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Database: PDB
Entry: 6B5I
LinkDB: 6B5I
Original site: 6B5I 
HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 29-SEP-17   6B5I              
TITLE     ALDH1A2 LIGANDED WITH 1-(4-CYANOPHENYL)-N-(3-FLUOROPHENYL)-3-[4-      
TITLE    2 (METHYLSULFONYL)PHENYL]-1H-PYRAZOLE-4-CARBOXAMIDE (COMPOUND CM121)   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RETINAL DEHYDROGENASE 2;                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 26-518;                                       
COMPND   5 SYNONYM: RALDH2, ALDEHYDE DEHYDROGENASE FAMILY 1 MEMBER A2,          
COMPND   6 RETINALDEHYDE-SPECIFIC DEHYDROGENASE TYPE 2, RALDH(II);              
COMPND   7 EC: 1.2.1.36;                                                        
COMPND   8 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: ALDH1A2, RALDH2;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21STAR(DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    RETINOIC ACID SIGNALING, MALE CONTRACEPTION, DRUG DISCOVERY, DRUG     
KEYWDS   2 DEVELOPMENT, OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.CHEN,J.-Y.ZHU,E.SCHONBRUNN                                          
REVDAT   4   11-DEC-19 6B5I    1       REMARK                                   
REVDAT   3   28-MAR-18 6B5I    1       JRNL                                     
REVDAT   2   17-JAN-18 6B5I    1       JRNL                                     
REVDAT   1   10-JAN-18 6B5I    0                                                
JRNL        AUTH   Y.CHEN,J.Y.ZHU,K.H.HONG,D.C.MIKLES,G.I.GEORG,A.S.GOLDSTEIN,  
JRNL        AUTH 2 J.K.AMORY,E.SCHONBRUNN                                       
JRNL        TITL   STRUCTURAL BASIS OF ALDH1A2 INHIBITION BY IRREVERSIBLE AND   
JRNL        TITL 2 REVERSIBLE SMALL MOLECULE INHIBITORS.                        
JRNL        REF    ACS CHEM. BIOL.               V.  13   582 2018              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   29240402                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.7B00685                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1-2575_2575                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 81.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 59833                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1077                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 81.5751 -  5.1997    0.99     7664   140  0.1917 0.2189        
REMARK   3     2  5.1997 -  4.1272    0.99     7414   136  0.1872 0.2384        
REMARK   3     3  4.1272 -  3.6055    1.00     7342   135  0.2115 0.2645        
REMARK   3     4  3.6055 -  3.2758    0.99     7306   134  0.2366 0.3263        
REMARK   3     5  3.2758 -  3.0410    0.99     7276   133  0.2500 0.3140        
REMARK   3     6  3.0410 -  2.8617    0.99     7275   133  0.2547 0.3617        
REMARK   3     7  2.8617 -  2.7184    0.99     7221   133  0.2658 0.2967        
REMARK   3     8  2.7184 -  2.6000    0.99     7258   133  0.2881 0.3656        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.430           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.24                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.26                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          15712                                  
REMARK   3   ANGLE     :  0.608          21280                                  
REMARK   3   CHIRALITY :  0.043           2304                                  
REMARK   3   PLANARITY :  0.004           2796                                  
REMARK   3   DIHEDRAL  :  6.015           9344                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6B5I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229411.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59848                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 81.535                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.368                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.44                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.070                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 6ALJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40 MG/ML ALDH1A2, 0.2 M SODIUM CITRATE   
REMARK 280  TRIBASIC DEHYDRATE, 25% W/V PEG3350, 1.3 MM CM121, 10% DMSO,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.41500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       81.53500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.73500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       81.53500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.73500            
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: 20330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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     LEU A    26                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     LEU C    26                                                      
REMARK 465     LEU D    26                                                      
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   O    GLN A   272     NE2  GLN C   272              2.17            
REMARK 500   OE1  GLU A   335     NH1  ARG A   339              2.19            
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    ASN A  32      -63.64     63.59                                   
REMARK 500    LEU A  33      119.56     67.84                                   
REMARK 500    CYS A  67     -169.28   -170.56                                   
REMARK 500    ASP A  73     -167.23   -129.49                                   
REMARK 500    THR A 245      -79.06   -100.18                                   
REMARK 500    SER A 278      -94.00    -88.57                                   
REMARK 500    LEU A 280       61.14     60.37                                   
REMARK 500    LYS A 290       72.87   -117.79                                   
REMARK 500    ASP A 298       32.57    -95.33                                   
REMARK 500    GLU A 416      103.82     61.21                                   
REMARK 500    THR A 430      131.12     69.18                                   
REMARK 500    SER A 441      147.33   -171.12                                   
REMARK 500    ALA A 476       71.10    -68.61                                   
REMARK 500    LYS A 487     -128.19     53.69                                   
REMARK 500    MET A 488       33.62    -92.75                                   
REMARK 500    MET A 495      165.19     66.99                                   
REMARK 500    GLN A 515      -76.33    -87.54                                   
REMARK 500    LYS A 516       91.91     69.70                                   
REMARK 500    PRO B  31      -79.33    -57.25                                   
REMARK 500    THR B  62      -14.54   -155.28                                   
REMARK 500    LYS B  74      -47.47    -27.64                                   
REMARK 500    ASP B 116       33.91    -82.68                                   
REMARK 500    VAL B 138      -68.46   -124.10                                   
REMARK 500    THR B 245      -71.86   -106.83                                   
REMARK 500    PHE B 261      -90.81    -87.40                                   
REMARK 500    THR B 262      109.99     73.20                                   
REMARK 500    SER B 278      -91.69   -104.13                                   
REMARK 500    ALA B 322       87.20     53.72                                   
REMARK 500    SER B 324      -81.03    -65.03                                   
REMARK 500    LYS B 390      -95.28   -127.27                                   
REMARK 500    LEU B 392       16.84   -144.45                                   
REMARK 500    ARG B 394       47.60   -152.80                                   
REMARK 500    LYS B 395        5.50    -66.94                                   
REMARK 500    ALA B 414       33.85    -90.37                                   
REMARK 500    LYS B 415        1.61   -159.22                                   
REMARK 500    GLU B 416     -164.03   -129.08                                   
REMARK 500    GLU B 417       50.70    -99.30                                   
REMARK 500    PHE B 419       33.11    -88.82                                   
REMARK 500    PHE B 443     -116.31    -76.47                                   
REMARK 500    GLN B 465       59.79    -99.44                                   
REMARK 500    LYS B 487     -122.26     58.11                                   
REMARK 500    SER B 489       59.87   -162.09                                   
REMARK 500    ASN B 491      122.16     70.90                                   
REMARK 500    MET B 495       40.78     72.47                                   
REMARK 500    LYS B 516      -94.52    -52.65                                   
REMARK 500    ASN B 517       94.37     58.49                                   
REMARK 500    THR C  62      -24.79   -149.60                                   
REMARK 500    CYS C  67     -164.66   -164.73                                   
REMARK 500    ASP C  73     -159.29   -157.89                                   
REMARK 500    ASP C 116       40.44    -86.92                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      83 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU4 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU4 C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU4 D 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6ALJ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6B5G   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6B5H   RELATED DB: PDB                                   
DBREF  6B5I A   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6B5I B   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6B5I C   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
DBREF  6B5I D   26   518  UNP    O94788   AL1A2_HUMAN     26    518             
SEQRES   1 A  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 A  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 A  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 A  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 A  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 A  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 A  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 A  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 A  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 A  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 A  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 A  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 A  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 A  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 A  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 A  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 A  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 A  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 A  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 A  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 A  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 A  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 A  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 A  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 A  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 A  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 A  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 A  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 A  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 A  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 A  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 A  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 A  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 A  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 A  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 A  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 A  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 A  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 B  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 B  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 B  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 B  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 B  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 B  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 B  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 B  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 B  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 B  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 B  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 B  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 B  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 B  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 B  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 B  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 B  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 B  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 B  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 B  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 B  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 B  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 B  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 B  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 B  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 B  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 B  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 B  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 B  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 B  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 B  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 B  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 B  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 B  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 B  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 B  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 B  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 B  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 C  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 C  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 C  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 C  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 C  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 C  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 C  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 C  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 C  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 C  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 C  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 C  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 C  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 C  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 C  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 C  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 C  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 C  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 C  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 C  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 C  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 C  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 C  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 C  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 C  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 C  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 C  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 C  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 C  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 C  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 C  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 C  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 C  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 C  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 C  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 C  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 C  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 C  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
SEQRES   1 D  493  LEU PRO SER PRO THR PRO ASN LEU GLU ILE LYS TYR THR          
SEQRES   2 D  493  LYS ILE PHE ILE ASN ASN GLU TRP GLN ASN SER GLU SER          
SEQRES   3 D  493  GLY ARG VAL PHE PRO VAL TYR ASN PRO ALA THR GLY GLU          
SEQRES   4 D  493  GLN VAL CYS GLU VAL GLN GLU ALA ASP LYS ALA ASP ILE          
SEQRES   5 D  493  ASP LYS ALA VAL GLN ALA ALA ARG LEU ALA PHE SER LEU          
SEQRES   6 D  493  GLY SER VAL TRP ARG ARG MET ASP ALA SER GLU ARG GLY          
SEQRES   7 D  493  ARG LEU LEU ASP LYS LEU ALA ASP LEU VAL GLU ARG ASP          
SEQRES   8 D  493  ARG ALA VAL LEU ALA THR MET GLU SER LEU ASN GLY GLY          
SEQRES   9 D  493  LYS PRO PHE LEU GLN ALA PHE TYR VAL ASP LEU GLN GLY          
SEQRES  10 D  493  VAL ILE LYS THR PHE ARG TYR TYR ALA GLY TRP ALA ASP          
SEQRES  11 D  493  LYS ILE HIS GLY MET THR ILE PRO VAL ASP GLY ASP TYR          
SEQRES  12 D  493  PHE THR PHE THR ARG HIS GLU PRO ILE GLY VAL CYS GLY          
SEQRES  13 D  493  GLN ILE ILE PRO TRP ASN PHE PRO LEU LEU MET PHE ALA          
SEQRES  14 D  493  TRP LYS ILE ALA PRO ALA LEU CYS CYS GLY ASN THR VAL          
SEQRES  15 D  493  VAL ILE LYS PRO ALA GLU GLN THR PRO LEU SER ALA LEU          
SEQRES  16 D  493  TYR MET GLY ALA LEU ILE LYS GLU ALA GLY PHE PRO PRO          
SEQRES  17 D  493  GLY VAL ILE ASN ILE LEU PRO GLY TYR GLY PRO THR ALA          
SEQRES  18 D  493  GLY ALA ALA ILE ALA SER HIS ILE GLY ILE ASP LYS ILE          
SEQRES  19 D  493  ALA PHE THR GLY SER THR GLU VAL GLY LYS LEU ILE GLN          
SEQRES  20 D  493  GLU ALA ALA GLY ARG SER ASN LEU LYS ARG VAL THR LEU          
SEQRES  21 D  493  GLU LEU GLY GLY LYS SER PRO ASN ILE ILE PHE ALA ASP          
SEQRES  22 D  493  ALA ASP LEU ASP TYR ALA VAL GLU GLN ALA HIS GLN GLY          
SEQRES  23 D  493  VAL PHE PHE ASN GLN GLY GLN CYS CYS THR ALA GLY SER          
SEQRES  24 D  493  ARG ILE PHE VAL GLU GLU SER ILE TYR GLU GLU PHE VAL          
SEQRES  25 D  493  ARG ARG SER VAL GLU ARG ALA LYS ARG ARG VAL VAL GLY          
SEQRES  26 D  493  SER PRO PHE ASP PRO THR THR GLU GLN GLY PRO GLN ILE          
SEQRES  27 D  493  ASP LYS LYS GLN TYR ASN LYS ILE LEU GLU LEU ILE GLN          
SEQRES  28 D  493  SER GLY VAL ALA GLU GLY ALA LYS LEU GLU CYS GLY GLY          
SEQRES  29 D  493  LYS GLY LEU GLY ARG LYS GLY PHE PHE ILE GLU PRO THR          
SEQRES  30 D  493  VAL PHE SER ASN VAL THR ASP ASP MET ARG ILE ALA LYS          
SEQRES  31 D  493  GLU GLU ILE PHE GLY PRO VAL GLN GLU ILE LEU ARG PHE          
SEQRES  32 D  493  LYS THR MET ASP GLU VAL ILE GLU ARG ALA ASN ASN SER          
SEQRES  33 D  493  ASP PHE GLY LEU VAL ALA ALA VAL PHE THR ASN ASP ILE          
SEQRES  34 D  493  ASN LYS ALA LEU THR VAL SER SER ALA MET GLN ALA GLY          
SEQRES  35 D  493  THR VAL TRP ILE ASN CYS TYR ASN ALA LEU ASN ALA GLN          
SEQRES  36 D  493  SER PRO PHE GLY GLY PHE LYS MET SER GLY ASN GLY ARG          
SEQRES  37 D  493  GLU MET GLY GLU PHE GLY LEU ARG GLU TYR SER GLU VAL          
SEQRES  38 D  493  LYS THR VAL THR VAL LYS ILE PRO GLN LYS ASN SER              
HET    CU4  A 601      33                                                       
HET    CU4  B 601      33                                                       
HET    CU4  C 601      33                                                       
HET    CU4  D 601      33                                                       
HETNAM     CU4 1-(4-CYANOPHENYL)-N-(3-FLUOROPHENYL)-3-[4-                       
HETNAM   2 CU4  (METHYLSULFONYL)PHENYL]-1H-PYRAZOLE-4-CARBOXAMIDE               
FORMUL   5  CU4    4(C24 H17 F N4 O3 S)                                         
FORMUL   9  HOH   *194(H2 O)                                                    
HELIX    1 AA1 ASP A   73  ALA A   87  1                                  15    
HELIX    2 AA2 SER A   92  MET A   97  1                                   6    
HELIX    3 AA3 ASP A   98  ASP A  116  1                                  19    
HELIX    4 AA4 ASP A  116  GLY A  129  1                                  14    
HELIX    5 AA5 PRO A  131  VAL A  138  1                                   8    
HELIX    6 AA6 VAL A  138  ALA A  154  1                                  17    
HELIX    7 AA7 ASP A  155  ILE A  157  5                                   3    
HELIX    8 AA8 PHE A  188  CYS A  203  1                                  16    
HELIX    9 AA9 PRO A  216  GLY A  230  1                                  15    
HELIX   10 AB1 THR A  245  SER A  252  1                                   8    
HELIX   11 AB2 SER A  264  SER A  278  1                                  15    
HELIX   12 AB3 ASP A  300  PHE A  314  1                                  15    
HELIX   13 AB4 ASN A  315  GLN A  318  5                                   4    
HELIX   14 AB5 ILE A  332  ARG A  347  1                                  16    
HELIX   15 AB6 ASP A  364  ALA A  380  1                                  17    
HELIX   16 AB7 THR A  430  ASN A  440  1                                  11    
HELIX   17 AB8 ASP A  453  MET A  464  1                                  12    
HELIX   18 AB9 GLY A  496  GLU A  502  5                                   7    
HELIX   19 AC1 ASP B   73  ALA B   87  1                                  15    
HELIX   20 AC2 SER B   92  MET B   97  1                                   6    
HELIX   21 AC3 ASP B   98  ASP B  116  1                                  19    
HELIX   22 AC4 ASP B  116  GLY B  129  1                                  14    
HELIX   23 AC5 PRO B  131  VAL B  138  1                                   8    
HELIX   24 AC6 VAL B  138  ALA B  154  1                                  17    
HELIX   25 AC7 ASP B  155  ILE B  157  5                                   3    
HELIX   26 AC8 PHE B  188  CYS B  203  1                                  16    
HELIX   27 AC9 PRO B  216  GLY B  230  1                                  15    
HELIX   28 AD1 THR B  245  SER B  252  1                                   8    
HELIX   29 AD2 SER B  264  SER B  278  1                                  15    
HELIX   30 AD3 ASP B  300  PHE B  314  1                                  15    
HELIX   31 AD4 ASN B  315  GLN B  318  5                                   4    
HELIX   32 AD5 ILE B  332  LYS B  345  1                                  14    
HELIX   33 AD6 ASP B  364  ALA B  380  1                                  17    
HELIX   34 AD7 ARG B  412  GLU B  416  5                                   5    
HELIX   35 AD8 THR B  430  ASN B  440  1                                  11    
HELIX   36 AD9 ASP B  453  MET B  464  1                                  12    
HELIX   37 AE1 GLU B  497  GLU B  502  1                                   6    
HELIX   38 AE2 ASP C   73  PHE C   88  1                                  16    
HELIX   39 AE3 SER C   92  MET C   97  1                                   6    
HELIX   40 AE4 ASP C   98  ASP C  116  1                                  19    
HELIX   41 AE5 ASP C  116  GLY C  129  1                                  14    
HELIX   42 AE6 PRO C  131  VAL C  138  1                                   8    
HELIX   43 AE7 VAL C  138  ALA C  154  1                                  17    
HELIX   44 AE8 LEU C  190  GLY C  204  1                                  15    
HELIX   45 AE9 PRO C  216  GLY C  230  1                                  15    
HELIX   46 AF1 ALA C  246  SER C  252  1                                   7    
HELIX   47 AF2 SER C  264  SER C  278  1                                  15    
HELIX   48 AF3 ASP C  300  PHE C  314  1                                  15    
HELIX   49 AF4 ASN C  315  GLN C  318  5                                   4    
HELIX   50 AF5 ILE C  332  ARG C  347  1                                  16    
HELIX   51 AF6 ASP C  364  GLU C  381  1                                  18    
HELIX   52 AF7 THR C  430  ASN C  440  1                                  11    
HELIX   53 AF8 ASP C  453  MET C  464  1                                  12    
HELIX   54 AF9 PHE C  486  MET C  488  5                                   3    
HELIX   55 AG1 GLY C  499  GLU C  502  5                                   4    
HELIX   56 AG2 ASP D   73  PHE D   88  1                                  16    
HELIX   57 AG3 SER D   92  MET D   97  1                                   6    
HELIX   58 AG4 ASP D   98  ASP D  116  1                                  19    
HELIX   59 AG5 ASP D  116  GLY D  129  1                                  14    
HELIX   60 AG6 PRO D  131  VAL D  138  1                                   8    
HELIX   61 AG7 VAL D  138  ALA D  154  1                                  17    
HELIX   62 AG8 ASP D  155  ILE D  157  5                                   3    
HELIX   63 AG9 PHE D  188  CYS D  203  1                                  16    
HELIX   64 AH1 PRO D  216  GLY D  230  1                                  15    
HELIX   65 AH2 THR D  245  SER D  252  1                                   8    
HELIX   66 AH3 SER D  264  SER D  278  1                                  15    
HELIX   67 AH4 ASP D  300  PHE D  314  1                                  15    
HELIX   68 AH5 ASN D  315  GLN D  318  5                                   4    
HELIX   69 AH6 ILE D  332  ARG D  346  1                                  15    
HELIX   70 AH7 ASP D  364  GLU D  381  1                                  18    
HELIX   71 AH8 MET D  411  GLU D  416  1                                   6    
HELIX   72 AH9 THR D  430  ASN D  440  1                                  11    
HELIX   73 AI1 ASP D  453  ALA D  463  1                                  11    
HELIX   74 AI2 GLY D  499  GLU D  502  5                                   4    
SHEET    1 AA1 2 ILE A  40  ILE A  42  0                                        
SHEET    2 AA1 2 GLU A  45  GLN A  47 -1  O  GLN A  47   N  ILE A  40           
SHEET    1 AA2 2 VAL A  54  TYR A  58  0                                        
SHEET    2 AA2 2 GLN A  65  GLN A  70 -1  O  VAL A  66   N  VAL A  57           
SHEET    1 AA310 THR A 161  ILE A 162  0                                        
SHEET    2 AA310 TYR A 168  PRO A 176 -1  O  THR A 170   N  ILE A 162           
SHEET    3 AA310 SER A 504  LYS A 512 -1  O  LYS A 507   N  ARG A 173           
SHEET    4 AA310 THR C 468  ILE C 471  1  O  VAL C 469   N  THR A 510           
SHEET    5 AA310 VAL C 446  PHE C 450  1  N  VAL C 449   O  TRP C 470           
SHEET    6 AA310 PRO C 292  ILE C 295  1  N  ILE C 294   O  ALA C 448           
SHEET    7 AA310 ARG C 325  GLU C 329  1  O  PHE C 327   N  ILE C 295           
SHEET    8 AA310 VAL C 422  PHE C 428  1  O  LEU C 426   N  ILE C 326           
SHEET    9 AA310 THR C 402  SER C 405  1  N  PHE C 404   O  GLN C 423           
SHEET   10 AA310 LYS C 384  CYS C 387 -1  N  LYS C 384   O  SER C 405           
SHEET    1 AA4 6 ILE A 236  ILE A 238  0                                        
SHEET    2 AA4 6 THR A 206  LYS A 210  1  N  VAL A 207   O  ASN A 237           
SHEET    3 AA4 6 VAL A 179  ILE A 183  1  N  CYS A 180   O  THR A 206           
SHEET    4 AA4 6 LYS A 258  THR A 262  1  O  ALA A 260   N  ILE A 183           
SHEET    5 AA4 6 ARG A 282  GLU A 286  1  O  THR A 284   N  PHE A 261           
SHEET    6 AA4 6 GLY A 490  ASN A 491 -1  O  ASN A 491   N  LEU A 285           
SHEET    1 AA510 LYS A 384  CYS A 387  0                                        
SHEET    2 AA510 THR A 402  SER A 405 -1  O  SER A 405   N  LYS A 384           
SHEET    3 AA510 VAL A 422  PHE A 428  1  O  GLN A 423   N  PHE A 404           
SHEET    4 AA510 ARG A 325  GLU A 329  1  N  ILE A 326   O  LEU A 426           
SHEET    5 AA510 PRO A 292  ILE A 295  1  N  ILE A 295   O  PHE A 327           
SHEET    6 AA510 VAL A 446  PHE A 450  1  O  ALA A 448   N  ILE A 294           
SHEET    7 AA510 THR A 468  ILE A 471  1  O  TRP A 470   N  ALA A 447           
SHEET    8 AA510 SER C 504  LYS C 512  1  O  THR C 510   N  ILE A 471           
SHEET    9 AA510 TYR C 168  PRO C 176 -1  N  PHE C 171   O  VAL C 509           
SHEET   10 AA510 THR C 161  ILE C 162 -1  N  ILE C 162   O  THR C 170           
SHEET    1 AA6 2 GLY A 391  LEU A 392  0                                        
SHEET    2 AA6 2 PHE A 398  ILE A 399 -1  O  PHE A 398   N  LEU A 392           
SHEET    1 AA7 2 PHE A 443  GLY A 444  0                                        
SHEET    2 AA7 2 PHE A 486  LYS A 487 -1  O  PHE A 486   N  GLY A 444           
SHEET    1 AA8 2 ILE B  40  PHE B  41  0                                        
SHEET    2 AA8 2 TRP B  46  GLN B  47 -1  O  GLN B  47   N  ILE B  40           
SHEET    1 AA9 2 VAL B  54  TYR B  58  0                                        
SHEET    2 AA9 2 GLN B  65  GLN B  70 -1  O  VAL B  66   N  VAL B  57           
SHEET    1 AB1 9 THR B 161  ILE B 162  0                                        
SHEET    2 AB1 9 TYR B 168  PRO B 176 -1  O  THR B 170   N  ILE B 162           
SHEET    3 AB1 9 SER B 504  LYS B 512 -1  O  GLU B 505   N  GLU B 175           
SHEET    4 AB1 9 THR D 468  ILE D 471  1  O  ILE D 471   N  THR B 510           
SHEET    5 AB1 9 VAL D 446  PHE D 450  1  N  ALA D 447   O  THR D 468           
SHEET    6 AB1 9 PRO D 292  ILE D 295  1  N  ILE D 294   O  ALA D 448           
SHEET    7 AB1 9 ARG D 325  GLU D 329  1  O  PHE D 327   N  ILE D 295           
SHEET    8 AB1 9 VAL D 422  PHE D 428  1  O  LEU D 426   N  ILE D 326           
SHEET    9 AB1 9 THR D 402  VAL D 403  1  N  THR D 402   O  GLN D 423           
SHEET    1 AB2 5 ILE B 236  ILE B 238  0                                        
SHEET    2 AB2 5 THR B 206  LYS B 210  1  N  ILE B 209   O  ASN B 237           
SHEET    3 AB2 5 VAL B 179  ILE B 183  1  N  CYS B 180   O  VAL B 208           
SHEET    4 AB2 5 LYS B 258  ALA B 260  1  O  ALA B 260   N  GLY B 181           
SHEET    5 AB2 5 ARG B 282  THR B 284  1  O  ARG B 282   N  ILE B 259           
SHEET    1 AB310 LYS B 384  CYS B 387  0                                        
SHEET    2 AB310 THR B 402  SER B 405 -1  O  VAL B 403   N  GLU B 386           
SHEET    3 AB310 VAL B 422  ILE B 425  1  O  GLN B 423   N  PHE B 404           
SHEET    4 AB310 ARG B 325  VAL B 328  1  N  ILE B 326   O  GLU B 424           
SHEET    5 AB310 ASN B 293  ILE B 295  1  N  ASN B 293   O  ARG B 325           
SHEET    6 AB310 VAL B 446  PHE B 450  1  O  ALA B 448   N  ILE B 294           
SHEET    7 AB310 THR B 468  ILE B 471  1  O  TRP B 470   N  VAL B 449           
SHEET    8 AB310 SER D 504  LYS D 512  1  O  THR D 508   N  VAL B 469           
SHEET    9 AB310 TYR D 168  PRO D 176 -1  N  GLU D 175   O  GLU D 505           
SHEET   10 AB310 THR D 161  ILE D 162 -1  N  ILE D 162   O  THR D 170           
SHEET    1 AB4 2 PHE B 483  GLY B 484  0                                        
SHEET    2 AB4 2 ARG B 493  GLU B 494 -1  O  GLU B 494   N  PHE B 483           
SHEET    1 AB5 2 ILE C  40  ILE C  42  0                                        
SHEET    2 AB5 2 GLU C  45  GLN C  47 -1  O  GLN C  47   N  ILE C  40           
SHEET    1 AB6 2 VAL C  54  TYR C  58  0                                        
SHEET    2 AB6 2 GLN C  65  GLN C  70 -1  O  VAL C  69   N  PHE C  55           
SHEET    1 AB7 6 ILE C 236  ILE C 238  0                                        
SHEET    2 AB7 6 THR C 206  LYS C 210  1  N  ILE C 209   O  ASN C 237           
SHEET    3 AB7 6 VAL C 179  ILE C 183  1  N  GLN C 182   O  LYS C 210           
SHEET    4 AB7 6 LYS C 258  THR C 262  1  O  LYS C 258   N  GLY C 181           
SHEET    5 AB7 6 ARG C 282  GLU C 286  1  O  THR C 284   N  PHE C 261           
SHEET    6 AB7 6 GLY C 490  ASN C 491 -1  O  ASN C 491   N  LEU C 285           
SHEET    1 AB8 2 ILE D  40  ILE D  42  0                                        
SHEET    2 AB8 2 GLU D  45  GLN D  47 -1  O  GLN D  47   N  ILE D  40           
SHEET    1 AB9 2 VAL D  54  TYR D  58  0                                        
SHEET    2 AB9 2 GLN D  65  GLN D  70 -1  O  VAL D  66   N  VAL D  57           
SHEET    1 AC1 6 ILE D 236  ILE D 238  0                                        
SHEET    2 AC1 6 THR D 206  LYS D 210  1  N  ILE D 209   O  ASN D 237           
SHEET    3 AC1 6 VAL D 179  ILE D 183  1  N  GLN D 182   O  LYS D 210           
SHEET    4 AC1 6 LYS D 258  THR D 262  1  O  LYS D 258   N  GLY D 181           
SHEET    5 AC1 6 ARG D 282  GLU D 286  1  O  THR D 284   N  PHE D 261           
SHEET    6 AC1 6 GLY D 490  ASN D 491 -1  O  ASN D 491   N  LEU D 285           
CISPEP   1 THR A  262    GLY A  263          0         0.03                     
CISPEP   2 ALA A  322    GLY A  323          0         7.16                     
CISPEP   3 THR B  321    ALA B  322          0        -8.00                     
CISPEP   4 ALA B  322    GLY B  323          0         9.58                     
CISPEP   5 SER B  489    GLY B  490          0        -0.73                     
CISPEP   6 PHE C  483    GLY C  484          0         4.79                     
CISPEP   7 GLY C  484    GLY C  485          0        10.34                     
SITE     1 AC1 15 VAL A 138  GLY A 142  THR A 146  ASN A 187                    
SITE     2 AC1 15 PHE A 188  TRP A 195  GLN A 310  PHE A 314                    
SITE     3 AC1 15 CYS A 320  THR A 321  ASN A 475  LEU A 477                    
SITE     4 AC1 15 ASN A 478  ALA A 479  PHE A 483                               
SITE     1 AC2 10 THR B 146  PHE B 188  TRP B 195  GLN B 310                    
SITE     2 AC2 10 PHE B 314  CYS B 320  THR B 321  ASN B 475                    
SITE     3 AC2 10 LEU B 477  PHE B 483                                          
SITE     1 AC3 15 GLY C 142  THR C 146  PHE C 188  MET C 192                    
SITE     2 AC3 15 TRP C 195  GLN C 310  PHE C 314  CYS C 319                    
SITE     3 AC3 15 CYS C 320  THR C 321  ASN C 475  LEU C 477                    
SITE     4 AC3 15 ASN C 478  ALA C 479  PHE C 483                               
SITE     1 AC4 12 VAL D 138  GLY D 142  THR D 146  PHE D 188                    
SITE     2 AC4 12 TRP D 195  GLN D 310  PHE D 314  CYS D 320                    
SITE     3 AC4 12 THR D 321  ASN D 475  LEU D 477  PHE D 483                    
CRYST1   84.830  139.470  163.070  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      0.011788  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007170  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006132        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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