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Database: PDB
Entry: 2HTB
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HEADER    ISOMERASE                               25-JUL-06   2HTB              
TITLE     CRYSTAL STRUCTURE OF A PUTATIVE MUTAROTASE (YEAD) FROM                
TITLE    2 SALMONELLA TYPHIMURIUM IN MONOCLINIC FORM                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE ENZYME RELATED TO ALDOSE 1-EPIMERASE;             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 5.1.3.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 STRAIN: IFO12529;                                                    
SOURCE   5 GENE: YEAD;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) PLYSS;                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET-C                                   
KEYWDS    SALMONELLA TYPHIMURIUM, CARBOHYDRATE, ALDOSE 1-EPIMERASE,             
KEYWDS   2 MUTAROTASE, YEAD, GALM, SUGAR PHOSPHATE, ISOMERASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.CHITTORI,D.K.SIMANSHU,H.S.SAVITHRI,M.R.N.MURTHY                     
REVDAT   2   24-FEB-09 2HTB    1       VERSN                                    
REVDAT   1   23-JAN-07 2HTB    0                                                
JRNL        AUTH   S.CHITTORI,D.K.SIMANSHU,H.S.SAVITHRI,M.R.MURTHY              
JRNL        TITL   STRUCTURE OF THE PUTATIVE MUTAROTASE YEAD FROM               
JRNL        TITL 2 SALMONELLA TYPHIMURIUM: STRUCTURAL COMPARISON WITH           
JRNL        TITL 3 GALACTOSE MUTAROTASES.                                       
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   197 2007              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   17242513                                                     
JRNL        DOI    10.1107/S090744490604618X                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 47276                          
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 + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2480                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3108                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.01                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 153                          
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9112                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 322                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 54.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.47                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.02000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.479         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.273         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.190         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.525         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.921                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9357 ; 0.028 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12794 ; 2.314 ; 1.937       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1179 ; 8.602 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   417 ;36.067 ;24.269       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1407 ;19.629 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    45 ;23.896 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1445 ; 0.157 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7231 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4232 ; 0.238 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6246 ; 0.325 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   532 ; 0.170 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    35 ; 0.271 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.212 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6046 ; 1.734 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9540 ; 2.174 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3764 ; 3.986 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3254 ; 5.548 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2HTB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JUL-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038736.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS                      
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50200                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY                : 22.220                             
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 0.9                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: MONOMER OF ORTHORHOMBIC FORM OF STYEAD (PDB          
REMARK 200  CODE 2HTA)                                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-25% PEG8K, 0.1M CITRATE PH 5.5,       
REMARK 280  0.2-0.5MM NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 300K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      109.77650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       23.79950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      109.77650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       23.79950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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     MET A   -14                                                      
REMARK 465     ARG A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     MET A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     MET B   -14                                                      
REMARK 465     ARG B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     MET B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     MET C   -14                                                      
REMARK 465     ARG C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     GLY C    -4                                                      
REMARK 465     MET C    -3                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     MET D   -14                                                      
REMARK 465     ARG D   -13                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     GLY D    -4                                                      
REMARK 465     MET D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A   0    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A   4    CE   NZ                                             
REMARK 470     GLU A 125    OE1  OE2                                            
REMARK 470     LYS A 129    NZ                                                  
REMARK 470     LYS A 142    CE   NZ                                             
REMARK 470     LYS A 145    NZ                                                  
REMARK 470     LYS A 187    NZ                                                  
REMARK 470     GLU A 279    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A 280    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 470     HIS B   0    ND1  CD2  CE1  NE2                                  
REMARK 470     LYS B   4    CG   CD   CE   NZ                                   
REMARK 470     LYS B  68    CD   CE   NZ                                        
REMARK 470     GLN B  89    CG   CD   OE1  NE2                                  
REMARK 470     GLN B  90    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 125    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 129    CG   CD   CE   NZ                                   
REMARK 470     LYS B 145    CG   CD   CE   NZ                                   
REMARK 470     LYS B 187    CD   CE   NZ                                        
REMARK 470     GLU B 279    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 281    CG   CD   CE   NZ                                   
REMARK 470     ARG B 284    CZ   NH1  NH2                                       
REMARK 470     LYS B 293    CD   CE   NZ                                        
REMARK 470     ARG B 294    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS C   0    ND1  CD2  CE1  NE2                                  
REMARK 470     GLU C 125    CD   OE1  OE2                                       
REMARK 470     LYS C 129    CD   CE   NZ                                        
REMARK 470     LYS C 145    CG   CD   CE   NZ                                   
REMARK 470     GLU C 279    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 281    CD   CE   NZ                                        
REMARK 470     LYS D   4    CG   CD   CE   NZ                                   
REMARK 470     GLU D 125    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 145    CE   NZ                                             
REMARK 470     LYS D 187    CE   NZ                                             
REMARK 470     GLU D 279    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 280    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 281    CG   CD   CE   NZ                                   
REMARK 470     ARG D 294    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PHE A  67   CE1   PHE A  67   CZ      0.127                       
REMARK 500    GLU A 156   CB    GLU A 156   CG      0.144                       
REMARK 500    TYR A 166   CE1   TYR A 166   CZ      0.081                       
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    ARG A  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP A  24   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A  25   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    VAL A  36   CB  -  CA  -  C   ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG A  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP A 111   CB  -  CG  -  OD1 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    VAL A 291   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    ARG B  20   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP B  27   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP B  27   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP B  32   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B  74   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ASP B 171   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    VAL C  36   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    ARG C 140   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG C 140   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG C 183   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG C 209   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG C 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    VAL C 291   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG D  21   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D  21   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    VAL D  36   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG D  74   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP D 182   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP D 205   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG D 209   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP D 230   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP D 230   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 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    ASP A  24     -111.11     52.35                                   
REMARK 500    LEU A  47      107.21    -59.70                                   
REMARK 500    TRP A  50      118.37   -160.13                                   
REMARK 500    PHE A  97       -8.21   -141.65                                   
REMARK 500    ASP A 171      113.94   -171.82                                   
REMARK 500    ASP A 182      -78.53   -122.45                                   
REMARK 500    ASN A 189       69.81   -116.84                                   
REMARK 500    ASP A 198        8.98   -150.59                                   
REMARK 500    PHE A 203       55.20   -140.38                                   
REMARK 500    ASP A 205     -166.99   -164.41                                   
REMARK 500    TYR A 260       -9.44    -59.56                                   
REMARK 500    ALA A 271      -36.91   -138.61                                   
REMARK 500    ASP B  24     -128.35     62.77                                   
REMARK 500    VAL B  53      122.40    -34.90                                   
REMARK 500    ASP B 111     -157.18   -144.53                                   
REMARK 500    ASP B 182      -75.97   -112.03                                   
REMARK 500    ASN B 189       64.79   -113.05                                   
REMARK 500    ASP B 198       15.15   -146.97                                   
REMARK 500    ASP B 205     -179.39   -175.34                                   
REMARK 500    ASN B 213       44.52   -153.42                                   
REMARK 500    ASN B 226       62.42     35.89                                   
REMARK 500    ALA B 271      -31.97   -146.87                                   
REMARK 500    ASP C  24     -121.58     41.59                                   
REMARK 500    ASN C  63        0.83    -67.69                                   
REMARK 500    PHE C  67       77.47   -112.67                                   
REMARK 500    TRP C 131      115.90   -170.90                                   
REMARK 500    HIS C 164       49.89    -94.73                                   
REMARK 500    ASN C 174       36.72    -97.60                                   
REMARK 500    ASP C 182      -70.50   -105.67                                   
REMARK 500    ASN C 189       61.77   -109.81                                   
REMARK 500    HIS C 235       13.57     57.55                                   
REMARK 500    ALA C 271      -51.97   -124.10                                   
REMARK 500    ALA C 292      118.72   -167.39                                   
REMARK 500    ASP D  24     -112.98     65.01                                   
REMARK 500    ALA D  45       43.56     39.72                                   
REMARK 500    GLU D  57      120.05    -34.97                                   
REMARK 500    PHE D  67       74.08   -112.76                                   
REMARK 500    ASP D 111     -158.23   -153.58                                   
REMARK 500    HIS D 164       50.90   -100.88                                   
REMARK 500    ASP D 171      115.56   -170.38                                   
REMARK 500    ASP D 182      -66.97   -127.16                                   
REMARK 500    ASN D 189       69.18   -114.20                                   
REMARK 500    ASP D 198       11.70   -140.32                                   
REMARK 500    ARG D 206      126.40    -35.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 HIS C    0     MET C    1                  136.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JOV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1L7J   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1Z45   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1LUR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1SNZ   RELATED DB: PDB                                   
DBREF  2HTB A    1   294  UNP    Q8ZPV9   Q8ZPV9_SALTY     1    294             
DBREF  2HTB B    1   294  UNP    Q8ZPV9   Q8ZPV9_SALTY     1    294             
DBREF  2HTB C    1   294  UNP    Q8ZPV9   Q8ZPV9_SALTY     1    294             
DBREF  2HTB D    1   294  UNP    Q8ZPV9   Q8ZPV9_SALTY     1    294             
SEQADV 2HTB MET A  -14  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ARG A  -13  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB GLY A  -12  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER A  -11  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS A  -10  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS A   -9  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS A   -8  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS A   -7  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS A   -6  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS A   -5  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB GLY A   -4  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET A   -3  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ALA A   -2  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER A   -1  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS A    0  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET B  -14  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ARG B  -13  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB GLY B  -12  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER B  -11  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS B  -10  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS B   -9  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS B   -8  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS B   -7  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS B   -6  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS B   -5  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB GLY B   -4  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET B   -3  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ALA B   -2  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER B   -1  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS B    0  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET C  -14  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ARG C  -13  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB GLY C  -12  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER C  -11  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS C  -10  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS C   -9  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS C   -8  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS C   -7  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS C   -6  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS C   -5  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB GLY C   -4  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET C   -3  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ALA C   -2  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER C   -1  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS C    0  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET D  -14  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ARG D  -13  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB GLY D  -12  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER D  -11  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS D  -10  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS D   -9  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS D   -8  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS D   -7  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS D   -6  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB HIS D   -5  UNP  Q8ZPV9              EXPRESSION TAG                 
SEQADV 2HTB GLY D   -4  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB MET D   -3  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB ALA D   -2  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB SER D   -1  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQADV 2HTB HIS D    0  UNP  Q8ZPV9              CLONING ARTIFACT               
SEQRES   1 A  309  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 A  309  SER HIS MET ILE ASN LYS ILE PHE ALA LEU PRO VAL ILE          
SEQRES   3 A  309  GLU GLN LEU THR PRO VAL LEU SER ARG ARG GLN LEU ASP          
SEQRES   4 A  309  ASP LEU ASP LEU ILE VAL VAL ASP HIS PRO GLN VAL LYS          
SEQRES   5 A  309  ALA SER PHE ALA LEU GLN GLY ALA HIS LEU LEU SER TRP          
SEQRES   6 A  309  LYS PRO VAL GLY GLU GLU GLU VAL LEU TRP LEU SER ASN          
SEQRES   7 A  309  ASN THR PRO PHE LYS THR GLY VAL ALA LEU ARG GLY GLY          
SEQRES   8 A  309  VAL PRO ILE CYS TRP PRO TRP PHE GLY PRO ALA ALA GLN          
SEQRES   9 A  309  GLN GLY LEU PRO SER HIS GLY PHE ALA ARG ASN LEU PRO          
SEQRES  10 A  309  TRP ALA LEU LYS ALA HIS ASN GLU ASP ASP ASN GLY VAL          
SEQRES  11 A  309  MET LEU THR PHE GLU LEU GLN SER SER GLU ALA THR ARG          
SEQRES  12 A  309  LYS TYR TRP PRO HIS ASP PHE THR LEU LEU ALA ARG PHE          
SEQRES  13 A  309  LYS VAL GLY LYS THR CYS GLU ILE GLU LEU GLU ALA HIS          
SEQRES  14 A  309  GLY GLU PHE ALA THR THR SER ALA LEU HIS SER TYR PHE          
SEQRES  15 A  309  ASN VAL GLY ASP ILE ALA ASN VAL LYS VAL SER GLY LEU          
SEQRES  16 A  309  GLY ASP ARG PHE ILE ASP LYS VAL ASN ASP ALA LYS GLU          
SEQRES  17 A  309  GLY VAL LEU THR ASP GLY ILE GLN THR PHE PRO ASP ARG          
SEQRES  18 A  309  THR ASP ARG VAL TYR LEU ASN PRO GLU ALA CYS SER VAL          
SEQRES  19 A  309  ILE HIS ASP ALA THR LEU ASN ARG THR ILE ASP VAL VAL          
SEQRES  20 A  309  HIS HIS HIS HIS LEU ASN VAL VAL GLY TRP ASN PRO GLY          
SEQRES  21 A  309  PRO ALA LEU SER VAL SER MET GLY ASP MET PRO ASP ASP          
SEQRES  22 A  309  GLY TYR LYS THR PHE VAL CYS VAL GLU THR VAL TYR ALA          
SEQRES  23 A  309  THR ALA PRO GLN GLN ALA THR GLU GLU LYS PRO SER ARG          
SEQRES  24 A  309  LEU ALA GLN THR ILE CYS VAL ALA LYS ARG                      
SEQRES   1 B  309  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 B  309  SER HIS MET ILE ASN LYS ILE PHE ALA LEU PRO VAL ILE          
SEQRES   3 B  309  GLU GLN LEU THR PRO VAL LEU SER ARG ARG GLN LEU ASP          
SEQRES   4 B  309  ASP LEU ASP LEU ILE VAL VAL ASP HIS PRO GLN VAL LYS          
SEQRES   5 B  309  ALA SER PHE ALA LEU GLN GLY ALA HIS LEU LEU SER TRP          
SEQRES   6 B  309  LYS PRO VAL GLY GLU GLU GLU VAL LEU TRP LEU SER ASN          
SEQRES   7 B  309  ASN THR PRO PHE LYS THR GLY VAL ALA LEU ARG GLY GLY          
SEQRES   8 B  309  VAL PRO ILE CYS TRP PRO TRP PHE GLY PRO ALA ALA GLN          
SEQRES   9 B  309  GLN GLY LEU PRO SER HIS GLY PHE ALA ARG ASN LEU PRO          
SEQRES  10 B  309  TRP ALA LEU LYS ALA HIS ASN GLU ASP ASP ASN GLY VAL          
SEQRES  11 B  309  MET LEU THR PHE GLU LEU GLN SER SER GLU ALA THR ARG          
SEQRES  12 B  309  LYS TYR TRP PRO HIS ASP PHE THR LEU LEU ALA ARG PHE          
SEQRES  13 B  309  LYS VAL GLY LYS THR CYS GLU ILE GLU LEU GLU ALA HIS          
SEQRES  14 B  309  GLY GLU PHE ALA THR THR SER ALA LEU HIS SER TYR PHE          
SEQRES  15 B  309  ASN VAL GLY ASP ILE ALA ASN VAL LYS VAL SER GLY LEU          
SEQRES  16 B  309  GLY ASP ARG PHE ILE ASP LYS VAL ASN ASP ALA LYS GLU          
SEQRES  17 B  309  GLY VAL LEU THR ASP GLY ILE GLN THR PHE PRO ASP ARG          
SEQRES  18 B  309  THR ASP ARG VAL TYR LEU ASN PRO GLU ALA CYS SER VAL          
SEQRES  19 B  309  ILE HIS ASP ALA THR LEU ASN ARG THR ILE ASP VAL VAL          
SEQRES  20 B  309  HIS HIS HIS HIS LEU ASN VAL VAL GLY TRP ASN PRO GLY          
SEQRES  21 B  309  PRO ALA LEU SER VAL SER MET GLY ASP MET PRO ASP ASP          
SEQRES  22 B  309  GLY TYR LYS THR PHE VAL CYS VAL GLU THR VAL TYR ALA          
SEQRES  23 B  309  THR ALA PRO GLN GLN ALA THR GLU GLU LYS PRO SER ARG          
SEQRES  24 B  309  LEU ALA GLN THR ILE CYS VAL ALA LYS ARG                      
SEQRES   1 C  309  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 C  309  SER HIS MET ILE ASN LYS ILE PHE ALA LEU PRO VAL ILE          
SEQRES   3 C  309  GLU GLN LEU THR PRO VAL LEU SER ARG ARG GLN LEU ASP          
SEQRES   4 C  309  ASP LEU ASP LEU ILE VAL VAL ASP HIS PRO GLN VAL LYS          
SEQRES   5 C  309  ALA SER PHE ALA LEU GLN GLY ALA HIS LEU LEU SER TRP          
SEQRES   6 C  309  LYS PRO VAL GLY GLU GLU GLU VAL LEU TRP LEU SER ASN          
SEQRES   7 C  309  ASN THR PRO PHE LYS THR GLY VAL ALA LEU ARG GLY GLY          
SEQRES   8 C  309  VAL PRO ILE CYS TRP PRO TRP PHE GLY PRO ALA ALA GLN          
SEQRES   9 C  309  GLN GLY LEU PRO SER HIS GLY PHE ALA ARG ASN LEU PRO          
SEQRES  10 C  309  TRP ALA LEU LYS ALA HIS ASN GLU ASP ASP ASN GLY VAL          
SEQRES  11 C  309  MET LEU THR PHE GLU LEU GLN SER SER GLU ALA THR ARG          
SEQRES  12 C  309  LYS TYR TRP PRO HIS ASP PHE THR LEU LEU ALA ARG PHE          
SEQRES  13 C  309  LYS VAL GLY LYS THR CYS GLU ILE GLU LEU GLU ALA HIS          
SEQRES  14 C  309  GLY GLU PHE ALA THR THR SER ALA LEU HIS SER TYR PHE          
SEQRES  15 C  309  ASN VAL GLY ASP ILE ALA ASN VAL LYS VAL SER GLY LEU          
SEQRES  16 C  309  GLY ASP ARG PHE ILE ASP LYS VAL ASN ASP ALA LYS GLU          
SEQRES  17 C  309  GLY VAL LEU THR ASP GLY ILE GLN THR PHE PRO ASP ARG          
SEQRES  18 C  309  THR ASP ARG VAL TYR LEU ASN PRO GLU ALA CYS SER VAL          
SEQRES  19 C  309  ILE HIS ASP ALA THR LEU ASN ARG THR ILE ASP VAL VAL          
SEQRES  20 C  309  HIS HIS HIS HIS LEU ASN VAL VAL GLY TRP ASN PRO GLY          
SEQRES  21 C  309  PRO ALA LEU SER VAL SER MET GLY ASP MET PRO ASP ASP          
SEQRES  22 C  309  GLY TYR LYS THR PHE VAL CYS VAL GLU THR VAL TYR ALA          
SEQRES  23 C  309  THR ALA PRO GLN GLN ALA THR GLU GLU LYS PRO SER ARG          
SEQRES  24 C  309  LEU ALA GLN THR ILE CYS VAL ALA LYS ARG                      
SEQRES   1 D  309  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY MET ALA          
SEQRES   2 D  309  SER HIS MET ILE ASN LYS ILE PHE ALA LEU PRO VAL ILE          
SEQRES   3 D  309  GLU GLN LEU THR PRO VAL LEU SER ARG ARG GLN LEU ASP          
SEQRES   4 D  309  ASP LEU ASP LEU ILE VAL VAL ASP HIS PRO GLN VAL LYS          
SEQRES   5 D  309  ALA SER PHE ALA LEU GLN GLY ALA HIS LEU LEU SER TRP          
SEQRES   6 D  309  LYS PRO VAL GLY GLU GLU GLU VAL LEU TRP LEU SER ASN          
SEQRES   7 D  309  ASN THR PRO PHE LYS THR GLY VAL ALA LEU ARG GLY GLY          
SEQRES   8 D  309  VAL PRO ILE CYS TRP PRO TRP PHE GLY PRO ALA ALA GLN          
SEQRES   9 D  309  GLN GLY LEU PRO SER HIS GLY PHE ALA ARG ASN LEU PRO          
SEQRES  10 D  309  TRP ALA LEU LYS ALA HIS ASN GLU ASP ASP ASN GLY VAL          
SEQRES  11 D  309  MET LEU THR PHE GLU LEU GLN SER SER GLU ALA THR ARG          
SEQRES  12 D  309  LYS TYR TRP PRO HIS ASP PHE THR LEU LEU ALA ARG PHE          
SEQRES  13 D  309  LYS VAL GLY LYS THR CYS GLU ILE GLU LEU GLU ALA HIS          
SEQRES  14 D  309  GLY GLU PHE ALA THR THR SER ALA LEU HIS SER TYR PHE          
SEQRES  15 D  309  ASN VAL GLY ASP ILE ALA ASN VAL LYS VAL SER GLY LEU          
SEQRES  16 D  309  GLY ASP ARG PHE ILE ASP LYS VAL ASN ASP ALA LYS GLU          
SEQRES  17 D  309  GLY VAL LEU THR ASP GLY ILE GLN THR PHE PRO ASP ARG          
SEQRES  18 D  309  THR ASP ARG VAL TYR LEU ASN PRO GLU ALA CYS SER VAL          
SEQRES  19 D  309  ILE HIS ASP ALA THR LEU ASN ARG THR ILE ASP VAL VAL          
SEQRES  20 D  309  HIS HIS HIS HIS LEU ASN VAL VAL GLY TRP ASN PRO GLY          
SEQRES  21 D  309  PRO ALA LEU SER VAL SER MET GLY ASP MET PRO ASP ASP          
SEQRES  22 D  309  GLY TYR LYS THR PHE VAL CYS VAL GLU THR VAL TYR ALA          
SEQRES  23 D  309  THR ALA PRO GLN GLN ALA THR GLU GLU LYS PRO SER ARG          
SEQRES  24 D  309  LEU ALA GLN THR ILE CYS VAL ALA LYS ARG                      
FORMUL   5  HOH   *322(H2 O)                                                    
HELIX    1   1 SER A   -1  ALA A    7  1                                   9    
HELIX    2   2 GLN A   43  ALA A   45  5                                   3    
HELIX    3   3 PHE A   97  LEU A  101  5                                   5    
HELIX    4   4 SER A  124  LYS A  129  1                                   6    
HELIX    5   5 ASP A  171  ALA A  173  5                                   3    
HELIX    6   6 PRO A  244  MET A  252  1                                   9    
HELIX    7   7 ASP A  258  LYS A  261  5                                   4    
HELIX    8   8 SER B   -1  LEU B    8  1                                  10    
HELIX    9   9 GLN B   43  ALA B   45  5                                   3    
HELIX   10  10 PHE B   97  LEU B  101  5                                   5    
HELIX   11  11 SER B  124  TRP B  131  1                                   8    
HELIX   12  12 ASP B  171  ALA B  173  5                                   3    
HELIX   13  13 PRO B  244  MET B  252  1                                   9    
HELIX   14  14 ASP B  258  LYS B  261  5                                   4    
HELIX   15  15 HIS C    0  LEU C    8  1                                   9    
HELIX   16  16 GLN C   43  ALA C   45  5                                   3    
HELIX   17  17 PHE C   97  LEU C  101  5                                   5    
HELIX   18  18 SER C  124  LYS C  129  1                                   6    
HELIX   19  19 ASP C  171  ALA C  173  5                                   3    
HELIX   20  20 PRO C  244  MET C  252  1                                   9    
HELIX   21  21 ASP C  258  LYS C  261  5                                   4    
HELIX   22  22 HIS D    0  LEU D    8  1                                   9    
HELIX   23  23 GLN D   43  ALA D   45  5                                   3    
HELIX   24  24 PHE D   97  LEU D  101  5                                   5    
HELIX   25  25 SER D  124  LYS D  129  1                                   6    
HELIX   26  26 ASP D  171  ALA D  173  5                                   3    
HELIX   27  27 GLY D  245  MET D  252  1                                   8    
HELIX   28  28 ASP D  258  LYS D  261  5                                   4    
SHEET    1   A 5 GLU A  12  GLN A  13  0                                        
SHEET    2   A 5 LEU A  18  LEU A  23 -1  O  ARG A  20   N  GLU A  12           
SHEET    3   A 5 LEU A  26  HIS A  33 -1  O  VAL A  30   N  SER A  19           
SHEET    4   A 5 VAL A  36  ALA A  41 -1  O  ALA A  38   N  VAL A  31           
SHEET    5   A 5 HIS A  46  PRO A  52 -1  O  LEU A  48   N  SER A  39           
SHEET    1   B 4 ILE A  79  CYS A  80  0                                        
SHEET    2   B 4 PHE A 157  LEU A 163 -1  O  ALA A 162   N  CYS A  80           
SHEET    3   B 4 PHE A 263  ALA A 277 -1  O  TYR A 270   N  SER A 161           
SHEET    4   B 4 TYR A 166  ASN A 168 -1  N  PHE A 167   O  VAL A 264           
SHEET    1   C 7 ILE A  79  CYS A  80  0                                        
SHEET    2   C 7 PHE A 157  LEU A 163 -1  O  ALA A 162   N  CYS A  80           
SHEET    3   C 7 PHE A 263  ALA A 277 -1  O  TYR A 270   N  SER A 161           
SHEET    4   C 7 ASN A 238  ASN A 243 -1  N  VAL A 240   O  GLU A 267           
SHEET    5   C 7 THR A 207  TYR A 211 -1  N  TYR A 211   O  VAL A 239           
SHEET    6   C 7 ARG A 183  ASP A 186 -1  N  ILE A 185   O  VAL A 210           
SHEET    7   C 7 GLU A 193  VAL A 195 -1  O  GLY A 194   N  PHE A 184           
SHEET    1   D 9 ALA A 104  GLU A 110  0                                        
SHEET    2   D 9 VAL A 115  GLN A 122 -1  O  THR A 118   N  ALA A 107           
SHEET    3   D 9 THR A 136  VAL A 143 -1  O  ALA A 139   N  PHE A 119           
SHEET    4   D 9 CYS A 147  HIS A 154 -1  O  GLU A 150   N  ARG A 140           
SHEET    5   D 9 SER A 283  LYS A 293 -1  O  SER A 283   N  ALA A 153           
SHEET    6   D 9 ARG A 227  HIS A 234 -1  N  HIS A 234   O  ALA A 286           
SHEET    7   D 9 CYS A 217  ASP A 222 -1  N  SER A 218   O  VAL A 231           
SHEET    8   D 9 VAL A 175  SER A 178 -1  N  LYS A 176   O  HIS A 221           
SHEET    9   D 9 GLN A 201  THR A 202 -1  O  GLN A 201   N  VAL A 177           
SHEET    1   E 5 GLU B  12  GLN B  13  0                                        
SHEET    2   E 5 LEU B  18  LEU B  23 -1  O  ARG B  20   N  GLU B  12           
SHEET    3   E 5 LEU B  26  HIS B  33 -1  O  LEU B  28   N  ARG B  21           
SHEET    4   E 5 VAL B  36  ALA B  41 -1  O  ALA B  38   N  VAL B  31           
SHEET    5   E 5 HIS B  46  PRO B  52 -1  O  LEU B  48   N  SER B  39           
SHEET    1   F 4 ILE B  79  CYS B  80  0                                        
SHEET    2   F 4 PHE B 157  LEU B 163 -1  O  ALA B 162   N  CYS B  80           
SHEET    3   F 4 PHE B 263  ALA B 277 -1  O  ALA B 277   N  PHE B 157           
SHEET    4   F 4 TYR B 166  ASN B 168 -1  N  PHE B 167   O  VAL B 264           
SHEET    1   G 7 ILE B  79  CYS B  80  0                                        
SHEET    2   G 7 PHE B 157  LEU B 163 -1  O  ALA B 162   N  CYS B  80           
SHEET    3   G 7 PHE B 263  ALA B 277 -1  O  ALA B 277   N  PHE B 157           
SHEET    4   G 7 ASN B 238  ASN B 243 -1  N  TRP B 242   O  CYS B 265           
SHEET    5   G 7 THR B 207  TYR B 211 -1  N  TYR B 211   O  VAL B 239           
SHEET    6   G 7 ARG B 183  ASP B 186 -1  N  ILE B 185   O  VAL B 210           
SHEET    7   G 7 LYS B 192  VAL B 195 -1  O  LYS B 192   N  ASP B 186           
SHEET    1   H 9 ALA B 104  GLU B 110  0                                        
SHEET    2   H 9 VAL B 115  GLN B 122 -1  O  MET B 116   N  ASN B 109           
SHEET    3   H 9 THR B 136  VAL B 143 -1  O  LEU B 137   N  LEU B 121           
SHEET    4   H 9 CYS B 147  HIS B 154 -1  O  GLU B 150   N  ARG B 140           
SHEET    5   H 9 SER B 283  LYS B 293 -1  O  SER B 283   N  ALA B 153           
SHEET    6   H 9 ARG B 227  HIS B 234 -1  N  VAL B 232   O  THR B 288           
SHEET    7   H 9 CYS B 217  ASP B 222 -1  N  SER B 218   O  VAL B 231           
SHEET    8   H 9 VAL B 175  SER B 178 -1  N  LYS B 176   O  HIS B 221           
SHEET    9   H 9 GLN B 201  THR B 202 -1  O  GLN B 201   N  VAL B 177           
SHEET    1   I 5 GLU C  12  GLN C  13  0                                        
SHEET    2   I 5 LEU C  18  LEU C  23 -1  O  ARG C  20   N  GLU C  12           
SHEET    3   I 5 LEU C  26  HIS C  33 -1  O  LEU C  28   N  ARG C  21           
SHEET    4   I 5 VAL C  36  ALA C  41 -1  O  PHE C  40   N  ILE C  29           
SHEET    5   I 5 HIS C  46  PRO C  52 -1  O  LYS C  51   N  LYS C  37           
SHEET    1   J 4 ILE C  79  CYS C  80  0                                        
SHEET    2   J 4 PHE C 157  LEU C 163 -1  O  ALA C 162   N  CYS C  80           
SHEET    3   J 4 PHE C 263  ALA C 277 -1  O  GLN C 275   N  THR C 159           
SHEET    4   J 4 TYR C 166  ASN C 168 -1  N  PHE C 167   O  VAL C 264           
SHEET    1   K 7 ILE C  79  CYS C  80  0                                        
SHEET    2   K 7 PHE C 157  LEU C 163 -1  O  ALA C 162   N  CYS C  80           
SHEET    3   K 7 PHE C 263  ALA C 277 -1  O  GLN C 275   N  THR C 159           
SHEET    4   K 7 ASN C 238  ASN C 243 -1  N  VAL C 240   O  GLU C 267           
SHEET    5   K 7 THR C 207  TYR C 211 -1  N  TYR C 211   O  VAL C 239           
SHEET    6   K 7 ARG C 183  ASP C 186 -1  N  ILE C 185   O  VAL C 210           
SHEET    7   K 7 LYS C 192  VAL C 195 -1  O  GLY C 194   N  PHE C 184           
SHEET    1   L 9 ALA C 104  GLU C 110  0                                        
SHEET    2   L 9 VAL C 115  GLN C 122 -1  O  THR C 118   N  ALA C 107           
SHEET    3   L 9 PHE C 135  VAL C 143 -1  O  PHE C 141   N  LEU C 117           
SHEET    4   L 9 CYS C 147  GLY C 155 -1  O  HIS C 154   N  THR C 136           
SHEET    5   L 9 SER C 283  LYS C 293 -1  O  LEU C 285   N  LEU C 151           
SHEET    6   L 9 ARG C 227  HIS C 234 -1  N  VAL C 232   O  THR C 288           
SHEET    7   L 9 CYS C 217  ASP C 222 -1  N  SER C 218   O  VAL C 231           
SHEET    8   L 9 VAL C 175  SER C 178 -1  N  LYS C 176   O  HIS C 221           
SHEET    9   L 9 GLN C 201  THR C 202 -1  O  GLN C 201   N  VAL C 177           
SHEET    1   M 5 GLU D  12  GLN D  13  0                                        
SHEET    2   M 5 LEU D  18  LEU D  23 -1  O  ARG D  20   N  GLU D  12           
SHEET    3   M 5 LEU D  26  ASP D  32 -1  O  LEU D  28   N  ARG D  21           
SHEET    4   M 5 VAL D  36  ALA D  41 -1  O  ALA D  38   N  VAL D  31           
SHEET    5   M 5 HIS D  46  PRO D  52 -1  O  LEU D  48   N  SER D  39           
SHEET    1   N 4 ILE D  79  CYS D  80  0                                        
SHEET    2   N 4 PHE D 157  LEU D 163 -1  O  ALA D 162   N  CYS D  80           
SHEET    3   N 4 PHE D 263  ALA D 277 -1  O  TYR D 270   N  SER D 161           
SHEET    4   N 4 TYR D 166  ASN D 168 -1  N  PHE D 167   O  VAL D 264           
SHEET    1   O 7 ILE D  79  CYS D  80  0                                        
SHEET    2   O 7 PHE D 157  LEU D 163 -1  O  ALA D 162   N  CYS D  80           
SHEET    3   O 7 PHE D 263  ALA D 277 -1  O  TYR D 270   N  SER D 161           
SHEET    4   O 7 ASN D 238  ASN D 243 -1  N  VAL D 240   O  GLU D 267           
SHEET    5   O 7 THR D 207  TYR D 211 -1  N  TYR D 211   O  VAL D 239           
SHEET    6   O 7 ARG D 183  ASP D 186 -1  N  ILE D 185   O  VAL D 210           
SHEET    7   O 7 LYS D 192  VAL D 195 -1  O  LYS D 192   N  ASP D 186           
SHEET    1   P 9 ALA D 104  GLU D 110  0                                        
SHEET    2   P 9 VAL D 115  GLN D 122 -1  O  MET D 116   N  ASN D 109           
SHEET    3   P 9 THR D 136  VAL D 143 -1  O  LEU D 137   N  LEU D 121           
SHEET    4   P 9 CYS D 147  HIS D 154 -1  O  HIS D 154   N  THR D 136           
SHEET    5   P 9 SER D 283  LYS D 293 -1  O  SER D 283   N  ALA D 153           
SHEET    6   P 9 ARG D 227  HIS D 234 -1  N  VAL D 232   O  THR D 288           
SHEET    7   P 9 CYS D 217  ASP D 222 -1  N  ILE D 220   O  ILE D 229           
SHEET    8   P 9 VAL D 175  SER D 178 -1  N  LYS D 176   O  HIS D 221           
SHEET    9   P 9 GLN D 201  THR D 202 -1  O  GLN D 201   N  VAL D 177           
CISPEP   1 TRP A   81    PRO A   82          0         2.80                     
CISPEP   2 TRP B   81    PRO B   82          0         1.69                     
CISPEP   3 TRP C   81    PRO C   82          0         0.06                     
CISPEP   4 TRP D   81    PRO D   82          0         7.36                     
CRYST1  219.553   47.599  138.086  90.00  91.82  90.00 C 1 2 1      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004555  0.000000  0.000144        0.00000                         
SCALE2      0.000000  0.021009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007246        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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