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Database: PDB
Entry: 1YXM
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Original site: 1YXM 
HEADER    OXIDOREDUCTASE                          22-FEB-05   1YXM              
TITLE     CRYSTAL STRUCTURE OF PEROXISOMAL TRANS 2-ENOYL COA REDUCTASE          
CAVEAT     1YXM    THERE ARE SEVERAL CHIRALITY ERRORS IN CHAIN D.               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOMAL TRANS 2-ENOYL COA REDUCTASE;                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PECRA;                                                      
COMPND   5 EC: 1.3.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PECR;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: HPECR-P11T                                
KEYWDS    PERIOXISOMES, FATTY ACID SYNTHESIS, ENOYL COA, SHORT-CHAIN            
KEYWDS   2 DEHYDROGENASES/REDUCTASES, STRUCTURAL GENOMICS, STRUCTURAL           
KEYWDS   3 GENOMICS CONSORTIUM, SGC, OXIDOREDUCTASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.JANSSON,S.NG,C.ARROWSMITH,S.SHARMA,A.M.EDWARDS,F.VON                
AUTHOR   2 DELFT,M.SUNDSTROM,U.OPPERMANN,STRUCTURAL GENOMICS                    
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   5   24-FEB-09 1YXM    1       VERSN                                    
REVDAT   4   03-MAY-05 1YXM    1       JRNL   AUTHOR                            
REVDAT   3   19-APR-05 1YXM    1       AUTHOR JRNL   REMARK                     
REVDAT   2   22-MAR-05 1YXM    1       AUTHOR JRNL                              
REVDAT   1   15-MAR-05 1YXM    0                                                
JRNL        AUTH   A.JANSSON,S.NG,C.ARROWSMITH,S.SHARMA,A.M.EDWARDS,            
JRNL        AUTH 2 F.VON DELFT,M.SUNDSTROM,U.OPPERMANN                          
JRNL        TITL   CRYSTAL STRUCTURE OF PERIXOMAL TRANS 2-ENOYL COA             
JRNL        TITL 2 REDUCTASE (PECRA)                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 81985                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4302                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5758                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.62                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 292                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8288                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 374                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.02000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.171         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.155         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.106         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.325         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8493 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  7732 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11560 ; 1.676 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17885 ; 0.879 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1133 ;12.739 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   296 ;42.773 ;24.459       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1284 ;13.487 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;11.128 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1341 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9583 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1658 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1823 ; 0.217 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  7682 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4307 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4889 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   302 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    18 ; 0.169 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    46 ; 0.172 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.349 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5701 ; 1.006 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2348 ; 0.422 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8943 ; 1.648 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3172 ; 2.531 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2615 ; 3.659 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C D                         
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      7       A     300      5                      
REMARK   3           1     B      8       B     298      5                      
REMARK   3           1     C      5       C     299      5                      
REMARK   3           1     D      8       D     300      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1480 ;  0.31 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1480 ;  0.44 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   1480 ;  0.37 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    D    (A):   1480 ;  0.32 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1965 ;  0.63 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1965 ;  0.59 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    C    (A):   1965 ;  0.56 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    D    (A):   1965 ;  0.56 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1480 ;  1.73 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1480 ;  2.79 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   1480 ;  2.62 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    D (A**2):   1480 ;  1.94 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1965 ;  2.28 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1965 ;  3.23 ; 10.00           
REMARK   3   LOOSE THERMAL      1    C (A**2):   1965 ;  3.32 ; 10.00           
REMARK   3   LOOSE THERMAL      1    D (A**2):   1965 ;  2.54 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 1YXM COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-MAR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032040.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88511                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.350                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 10.000                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 42.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.44500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: PDB ENTRY 1VL8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM CHLORIDE,      
REMARK 280  SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,           
REMARK 280  TEMPERATURE 294K                                                    
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       39.07600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.95450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.50700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.95450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.07600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.50700            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     TRP A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     TRP B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     VAL B   210                                                      
REMARK 465     GLU B   211                                                      
REMARK 465     ASN B   212                                                      
REMARK 465     TYR B   213                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     TRP B   216                                                      
REMARK 465     GLY B   217                                                      
REMARK 465     GLU B   299                                                      
REMARK 465     LYS B   300                                                      
REMARK 465     ALA B   301                                                      
REMARK 465     LYS B   302                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     TRP C     4                                                      
REMARK 465     PRO C    67                                                      
REMARK 465     PRO C    68                                                      
REMARK 465     THR C    69                                                      
REMARK 465     GLY C   109                                                      
REMARK 465     GLY C   110                                                      
REMARK 465     GLN C   111                                                      
REMARK 465     PHE C   112                                                      
REMARK 465     LEU C   113                                                      
REMARK 465     SER C   114                                                      
REMARK 465     PRO C   115                                                      
REMARK 465     ALA C   116                                                      
REMARK 465     GLU C   117                                                      
REMARK 465     HIS C   118                                                      
REMARK 465     ILE C   119                                                      
REMARK 465     SER C   120                                                      
REMARK 465     SER C   121                                                      
REMARK 465     LYS C   122                                                      
REMARK 465     GLY C   123                                                      
REMARK 465     THR C   161                                                      
REMARK 465     LYS C   162                                                      
REMARK 465     ALA C   163                                                      
REMARK 465     GLU C   211                                                      
REMARK 465     ASN C   212                                                      
REMARK 465     TYR C   213                                                      
REMARK 465     GLY C   214                                                      
REMARK 465     SER C   215                                                      
REMARK 465     TRP C   216                                                      
REMARK 465     GLY C   217                                                      
REMARK 465     GLN C   218                                                      
REMARK 465     SER C   219                                                      
REMARK 465     PHE C   220                                                      
REMARK 465     LYS C   300                                                      
REMARK 465     ALA C   301                                                      
REMARK 465     LYS C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     SER D     3                                                      
REMARK 465     TRP D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     LYS D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     PRO D    67                                                      
REMARK 465     PRO D    68                                                      
REMARK 465     THR D    69                                                      
REMARK 465     LYS D    70                                                      
REMARK 465     GLN D    71                                                      
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     ARG A   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  32    CE   NZ                                             
REMARK 470     ARG A  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     LEU A  52    CG   CD1  CD2                                       
REMARK 470     ARG A  54    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A  56    CD   CE   NZ                                        
REMARK 470     GLU A  61    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  63    CD   OE1  NE2                                       
REMARK 470     ASN A  65    CG   OD1  ND2                                       
REMARK 470     LEU A  66    CB   CG   CD1  CD2                                  
REMARK 470     GLU A  85    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  92    CD   CE   NZ                                        
REMARK 470     LYS A 122    CD   CE   NZ                                        
REMARK 470     GLU A 129    CD   OE1  OE2                                       
REMARK 470     GLU A 149    CD   OE1  OE2                                       
REMARK 470     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     GLN A 207    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS A 227    CD   CE   NZ                                        
REMARK 470     GLU A 273    CD   OE1  OE2                                       
REMARK 470     LYS A 282    CG   CD   CE   NZ                                   
REMARK 470     ASP A 286    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     GLU A 295    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 299    CD   OE1  OE2                                       
REMARK 470     LYS A 302    CE   NZ                                             
REMARK 470     LEU A 303    CG   CD1  CD2                                       
REMARK 470     ARG B   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  51    CD   CE   NZ                                        
REMARK 470     GLU B  53    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  54    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 122    CD   CE   NZ                                        
REMARK 470     GLU B 149    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 162    CG   CD   CE   NZ                                   
REMARK 470     GLN B 207    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 218    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 282    CD   CE   NZ                                        
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     GLU B 295    CD   OE1  OE2                                       
REMARK 470     ARG C   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C  39    O                                                   
REMARK 470     ARG C  50    NE   CZ   NH1  NH2                                  
REMARK 470     LYS C  51    CB   CG   CD   CE   NZ                              
REMARK 470     GLU C  53    CG   CD   OE1  OE2                                  
REMARK 470     ARG C  54    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LEU C  55    CB   CG   CD1  CD2                                  
REMARK 470     LYS C  56    CB   CG   CD   CE   NZ                              
REMARK 470     ASP C  60    CG   OD1  OD2                                       
REMARK 470     GLU C  61    CG   CD   OE1  OE2                                  
REMARK 470     LYS C  70    CB   CG   CD   CE   NZ                              
REMARK 470     GLN C  71    CB   CG   CD   OE1  NE2                             
REMARK 470     ARG C  73    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN C  83    CG   OD1  ND2                                       
REMARK 470     GLU C  85    CG   CD   OE1  OE2                                  
REMARK 470     GLN C 207    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 222    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 227    CD   CE   NZ                                        
REMARK 470     GLU C 273    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 282    CD   CE   NZ                                        
REMARK 470     LYS C 291    CG   CD   CE   NZ                                   
REMARK 470     LYS C 292    CB   CG   CD   CE   NZ                              
REMARK 470     GLU C 295    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 298    CG   CD   CE   NZ                                   
REMARK 470     GLU C 299    CG   CD   OE1  OE2                                  
REMARK 470     ARG D   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  36    CD   CE   NZ                                        
REMARK 470     LYS D  51    CG   CD   CE   NZ                                   
REMARK 470     ARG D  54    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  56    CG   CD   CE   NZ                                   
REMARK 470     GLU D  85    CG   CD   OE1  OE2                                  
REMARK 470     ASN D  89    CG   OD1  ND2                                       
REMARK 470     LYS D  92    CG   CD   CE   NZ                                   
REMARK 470     GLN D 111    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 122    CG   CD   CE   NZ                                   
REMARK 470     GLU D 129    CD   OE1  OE2                                       
REMARK 470     GLU D 149    CD   OE1  OE2                                       
REMARK 470     GLN D 218    CD   OE1  NE2                                       
REMARK 470     LYS D 282    CD   CE   NZ                                        
REMARK 470     LYS D 291    CD   CE   NZ                                        
REMARK 470     LYS D 292    CG   CD   CE   NZ                                   
REMARK 470     GLU D 295    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 299    OE1  OE2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CD2  LEU D    52     NE2  GLN D    78              1.43            
REMARK 500   CD2  LEU D    52     CD   GLN D    78              1.80            
REMARK 500   O    HOH B  4090     O    HOH B  4091              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A 111   C     PHE A 112   N      -0.196                       
REMARK 500    ILE D 194   C     ARG D 195   N      -0.351                       
REMARK 500    ARG D 195   C     ILE D 196   N       0.227                       
REMARK 500    CYS D 198   CB    CYS D 198   SG     -0.098                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A 110   O   -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    GLN A 111   C   -  N   -  CA  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    GLN B 111   O   -  C   -  N   ANGL. DEV. = -10.0 DEGREES          
REMARK 500    LEU C 104   CB  -  CG  -  CD2 ANGL. DEV. =  10.7 DEGREES          
REMARK 500    GLY C 285   CA  -  C   -  N   ANGL. DEV. =  13.5 DEGREES          
REMARK 500    GLY C 285   O   -  C   -  N   ANGL. DEV. = -16.2 DEGREES          
REMARK 500    ASP C 286   C   -  N   -  CA  ANGL. DEV. =  25.2 DEGREES          
REMARK 500    ARG D 195   NE  -  CZ  -  NH1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG D 195   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ARG D 195   CA  -  C   -  N   ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG D 195   O   -  C   -  N   ANGL. DEV. = -27.4 DEGREES          
REMARK 500    ILE D 196   C   -  N   -  CA  ANGL. DEV. =  17.7 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    GLN A 111      147.17    171.69                                   
REMARK 500    TRP A 146      -54.48   -163.76                                   
REMARK 500    ILE A 158     -156.30   -120.62                                   
REMARK 500    PHE A 165       73.79   -151.14                                   
REMARK 500    LEU A 167       -2.88     75.37                                   
REMARK 500    ASP A 262       15.56   -149.45                                   
REMARK 500    TRP B 146      -54.07   -154.42                                   
REMARK 500    ILE B 158     -157.07   -117.67                                   
REMARK 500    ALA B 168       59.62   -150.21                                   
REMARK 500    VAL B 261       77.67   -117.02                                   
REMARK 500    ASP B 262       12.15   -144.10                                   
REMARK 500    ARG C  54     -107.93     55.10                                   
REMARK 500    LEU C  55      -80.19    -60.32                                   
REMARK 500    LYS C  56      -69.33     -4.82                                   
REMARK 500    LEU C 132      -62.17    -91.39                                   
REMARK 500    TRP C 146      -52.65   -148.66                                   
REMARK 500    ILE C 158     -143.72   -113.91                                   
REMARK 500    LEU C 167       -9.67     83.22                                   
REMARK 500    ASP C 262       10.60   -145.27                                   
REMARK 500    GLU D  53     -145.44    137.47                                   
REMARK 500    ALA D  64        0.48    -69.73                                   
REMARK 500    SER D 114      140.56   -170.44                                   
REMARK 500    LEU D 132      -61.27    -92.92                                   
REMARK 500    TRP D 146      -51.81   -159.12                                   
REMARK 500    ILE D 158     -149.67   -119.76                                   
REMARK 500    PHE D 165       74.43   -151.99                                   
REMARK 500    ALA D 168       65.54   -150.92                                   
REMARK 500    VAL D 261       79.40   -115.20                                   
REMARK 500    ASP D 262       15.77   -142.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A   97     PHE A   98                 -127.51                    
REMARK 500 PHE A   98     GLY A   99                  -58.45                    
REMARK 500 GLN B  207     THR B  208                   81.10                    
REMARK 500 LYS C    6     GLY C    7                  -31.92                    
REMARK 500 LYS C   51     LEU C   52                  142.58                    
REMARK 500 GLU C   53     ARG C   54                  113.04                    
REMARK 500 LYS D   51     LEU D   52                  -75.84                    
REMARK 500 GLU D   53     ARG D   54                  127.55                    
REMARK 500 GLY D  214     SER D  215                 -119.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLY A 110        -10.79                                           
REMARK 500    GLN B 111         10.13                                           
REMARK 500    ILE D 194        -10.17                                           
REMARK 500    ARG D 195         26.73                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     LEU D  52       122.4                     ALPHA-CARBON           
REMARK 500     GLU D  53       132.4                     ALPHA-CARBON           
REMARK 500     ARG D  54       128.5                     ALPHA-CARBON           
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 C 364        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH C 369        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH C 370        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH D2076        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH B4091        DISTANCE =  6.16 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 1001                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2001                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 3001                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4001                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE B 4002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1W6U   RELATED DB: PDB                                   
REMARK 900 BINARY STRUCTURE OF HUMAN DECR                                       
REMARK 900 RELATED ID: 1W73   RELATED DB: PDB                                   
REMARK 900 BINARY STRUCTURE OF HUMAN DECR SOLVED BY SEMET SAD                   
REMARK 900 RELATED ID: 1W8D   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN DECR TERNARY COMPLEX                              
DBREF  1YXM A    1   303  UNP    Q9BY49   PECR_HUMAN       1    303             
DBREF  1YXM B    1   303  UNP    Q9BY49   PECR_HUMAN       1    303             
DBREF  1YXM C    1   303  UNP    Q9BY49   PECR_HUMAN       1    303             
DBREF  1YXM D    1   303  UNP    Q9BY49   PECR_HUMAN       1    303             
SEQRES   1 A  303  MET ALA SER TRP ALA LYS GLY ARG SER TYR LEU ALA PRO          
SEQRES   2 A  303  GLY LEU LEU GLN GLY GLN VAL ALA ILE VAL THR GLY GLY          
SEQRES   3 A  303  ALA THR GLY ILE GLY LYS ALA ILE VAL LYS GLU LEU LEU          
SEQRES   4 A  303  GLU LEU GLY SER ASN VAL VAL ILE ALA SER ARG LYS LEU          
SEQRES   5 A  303  GLU ARG LEU LYS SER ALA ALA ASP GLU LEU GLN ALA ASN          
SEQRES   6 A  303  LEU PRO PRO THR LYS GLN ALA ARG VAL ILE PRO ILE GLN          
SEQRES   7 A  303  CYS ASN ILE ARG ASN GLU GLU GLU VAL ASN ASN LEU VAL          
SEQRES   8 A  303  LYS SER THR LEU ASP THR PHE GLY LYS ILE ASN PHE LEU          
SEQRES   9 A  303  VAL ASN ASN GLY GLY GLY GLN PHE LEU SER PRO ALA GLU          
SEQRES  10 A  303  HIS ILE SER SER LYS GLY TRP HIS ALA VAL LEU GLU THR          
SEQRES  11 A  303  ASN LEU THR GLY THR PHE TYR MET CYS LYS ALA VAL TYR          
SEQRES  12 A  303  SER SER TRP MET LYS GLU HIS GLY GLY SER ILE VAL ASN          
SEQRES  13 A  303  ILE ILE VAL PRO THR LYS ALA GLY PHE PRO LEU ALA VAL          
SEQRES  14 A  303  HIS SER GLY ALA ALA ARG ALA GLY VAL TYR ASN LEU THR          
SEQRES  15 A  303  LYS SER LEU ALA LEU GLU TRP ALA CYS SER GLY ILE ARG          
SEQRES  16 A  303  ILE ASN CYS VAL ALA PRO GLY VAL ILE TYR SER GLN THR          
SEQRES  17 A  303  ALA VAL GLU ASN TYR GLY SER TRP GLY GLN SER PHE PHE          
SEQRES  18 A  303  GLU GLY SER PHE GLN LYS ILE PRO ALA LYS ARG ILE GLY          
SEQRES  19 A  303  VAL PRO GLU GLU VAL SER SER VAL VAL CYS PHE LEU LEU          
SEQRES  20 A  303  SER PRO ALA ALA SER PHE ILE THR GLY GLN SER VAL ASP          
SEQRES  21 A  303  VAL ASP GLY GLY ARG SER LEU TYR THR HIS SER TYR GLU          
SEQRES  22 A  303  VAL PRO ASP HIS ASP ASN TRP PRO LYS GLY ALA GLY ASP          
SEQRES  23 A  303  LEU SER VAL VAL LYS LYS MET LYS GLU THR PHE LYS GLU          
SEQRES  24 A  303  LYS ALA LYS LEU                                              
SEQRES   1 B  303  MET ALA SER TRP ALA LYS GLY ARG SER TYR LEU ALA PRO          
SEQRES   2 B  303  GLY LEU LEU GLN GLY GLN VAL ALA ILE VAL THR GLY GLY          
SEQRES   3 B  303  ALA THR GLY ILE GLY LYS ALA ILE VAL LYS GLU LEU LEU          
SEQRES   4 B  303  GLU LEU GLY SER ASN VAL VAL ILE ALA SER ARG LYS LEU          
SEQRES   5 B  303  GLU ARG LEU LYS SER ALA ALA ASP GLU LEU GLN ALA ASN          
SEQRES   6 B  303  LEU PRO PRO THR LYS GLN ALA ARG VAL ILE PRO ILE GLN          
SEQRES   7 B  303  CYS ASN ILE ARG ASN GLU GLU GLU VAL ASN ASN LEU VAL          
SEQRES   8 B  303  LYS SER THR LEU ASP THR PHE GLY LYS ILE ASN PHE LEU          
SEQRES   9 B  303  VAL ASN ASN GLY GLY GLY GLN PHE LEU SER PRO ALA GLU          
SEQRES  10 B  303  HIS ILE SER SER LYS GLY TRP HIS ALA VAL LEU GLU THR          
SEQRES  11 B  303  ASN LEU THR GLY THR PHE TYR MET CYS LYS ALA VAL TYR          
SEQRES  12 B  303  SER SER TRP MET LYS GLU HIS GLY GLY SER ILE VAL ASN          
SEQRES  13 B  303  ILE ILE VAL PRO THR LYS ALA GLY PHE PRO LEU ALA VAL          
SEQRES  14 B  303  HIS SER GLY ALA ALA ARG ALA GLY VAL TYR ASN LEU THR          
SEQRES  15 B  303  LYS SER LEU ALA LEU GLU TRP ALA CYS SER GLY ILE ARG          
SEQRES  16 B  303  ILE ASN CYS VAL ALA PRO GLY VAL ILE TYR SER GLN THR          
SEQRES  17 B  303  ALA VAL GLU ASN TYR GLY SER TRP GLY GLN SER PHE PHE          
SEQRES  18 B  303  GLU GLY SER PHE GLN LYS ILE PRO ALA LYS ARG ILE GLY          
SEQRES  19 B  303  VAL PRO GLU GLU VAL SER SER VAL VAL CYS PHE LEU LEU          
SEQRES  20 B  303  SER PRO ALA ALA SER PHE ILE THR GLY GLN SER VAL ASP          
SEQRES  21 B  303  VAL ASP GLY GLY ARG SER LEU TYR THR HIS SER TYR GLU          
SEQRES  22 B  303  VAL PRO ASP HIS ASP ASN TRP PRO LYS GLY ALA GLY ASP          
SEQRES  23 B  303  LEU SER VAL VAL LYS LYS MET LYS GLU THR PHE LYS GLU          
SEQRES  24 B  303  LYS ALA LYS LEU                                              
SEQRES   1 C  303  MET ALA SER TRP ALA LYS GLY ARG SER TYR LEU ALA PRO          
SEQRES   2 C  303  GLY LEU LEU GLN GLY GLN VAL ALA ILE VAL THR GLY GLY          
SEQRES   3 C  303  ALA THR GLY ILE GLY LYS ALA ILE VAL LYS GLU LEU LEU          
SEQRES   4 C  303  GLU LEU GLY SER ASN VAL VAL ILE ALA SER ARG LYS LEU          
SEQRES   5 C  303  GLU ARG LEU LYS SER ALA ALA ASP GLU LEU GLN ALA ASN          
SEQRES   6 C  303  LEU PRO PRO THR LYS GLN ALA ARG VAL ILE PRO ILE GLN          
SEQRES   7 C  303  CYS ASN ILE ARG ASN GLU GLU GLU VAL ASN ASN LEU VAL          
SEQRES   8 C  303  LYS SER THR LEU ASP THR PHE GLY LYS ILE ASN PHE LEU          
SEQRES   9 C  303  VAL ASN ASN GLY GLY GLY GLN PHE LEU SER PRO ALA GLU          
SEQRES  10 C  303  HIS ILE SER SER LYS GLY TRP HIS ALA VAL LEU GLU THR          
SEQRES  11 C  303  ASN LEU THR GLY THR PHE TYR MET CYS LYS ALA VAL TYR          
SEQRES  12 C  303  SER SER TRP MET LYS GLU HIS GLY GLY SER ILE VAL ASN          
SEQRES  13 C  303  ILE ILE VAL PRO THR LYS ALA GLY PHE PRO LEU ALA VAL          
SEQRES  14 C  303  HIS SER GLY ALA ALA ARG ALA GLY VAL TYR ASN LEU THR          
SEQRES  15 C  303  LYS SER LEU ALA LEU GLU TRP ALA CYS SER GLY ILE ARG          
SEQRES  16 C  303  ILE ASN CYS VAL ALA PRO GLY VAL ILE TYR SER GLN THR          
SEQRES  17 C  303  ALA VAL GLU ASN TYR GLY SER TRP GLY GLN SER PHE PHE          
SEQRES  18 C  303  GLU GLY SER PHE GLN LYS ILE PRO ALA LYS ARG ILE GLY          
SEQRES  19 C  303  VAL PRO GLU GLU VAL SER SER VAL VAL CYS PHE LEU LEU          
SEQRES  20 C  303  SER PRO ALA ALA SER PHE ILE THR GLY GLN SER VAL ASP          
SEQRES  21 C  303  VAL ASP GLY GLY ARG SER LEU TYR THR HIS SER TYR GLU          
SEQRES  22 C  303  VAL PRO ASP HIS ASP ASN TRP PRO LYS GLY ALA GLY ASP          
SEQRES  23 C  303  LEU SER VAL VAL LYS LYS MET LYS GLU THR PHE LYS GLU          
SEQRES  24 C  303  LYS ALA LYS LEU                                              
SEQRES   1 D  303  MET ALA SER TRP ALA LYS GLY ARG SER TYR LEU ALA PRO          
SEQRES   2 D  303  GLY LEU LEU GLN GLY GLN VAL ALA ILE VAL THR GLY GLY          
SEQRES   3 D  303  ALA THR GLY ILE GLY LYS ALA ILE VAL LYS GLU LEU LEU          
SEQRES   4 D  303  GLU LEU GLY SER ASN VAL VAL ILE ALA SER ARG LYS LEU          
SEQRES   5 D  303  GLU ARG LEU LYS SER ALA ALA ASP GLU LEU GLN ALA ASN          
SEQRES   6 D  303  LEU PRO PRO THR LYS GLN ALA ARG VAL ILE PRO ILE GLN          
SEQRES   7 D  303  CYS ASN ILE ARG ASN GLU GLU GLU VAL ASN ASN LEU VAL          
SEQRES   8 D  303  LYS SER THR LEU ASP THR PHE GLY LYS ILE ASN PHE LEU          
SEQRES   9 D  303  VAL ASN ASN GLY GLY GLY GLN PHE LEU SER PRO ALA GLU          
SEQRES  10 D  303  HIS ILE SER SER LYS GLY TRP HIS ALA VAL LEU GLU THR          
SEQRES  11 D  303  ASN LEU THR GLY THR PHE TYR MET CYS LYS ALA VAL TYR          
SEQRES  12 D  303  SER SER TRP MET LYS GLU HIS GLY GLY SER ILE VAL ASN          
SEQRES  13 D  303  ILE ILE VAL PRO THR LYS ALA GLY PHE PRO LEU ALA VAL          
SEQRES  14 D  303  HIS SER GLY ALA ALA ARG ALA GLY VAL TYR ASN LEU THR          
SEQRES  15 D  303  LYS SER LEU ALA LEU GLU TRP ALA CYS SER GLY ILE ARG          
SEQRES  16 D  303  ILE ASN CYS VAL ALA PRO GLY VAL ILE TYR SER GLN THR          
SEQRES  17 D  303  ALA VAL GLU ASN TYR GLY SER TRP GLY GLN SER PHE PHE          
SEQRES  18 D  303  GLU GLY SER PHE GLN LYS ILE PRO ALA LYS ARG ILE GLY          
SEQRES  19 D  303  VAL PRO GLU GLU VAL SER SER VAL VAL CYS PHE LEU LEU          
SEQRES  20 D  303  SER PRO ALA ALA SER PHE ILE THR GLY GLN SER VAL ASP          
SEQRES  21 D  303  VAL ASP GLY GLY ARG SER LEU TYR THR HIS SER TYR GLU          
SEQRES  22 D  303  VAL PRO ASP HIS ASP ASN TRP PRO LYS GLY ALA GLY ASP          
SEQRES  23 D  303  LEU SER VAL VAL LYS LYS MET LYS GLU THR PHE LYS GLU          
SEQRES  24 D  303  LYS ALA LYS LEU                                              
HET    SO4  A 304       5                                                       
HET    SO4  D1001       5                                                       
HET    SO4  D2001       5                                                       
HET    PO4  B3001       5                                                       
HET    SO4  B4001       5                                                       
HET    ADE  B4002      10                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADE ADENINE                                                          
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   8  PO4    O4 P 3-                                                      
FORMUL  10  ADE    C5 H5 N5                                                     
FORMUL  11  HOH   *374(H2 O)                                                    
HELIX    1   1 THR A   28  LEU A   41  1                                  14    
HELIX    2   2 LYS A   51  ASN A   65  1                                  15    
HELIX    3   3 ASN A   83  GLY A   99  1                                  17    
HELIX    4   4 PRO A  115  ILE A  119  5                                   5    
HELIX    5   5 SER A  120  LEU A  132  1                                  13    
HELIX    6   6 LEU A  132  TRP A  146  1                                  15    
HELIX    7   7 TRP A  146  GLY A  151  1                                   6    
HELIX    8   8 ALA A  168  TRP A  189  1                                  22    
HELIX    9   9 ALA A  190  SER A  192  5                                   3    
HELIX   10  10 GLN A  207  GLU A  211  5                                   5    
HELIX   11  11 TYR A  213  GLU A  222  5                                  10    
HELIX   12  12 GLY A  223  ILE A  228  5                                   6    
HELIX   13  13 PRO A  236  SER A  248  1                                  13    
HELIX   14  14 PRO A  249  SER A  252  5                                   4    
HELIX   15  15 GLY A  264  TYR A  268  5                                   5    
HELIX   16  16 LEU A  287  LEU A  303  1                                  17    
HELIX   17  17 THR B   28  LEU B   41  1                                  14    
HELIX   18  18 LYS B   51  ASN B   65  1                                  15    
HELIX   19  19 ASN B   83  GLY B   99  1                                  17    
HELIX   20  20 PRO B  115  ILE B  119  5                                   5    
HELIX   21  21 SER B  120  LEU B  132  1                                  13    
HELIX   22  22 LEU B  132  TRP B  146  1                                  15    
HELIX   23  23 TRP B  146  GLY B  151  1                                   6    
HELIX   24  24 ALA B  168  TRP B  189  1                                  22    
HELIX   25  25 ALA B  190  SER B  192  5                                   3    
HELIX   26  26 GLN B  218  SER B  224  1                                   7    
HELIX   27  27 PHE B  225  ILE B  228  5                                   4    
HELIX   28  28 PRO B  236  SER B  248  1                                  13    
HELIX   29  29 PRO B  249  SER B  252  5                                   4    
HELIX   30  30 GLY B  264  TYR B  268  5                                   5    
HELIX   31  31 LEU B  287  LYS B  298  1                                  12    
HELIX   32  32 THR C   28  LEU C   39  1                                  12    
HELIX   33  33 GLU C   53  ASN C   65  1                                  13    
HELIX   34  34 ASN C   83  GLY C   99  1                                  17    
HELIX   35  35 TRP C  124  LEU C  132  1                                   9    
HELIX   36  36 LEU C  132  TRP C  146  1                                  15    
HELIX   37  37 TRP C  146  GLY C  151  1                                   6    
HELIX   38  38 ALA C  168  TRP C  189  1                                  22    
HELIX   39  39 ALA C  190  SER C  192  5                                   3    
HELIX   40  40 GLY C  223  ILE C  228  5                                   6    
HELIX   41  41 VAL C  235  SER C  248  1                                  14    
HELIX   42  42 PRO C  249  SER C  252  5                                   4    
HELIX   43  43 GLY C  264  TYR C  268  5                                   5    
HELIX   44  44 LEU C  287  GLU C  299  1                                  13    
HELIX   45  45 THR D   28  LEU D   41  1                                  14    
HELIX   46  46 GLU D   53  ALA D   64  1                                  12    
HELIX   47  47 ASN D   83  GLY D   99  1                                  17    
HELIX   48  48 PRO D  115  ILE D  119  5                                   5    
HELIX   49  49 SER D  120  LEU D  132  1                                  13    
HELIX   50  50 LEU D  132  TRP D  146  1                                  15    
HELIX   51  51 TRP D  146  GLY D  151  1                                   6    
HELIX   52  52 ALA D  168  TRP D  189  1                                  22    
HELIX   53  53 ALA D  190  SER D  192  5                                   3    
HELIX   54  54 SER D  206  TYR D  213  1                                   8    
HELIX   55  55 TRP D  216  SER D  224  1                                   9    
HELIX   56  56 PHE D  225  ILE D  228  5                                   4    
HELIX   57  57 PRO D  236  SER D  248  1                                  13    
HELIX   58  58 PRO D  249  SER D  252  5                                   4    
HELIX   59  59 GLY D  264  TYR D  268  5                                   5    
HELIX   60  60 LEU D  287  LYS D  302  1                                  16    
SHEET    1   A 7 VAL A  74  GLN A  78  0                                        
SHEET    2   A 7 ASN A  44  SER A  49  1  N  ILE A  47   O  ILE A  77           
SHEET    3   A 7 VAL A  20  THR A  24  1  N  ALA A  21   O  VAL A  46           
SHEET    4   A 7 PHE A 103  ASN A 106  1  O  VAL A 105   N  ILE A  22           
SHEET    5   A 7 GLY A 152  ILE A 157  1  O  ILE A 157   N  ASN A 106           
SHEET    6   A 7 ILE A 194  PRO A 201  1  O  VAL A 199   N  ASN A 156           
SHEET    7   A 7 SER A 258  VAL A 261  1  O  VAL A 259   N  ALA A 200           
SHEET    1   B 7 VAL B  74  GLN B  78  0                                        
SHEET    2   B 7 ASN B  44  SER B  49  1  N  ILE B  47   O  ILE B  77           
SHEET    3   B 7 VAL B  20  THR B  24  1  N  VAL B  23   O  VAL B  46           
SHEET    4   B 7 PHE B 103  ASN B 106  1  O  VAL B 105   N  ILE B  22           
SHEET    5   B 7 GLY B 152  ILE B 157  1  O  VAL B 155   N  LEU B 104           
SHEET    6   B 7 ILE B 194  PRO B 201  1  O  ARG B 195   N  ILE B 154           
SHEET    7   B 7 SER B 258  VAL B 261  1  O  VAL B 259   N  ALA B 200           
SHEET    1   C 7 VAL C  74  GLN C  78  0                                        
SHEET    2   C 7 ASN C  44  SER C  49  1  N  ILE C  47   O  ILE C  77           
SHEET    3   C 7 VAL C  20  THR C  24  1  N  ALA C  21   O  VAL C  46           
SHEET    4   C 7 PHE C 103  ASN C 106  1  O  VAL C 105   N  ILE C  22           
SHEET    5   C 7 GLY C 152  ILE C 157  1  O  ILE C 157   N  ASN C 106           
SHEET    6   C 7 ILE C 194  PRO C 201  1  O  ARG C 195   N  ILE C 154           
SHEET    7   C 7 SER C 258  VAL C 261  1  O  VAL C 259   N  ALA C 200           
SHEET    1   D 7 VAL D  74  GLN D  78  0                                        
SHEET    2   D 7 ASN D  44  SER D  49  1  N  ILE D  47   O  ILE D  77           
SHEET    3   D 7 VAL D  20  THR D  24  1  N  ALA D  21   O  VAL D  46           
SHEET    4   D 7 PHE D 103  ASN D 106  1  O  VAL D 105   N  ILE D  22           
SHEET    5   D 7 GLY D 152  ILE D 157  1  O  VAL D 155   N  LEU D 104           
SHEET    6   D 7 ILE D 194  PRO D 201  1  O  VAL D 199   N  ASN D 156           
SHEET    7   D 7 SER D 258  VAL D 261  1  O  VAL D 259   N  ALA D 200           
CISPEP   1 LEU C   52    GLU C   53          0        28.31                     
CISPEP   2 LEU D   52    GLU D   53          0        19.06                     
SITE     1 AC1  4 GLN A  17  LYS A  70  GLN A  71  ALA A  72                    
SITE     1 AC2  8 THR D  28  GLY D  29  ILE D  30  GLY D  31                    
SITE     2 AC2  8 ASN D 107  HOH D2056  HOH D2086  HOH D2088                    
SITE     1 AC3  4 GLY D  29  SER D 206  GLN D 207  THR D 208                    
SITE     1 AC4  4 SER B  49  ARG B  50  LYS B  51  ADE B4002                    
SITE     1 AC5  5 GLN B  17  LYS B  70  GLN B  71  ALA B  72                    
SITE     2 AC5  5 SER B 219                                                     
SITE     1 AC6  8 SER B  49  ARG B  50  CYS B  79  ASN B  80                    
SITE     2 AC6  8 ILE B  81  GLY B 109  THR B 130  PO4 B3001                    
CRYST1   78.152  119.014  119.909  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012796  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008402  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008340        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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