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Entry: 1GSO
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HEADER    LIGASE                                  08-SEP-98   1GSO              
TITLE     GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E.               
TITLE    2 COLI.                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE);           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PURD GEN PRODUCT;                                           
COMPND   5 EC: 6.3.4.13;                                                        
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 STRAIN: TX635;                                                       
SOURCE   5 CELL_LINE: B834(DE3)                                                 
KEYWDS    GAR-SYN, GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE, ATP-GRASP,            
KEYWDS   2 PURINE DE NOVO BIOSYNTHETIC PATHWAY, SUBSTRATE CHANNELING,           
KEYWDS   3 LIGASE                                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.WANG,T.J.KAPPOCK,J.STUBBE,S.E.EALICK                                
REVDAT   5   24-FEB-09 1GSO    1       VERSN                                    
REVDAT   4   01-APR-03 1GSO    1       JRNL                                     
REVDAT   3   05-MAY-00 1GSO    1       JRNL                                     
REVDAT   2   22-DEC-99 1GSO    4       HEADER COMPND REMARK JRNL                
REVDAT   2 2                   4       ATOM   SOURCE SEQRES                     
REVDAT   1   09-DEC-98 1GSO    0                                                
JRNL        AUTH   W.WANG,T.J.KAPPOCK,J.STUBBE,S.E.EALICK                       
JRNL        TITL   X-RAY CRYSTAL STRUCTURE OF GLYCINAMIDE                       
JRNL        TITL 2 RIBONUCLEOTIDE SYNTHETASE FROM ESCHERICHIA COLI.             
JRNL        REF    BIOCHEMISTRY                  V.  37 15647 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9843369                                                      
JRNL        DOI    10.1021/BI981405N                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.M.WEAVER,W.WANG,S.E.EALICK                                 
REMARK   1  TITL   PURIFICATION, CRYSTALLIZATION AND PRELIMINARY                
REMARK   1  TITL 2 X-RAY DIFFRACTION DATA FROM SELENOMETHIONE                   
REMARK   1  TITL 3 GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE                        
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  55   518 1999              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 58307                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.247                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5925                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.67                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5578                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 604                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3161                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : NULL                                    
REMARK   3   SOLVENT ATOMS            : 305                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.25                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.15                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GSO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB008093.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-AUG-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F2                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979419, 0.979104, 0.967642,      
REMARK 200                                   0.9190                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58385                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 4.30000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 17.40000                           
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MADSYS, SNB, MLPHARE, DM                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.3, 0.2M AMMONIUM            
REMARK 280  SULFATE, 26% PEG 5K MONOMETHYLETHER, HANGING DROP VAPOR             
REMARK 280  DEFFUSION, VAPOR DIFFUSION - HANGING DROP                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.11000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.88500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.21000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.88500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.11000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.21000            
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: 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 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     ASP A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     ALA A   150                                                      
REMARK 465     ALA A   151                                                      
REMARK 465     GLY A   152                                                      
REMARK 465     ASP A   373                                                      
REMARK 465     ASP A   374                                                      
REMARK 465     GLU A   375                                                      
REMARK 465     GLU A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     ASN A   429                                                      
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    ASN A   8       21.19   -148.84                                   
REMARK 500    GLU A 129      -55.53    122.67                                   
REMARK 500    MET A 209      -80.57   -109.95                                   
REMARK 500    CYS A 289       30.15    -85.94                                   
REMARK 500    ASP A 293      -75.17    -48.30                                   
REMARK 500    ALA A 367      -90.33   -118.49                                   
REMARK 500    ASN A 380       46.35   -156.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 752        DISTANCE =  5.54 ANGSTROMS                       
DBREF  1GSO A    1   429  UNP    P15640   PUR2_ECOLI       1    429             
SEQADV 1GSO GLU A   -2  UNP  P15640              INSERTION                      
SEQADV 1GSO PHE A   -1  UNP  P15640              INSERTION                      
SEQADV 1GSO LEU A  294  UNP  P15640    PRO   294 ENGINEERED                     
SEQRES   1 A  431  GLU PHE MET LYS VAL LEU VAL ILE GLY ASN GLY GLY ARG          
SEQRES   2 A  431  GLU HIS ALA LEU ALA TRP LYS ALA ALA GLN SER PRO LEU          
SEQRES   3 A  431  VAL GLU THR VAL PHE VAL ALA PRO GLY ASN ALA GLY THR          
SEQRES   4 A  431  ALA LEU GLU PRO ALA LEU GLN ASN VAL ALA ILE GLY VAL          
SEQRES   5 A  431  THR ASP ILE PRO ALA LEU LEU ASP PHE ALA GLN ASN GLU          
SEQRES   6 A  431  LYS ILE ASP LEU THR ILE VAL GLY PRO GLU ALA PRO LEU          
SEQRES   7 A  431  VAL LYS GLY VAL VAL ASP THR PHE ARG ALA ALA GLY LEU          
SEQRES   8 A  431  LYS ILE PHE GLY PRO THR ALA GLY ALA ALA GLN LEU GLU          
SEQRES   9 A  431  GLY SER LYS ALA PHE THR LYS ASP PHE LEU ALA ARG HIS          
SEQRES  10 A  431  LYS ILE PRO THR ALA GLU TYR GLN ASN PHE THR GLU VAL          
SEQRES  11 A  431  GLU PRO ALA LEU ALA TYR LEU ARG GLU LYS GLY ALA PRO          
SEQRES  12 A  431  ILE VAL ILE LYS ALA ASP GLY LEU ALA ALA GLY LYS GLY          
SEQRES  13 A  431  VAL ILE VAL ALA MET THR LEU GLU GLU ALA GLU ALA ALA          
SEQRES  14 A  431  VAL HIS ASP MET LEU ALA GLY ASN ALA PHE GLY ASP ALA          
SEQRES  15 A  431  GLY HIS ARG ILE VAL ILE GLU GLU PHE LEU ASP GLY GLU          
SEQRES  16 A  431  GLU ALA SER PHE ILE VAL MET VAL ASP GLY GLU HIS VAL          
SEQRES  17 A  431  LEU PRO MET ALA THR SER GLN ASP HIS LYS ARG VAL GLY          
SEQRES  18 A  431  ASP LYS ASP THR GLY PRO ASN THR GLY GLY MET GLY ALA          
SEQRES  19 A  431  TYR SER PRO ALA PRO VAL VAL THR ASP ASP VAL HIS GLN          
SEQRES  20 A  431  ARG THR MET GLU ARG ILE ILE TRP PRO THR VAL LYS GLY          
SEQRES  21 A  431  MET ALA ALA GLU GLY ASN THR TYR THR GLY PHE LEU TYR          
SEQRES  22 A  431  ALA GLY LEU MET ILE ASP LYS GLN GLY ASN PRO LYS VAL          
SEQRES  23 A  431  ILE GLU PHE ASN CYS ARG PHE GLY ASP LEU GLU THR GLN          
SEQRES  24 A  431  PRO ILE MET LEU ARG MET LYS SER ASP LEU VAL GLU LEU          
SEQRES  25 A  431  CYS LEU ALA ALA CYS GLU SER LYS LEU ASP GLU LYS THR          
SEQRES  26 A  431  SER GLU TRP ASP GLU ARG ALA SER LEU GLY VAL VAL MET          
SEQRES  27 A  431  ALA ALA GLY GLY TYR PRO GLY ASP TYR ARG THR GLY ASP          
SEQRES  28 A  431  VAL ILE HIS GLY LEU PRO LEU GLU GLU VAL ALA GLY GLY          
SEQRES  29 A  431  LYS VAL PHE HIS ALA GLY THR LYS LEU ALA ASP ASP GLU          
SEQRES  30 A  431  GLN VAL VAL THR ASN GLY GLY ARG VAL LEU CYS VAL THR          
SEQRES  31 A  431  ALA LEU GLY HIS THR VAL ALA GLU ALA GLN LYS ARG ALA          
SEQRES  32 A  431  TYR ALA LEU MET THR ASP ILE HIS TRP ASP ASP CYS PHE          
SEQRES  33 A  431  CYS ARG LYS ASP ILE GLY TRP ARG ALA ILE GLU ARG GLU          
SEQRES  34 A  431  GLN ASN                                                      
FORMUL   2  HOH   *299(H2 O)                                                    
HELIX    1   1 GLY A   10  GLN A   21  1                                  12    
HELIX    2   2 ALA A   35  LEU A   39  1                                   5    
HELIX    3   3 ILE A   53  ASN A   62  1                                  10    
HELIX    4   4 GLU A   73  VAL A   77  1                                   5    
HELIX    5   5 VAL A   80  ALA A   86  1                                   7    
HELIX    6   6 ALA A   98  GLY A  103  5                                   6    
HELIX    7   7 LYS A  105  ARG A  114  1                                  10    
HELIX    8   8 PRO A  130  LYS A  138  1                                   9    
HELIX    9   9 LEU A  161  HIS A  169  1                                   9    
HELIX   10  10 ASP A  241  ARG A  250  1                                  10    
HELIX   11  11 ILE A  252  ALA A  261  1                                  10    
HELIX   12  12 GLU A  295  ARG A  302  1                                   8    
HELIX   13  13 LEU A  307  GLU A  316  1                                  10    
HELIX   14  14 LEU A  319  GLU A  321  5                                   3    
HELIX   15  15 VAL A  394  MET A  405  1                                  12    
HELIX   16  16 TRP A  421  GLU A  425  1                                   5    
SHEET    1   A 4 LEU A  67  VAL A  70  0                                        
SHEET    2   A 4 MET A   1  GLY A   7  1  N  LEU A   4   O  LEU A  67           
SHEET    3   A 4 VAL A  25  PRO A  32  1  N  GLU A  26   O  MET A   1           
SHEET    4   A 4 LEU A  43  ASN A  45  1  N  GLN A  44   O  VAL A  28           
SHEET    1   B 4 TYR A 122  PHE A 125  0                                        
SHEET    2   B 4 ILE A 184  GLU A 188 -1  N  ILE A 186   O  GLN A 123           
SHEET    3   B 4 ILE A 142  LYS A 145 -1  N  LYS A 145   O  VAL A 185           
SHEET    4   B 4 VAL A 155  ALA A 158 -1  N  ALA A 158   O  ILE A 142           
SHEET    1   C 4 VAL A 206  SER A 212  0                                        
SHEET    2   C 4 GLY A 192  ASP A 202 -1  N  MET A 200   O  LEU A 207           
SHEET    3   C 4 THR A 267  ASP A 277 -1  N  ILE A 276   O  GLU A 193           
SHEET    4   C 4 PRO A 282  ASN A 288 -1  N  ASN A 288   O  TYR A 271           
SHEET    1   D 5 GLN A 213  HIS A 215  0                                        
SHEET    2   D 5 GLY A 231  SER A 234 -1  N  TYR A 233   O  GLN A 213           
SHEET    3   D 5 SER A 331  ALA A 337 -1  N  GLY A 333   O  ALA A 232           
SHEET    4   D 5 ARG A 383  THR A 388 -1  N  VAL A 387   O  VAL A 334           
SHEET    5   D 5 LYS A 363  HIS A 366 -1  N  PHE A 365   O  CYS A 386           
CISPEP   1 ALA A   31    PRO A   32          0        -0.22                     
CISPEP   2 ALA A  140    PRO A  141          0        -0.04                     
CISPEP   3 SER A  234    PRO A  235          0        -0.22                     
CISPEP   4 TYR A  341    PRO A  342          0        -0.33                     
CRYST1   56.220   62.420  129.770  90.00  90.00  90.00 P 21 21 21    4          
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      0.017787  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016020  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007706        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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