE F 234   O  LYS F 292           
SHEET    1   N 4 PHE F 137  ARG F 141  0                                        
SHEET    2   N 4 VAL F 156  VAL F 162 -1  O  ASP F 160   N  THR F 138           
SHEET    3   N 4 VAL F 190  ILE F 193  1  O  ASN F 192   N  GLY F 157           
SHEET    4   N 4 LEU F 182  PRO F 184 -1  N  ALA F 183   O  HIS F 191           
LINK         C   ALA A  41                 N   MSE A  42     1555   1555  1.33  
LINK         C   MSE A  42                 N   THR A  43     1555   1555  1.33  
LINK         C   ASP A  54                 N   MSE A  55     1555   1555  1.33  
LINK         C   MSE A  55                 N   ALA A  56     1555   1555  1.33  
LINK         C   ALA A  77                 N   MSE A  78     1555   1555  1.33  
LINK         C   MSE A  78                 N   LEU A  79     1555   1555  1.33  
LINK         C   ARG A 104                 N   MSE A 105     1555   1555  1.33  
LINK         C   MSE A 105                 N   VAL A 106     1555   1555  1.33  
LINK         C   ALA A 166                 N   MSE A 167     1555   1555  1.33  
LINK         C   MSE A 167                 N   LEU A 168     1555   1555  1.33  
LINK         C   LEU A 212                 N   MSE A 213     1555   1555  1.33  
LINK         C   MSE A 213                 N   LEU A 214     1555   1555  1.33  
LINK         C   GLY A 249                 N   MSE A 250     1555   1555  1.33  
LINK         C   MSE A 250                 N   VAL A 251     1555   1555  1.33  
LINK         C   ALA B  41                 N   MSE B  42     1555   1555  1.33  
LINK         C   MSE B  42                 N   THR B  43     1555   1555  1.33  
LINK         C   ASP B  54                 N   MSE B  55     1555   1555  1.33  
LINK         C   MSE B  55                 N   ALA B  56     1555   1555  1.33  
LINK         C   ALA B  77                 N   MSE B  78     1555   1555  1.33  
LINK         C   MSE B  78                 N   LEU B  79     1555   1555  1.33  
LINK         C   ARG B 104                 N   MSE B 105     1555   1555  1.33  
LINK         C   MSE B 105                 N   VAL B 106     1555   1555  1.33  
LINK         C   ALA B 166                 N   MSE B 167     1555   1555  1.33  
LINK         C   MSE B 167                 N   LEU B 168     1555   1555  1.33  
LINK         C   LEU B 212                 N   MSE B 213     1555   1555  1.33  
LINK         C   MSE B 213                 N   LEU B 214     1555   1555  1.33  
LINK         C   GLY B 249                 N   MSE B 250     1555   1555  1.33  
LINK         C   MSE B 250                 N   VAL B 251     1555   1555  1.33  
LINK         C   ALA C  41                 N   MSE C  42     1555   1555  1.33  
LINK         C   MSE C  42                 N   THR C  43     1555   1555  1.33  
LINK         C   ASP C  54                 N   MSE C  55     1555   1555  1.33  
LINK         C   MSE C  55                 N   ALA C  56     1555   1555  1.33  
LINK         C   ALA C  77                 N   MSE C  78     1555   1555  1.33  
LINK         C   MSE C  78                 N   LEU C  79     1555   1555  1.33  
LINK         C   ARG C 104                 N   MSE C 105     1555   1555  1.33  
LINK         C   MSE C 105                 N   VAL C 106     1555   1555  1.33  
LINK         C   ALA C 166                 N   MSE C 167     1555   1555  1.33  
LINK         C   MSE C 167                 N   LEU C 168     1555   1555  1.33  
LINK         C   LEU C 212                 N   MSE C 213     1555   1555  1.33  
LINK         C   MSE C 213                 N   LEU C 214     1555   1555  1.33  
LINK         C   GLY C 249                 N   MSE C 250     1555   1555  1.33  
LINK         C   MSE C 250                 N   VAL C 251     1555   1555  1.33  
LINK         C   ALA D  41                 N   MSE D  42     1555   1555  1.33  
LINK         C   MSE D  42                 N   THR D  43     1555   1555  1.33  
LINK         C   ASP D  54                 N   MSE D  55     1555   1555  1.33  
LINK         C   MSE D  55                 N   ALA D  56     1555   1555  1.33  
LINK         C   ALA D  77                 N   MSE D  78     1555   1555  1.33  
LINK         C   MSE D  78                 N   LEU D  79     1555   1555  1.33  
LINK         C   ARG D 104                 N   MSE D 105     1555   1555  1.33  
LINK         C   MSE D 105                 N   VAL D 106     1555   1555  1.33  
LINK         C   ALA D 166                 N   MSE D 167     1555   1555  1.33  
LINK         C   MSE D 167                 N   LEU D 168     1555   1555  1.33  
LINK         C   LEU D 212                 N   MSE D 213     1555   1555  1.33  
LINK         C   MSE D 213                 N   LEU D 214     1555   1555  1.33  
LINK         C   GLY D 249                 N   MSE D 250     1555   1555  1.33  
LINK         C   MSE D 250                 N   VAL D 251     1555   1555  1.33  
LINK         C   ALA E  41                 N   MSE E  42     1555   1555  1.33  
LINK         C   MSE E  42                 N   THR E  43     1555   1555  1.33  
LINK         C   ASP E  54                 N   MSE E  55     1555   1555  1.33  
LINK         C   MSE E  55                 N   ALA E  56     1555   1555  1.33  
LINK         C   ALA E  77                 N   MSE E  78     1555   1555  1.33  
LINK         C   MSE E  78                 N   LEU E  79     1555   1555  1.33  
LINK         C   ARG E 104                 N   MSE E 105     1555   1555  1.33  
LINK         C   MSE E 105                 N   VAL E 106     1555   1555  1.33  
LINK         C   ALA E 166                 N   MSE E 167     1555   1555  1.33  
LINK         C   MSE E 167                 N   LEU E 168     1555   1555  1.33  
LINK         C   LEU E 212                 N   MSE E 213     1555   1555  1.33  
LINK         C   MSE E 213                 N   LEU E 214     1555   1555  1.33  
LINK         C   GLY E 249                 N   MSE E 250     1555   1555  1.33  
LINK         C   MSE E 250                 N   VAL E 251     1555   1555  1.33  
LINK         C   ALA F  41                 N   MSE F  42     1555   1555  1.33  
LINK         C   MSE F  42                 N   THR F  43     1555   1555  1.33  
LINK         C   ASP F  54                 N   MSE F  55     1555   1555  1.33  
LINK         C   MSE F  55                 N   ALA F  56     1555   1555  1.33  
LINK         C   ALA F  77                 N   MSE F  78     1555   1555  1.33  
LINK         C   MSE F  78                 N   LEU F  79     1555   1555  1.33  
LINK         C   ARG F 104                 N   MSE F 105     1555   1555  1.33  
LINK         C   MSE F 105                 N   VAL F 106     1555   1555  1.33  
LINK         C   ALA F 166                 N   MSE F 167     1555   1555  1.33  
LINK         C   MSE F 167                 N   LEU F 168     1555   1555  1.33  
LINK         C   LEU F 212                 N   MSE F 213     1555   1555  1.33  
LINK         C   MSE F 213                 N   LEU F 214     1555   1555  1.33  
LINK         C   GLY F 249                 N   MSE F 250     1555   1555  1.33  
LINK         C   MSE F 250                 N   VAL F 251     1555   1555  1.33  
LINK         OD2 ASP A 235                MG    MG A1002     1555   1555  2.09  
LINK         O   HIS A 301                MG    MG A1002     1555   1555  2.42  
LINK         NE2 HIS A 303                NI    NI A1003     1555   1555  2.45  
LINK         O   HIS A 304                MG    MG A1002     1555   1555  2.47  
CISPEP   1 TRP F  224    PRO F  225          0         0.60                     
SITE     1 AC1  1 GLU D 282                                                     
SITE     1 AC2  3 ASP A 235  HIS A 301  HIS A 304                               
SITE     1 AC3  1 HIS A 303                                                     
CRYST1   88.024  122.996  194.581  90.00  90.00  90.00 P 21 21 21   24          
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      0.011361  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008130  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005139        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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