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Database: PDB
Entry: 3LN7
LinkDB: 3LN7
Original site: 3LN7 
HEADER    LIGASE                                  02-FEB-10   3LN7              
TITLE     CRYSTAL STRUCTURE OF A BIFUNCTIONAL GLUTATHIONE SYNTHETASE FROM       
TITLE    2 PASTEURELLA MULTOCIDA                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE BIOSYNTHESIS BIFUNCTIONAL PROTEIN GSHAB;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: GAMMA-GCS-GS, GCS-GS, GLUTAMATE--CYSTEINE LIGASE, GAMMA-    
COMPND   5 GLUTAMYLCYSTEINE SYNTHETASE, GAMMA-ECS, GCS, GLUTATHIONE SYNTHETASE, 
COMPND   6 GLUTATHIONE SYNTHASE, GSH SYNTHETASE, GSH-S, GSHASE, GS;             
COMPND   7 EC: 6.3.2.2, 6.3.2.3;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PASTEURELLA MULTOCIDA;                          
SOURCE   3 ORGANISM_TAXID: 747;                                                 
SOURCE   4 GENE: GSHAB, GSHF, PM1048;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: B834;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    GAMMA-GLUTAMYLCYSTEINE LIGASE DOMAIN, ATP-GRASP DOMAIN, HYBRID        
KEYWDS   2 ENZYME, ATP-BINDING, GLUTATHIONE BIOSYNTHESIS, LIGASE, METAL-        
KEYWDS   3 BINDING, MULTIFUNCTIONAL ENZYME, NUCLEOTIDE-BINDING                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.STOUT,B.VERGAUWEN,S.N.SAVVIDES                                      
REVDAT   1   13-APR-11 3LN7    0                                                
JRNL        AUTH   J.STOUT,D.DE VOS,B.VERGAUWEN,S.N.SAVVIDES                    
JRNL        TITL   STRUCTURES OF TWO BIFUNCTIONAL GAMMA-GLUTAMATE-CYSTEINE      
JRNL        TITL 2 LIGASE/GLUTATHIONE SYNTHETASES (GSHF) REVEAL A NOVEL HYBRID  
JRNL        TITL 3 ATP-GRASP FOLD                                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 33398                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.275                           
REMARK   3   FREE R VALUE                     : 0.314                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1670                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  3.2900 -  3.2000    0.76        0   106  0.3570 0.3850        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.43                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.07000                                              
REMARK   3    B22 (A**2) : -3.60000                                             
REMARK   3    B33 (A**2) : 3.53000                                              
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : 8.75000                                              
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           NULL                                  
REMARK   3   ANGLE     :  1.475           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMIM LIKELIHOOD REFINEMENT PROCEDURE   
REMARK   4                                                                      
REMARK   4 3LN7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-FEB-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057485.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33404                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 67.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: GSHF FROM STREPTOCOCCUS AGALACTIAE                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-15% PEG 3350, 0.2M KSCN, 100MM NA/K   
REMARK 280  PHOSPHATE, PH7.0-7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE    
REMARK 280  298K                                                                
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      102.62000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.53500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      102.62000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.53500            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 62270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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     MSE A     1                                                      
REMARK 465     GLU A   109                                                      
REMARK 465     GLU A   110                                                      
REMARK 465     GLN A   111                                                      
REMARK 465     VAL A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     SER A   201                                                      
REMARK 465     ALA A   202                                                      
REMARK 465     GLY A   253                                                      
REMARK 465     GLU A   757                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     ASP B   118                                                      
REMARK 465     ASN B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     GLU B   121                                                      
REMARK 465     ASP B   122                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     ALA B   124                                                      
REMARK 465     TYR B   125                                                      
REMARK 465     ALA B   202                                                      
REMARK 465     TYR B   203                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     LEU B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     LYS B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     ASP B   229                                                      
REMARK 465     THR B   252                                                      
REMARK 465     GLY B   253                                                      
REMARK 465     LYS B   254                                                      
REMARK 465     LEU B   255                                                      
REMARK 465     ILE B   256                                                      
REMARK 465     THR B   320                                                      
REMARK 465     ALA B   321                                                      
REMARK 465     GLU B   524                                                      
REMARK 465     ASN B   525                                                      
REMARK 465     GLU B   757                                                      
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     LYS A   2    CG   CD   CE   NZ                                   
REMARK 470     ILE A   3    CG1  CG2  CD1                                       
REMARK 470     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     ILE A   7    CD1                                                 
REMARK 470     HIS A   8    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU A   9    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  10    CG   OD1                                            
REMARK 470     GLN A  11    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  14    CG   CD1  CD2                                       
REMARK 470     SER A  27    OG                                                  
REMARK 470     VAL A  37    CG1  CG2                                            
REMARK 470     VAL A  44    CG1  CG2                                            
REMARK 470     ASN A  47    OD1                                                 
REMARK 470     ARG A  49    CD   NE   CZ   NH1  NH2                             
REMARK 470     PHE A  58    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ILE A  66    CD1                                                 
REMARK 470     LYS A  71    CG   CD   CE   NZ                                   
REMARK 470     LYS A  72    CE   NZ                                             
REMARK 470     SER A  81    OG                                                  
REMARK 470     VAL A  82    CG1  CG2                                            
REMARK 470     HIS A  84    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A  87    CG1  CG2                                            
REMARK 470     GLU A  93    CD   OE1  OE2                                       
REMARK 470     LEU A 106    CG   CD1  CD2                                       
REMARK 470     ILE A 112    CG1  CG2  CD1                                       
REMARK 470     ARG A 113    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 114    CG1  CG2                                            
REMARK 470     LEU A 117    CG   CD1  CD2                                       
REMARK 470     ASP A 118    CG   OD1  OD2                                       
REMARK 470     PRO A 120    CG   CD                                             
REMARK 470     GLU A 121    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 122    CG   OD1  OD2                                       
REMARK 470     VAL A 123    CG1  CG2                                            
REMARK 470     TYR A 125    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 127    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 130    CG1  CG2                                            
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     ILE A 132    CG1  CG2  CD1                                       
REMARK 470     TYR A 133    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 135    CG   CD   CE   NZ                                   
REMARK 470     LYS A 137    CG   CD   CE   NZ                                   
REMARK 470     SER A 141    OG                                                  
REMARK 470     SER A 150    OG                                                  
REMARK 470     ASP A 152    OD1  OD2                                            
REMARK 470     THR A 155    CG2                                                 
REMARK 470     ARG A 159    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 160    CG   CD1  CD2                                       
REMARK 470     GLN A 161    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 163    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 165    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 169    CG   OD1  OD2                                       
REMARK 470     ASP A 173    CG   OD1  OD2                                       
REMARK 470     ILE A 188    CD1                                                 
REMARK 470     THR A 196    OG1  CG2                                            
REMARK 470     TYR A 203    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE A 204    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     ASP A 206    CG   OD1  OD2                                       
REMARK 470     SER A 208    OG                                                  
REMARK 470     LEU A 210    CG   CD1  CD2                                       
REMARK 470     LYS A 212    CG   CD   CE   NZ                                   
REMARK 470     GLN A 214    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 215    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 216    CG1  CG2                                            
REMARK 470     LEU A 219    CG   CD1  CD2                                       
REMARK 470     ARG A 220    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 222    OG                                                  
REMARK 470     GLN A 223    CG   CD   OE1  NE2                                  
REMARK 470     TYR A 224    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 227    CG1  CG2                                            
REMARK 470     ASP A 229    CG   OD1  OD2                                       
REMARK 470     GLU A 231    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 232    CD1                                                 
REMARK 470     PHE A 236    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL A 239    CG1  CG2                                            
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 246    CG   CD1  CD2                                       
REMARK 470     HIS A 248    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL A 250    CG1  CG2                                            
REMARK 470     SER A 251    OG                                                  
REMARK 470     THR A 252    OG1  CG2                                            
REMARK 470     LYS A 254    CG   CD   CE   NZ                                   
REMARK 470     ILE A 256    CG1  CG2  CD1                                       
REMARK 470     GLU A 258    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     GLU A 260    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 266    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 272    CG   CD   CE   NZ                                   
REMARK 470     GLU A 275    CG   CD   OE1  OE2                                  
REMARK 470     THR A 278    OG1  CG2                                            
REMARK 470     THR A 279    OG1  CG2                                            
REMARK 470     ILE A 281    CD1                                                 
REMARK 470     LYS A 302    CG   CD   CE   NZ                                   
REMARK 470     HIS A 319    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR A 320    OG1  CG2                                            
REMARK 470     ASP A 322    CG   OD1  OD2                                       
REMARK 470     GLN A 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 324    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 325    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 326    CG1  CG2                                            
REMARK 470     GLU A 327    CD   OE1  OE2                                       
REMARK 470     LYS A 330    CE   NZ                                             
REMARK 470     GLU A 335    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 336    CG1  CG2                                            
REMARK 470     LEU A 342    CG   CD1  CD2                                       
REMARK 470     THR A 345    OG1  CG2                                            
REMARK 470     LEU A 356    CG   CD1  CD2                                       
REMARK 470     GLU A 357    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 364    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 365    CD1                                                 
REMARK 470     GLU A 370    OE2                                                 
REMARK 470     LYS A 376    CE   NZ                                             
REMARK 470     GLU A 377    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 378    CD   CE   NZ                                        
REMARK 470     THR A 380    OG1  CG2                                            
REMARK 470     THR A 383    CG2                                                 
REMARK 470     SER A 386    OG                                                  
REMARK 470     ARG A 392    CZ   NH1  NH2                                       
REMARK 470     LEU A 393    CG   CD1  CD2                                       
REMARK 470     VAL A 394    CG2                                                 
REMARK 470     ILE A 397    CD1                                                 
REMARK 470     GLU A 398    CG   CD   OE1  OE2                                  
REMARK 470     SER A 402    OG                                                  
REMARK 470     GLN A 405    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 409    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 413    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 422    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     ASP A 429    CG   OD1  OD2                                       
REMARK 470     LYS A 445    CG   CD   CE   NZ                                   
REMARK 470     ASP A 456    CG   OD1  OD2                                       
REMARK 470     LYS A 462    NZ                                                  
REMARK 470     ASP A 465    CG   OD1  OD2                                       
REMARK 470     ILE A 467    CD1                                                 
REMARK 470     ILE A 482    CD1                                                 
REMARK 470     LYS A 490    CG   CD   CE   NZ                                   
REMARK 470     VAL A 496    CG1  CG2                                            
REMARK 470     GLN A 498    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 499    CD   CE   NZ                                        
REMARK 470     ASN A 503    CG   OD1                                            
REMARK 470     THR A 511    OG1  CG2                                            
REMARK 470     GLU A 514    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 515    CG   CD   CE   NZ                                   
REMARK 470     VAL A 517    CG1  CG2                                            
REMARK 470     SER A 519    OG                                                  
REMARK 470     LEU A 522    CG   CD1  CD2                                       
REMARK 470     GLU A 524    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 526    NE   CZ   NH1  NH2                                  
REMARK 470     VAL A 528    CG1  CG2                                            
REMARK 470     LYS A 531    CE   NZ                                             
REMARK 470     LYS A 533    CG   CD   CE   NZ                                   
REMARK 470     SER A 534    OG                                                  
REMARK 470     THR A 535    OG1  CG2                                            
REMARK 470     ASN A 536    CG   OD1                                            
REMARK 470     ILE A 541    CD1                                                 
REMARK 470     GLN A 546    CG   CD   OE1  NE2                                  
REMARK 470     VAL A 548    CG1  CG2                                            
REMARK 470     ASN A 550    CG   OD1                                            
REMARK 470     ASP A 553    CG   OD1  OD2                                       
REMARK 470     LEU A 558    CG   CD1  CD2                                       
REMARK 470     GLU A 559    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 560    CD1                                                 
REMARK 470     ARG A 563    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 564    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 566    CD   CE   NZ                                        
REMARK 470     GLU A 567    CG   CD   OE1  OE2                                  
REMARK 470     MSE A 569    CG  SE    CE                                        
REMARK 470     ASP A 602    CG   OD1  OD2                                       
REMARK 470     SER A 603    OG                                                  
REMARK 470     ARG A 625    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 626    CG2                                                 
REMARK 470     LYS A 629    CG   CD   CE   NZ                                   
REMARK 470     ILE A 631    CD1                                                 
REMARK 470     ILE A 636    CG1  CG2  CD1                                       
REMARK 470     GLN A 638    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 639    CG   CD1  CD2                                       
REMARK 470     LYS A 642    CG   CD   CE   NZ                                   
REMARK 470     ILE A 648    CG1  CG2  CD1                                       
REMARK 470     LYS A 654    CG   CD   CE   NZ                                   
REMARK 470     ASP A 655    CG   OD1  OD2                                       
REMARK 470     ILE A 666    CD1                                                 
REMARK 470     VAL A 688    CG1  CG2                                            
REMARK 470     ILE A 704    CD1                                                 
REMARK 470     LYS A 709    CD   CE   NZ                                        
REMARK 470     PRO A 711    CG   CD                                             
REMARK 470     THR A 713    OG1  CG2                                            
REMARK 470     SER A 718    OG                                                  
REMARK 470     ILE A 722    CD1                                                 
REMARK 470     MSE A 732    CE                                                  
REMARK 470     LYS A 740    CE   NZ                                             
REMARK 470     SER A 741    OG                                                  
REMARK 470     LYS A 750    CG   CD   CE   NZ                                   
REMARK 470     LYS B   2    CG   CD   CE   NZ                                   
REMARK 470     ILE B   3    CG1  CG2  CD1                                       
REMARK 470     ILE B   6    CG1  CG2  CD1                                       
REMARK 470     ILE B   7    CG1  CG2  CD1                                       
REMARK 470     HIS B   8    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B   9    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  11    CG   CD   OE1  NE2                                  
REMARK 470     LEU B  14    CG   CD1  CD2                                       
REMARK 470     PHE B  16    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B  28    CD   OE1  NE2                                       
REMARK 470     THR B  31    CG2                                                 
REMARK 470     ASP B  33    CG   OD1  OD2                                       
REMARK 470     ILE B  36    CG1  CG2  CD1                                       
REMARK 470     VAL B  37    CG1  CG2                                            
REMARK 470     THR B  38    CG2                                                 
REMARK 470     ASN B  47    OD1                                                 
REMARK 470     ARG B  48    CZ   NH1  NH2                                       
REMARK 470     ARG B  49    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B  58    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B  61    OG                                                  
REMARK 470     ILE B  66    CD1                                                 
REMARK 470     LYS B  71    CG   CD   CE   NZ                                   
REMARK 470     LYS B  72    CD   CE   NZ                                        
REMARK 470     VAL B  82    CG1  CG2                                            
REMARK 470     HIS B  84    ND1  CD2  CE1  NE2                                  
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     SER B  90    OG                                                  
REMARK 470     GLU B  93    CD   OE1  OE2                                       
REMARK 470     ILE B  97    CD1                                                 
REMARK 470     LEU B 100    CG   CD1  CD2                                       
REMARK 470     LEU B 106    CG   CD1  CD2                                       
REMARK 470     GLU B 109    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 110    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 111    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 112    CG1  CG2  CD1                                       
REMARK 470     ARG B 113    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 114    CG1  CG2                                            
REMARK 470     GLN B 116    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 126    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 127    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 128    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU B 129    CG   CD1  CD2                                       
REMARK 470     VAL B 130    CG1  CG2                                            
REMARK 470     LYS B 131    CG   CD   CE   NZ                                   
REMARK 470     ILE B 132    CG1  CG2  CD1                                       
REMARK 470     LYS B 135    CG   CD   CE   NZ                                   
REMARK 470     LYS B 137    CG   CD   CE   NZ                                   
REMARK 470     ILE B 143    CD1                                                 
REMARK 470     SER B 150    OG                                                  
REMARK 470     ARG B 156    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 159    CZ   NH1  NH2                                       
REMARK 470     LEU B 160    CG   CD1  CD2                                       
REMARK 470     GLN B 161    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 162    CG   OD1                                            
REMARK 470     GLU B 163    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 165    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 177    CD   CE   NZ                                        
REMARK 470     LYS B 180    CD   CE   NZ                                        
REMARK 470     ARG B 184    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 190    CD1  CD2                                            
REMARK 470     LEU B 193    CG   CD1  CD2                                       
REMARK 470     VAL B 199    CG1  CG2                                            
REMARK 470     GLU B 200    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 470     ASP B 206    CG   OD1  OD2                                       
REMARK 470     SER B 208    OG                                                  
REMARK 470     GLN B 214    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 215    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B 216    CG1  CG2                                            
REMARK 470     SER B 218    OG                                                  
REMARK 470     LEU B 219    CG   CD1  CD2                                       
REMARK 470     SER B 221    OG                                                  
REMARK 470     SER B 222    OG                                                  
REMARK 470     TYR B 226    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL B 227    CG1  CG2                                            
REMARK 470     ASN B 228    CG   OD1                                            
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 232    CD1                                                 
REMARK 470     ASN B 233    CG   OD1                                            
REMARK 470     SER B 235    OG                                                  
REMARK 470     PHE B 236    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL B 239    CG1  CG2                                            
REMARK 470     GLU B 240    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 248    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU B 258    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 259    CG   CD   CE   NZ                                   
REMARK 470     GLU B 260    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 262    CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 470     SER B 263    OG                                                  
REMARK 470     ARG B 266    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 271    CD   CE   NZ                                        
REMARK 470     LYS B 272    CG   CD   CE   NZ                                   
REMARK 470     GLU B 275    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 277    CG   CD1  CD2                                       
REMARK 470     THR B 278    OG1  CG2                                            
REMARK 470     THR B 279    OG1  CG2                                            
REMARK 470     ILE B 281    CD1                                                 
REMARK 470     GLU B 295    CD   OE1  OE2                                       
REMARK 470     ILE B 296    CD1                                                 
REMARK 470     LYS B 302    CG   CD   CE   NZ                                   
REMARK 470     ASP B 303    CG   OD1  OD2                                       
REMARK 470     PHE B 306    CD1  CD2  CE1  CE2  CZ                              
REMARK 470     VAL B 309    CG1  CG2                                            
REMARK 470     ILE B 315    CG1  CG2  CD1                                       
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 325    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 327    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 330    CD   CE   NZ                                        
REMARK 470     ARG B 332    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 336    CG1  CG2                                            
REMARK 470     PHE B 338    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 342    CG   CD1  CD2                                       
REMARK 470     GLU B 343    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 344    CG   CD   CE   NZ                                   
REMARK 470     TYR B 347    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B 352    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 353    CG   CD1  CD2                                       
REMARK 470     LEU B 355    CG   CD1  CD2                                       
REMARK 470     LEU B 356    CG   CD1  CD2                                       
REMARK 470     GLU B 357    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 359    CG   CD1  CD2                                       
REMARK 470     GLN B 364    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 368    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 376    CD   CE   NZ                                        
REMARK 470     GLU B 377    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 379    CG   CD1  CD2                                       
REMARK 470     THR B 380    OG1  CG2                                            
REMARK 470     PHE B 382    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 383    CG2                                                 
REMARK 470     SER B 386    OG                                                  
REMARK 470     LYS B 387    CD   CE   NZ                                        
REMARK 470     VAL B 389    CG1  CG2                                            
REMARK 470     ARG B 392    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 394    CG2                                                 
REMARK 470     ARG B 395    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 398    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 399    CG   CD   OE1  NE2                                  
REMARK 470     SER B 402    OG                                                  
REMARK 470     ASP B 403    CG   OD1  OD2                                       
REMARK 470     GLN B 405    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 421    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 445    CG   CD   CE   NZ                                   
REMARK 470     LYS B 462    CE   NZ                                             
REMARK 470     ILE B 467    CD1                                                 
REMARK 470     TYR B 481    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE B 482    CD1                                                 
REMARK 470     SER B 483    OG                                                  
REMARK 470     GLU B 488    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 495    CG   CD   CE   NZ                                   
REMARK 470     GLN B 498    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 499    CD   CE   NZ                                        
REMARK 470     GLN B 506    CG   CD   OE1  NE2                                  
REMARK 470     THR B 511    OG1  CG2                                            
REMARK 470     LYS B 515    CD   CE   NZ                                        
REMARK 470     VAL B 517    CG1  CG2                                            
REMARK 470     SER B 519    OG                                                  
REMARK 470     ARG B 526    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 528    CG1  CG2                                            
REMARK 470     LYS B 531    CD   CE   NZ                                        
REMARK 470     LYS B 533    CG   CD   CE   NZ                                   
REMARK 470     SER B 534    OG                                                  
REMARK 470     THR B 535    OG1  CG2                                            
REMARK 470     GLN B 546    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 548    CG1  CG2                                            
REMARK 470     ARG B 551    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 552    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 556    CG   CD   CE   NZ                                   
REMARK 470     GLU B 559    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 565    CG   OD1  OD2                                       
REMARK 470     LYS B 566    CG   CD   CE   NZ                                   
REMARK 470     GLU B 567    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 568    CG1  CG2                                            
REMARK 470     MSE B 569    CG  SE    CE                                        
REMARK 470     ASP B 602    CG   OD1  OD2                                       
REMARK 470     SER B 603    OG                                                  
REMARK 470     SER B 606    OG                                                  
REMARK 470     SER B 624    OG                                                  
REMARK 470     ARG B 625    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 629    CG   CD   CE   NZ                                   
REMARK 470     LYS B 630    CG   CD   CE   NZ                                   
REMARK 470     ILE B 631    CD1                                                 
REMARK 470     ILE B 636    CG1  CG2  CD1                                       
REMARK 470     GLU B 643    CG   CD   OE1  OE2                                  
REMARK 470     ILE B 648    CD1                                                 
REMARK 470     ILE B 651    CD1                                                 
REMARK 470     LYS B 654    CE   NZ                                             
REMARK 470     ILE B 666    CD1                                                 
REMARK 470     GLU B 678    OE1  OE2                                            
REMARK 470     VAL B 688    CG1  CG2                                            
REMARK 470     LYS B 692    NZ                                                  
REMARK 470     MSE B 694    CE                                                  
REMARK 470     ILE B 704    CD1                                                 
REMARK 470     LYS B 709    CD   CE   NZ                                        
REMARK 470     PRO B 711    CG   CD                                             
REMARK 470     ASN B 715    CG   OD1                                            
REMARK 470     LEU B 716    CG   CD1  CD2                                       
REMARK 470     THR B 717    OG1  CG2                                            
REMARK 470     ILE B 722    CD1                                                 
REMARK 470     MSE B 732   SE    CE                                             
REMARK 470     LYS B 740    CG   CD   CE   NZ                                   
REMARK 470     SER B 741    OG                                                  
REMARK 470     GLN B 746    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 749    CD1                                                 
REMARK 470     LYS B 750    CG   CD   CE   NZ                                   
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    MSE A 679   CG  - SE   -  CE  ANGL. DEV. =  13.5 DEGREES          
REMARK 500    PRO B 107   C   -  N   -  CD  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    PRO B 711   C   -  N   -  CA  ANGL. DEV. =   9.4 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    PHE A  58      -73.75   -137.29                                   
REMARK 500    GLN A 116       32.24     70.17                                   
REMARK 500    GLN A 165      -50.44     81.80                                   
REMARK 500    ASP A 206       68.84   -155.43                                   
REMARK 500    GLN A 214       90.60    -69.30                                   
REMARK 500    TYR A 347       48.91   -109.01                                   
REMARK 500    GLN A 457       13.95     90.81                                   
REMARK 500    ASN A 472       33.47     70.55                                   
REMARK 500    LYS A 490      -37.08     70.58                                   
REMARK 500    GLU A 524      -84.78   -119.42                                   
REMARK 500    ASN A 525       42.88    -81.44                                   
REMARK 500    ALA A 597      143.13    -35.25                                   
REMARK 500    LEU A 633       58.37    -90.19                                   
REMARK 500    LYS A 654       74.40     60.11                                   
REMARK 500    PHE B  58      -68.77   -133.61                                   
REMARK 500    LYS B 490      -48.62     78.72                                   
REMARK 500    VAL B 548       46.18    -73.31                                   
REMARK 500    ASP B 622      160.59    -48.97                                   
REMARK 500    LEU B 716        2.37    -69.58                                   
REMARK 500    MSE B 730      -55.16     75.85                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3LN6   RELATED DB: PDB                                   
DBREF  3LN7 A    1   757  UNP    Q9CM00   GSHAB_PASMU      1    757             
DBREF  3LN7 B    1   757  UNP    Q9CM00   GSHAB_PASMU      1    757             
SEQRES   1 A  757  MSE LYS ILE GLN HIS ILE ILE HIS GLU ASN GLN LEU GLY          
SEQRES   2 A  757  LEU LEU PHE GLN GLN GLY SER PHE GLY LEU GLU LYS GLU          
SEQRES   3 A  757  SER GLN ARG VAL THR ALA ASP GLY ALA ILE VAL THR THR          
SEQRES   4 A  757  PRO HIS PRO ALA VAL PHE GLY ASN ARG ARG TYR HIS PRO          
SEQRES   5 A  757  TYR ILE GLN THR ASP PHE ALA GLU SER GLN LEU GLU LEU          
SEQRES   6 A  757  ILE THR PRO PRO THR LYS LYS LEU GLU ASP THR PHE ARG          
SEQRES   7 A  757  TRP LEU SER VAL ILE HIS GLU VAL VAL GLN ARG SER LEU          
SEQRES   8 A  757  PRO GLU GLU GLU TYR ILE PHE PRO LEU SER MSE PRO ALA          
SEQRES   9 A  757  GLY LEU PRO ALA GLU GLU GLN ILE ARG VAL ALA GLN LEU          
SEQRES  10 A  757  ASP ASN PRO GLU ASP VAL ALA TYR ARG GLU TYR LEU VAL          
SEQRES  11 A  757  LYS ILE TYR GLY LYS ASN LYS GLN MSE VAL SER GLY ILE          
SEQRES  12 A  757  HIS TYR ASN PHE GLN LEU SER PRO ASP LEU ILE THR ARG          
SEQRES  13 A  757  LEU PHE ARG LEU GLN ASN GLU TYR GLN SER ALA VAL ASP          
SEQRES  14 A  757  PHE GLN ASN ASP LEU TYR LEU LYS MSE ALA LYS ASN PHE          
SEQRES  15 A  757  LEU ARG TYR GLN TRP ILE LEU LEU TYR LEU LEU ALA ALA          
SEQRES  16 A  757  THR PRO THR VAL GLU SER ALA TYR PHE LYS ASP GLY SER          
SEQRES  17 A  757  PRO LEU ALA LYS GLY GLN PHE VAL ARG SER LEU ARG SER          
SEQRES  18 A  757  SER GLN TYR GLY TYR VAL ASN ASP PRO GLU ILE ASN VAL          
SEQRES  19 A  757  SER PHE ASP SER VAL GLU LYS TYR VAL GLU SER LEU GLU          
SEQRES  20 A  757  HIS TRP VAL SER THR GLY LYS LEU ILE ALA GLU LYS GLU          
SEQRES  21 A  757  PHE TYR SER ASN VAL ARG LEU ARG GLY ALA LYS LYS ALA          
SEQRES  22 A  757  ARG GLU PHE LEU THR THR GLY ILE GLN TYR LEU GLU PHE          
SEQRES  23 A  757  ARG LEU PHE ASP LEU ASN PRO PHE GLU ILE TYR GLY ILE          
SEQRES  24 A  757  SER LEU LYS ASP ALA LYS PHE ILE HIS VAL PHE ALA LEU          
SEQRES  25 A  757  PHE MSE ILE TRP MSE ASP HIS THR ALA ASP GLN GLU GLU          
SEQRES  26 A  757  VAL GLU LEU GLY LYS ALA ARG LEU ALA GLU VAL ALA PHE          
SEQRES  27 A  757  GLU HIS PRO LEU GLU LYS THR ALA TYR ALA VAL GLU GLY          
SEQRES  28 A  757  GLU LEU VAL LEU LEU GLU LEU LEU SER MSE LEU GLU GLN          
SEQRES  29 A  757  ILE GLY ALA GLU PRO GLU LEU PHE GLU ILE VAL LYS GLU          
SEQRES  30 A  757  LYS LEU THR GLN PHE THR ASP PRO SER LYS THR VAL ALA          
SEQRES  31 A  757  GLY ARG LEU VAL ARG ALA ILE GLU GLN ALA GLY SER ASP          
SEQRES  32 A  757  GLN GLN LEU GLY ALA GLN LEU ALA GLN GLN TYR LYS ALA          
SEQRES  33 A  757  GLN ALA PHE GLU ARG PHE TYR ALA LEU SER ALA PHE ASP          
SEQRES  34 A  757  ASN MSE GLU LEU SER THR GLN ALA LEU LEU PHE ASP VAL          
SEQRES  35 A  757  ILE GLN LYS GLY ILE HIS THR GLU ILE LEU ASP GLU ASN          
SEQRES  36 A  757  ASP GLN PHE LEU CYS LEU LYS TYR GLY ASP HIS ILE GLU          
SEQRES  37 A  757  TYR VAL LYS ASN GLY ASN MSE THR SER HIS ASP SER TYR          
SEQRES  38 A  757  ILE SER PRO LEU ILE MSE GLU ASN LYS VAL VAL THR LYS          
SEQRES  39 A  757  LYS VAL LEU GLN LYS ALA GLY PHE ASN VAL PRO GLN SER          
SEQRES  40 A  757  VAL GLU PHE THR SER LEU GLU LYS ALA VAL ALA SER TYR          
SEQRES  41 A  757  ALA LEU PHE GLU ASN ARG ALA VAL VAL ILE LYS PRO LYS          
SEQRES  42 A  757  SER THR ASN TYR GLY LEU GLY ILE THR ILE PHE GLN GLN          
SEQRES  43 A  757  GLY VAL GLN ASN ARG GLU ASP PHE ALA LYS ALA LEU GLU          
SEQRES  44 A  757  ILE ALA PHE ARG GLU ASP LYS GLU VAL MSE VAL GLU ASP          
SEQRES  45 A  757  TYR LEU VAL GLY THR GLU TYR ARG PHE PHE VAL LEU GLY          
SEQRES  46 A  757  ASP GLU THR LEU ALA VAL LEU LEU ARG VAL PRO ALA ASN          
SEQRES  47 A  757  VAL VAL GLY ASP SER VAL HIS SER VAL ALA GLU LEU VAL          
SEQRES  48 A  757  ALA MSE LYS ASN ASP HIS PRO LEU ARG GLY ASP GLY SER          
SEQRES  49 A  757  ARG THR PRO LEU LYS LYS ILE ALA LEU GLY GLU ILE GLU          
SEQRES  50 A  757  GLN LEU GLN LEU LYS GLU GLN GLY LEU THR ILE ASP SER          
SEQRES  51 A  757  ILE PRO ALA LYS ASP GLN LEU VAL GLN LEU ARG ALA ASN          
SEQRES  52 A  757  SER ASN ILE SER THR GLY GLY ASP SER ILE ASP MSE THR          
SEQRES  53 A  757  ASP GLU MSE HIS GLU SER TYR LYS GLN LEU ALA VAL GLY          
SEQRES  54 A  757  ILE THR LYS ALA MSE GLY ALA ALA VAL CYS GLY VAL ASP          
SEQRES  55 A  757  LEU ILE ILE PRO ASP LEU LYS GLN PRO ALA THR PRO ASN          
SEQRES  56 A  757  LEU THR SER TRP GLY VAL ILE GLU ALA ASN PHE ASN PRO          
SEQRES  57 A  757  MSE MSE MSE MSE HIS ILE PHE PRO TYR ALA GLY LYS SER          
SEQRES  58 A  757  ARG ARG LEU THR GLN ASN VAL ILE LYS MSE LEU PHE PRO          
SEQRES  59 A  757  GLU LEU GLU                                                  
SEQRES   1 B  757  MSE LYS ILE GLN HIS ILE ILE HIS GLU ASN GLN LEU GLY          
SEQRES   2 B  757  LEU LEU PHE GLN GLN GLY SER PHE GLY LEU GLU LYS GLU          
SEQRES   3 B  757  SER GLN ARG VAL THR ALA ASP GLY ALA ILE VAL THR THR          
SEQRES   4 B  757  PRO HIS PRO ALA VAL PHE GLY ASN ARG ARG TYR HIS PRO          
SEQRES   5 B  757  TYR ILE GLN THR ASP PHE ALA GLU SER GLN LEU GLU LEU          
SEQRES   6 B  757  ILE THR PRO PRO THR LYS LYS LEU GLU ASP THR PHE ARG          
SEQRES   7 B  757  TRP LEU SER VAL ILE HIS GLU VAL VAL GLN ARG SER LEU          
SEQRES   8 B  757  PRO GLU GLU GLU TYR ILE PHE PRO LEU SER MSE PRO ALA          
SEQRES   9 B  757  GLY LEU PRO ALA GLU GLU GLN ILE ARG VAL ALA GLN LEU          
SEQRES  10 B  757  ASP ASN PRO GLU ASP VAL ALA TYR ARG GLU TYR LEU VAL          
SEQRES  11 B  757  LYS ILE TYR GLY LYS ASN LYS GLN MSE VAL SER GLY ILE          
SEQRES  12 B  757  HIS TYR ASN PHE GLN LEU SER PRO ASP LEU ILE THR ARG          
SEQRES  13 B  757  LEU PHE ARG LEU GLN ASN GLU TYR GLN SER ALA VAL ASP          
SEQRES  14 B  757  PHE GLN ASN ASP LEU TYR LEU LYS MSE ALA LYS ASN PHE          
SEQRES  15 B  757  LEU ARG TYR GLN TRP ILE LEU LEU TYR LEU LEU ALA ALA          
SEQRES  16 B  757  THR PRO THR VAL GLU SER ALA TYR PHE LYS ASP GLY SER          
SEQRES  17 B  757  PRO LEU ALA LYS GLY GLN PHE VAL ARG SER LEU ARG SER          
SEQRES  18 B  757  SER GLN TYR GLY TYR VAL ASN ASP PRO GLU ILE ASN VAL          
SEQRES  19 B  757  SER PHE ASP SER VAL GLU LYS TYR VAL GLU SER LEU GLU          
SEQRES  20 B  757  HIS TRP VAL SER THR GLY LYS LEU ILE ALA GLU LYS GLU          
SEQRES  21 B  757  PHE TYR SER ASN VAL ARG LEU ARG GLY ALA LYS LYS ALA          
SEQRES  22 B  757  ARG GLU PHE LEU THR THR GLY ILE GLN TYR LEU GLU PHE          
SEQRES  23 B  757  ARG LEU PHE ASP LEU ASN PRO PHE GLU ILE TYR GLY ILE          
SEQRES  24 B  757  SER LEU LYS ASP ALA LYS PHE ILE HIS VAL PHE ALA LEU          
SEQRES  25 B  757  PHE MSE ILE TRP MSE ASP HIS THR ALA ASP GLN GLU GLU          
SEQRES  26 B  757  VAL GLU LEU GLY LYS ALA ARG LEU ALA GLU VAL ALA PHE          
SEQRES  27 B  757  GLU HIS PRO LEU GLU LYS THR ALA TYR ALA VAL GLU GLY          
SEQRES  28 B  757  GLU LEU VAL LEU LEU GLU LEU LEU SER MSE LEU GLU GLN          
SEQRES  29 B  757  ILE GLY ALA GLU PRO GLU LEU PHE GLU ILE VAL LYS GLU          
SEQRES  30 B  757  LYS LEU THR GLN PHE THR ASP PRO SER LYS THR VAL ALA          
SEQRES  31 B  757  GLY ARG LEU VAL ARG ALA ILE GLU GLN ALA GLY SER ASP          
SEQRES  32 B  757  GLN GLN LEU GLY ALA GLN LEU ALA GLN GLN TYR LYS ALA          
SEQRES  33 B  757  GLN ALA PHE GLU ARG PHE TYR ALA LEU SER ALA PHE ASP          
SEQRES  34 B  757  ASN MSE GLU LEU SER THR GLN ALA LEU LEU PHE ASP VAL          
SEQRES  35 B  757  ILE GLN LYS GLY ILE HIS THR GLU ILE LEU ASP GLU ASN          
SEQRES  36 B  757  ASP GLN PHE LEU CYS LEU LYS TYR GLY ASP HIS ILE GLU          
SEQRES  37 B  757  TYR VAL LYS ASN GLY ASN MSE THR SER HIS ASP SER TYR          
SEQRES  38 B  757  ILE SER PRO LEU ILE MSE GLU ASN LYS VAL VAL THR LYS          
SEQRES  39 B  757  LYS VAL LEU GLN LYS ALA GLY PHE ASN VAL PRO GLN SER          
SEQRES  40 B  757  VAL GLU PHE THR SER LEU GLU LYS ALA VAL ALA SER TYR          
SEQRES  41 B  757  ALA LEU PHE GLU ASN ARG ALA VAL VAL ILE LYS PRO LYS          
SEQRES  42 B  757  SER THR ASN TYR GLY LEU GLY ILE THR ILE PHE GLN GLN          
SEQRES  43 B  757  GLY VAL GLN ASN ARG GLU ASP PHE ALA LYS ALA LEU GLU          
SEQRES  44 B  757  ILE ALA PHE ARG GLU ASP LYS GLU VAL MSE VAL GLU ASP          
SEQRES  45 B  757  TYR LEU VAL GLY THR GLU TYR ARG PHE PHE VAL LEU GLY          
SEQRES  46 B  757  ASP GLU THR LEU ALA VAL LEU LEU ARG VAL PRO ALA ASN          
SEQRES  47 B  757  VAL VAL GLY ASP SER VAL HIS SER VAL ALA GLU LEU VAL          
SEQRES  48 B  757  ALA MSE LYS ASN ASP HIS PRO LEU ARG GLY ASP GLY SER          
SEQRES  49 B  757  ARG THR PRO LEU LYS LYS ILE ALA LEU GLY GLU ILE GLU          
SEQRES  50 B  757  GLN LEU GLN LEU LYS GLU GLN GLY LEU THR ILE ASP SER          
SEQRES  51 B  757  ILE PRO ALA LYS ASP GLN LEU VAL GLN LEU ARG ALA ASN          
SEQRES  52 B  757  SER ASN ILE SER THR GLY GLY ASP SER ILE ASP MSE THR          
SEQRES  53 B  757  ASP GLU MSE HIS GLU SER TYR LYS GLN LEU ALA VAL GLY          
SEQRES  54 B  757  ILE THR LYS ALA MSE GLY ALA ALA VAL CYS GLY VAL ASP          
SEQRES  55 B  757  LEU ILE ILE PRO ASP LEU LYS GLN PRO ALA THR PRO ASN          
SEQRES  56 B  757  LEU THR SER TRP GLY VAL ILE GLU ALA ASN PHE ASN PRO          
SEQRES  57 B  757  MSE MSE MSE MSE HIS ILE PHE PRO TYR ALA GLY LYS SER          
SEQRES  58 B  757  ARG ARG LEU THR GLN ASN VAL ILE LYS MSE LEU PHE PRO          
SEQRES  59 B  757  GLU LEU GLU                                                  
MODRES 3LN7 MSE A  102  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  178  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  314  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  317  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  361  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  431  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  475  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  487  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  569  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  613  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  675  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  679  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  694  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  729  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  730  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  731  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  732  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE A  751  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  102  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  139  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  178  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  314  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  317  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  361  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  431  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  475  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  487  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  569  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  613  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  675  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  679  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  694  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  729  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  730  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  731  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  732  MET  SELENOMETHIONINE                                   
MODRES 3LN7 MSE B  751  MET  SELENOMETHIONINE                                   
HET    MSE  A 102       8                                                       
HET    MSE  A 139       8                                                       
HET    MSE  A 178       8                                                       
HET    MSE  A 314       8                                                       
HET    MSE  A 317       8                                                       
HET    MSE  A 361       8                                                       
HET    MSE  A 431       8                                                       
HET    MSE  A 475       8                                                       
HET    MSE  A 487       8                                                       
HET    MSE  A 569       5                                                       
HET    MSE  A 613       8                                                       
HET    MSE  A 675       8                                                       
HET    MSE  A 679       8                                                       
HET    MSE  A 694       8                                                       
HET    MSE  A 729       8                                                       
HET    MSE  A 730       8                                                       
HET    MSE  A 731       8                                                       
HET    MSE  A 732       7                                                       
HET    MSE  A 751       8                                                       
HET    MSE  B 102       8                                                       
HET    MSE  B 139       8                                                       
HET    MSE  B 178       8                                                       
HET    MSE  B 314       8                                                       
HET    MSE  B 317       8                                                       
HET    MSE  B 361       8                                                       
HET    MSE  B 431       8                                                       
HET    MSE  B 475       8                                                       
HET    MSE  B 487       8                                                       
HET    MSE  B 569       5                                                       
HET    MSE  B 613       8                                                       
HET    MSE  B 675       8                                                       
HET    MSE  B 679       8                                                       
HET    MSE  B 694       7                                                       
HET    MSE  B 729       8                                                       
HET    MSE  B 730       8                                                       
HET    MSE  B 731       8                                                       
HET    MSE  B 732       6                                                       
HET    MSE  B 751       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    38(C5 H11 N O2 SE)                                           
HELIX    1   1 GLN A    4  GLN A   11  5                                   8    
HELIX    2   2 LEU A   12  GLN A   18  1                                   7    
HELIX    3   3 LYS A   72  LEU A   91  1                                  20    
HELIX    4   4 ASN A  119  GLY A  134  1                                  16    
HELIX    5   5 LYS A  135  VAL A  140  1                                   6    
HELIX    6   6 SER A  150  GLN A  161  1                                  12    
HELIX    7   7 SER A  166  LEU A  193  1                                  28    
HELIX    8   8 SER A  238  THR A  252  1                                  15    
HELIX    9   9 LYS A  272  ARG A  274  5                                   3    
HELIX   10  10 GLU A  275  GLY A  280  1                                   6    
HELIX   11  11 SER A  300  MSE A  317  1                                  18    
HELIX   12  12 ASP A  322  GLU A  339  1                                  18    
HELIX   13  13 TYR A  347  ILE A  365  1                                  19    
HELIX   14  14 GLU A  368  ASP A  384  1                                  17    
HELIX   15  15 PRO A  385  LYS A  387  5                                   3    
HELIX   16  16 THR A  388  ALA A  400  1                                  13    
HELIX   17  17 SER A  402  GLU A  420  1                                  19    
HELIX   18  18 GLU A  432  GLY A  446  1                                  15    
HELIX   19  19 TYR A  481  LYS A  490  1                                  10    
HELIX   20  20 LYS A  490  GLY A  501  1                                  12    
HELIX   21  21 SER A  512  SER A  519  1                                   8    
HELIX   22  22 TYR A  520  PHE A  523  5                                   4    
HELIX   23  23 ASN A  550  ASP A  565  1                                  16    
HELIX   24  24 ASP A  602  VAL A  604  5                                   3    
HELIX   25  25 SER A  606  ASP A  616  1                                  11    
HELIX   26  26 GLY A  634  GLY A  645  1                                  12    
HELIX   27  27 ASN A  665  GLY A  669  5                                   5    
HELIX   28  28 HIS A  680  GLY A  695  1                                  16    
HELIX   29  29 MSE A  729  PHE A  735  1                                   7    
HELIX   30  30 LEU A  744  PHE A  753  1                                  10    
HELIX   31  31 ILE B    6  GLN B   11  1                                   6    
HELIX   32  32 LEU B   12  GLN B   18  1                                   7    
HELIX   33  33 LYS B   72  LEU B   91  1                                  20    
HELIX   34  34 ARG B  126  GLY B  134  1                                   9    
HELIX   35  35 LYS B  135  VAL B  140  5                                   6    
HELIX   36  36 SER B  150  GLN B  161  1                                  12    
HELIX   37  37 SER B  166  LEU B  193  1                                  28    
HELIX   38  38 SER B  238  SER B  251  1                                  14    
HELIX   39  39 ALA B  273  GLY B  280  1                                   8    
HELIX   40  40 SER B  300  MSE B  317  1                                  18    
HELIX   41  41 ASP B  322  GLU B  339  1                                  18    
HELIX   42  42 TYR B  347  GLY B  366  1                                  20    
HELIX   43  43 GLU B  368  ASP B  384  1                                  17    
HELIX   44  44 PRO B  385  LYS B  387  5                                   3    
HELIX   45  45 THR B  388  GLY B  401  1                                  14    
HELIX   46  46 SER B  402  PHE B  419  1                                  18    
HELIX   47  47 GLU B  420  PHE B  422  5                                   3    
HELIX   48  48 LEU B  425  ASP B  429  5                                   5    
HELIX   49  49 GLU B  432  GLY B  446  1                                  15    
HELIX   50  50 TYR B  481  LYS B  490  1                                  10    
HELIX   51  51 LYS B  490  GLY B  501  1                                  12    
HELIX   52  52 SER B  512  SER B  519  1                                   8    
HELIX   53  53 TYR B  520  PHE B  523  5                                   4    
HELIX   54  54 ASN B  550  ASP B  565  1                                  16    
HELIX   55  55 SER B  606  ASN B  615  1                                  10    
HELIX   56  56 GLY B  634  GLN B  644  1                                  11    
HELIX   57  57 HIS B  680  GLY B  695  1                                  16    
HELIX   58  58 MSE B  730  PHE B  735  1                                   6    
HELIX   59  59 ARG B  743  PHE B  753  1                                  11    
SHEET    1   A 6 ILE A  54  GLN A  55  0                                        
SHEET    2   A 6 GLN A  62  THR A  70 -1  O  GLU A  64   N  GLN A  55           
SHEET    3   A 6 GLY A  19  GLN A  28 -1  N  SER A  27   O  LEU A  63           
SHEET    4   A 6 HIS A 144  LEU A 149 -1  O  HIS A 144   N  GLU A  24           
SHEET    5   A 6 TYR A 283  PHE A 286 -1  O  PHE A 286   N  TYR A 145           
SHEET    6   A 6 VAL A 265  ARG A 268 -1  N  ARG A 266   O  GLU A 285           
SHEET    1   B 2 VAL A  30  THR A  31  0                                        
SHEET    2   B 2 GLU A  95  TYR A  96 -1  O  TYR A  96   N  VAL A  30           
SHEET    1   C 3 HIS A 448  ASP A 453  0                                        
SHEET    2   C 3 PHE A 458  TYR A 463 -1  O  LYS A 462   N  HIS A 448           
SHEET    3   C 3 HIS A 466  LYS A 471 -1  O  HIS A 466   N  TYR A 463           
SHEET    1   D 4 SER A 507  PHE A 510  0                                        
SHEET    2   D 4 VAL A 568  ASP A 572 -1  O  VAL A 568   N  PHE A 510           
SHEET    3   D 4 VAL A 528  PRO A 532 -1  N  VAL A 529   O  GLU A 571           
SHEET    4   D 4 THR A 542  ILE A 543 -1  O  THR A 542   N  ILE A 530           
SHEET    1   E 5 SER A 672  ASP A 674  0                                        
SHEET    2   E 5 GLU A 587  ARG A 594 -1  N  LEU A 593   O  ILE A 673           
SHEET    3   E 5 THR A 577  LEU A 584 -1  N  PHE A 582   O  ALA A 590           
SHEET    4   E 5 VAL A 698  ILE A 705 -1  O  LEU A 703   N  TYR A 579           
SHEET    5   E 5 GLY A 720  ASN A 725 -1  O  GLU A 723   N  ASP A 702           
SHEET    1   F 2 ASN A 598  VAL A 600  0                                        
SHEET    2   F 2 LEU A 657  GLN A 659 -1  O  VAL A 658   N  VAL A 599           
SHEET    1   G 2 ARG A 620  GLY A 621  0                                        
SHEET    2   G 2 LEU A 628  LYS A 629  1  O  LEU A 628   N  GLY A 621           
SHEET    1   H 4 ILE B  54  THR B  56  0                                        
SHEET    2   H 4 GLN B  62  THR B  70 -1  O  GLU B  64   N  GLN B  55           
SHEET    3   H 4 GLY B  19  THR B  31 -1  N  SER B  27   O  LEU B  63           
SHEET    4   H 4 GLU B  95  ILE B  97 -1  O  TYR B  96   N  VAL B  30           
SHEET    1   I 6 ILE B  54  THR B  56  0                                        
SHEET    2   I 6 GLN B  62  THR B  70 -1  O  GLU B  64   N  GLN B  55           
SHEET    3   I 6 GLY B  19  THR B  31 -1  N  SER B  27   O  LEU B  63           
SHEET    4   I 6 GLY B 142  LEU B 149 -1  O  GLY B 142   N  GLU B  26           
SHEET    5   I 6 LEU B 284  ASP B 290 -1  O  PHE B 286   N  TYR B 145           
SHEET    6   I 6 VAL B 265  ARG B 266 -1  N  ARG B 266   O  GLU B 285           
SHEET    1   J 3 HIS B 448  ASP B 453  0                                        
SHEET    2   J 3 PHE B 458  TYR B 463 -1  O  LYS B 462   N  HIS B 448           
SHEET    3   J 3 HIS B 466  LYS B 471 -1  O  GLU B 468   N  LEU B 461           
SHEET    1   K 3 SER B 507  PHE B 510  0                                        
SHEET    2   K 3 VAL B 568  ASP B 572 -1  O  VAL B 570   N  VAL B 508           
SHEET    3   K 3 VAL B 528  PRO B 532 -1  N  LYS B 531   O  MSE B 569           
SHEET    1   L 5 ASP B 671  ASP B 674  0                                        
SHEET    2   L 5 GLU B 587  VAL B 595 -1  N  LEU B 593   O  ILE B 673           
SHEET    3   L 5 THR B 577  LEU B 584 -1  N  ARG B 580   O  LEU B 592           
SHEET    4   L 5 GLY B 700  ILE B 705 -1  O  LEU B 703   N  TYR B 579           
SHEET    5   L 5 GLY B 720  ASN B 725 -1  O  ASN B 725   N  GLY B 700           
SHEET    1   M 2 ASN B 598  VAL B 600  0                                        
SHEET    2   M 2 LEU B 657  GLN B 659 -1  O  VAL B 658   N  VAL B 599           
LINK         C   SER A 101                 N   MSE A 102     1555   1555  1.33  
LINK         C   MSE A 102                 N   PRO A 103     1555   1555  1.34  
LINK         C   GLN A 138                 N   MSE A 139     1555   1555  1.32  
LINK         C   MSE A 139                 N   VAL A 140     1555   1555  1.32  
LINK         C   LYS A 177                 N   MSE A 178     1555   1555  1.32  
LINK         C   MSE A 178                 N   ALA A 179     1555   1555  1.32  
LINK         C   PHE A 313                 N   MSE A 314     1555   1555  1.32  
LINK         C   MSE A 314                 N   ILE A 315     1555   1555  1.32  
LINK         C   TRP A 316                 N   MSE A 317     1555   1555  1.32  
LINK         C   MSE A 317                 N   ASP A 318     1555   1555  1.33  
LINK         C   SER A 360                 N   MSE A 361     1555   1555  1.32  
LINK         C   MSE A 361                 N   LEU A 362     1555   1555  1.32  
LINK         C   ASN A 430                 N   MSE A 431     1555   1555  1.32  
LINK         C   MSE A 431                 N   GLU A 432     1555   1555  1.33  
LINK         C   ASN A 474                 N   MSE A 475     1555   1555  1.33  
LINK         C   MSE A 475                 N   THR A 476     1555   1555  1.32  
LINK         C   ILE A 486                 N   MSE A 487     1555   1555  1.32  
LINK         C   MSE A 487                 N   GLU A 488     1555   1555  1.34  
LINK         C   VAL A 568                 N   MSE A 569     1555   1555  1.32  
LINK         C   MSE A 569                 N   VAL A 570     1555   1555  1.32  
LINK         C   ALA A 612                 N   MSE A 613     1555   1555  1.31  
LINK         C   MSE A 613                 N   LYS A 614     1555   1555  1.34  
LINK         C   ASP A 674                 N   MSE A 675     1555   1555  1.33  
LINK         C   MSE A 675                 N   THR A 676     1555   1555  1.32  
LINK         C   GLU A 678                 N   MSE A 679     1555   1555  1.33  
LINK         C   MSE A 679                 N   HIS A 680     1555   1555  1.32  
LINK         C   ALA A 693                 N   MSE A 694     1555   1555  1.32  
LINK         C   MSE A 694                 N   GLY A 695     1555   1555  1.32  
LINK         C   PRO A 728                 N   MSE A 729     1555   1555  1.33  
LINK         C   MSE A 729                 N   MSE A 730     1555   1555  1.32  
LINK         C   MSE A 730                 N   MSE A 731     1555   1555  1.32  
LINK         C   MSE A 731                 N   MSE A 732     1555   1555  1.32  
LINK         C   MSE A 732                 N   HIS A 733     1555   1555  1.33  
LINK         C   LYS A 750                 N   MSE A 751     1555   1555  1.31  
LINK         C   MSE A 751                 N   LEU A 752     1555   1555  1.33  
LINK         C   SER B 101                 N   MSE B 102     1555   1555  1.33  
LINK         C   MSE B 102                 N   PRO B 103     1555   1555  1.35  
LINK         C   GLN B 138                 N   MSE B 139     1555   1555  1.33  
LINK         C   MSE B 139                 N   VAL B 140     1555   1555  1.33  
LINK         C   LYS B 177                 N   MSE B 178     1555   1555  1.33  
LINK         C   MSE B 178                 N   ALA B 179     1555   1555  1.32  
LINK         C   PHE B 313                 N   MSE B 314     1555   1555  1.33  
LINK         C   MSE B 314                 N   ILE B 315     1555   1555  1.33  
LINK         C   TRP B 316                 N   MSE B 317     1555   1555  1.33  
LINK         C   MSE B 317                 N   ASP B 318     1555   1555  1.33  
LINK         C   SER B 360                 N   MSE B 361     1555   1555  1.33  
LINK         C   MSE B 361                 N   LEU B 362     1555   1555  1.34  
LINK         C   ASN B 430                 N   MSE B 431     1555   1555  1.32  
LINK         C   MSE B 431                 N   GLU B 432     1555   1555  1.32  
LINK         C   ASN B 474                 N   MSE B 475     1555   1555  1.33  
LINK         C   MSE B 475                 N   THR B 476     1555   1555  1.33  
LINK         C   ILE B 486                 N   MSE B 487     1555   1555  1.32  
LINK         C   MSE B 487                 N   GLU B 488     1555   1555  1.33  
LINK         C   VAL B 568                 N   MSE B 569     1555   1555  1.33  
LINK         C   MSE B 569                 N   VAL B 570     1555   1555  1.33  
LINK         C   ALA B 612                 N   MSE B 613     1555   1555  1.32  
LINK         C   MSE B 613                 N   LYS B 614     1555   1555  1.32  
LINK         C   ASP B 674                 N   MSE B 675     1555   1555  1.33  
LINK         C   MSE B 675                 N   THR B 676     1555   1555  1.32  
LINK         C   GLU B 678                 N   MSE B 679     1555   1555  1.32  
LINK         C   MSE B 679                 N   HIS B 680     1555   1555  1.33  
LINK         C   ALA B 693                 N   MSE B 694     1555   1555  1.33  
LINK         C   MSE B 694                 N   GLY B 695     1555   1555  1.31  
LINK         C   PRO B 728                 N   MSE B 729     1555   1555  1.33  
LINK         C   MSE B 729                 N   MSE B 730     1555   1555  1.33  
LINK         C   MSE B 730                 N   MSE B 731     1555   1555  1.32  
LINK         C   MSE B 731                 N   MSE B 732     1555   1555  1.33  
LINK         C   MSE B 732                 N   HIS B 733     1555   1555  1.33  
LINK         C   LYS B 750                 N   MSE B 751     1555   1555  1.32  
LINK         C   MSE B 751                 N   LEU B 752     1555   1555  1.33  
CRYST1  205.240   87.070  145.980  90.00 126.53  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004872  0.000000  0.003609        0.00000                         
SCALE2      0.000000  0.011485  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system