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LongText Report for: 1NX9-pdb

Name Class
1NX9-pdb
HEADER    HYDROLASE                               10-FEB-03   1NX9              
TITLE     ACETOBACTER TURBIDANS ALPHA-AMINO ACID ESTER HYDROLASE                
TITLE    2 S205A MUTANT COMPLEXED WITH AMPICILLIN                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMINO ACID ESTER HYDROLASE;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.1.43;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACETOBACTER PASTEURIANUS;                       
SOURCE   3 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   4 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   5 EXPRESSION_SYSTEM_STRAIN: TOP10;                                     
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PBADATS205AMYC-HISA                       
KEYWDS    ALPHA/BETA HYDROLASE, JELLYROLL                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,D.B.JANSSEN,             
AUTHOR   2 B.W.DIJKSTRA                                                         
REVDAT   1   09-MAR-04 1NX9    0                                                
JRNL        AUTH   T.R.M.BARENDS,J.J.POLDERMAN-TIJMES,P.A.JEKEL,                
JRNL        AUTH 2 D.B.JANSSEN,B.W.DIJKSTRA                                     
JRNL        TITL   THE STRUCTURE OF THE ACETOBACTER TURBIDANS                   
JRNL        TITL 2 ALPHA-AMINO ACID ESTER HYDROLASE SHOWS COMMON                
JRNL        TITL 3 FEATURES OF A FAMILY OF BETA-LACTAM ACYLASES                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.20 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.19                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 304675                         
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) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 16078                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH           : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW            : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 22491                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2100                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1230                         
REMARK   3   BIN FREE R VALUE                    : 0.2340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   ALL ATOMS                : 21877                                   
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.119         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.111         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.070         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.768         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.965                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20292 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27728 ; 1.064 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2464 ; 2.210 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2868 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 16172 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  9512 ; 0.172 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2026 ; 0.101 ; 0.500       
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):    61 ; 0.121 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    33 ; 0.148 ; 0.500       
REMARK   3   SYMMETRY H-BOND 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): 12360 ; 1.309 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20000 ; 2.212 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7932 ; 3.642 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  7720 ; 5.286 ; 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 : 0                                 
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 0                                          
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1NX9 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-2003.                
REMARK 100 THE RCSB ID CODE IS RCSB018310.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-2002                        
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8463                             
REMARK 200  MONOCHROMATOR                  : TRIANGULAR                         
REMARK 200  OPTICS                         : PREMIRROR, TRIANGULAR              
REMARK 200                                   MONOCHROMATOR, BENT MIRROR         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 322911                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08100                            
REMARK 200   FOR THE DATA SET  : 14.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32200                            
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, SODIUM CITRATE BUFFER,         
REMARK 280  SODIUM AMPICILLIN, PH 5.6, VAPOR DIFFUSION, HANGING DROP,           
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   1/2+X,1/2+Y,1/2+Z                                       
REMARK 290      14555   1/2-X,1/2-Y,1/2+Z                                       
REMARK 290      15555   1/2-X,1/2+Y,1/2-Z                                       
REMARK 290      16555   1/2+X,1/2-Y,1/2-Z                                       
REMARK 290      17555   1/2+Z,1/2+X,1/2+Y                                       
REMARK 290      18555   1/2+Z,1/2-X,1/2-Y                                       
REMARK 290      19555   1/2-Z,1/2-X,1/2+Y                                       
REMARK 290      20555   1/2-Z,1/2+X,1/2-Y                                       
REMARK 290      21555   1/2+Y,1/2+Z,1/2+X                                       
REMARK 290      22555   1/2-Y,1/2+Z,1/2-X                                       
REMARK 290      23555   1/2+Y,1/2-Z,1/2-X                                       
REMARK 290      24555   1/2-Y,1/2-Z,1/2+X                                       
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000      170.91400            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000      170.91400            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000      170.91400            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000      170.91400            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000      170.91400            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000      170.91400            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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     ALA A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     ALA A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     GLN A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     GLN A   667                                                      
REMARK 465     LYS A   668                                                      
REMARK 465     LEU A   669                                                      
REMARK 465     GLY A   670                                                      
REMARK 465     PRO A   671                                                      
REMARK 465     GLU A   672                                                      
REMARK 465     GLN A   673                                                      
REMARK 465     LYS A   674                                                      
REMARK 465     LEU A   675                                                      
REMARK 465     ILE A   676                                                      
REMARK 465     SER A   677                                                      
REMARK 465     GLU A   678                                                      
REMARK 465     GLU A   679                                                      
REMARK 465     ASP A   680                                                      
REMARK 465     LEU A   681                                                      
REMARK 465     ASN A   682                                                      
REMARK 465     SER A   683                                                      
REMARK 465     ALA A   684                                                      
REMARK 465     VAL A   685                                                      
REMARK 465     ASP A   686                                                      
REMARK 465     HIS A   687                                                      
REMARK 465     HIS A   688                                                      
REMARK 465     HIS A   689                                                      
REMARK 465     HIS A   690                                                      
REMARK 465     HIS A   691                                                      
REMARK 465     HIS A   692                                                      
REMARK 465     ALA B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     ALA B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     ALA B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     GLN B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     GLN B   667                                                      
REMARK 465     LYS B   668                                                      
REMARK 465     LEU B   669                                                      
REMARK 465     GLY B   670                                                      
REMARK 465     PRO B   671                                                      
REMARK 465     GLU B   672                                                      
REMARK 465     GLN B   673                                                      
REMARK 465     LYS B   674                                                      
REMARK 465     LEU B   675                                                      
REMARK 465     ILE B   676                                                      
REMARK 465     SER B   677                                                      
REMARK 465     GLU B   678                                                      
REMARK 465     GLU B   679                                                      
REMARK 465     ASP B   680                                                      
REMARK 465     LEU B   681                                                      
REMARK 465     ASN B   682                                                      
REMARK 465     SER B   683                                                      
REMARK 465     ALA B   684                                                      
REMARK 465     VAL B   685                                                      
REMARK 465     ASP B   686                                                      
REMARK 465     HIS B   687                                                      
REMARK 465     HIS B   688                                                      
REMARK 465     HIS B   689                                                      
REMARK 465     HIS B   690                                                      
REMARK 465     HIS B   691                                                      
REMARK 465     HIS B   692                                                      
REMARK 465     ALA C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     ALA C    44                                                      
REMARK 465     ASP C    45                                                      
REMARK 465     ALA C    46                                                      
REMARK 465     ALA C    47                                                      
REMARK 465     GLN C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     GLN C   667                                                      
REMARK 465     LYS C   668                                                      
REMARK 465     LEU C   669                                                      
REMARK 465     GLY C   670                                                      
REMARK 465     PRO C   671                                                      
REMARK 465     GLU C   672                                                      
REMARK 465     GLN C   673                                                      
REMARK 465     LYS C   674                                                      
REMARK 465     LEU C   675                                                      
REMARK 465     ILE C   676                                                      
REMARK 465     SER C   677                                                      
REMARK 465     GLU C   678                                                      
REMARK 465     GLU C   679                                                      
REMARK 465     ASP C   680                                                      
REMARK 465     LEU C   681                                                      
REMARK 465     ASN C   682                                                      
REMARK 465     SER C   683                                                      
REMARK 465     ALA C   684                                                      
REMARK 465     VAL C   685                                                      
REMARK 465     ASP C   686                                                      
REMARK 465     HIS C   687                                                      
REMARK 465     HIS C   688                                                      
REMARK 465     HIS C   689                                                      
REMARK 465     HIS C   690                                                      
REMARK 465     HIS C   691                                                      
REMARK 465     HIS C   692                                                      
REMARK 465     ALA D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     ALA D    43                                                      
REMARK 465     ALA D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     ALA D    46                                                      
REMARK 465     ALA D    47                                                      
REMARK 465     GLN D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     GLN D   667                                                      
REMARK 465     LYS D   668                                                      
REMARK 465     LEU D   669                                                      
REMARK 465     GLY D   670                                                      
REMARK 465     PRO D   671                                                      
REMARK 465     GLU D   672                                                      
REMARK 465     GLN D   673                                                      
REMARK 465     LYS D   674                                                      
REMARK 465     LEU D   675                                                      
REMARK 465     ILE D   676                                                      
REMARK 465     SER D   677                                                      
REMARK 465     GLU D   678                                                      
REMARK 465     GLU D   679                                                      
REMARK 465     ASP D   680                                                      
REMARK 465     LEU D   681                                                      
REMARK 465     ASN D   682                                                      
REMARK 465     SER D   683                                                      
REMARK 465     ALA D   684                                                      
REMARK 465     VAL D   685                                                      
REMARK 465     ASP D   686                                                      
REMARK 465     HIS D   687                                                      
REMARK 465     HIS D   688                                                      
REMARK 465     HIS D   689                                                      
REMARK 465     HIS D   690                                                      
REMARK 465     HIS D   691                                                      
REMARK 465     HIS D   692                                                      
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),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 495   CB    PRO A 495   CG     0.048                        
REMARK 500    PRO A 495   CG    PRO A 495   CD     0.041                        
REMARK 500    PRO B  68   CB    PRO B  68   CG     0.041                        
REMARK 500    MET B 236   SD    MET B 236   CE    -0.040                        
REMARK 500    PRO B 495   CB    PRO B 495   CG     0.050                        
REMARK 500    PRO B 495   CG    PRO B 495   CD     0.039                        
REMARK 500    MET C 302   SD    MET C 302   CE    -0.041                        
REMARK 500    PRO C 435   CB    PRO C 435   CG     0.041                        
REMARK 500    PRO C 495   CB    PRO C 495   CG     0.042                        
REMARK 500    PRO C 495   CG    PRO C 495   CD     0.042                        
REMARK 500    MET C 613   SD    MET C 613   CE     0.040                        
REMARK 500    PRO D 495   CB    PRO D 495   CG     0.049                        
REMARK 500    PRO D 622   CB    PRO D 622   CG     0.045                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL A 121   N   -  CA  -  C   ANGL. DEV. = -9.6 DEGREES           
REMARK 500    ILE A 144   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
REMARK 500    ASP A 239   N   -  CA  -  C   ANGL. DEV. =  8.8 DEGREES           
REMARK 500    HIS A 242   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES           
REMARK 500    GLY A 344   N   -  CA  -  C   ANGL. DEV. = 11.0 DEGREES           
REMARK 500    LEU A 451   N   -  CA  -  C   ANGL. DEV. = -7.7 DEGREES           
REMARK 500    GLY A 575   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES           
REMARK 500    ASN A 603   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    ILE A 612   N   -  CA  -  C   ANGL. DEV. = -8.0 DEGREES           
REMARK 500    LYS A 630   N   -  CA  -  C   ANGL. DEV. = -8.4 DEGREES           
REMARK 500    VAL B 121   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    MET B 231   N   -  CA  -  C   ANGL. DEV. = -8.0 DEGREES           
REMARK 500    ASP B 239   N   -  CA  -  C   ANGL. DEV. =  8.9 DEGREES           
REMARK 500    HIS B 242   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    GLY B 344   N   -  CA  -  C   ANGL. DEV. = 11.1 DEGREES           
REMARK 500    LEU B 451   N   -  CA  -  C   ANGL. DEV. = -7.6 DEGREES           
REMARK 500    GLY B 575   N   -  CA  -  C   ANGL. DEV. =  8.0 DEGREES           
REMARK 500    ASN B 603   N   -  CA  -  C   ANGL. DEV. = -9.9 DEGREES           
REMARK 500    ILE B 612   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES           
REMARK 500    LYS B 630   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    ILE B 660   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
REMARK 500    VAL C 121   N   -  CA  -  C   ANGL. DEV. = -9.8 DEGREES           
REMARK 500    ASP C 239   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
REMARK 500    HIS C 242   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    GLY C 344   N   -  CA  -  C   ANGL. DEV. = 10.6 DEGREES           
REMARK 500    GLY C 575   N   -  CA  -  C   ANGL. DEV. =  8.2 DEGREES           
REMARK 500    ASN C 603   N   -  CA  -  C   ANGL. DEV. =-10.2 DEGREES           
REMARK 500    ILE C 612   N   -  CA  -  C   ANGL. DEV. = -8.3 DEGREES           
REMARK 500    ASN C 627   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
REMARK 500    LYS C 630   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES           
REMARK 500    ILE C 660   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
REMARK 500    VAL D 121   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    ASP D 239   N   -  CA  -  C   ANGL. DEV. =  8.6 DEGREES           
REMARK 500    HIS D 242   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    GLY D 344   N   -  CA  -  C   ANGL. DEV. =  9.9 DEGREES           
REMARK 500    GLY D 575   N   -  CA  -  C   ANGL. DEV. =  8.1 DEGREES           
REMARK 500    ASN D 603   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    ILE D 612   N   -  CA  -  C   ANGL. DEV. = -8.2 DEGREES           
REMARK 500    LYS D 630   N   -  CA  -  C   ANGL. DEV. = -8.9 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 154     -108.49     48.23                                   
REMARK 500    ALA A 205     -115.19     61.96                                   
REMARK 500    TYR B 154     -111.80     45.99                                   
REMARK 500    ALA B 205     -115.34     63.46                                   
REMARK 500    TYR C 154     -110.03     49.28                                   
REMARK 500    ALA C 205     -118.35     62.99                                   
REMARK 500    TYR D 154     -109.06     49.21                                   
REMARK 500    ALA D 205     -114.21     63.08                                   
DBREF  1NX9 A   41   667  GB     18139885 AAL60195        41    667             
DBREF  1NX9 B   41   667  GB     18139885 AAL60195        41    667             
DBREF  1NX9 C   41   667  GB     18139885 AAL60195        41    667             
DBREF  1NX9 D   41   667  GB     18139885 AAL60195        41    667             
SEQADV 1NX9 ALA A  205  GB   18139885  SER   205 ENGINEERED                     
SEQADV 1NX9 LYS A  668  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU A  669  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLY A  670  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 PRO A  671  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU A  672  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLN A  673  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LYS A  674  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU A  675  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ILE A  676  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER A  677  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU A  678  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU A  679  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP A  680  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU A  681  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASN A  682  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER A  683  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ALA A  684  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 VAL A  685  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP A  686  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 HIS A  687  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS A  688  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS A  689  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS A  690  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS A  691  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS A  692  GB   18139885            HIS TAG                        
SEQADV 1NX9 ALA B  205  GB   18139885  SER   205 ENGINEERED                     
SEQADV 1NX9 LYS B  668  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU B  669  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLY B  670  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 PRO B  671  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU B  672  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLN B  673  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LYS B  674  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU B  675  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ILE B  676  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER B  677  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU B  678  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU B  679  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP B  680  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU B  681  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASN B  682  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER B  683  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ALA B  684  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 VAL B  685  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP B  686  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 HIS B  687  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS B  688  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS B  689  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS B  690  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS B  691  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS B  692  GB   18139885            HIS TAG                        
SEQADV 1NX9 ALA C  205  GB   18139885  SER   205 ENGINEERED                     
SEQADV 1NX9 LYS C  668  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU C  669  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLY C  670  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 PRO C  671  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU C  672  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLN C  673  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LYS C  674  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU C  675  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ILE C  676  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER C  677  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU C  678  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU C  679  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP C  680  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU C  681  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASN C  682  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER C  683  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ALA C  684  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 VAL C  685  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP C  686  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 HIS C  687  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS C  688  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS C  689  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS C  690  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS C  691  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS C  692  GB   18139885            HIS TAG                        
SEQADV 1NX9 ALA D  205  GB   18139885  SER   205 ENGINEERED                     
SEQADV 1NX9 LYS D  668  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU D  669  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLY D  670  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 PRO D  671  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU D  672  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLN D  673  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LYS D  674  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU D  675  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ILE D  676  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER D  677  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU D  678  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 GLU D  679  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP D  680  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 LEU D  681  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASN D  682  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 SER D  683  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ALA D  684  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 VAL D  685  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 ASP D  686  GB   18139885            MYC EPITOPE                    
SEQADV 1NX9 HIS D  687  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS D  688  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS D  689  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS D  690  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS D  691  GB   18139885            HIS TAG                        
SEQADV 1NX9 HIS D  692  GB   18139885            HIS TAG                        
SEQRES   1 A  652  ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU          
SEQRES   2 A  652  SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS          
SEQRES   3 A  652  MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU          
SEQRES   4 A  652  VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR          
SEQRES   5 A  652  VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE          
SEQRES   6 A  652  LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA          
SEQRES   7 A  652  ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU          
SEQRES   8 A  652  PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE          
SEQRES   9 A  652  ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN          
SEQRES  10 A  652  GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU          
SEQRES  11 A  652  ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP          
SEQRES  12 A  652  THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN          
SEQRES  13 A  652  GLY ARG VAL GLY MET THR GLY SER ALA TYR GLU GLY PHE          
SEQRES  14 A  652  THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU          
SEQRES  15 A  652  LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP          
SEQRES  16 A  652  MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN          
SEQRES  17 A  652  GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG          
SEQRES  18 A  652  GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP          
SEQRES  19 A  652  TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE          
SEQRES  20 A  652  ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN          
SEQRES  21 A  652  ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN          
SEQRES  22 A  652  GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO          
SEQRES  23 A  652  THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN          
SEQRES  24 A  652  GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU          
SEQRES  25 A  652  LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET          
SEQRES  26 A  652  GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER          
SEQRES  27 A  652  THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS          
SEQRES  28 A  652  GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU          
SEQRES  29 A  652  TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP          
SEQRES  30 A  652  ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR          
SEQRES  31 A  652  TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR          
SEQRES  32 A  652  GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY          
SEQRES  33 A  652  LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER          
SEQRES  34 A  652  TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER          
SEQRES  35 A  652  ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO          
SEQRES  36 A  652  TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO          
SEQRES  37 A  652  ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO          
SEQRES  38 A  652  VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA          
SEQRES  39 A  652  ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU          
SEQRES  40 A  652  ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS          
SEQRES  41 A  652  MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE          
SEQRES  42 A  652  ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA          
SEQRES  43 A  652  LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU          
SEQRES  44 A  652  PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE          
SEQRES  45 A  652  MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP          
SEQRES  46 A  652  ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA          
SEQRES  47 A  652  LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS          
SEQRES  48 A  652  HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL          
SEQRES  49 A  652  VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER          
SEQRES  50 A  652  GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS          
SEQRES  51 A  652  HIS HIS                                                      
SEQRES   1 B  652  ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU          
SEQRES   2 B  652  SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS          
SEQRES   3 B  652  MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU          
SEQRES   4 B  652  VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR          
SEQRES   5 B  652  VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE          
SEQRES   6 B  652  LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA          
SEQRES   7 B  652  ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU          
SEQRES   8 B  652  PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE          
SEQRES   9 B  652  ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN          
SEQRES  10 B  652  GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU          
SEQRES  11 B  652  ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP          
SEQRES  12 B  652  THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN          
SEQRES  13 B  652  GLY ARG VAL GLY MET THR GLY SER ALA TYR GLU GLY PHE          
SEQRES  14 B  652  THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU          
SEQRES  15 B  652  LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP          
SEQRES  16 B  652  MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN          
SEQRES  17 B  652  GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG          
SEQRES  18 B  652  GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP          
SEQRES  19 B  652  TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE          
SEQRES  20 B  652  ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN          
SEQRES  21 B  652  ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN          
SEQRES  22 B  652  GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO          
SEQRES  23 B  652  THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN          
SEQRES  24 B  652  GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU          
SEQRES  25 B  652  LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET          
SEQRES  26 B  652  GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER          
SEQRES  27 B  652  THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS          
SEQRES  28 B  652  GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU          
SEQRES  29 B  652  TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP          
SEQRES  30 B  652  ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR          
SEQRES  31 B  652  TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR          
SEQRES  32 B  652  GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY          
SEQRES  33 B  652  LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER          
SEQRES  34 B  652  TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER          
SEQRES  35 B  652  ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO          
SEQRES  36 B  652  TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO          
SEQRES  37 B  652  ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO          
SEQRES  38 B  652  VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA          
SEQRES  39 B  652  ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU          
SEQRES  40 B  652  ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS          
SEQRES  41 B  652  MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE          
SEQRES  42 B  652  ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA          
SEQRES  43 B  652  LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU          
SEQRES  44 B  652  PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE          
SEQRES  45 B  652  MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP          
SEQRES  46 B  652  ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA          
SEQRES  47 B  652  LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS          
SEQRES  48 B  652  HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL          
SEQRES  49 B  652  VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER          
SEQRES  50 B  652  GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS          
SEQRES  51 B  652  HIS HIS                                                      
SEQRES   1 C  652  ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU          
SEQRES   2 C  652  SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS          
SEQRES   3 C  652  MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU          
SEQRES   4 C  652  VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR          
SEQRES   5 C  652  VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE          
SEQRES   6 C  652  LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA          
SEQRES   7 C  652  ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU          
SEQRES   8 C  652  PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE          
SEQRES   9 C  652  ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN          
SEQRES  10 C  652  GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU          
SEQRES  11 C  652  ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP          
SEQRES  12 C  652  THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN          
SEQRES  13 C  652  GLY ARG VAL GLY MET THR GLY SER ALA TYR GLU GLY PHE          
SEQRES  14 C  652  THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU          
SEQRES  15 C  652  LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP          
SEQRES  16 C  652  MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN          
SEQRES  17 C  652  GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG          
SEQRES  18 C  652  GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP          
SEQRES  19 C  652  TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE          
SEQRES  20 C  652  ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN          
SEQRES  21 C  652  ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN          
SEQRES  22 C  652  GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO          
SEQRES  23 C  652  THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN          
SEQRES  24 C  652  GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU          
SEQRES  25 C  652  LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET          
SEQRES  26 C  652  GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER          
SEQRES  27 C  652  THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS          
SEQRES  28 C  652  GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU          
SEQRES  29 C  652  TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP          
SEQRES  30 C  652  ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR          
SEQRES  31 C  652  TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR          
SEQRES  32 C  652  GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY          
SEQRES  33 C  652  LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER          
SEQRES  34 C  652  TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER          
SEQRES  35 C  652  ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO          
SEQRES  36 C  652  TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO          
SEQRES  37 C  652  ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO          
SEQRES  38 C  652  VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA          
SEQRES  39 C  652  ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU          
SEQRES  40 C  652  ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS          
SEQRES  41 C  652  MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE          
SEQRES  42 C  652  ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA          
SEQRES  43 C  652  LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU          
SEQRES  44 C  652  PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE          
SEQRES  45 C  652  MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP          
SEQRES  46 C  652  ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA          
SEQRES  47 C  652  LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS          
SEQRES  48 C  652  HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL          
SEQRES  49 C  652  VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER          
SEQRES  50 C  652  GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS          
SEQRES  51 C  652  HIS HIS                                                      
SEQRES   1 D  652  ALA PRO ALA ALA ASP ALA ALA GLN ALA HIS ASP PRO LEU          
SEQRES   2 D  652  SER VAL GLN THR GLY SER ASP ILE PRO ALA SER VAL HIS          
SEQRES   3 D  652  MET PRO THR ASP GLN GLN ARG ASP TYR ILE LYS ARG GLU          
SEQRES   4 D  652  VAL MET VAL PRO MET ARG ASP GLY VAL LYS LEU TYR THR          
SEQRES   5 D  652  VAL ILE VAL ILE PRO LYS ASN ALA ARG ASN ALA PRO ILE          
SEQRES   6 D  652  LEU LEU THR ARG THR PRO TYR ASN ALA LYS GLY ARG ALA          
SEQRES   7 D  652  ASN ARG VAL PRO ASN ALA LEU THR MET ARG GLU VAL LEU          
SEQRES   8 D  652  PRO GLN GLY ASP ASP VAL PHE VAL GLU GLY GLY TYR ILE          
SEQRES   9 D  652  ARG VAL PHE GLN ASP ILE ARG GLY LYS TYR GLY SER GLN          
SEQRES  10 D  652  GLY ASP TYR VAL MET THR ARG PRO PRO HIS GLY PRO LEU          
SEQRES  11 D  652  ASN PRO THR LYS THR ASP GLU THR THR ASP ALA TRP ASP          
SEQRES  12 D  652  THR VAL ASP TRP LEU VAL HIS ASN VAL PRO GLU SER ASN          
SEQRES  13 D  652  GLY ARG VAL GLY MET THR GLY SER ALA TYR GLU GLY PHE          
SEQRES  14 D  652  THR VAL VAL MET ALA LEU LEU ASP PRO HIS PRO ALA LEU          
SEQRES  15 D  652  LYS VAL ALA ALA PRO GLU SER PRO MET VAL ASP GLY TRP          
SEQRES  16 D  652  MET GLY ASP ASP TRP PHE HIS TYR GLY ALA PHE ARG GLN          
SEQRES  17 D  652  GLY ALA PHE ASP TYR PHE VAL SER GLN MET THR ALA ARG          
SEQRES  18 D  652  GLY GLY GLY ASN ASP ILE PRO ARG ARG ASP ALA ASP ASP          
SEQRES  19 D  652  TYR THR ASN PHE LEU LYS ALA GLY SER ALA GLY SER PHE          
SEQRES  20 D  652  ALA THR GLN ALA GLY LEU ASP GLN TYR PRO PHE TRP GLN          
SEQRES  21 D  652  ARG MET HIS ALA HIS PRO ALA TYR ASP ALA PHE TRP GLN          
SEQRES  22 D  652  GLY GLN ALA LEU ASP LYS ILE LEU ALA GLN ARG LYS PRO          
SEQRES  23 D  652  THR VAL PRO MET LEU TRP GLU GLN GLY LEU TRP ASP GLN          
SEQRES  24 D  652  GLU ASP MET TRP GLY ALA ILE HIS ALA TRP GLN ALA LEU          
SEQRES  25 D  652  LYS ASP ALA ASP VAL LYS ALA PRO ASN THR LEU VAL MET          
SEQRES  26 D  652  GLY PRO TRP ARG HIS SER GLY VAL ASN TYR ASN GLY SER          
SEQRES  27 D  652  THR LEU GLY PRO LEU GLU PHE GLU GLY ASP THR ALA HIS          
SEQRES  28 D  652  GLN TYR ARG ARG ASP VAL PHE ARG PRO PHE PHE ASP GLU          
SEQRES  29 D  652  TYR LEU LYS PRO GLY SER ALA SER VAL HIS LEU PRO ASP          
SEQRES  30 D  652  ALA ILE ILE TYR ASN THR GLY ASP GLN LYS TRP ASP TYR          
SEQRES  31 D  652  TYR ARG SER TRP PRO SER VAL CYS GLU SER ASN CYS THR          
SEQRES  32 D  652  GLY GLY LEU THR PRO LEU TYR LEU ALA ASP GLY HIS GLY          
SEQRES  33 D  652  LEU SER PHE THR HIS PRO ALA ALA ASP GLY ALA ASP SER          
SEQRES  34 D  652  TYR VAL SER ASP PRO ALA HIS PRO VAL PRO PHE ILE SER          
SEQRES  35 D  652  ARG PRO PHE ALA PHE ALA GLN SER SER ARG TRP LYS PRO          
SEQRES  36 D  652  TRP LEU VAL GLN ASP GLN ARG GLU ALA GLU SER ARG PRO          
SEQRES  37 D  652  ASP VAL VAL THR TYR GLU THR GLU VAL LEU ASP GLU PRO          
SEQRES  38 D  652  VAL ARG VAL SER GLY VAL PRO VAL ALA ASP LEU PHE ALA          
SEQRES  39 D  652  ALA THR SER GLY THR ASP SER ASP TRP VAL VAL LYS LEU          
SEQRES  40 D  652  ILE ASP VAL GLN PRO ALA MET THR PRO ASP ASP PRO LYS          
SEQRES  41 D  652  MET GLY GLY TYR GLU LEU PRO VAL SER MET ASP ILE PHE          
SEQRES  42 D  652  ARG GLY ARG TYR ARG LYS ASP PHE ALA LYS PRO GLU ALA          
SEQRES  43 D  652  LEU GLN PRO ASP ALA THR LEU HIS TYR HIS PHE THR LEU          
SEQRES  44 D  652  PRO ALA VAL ASN HIS VAL PHE ALA LYS GLY HIS ARG ILE          
SEQRES  45 D  652  MET VAL GLN ILE GLN SER SER TRP PHE PRO LEU TYR ASP          
SEQRES  46 D  652  ARG ASN PRO GLN LYS PHE VAL PRO ASN ILE PHE ASP ALA          
SEQRES  47 D  652  LYS PRO ALA ASP TYR THR VAL ALA THR GLN SER ILE HIS          
SEQRES  48 D  652  HIS GLY GLY LYS GLU ALA THR SER ILE LEU LEU PRO VAL          
SEQRES  49 D  652  VAL LYS GLN LYS LEU GLY PRO GLU GLN LYS LEU ILE SER          
SEQRES  50 D  652  GLU GLU ASP LEU ASN SER ALA VAL ASP HIS HIS HIS HIS          
SEQRES  51 D  652  HIS HIS                                                      
HET    AIC   5001      24                                                       
HET    AIC   5002      24                                                       
HET    AIC   5003      24                                                       
HET    AIC   5004      24                                                       
HET    GOL   6002       6                                                       
HET    GOL   6004       6                                                       
HET    GOL   6006       6                                                       
HET    GOL   6008       6                                                       
HETNAM     AIC (2S,5R,6R)-6-{[(2R)-2-AMINO-2-PHENYLETHANOYL]AMINO}-3,           
HETNAM   2 AIC  3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-           
HETNAM   3 AIC  CARBOXYLIC ACID                                                 
HETNAM     GOL GLYCEROL                                                         
HETSYN     AIC AMPICILLIN; D(-)-ALPHA-AMINOBENZYLPENICILLIN; 6-[D(-)-           
HETSYN   2 AIC  ALPHA-AMINOPHENYLLACETAMIDO]PENICILLANIC ACID                   
FORMUL   5  AIC    4(C16 H19 N3 O4 S1)                                          
FORMUL   9  GOL    4(C3 H8 O3)                                                  
FORMUL  13  HOH   *2229(H2 O1)                                                  
HELIX    1   1 MET A   67  GLN A   71  5                                   5    
HELIX    2   2 ASN A  113  ALA A  118  1                                   6    
HELIX    3   3 THR A  126  LEU A  131  1                                   6    
HELIX    4   4 PRO A  132  GLY A  134  5                                   3    
HELIX    5   5 ASP A  135  GLY A  141  1                                   7    
HELIX    6   6 ASP A  176  VAL A  192  1                                  17    
HELIX    7   7 ALA A  205  LEU A  216  1                                  12    
HELIX    8   8 GLY A  249  THR A  259  1                                  11    
HELIX    9   9 ASP A  273  GLY A  282  1                                  10    
HELIX   10  10 SER A  283  GLY A  292  1                                  10    
HELIX   11  11 LEU A  293  GLN A  295  5                                   3    
HELIX   12  12 TYR A  296  HIS A  305  1                                  10    
HELIX   13  13 ASP A  309  GLY A  314  1                                   6    
HELIX   14  14 ALA A  316  LYS A  325  1                                  10    
HELIX   15  15 TRP A  343  ALA A  355  1                                  13    
HELIX   16  16 SER A  371  TYR A  375  5                                   5    
HELIX   17  17 ASP A  388  VAL A  397  1                                  10    
HELIX   18  18 VAL A  397  LYS A  407  1                                  11    
HELIX   19  19 ASP A  453  HIS A  455  5                                   3    
HELIX   20  20 GLN A  489  LYS A  494  1                                   6    
HELIX   21  21 PRO A  495  GLN A  499  5                                   5    
HELIX   22  22 GLN A  501  SER A  506  1                                   6    
HELIX   23  23 ASP A  558  GLY A  562  5                                   5    
HELIX   24  24 ARG A  576  ARG A  578  5                                   3    
HELIX   25  25 ASN A  634  ALA A  638  5                                   5    
HELIX   26  26 LYS A  639  TYR A  643  5                                   5    
HELIX   27  27 GLY A  653  ALA A  657  5                                   5    
HELIX   28  28 MET B   67  ARG B   73  5                                   7    
HELIX   29  29 ASN B  113  ALA B  118  1                                   6    
HELIX   30  30 THR B  126  LEU B  131  1                                   6    
HELIX   31  31 PRO B  132  GLY B  134  5                                   3    
HELIX   32  32 ASP B  135  GLY B  141  1                                   7    
HELIX   33  33 ASP B  176  VAL B  192  1                                  17    
HELIX   34  34 ALA B  205  LEU B  216  1                                  12    
HELIX   35  35 GLY B  249  THR B  259  1                                  11    
HELIX   36  36 ASP B  273  GLY B  282  1                                  10    
HELIX   37  37 SER B  283  GLY B  292  1                                  10    
HELIX   38  38 LEU B  293  GLN B  295  5                                   3    
HELIX   39  39 TYR B  296  HIS B  305  1                                  10    
HELIX   40  40 ASP B  309  GLY B  314  1                                   6    
HELIX   41  41 ALA B  316  LYS B  325  1                                  10    
HELIX   42  42 TRP B  343  ALA B  355  1                                  13    
HELIX   43  43 SER B  371  TYR B  375  5                                   5    
HELIX   44  44 ASP B  388  VAL B  397  1                                  10    
HELIX   45  45 VAL B  397  LYS B  407  1                                  11    
HELIX   46  46 ASP B  453  HIS B  455  5                                   3    
HELIX   47  47 GLN B  489  LYS B  494  1                                   6    
HELIX   48  48 PRO B  495  GLN B  499  5                                   5    
HELIX   49  49 GLN B  501  SER B  506  1                                   6    
HELIX   50  50 ASP B  558  GLY B  562  5                                   5    
HELIX   51  51 ARG B  576  ARG B  578  5                                   3    
HELIX   52  52 ASN B  634  ALA B  638  5                                   5    
HELIX   53  53 LYS B  639  TYR B  643  5                                   5    
HELIX   54  54 GLY B  653  ALA B  657  5                                   5    
HELIX   55  55 ASN C  113  ALA C  118  1                                   6    
HELIX   56  56 THR C  126  LEU C  131  1                                   6    
HELIX   57  57 PRO C  132  GLY C  134  5                                   3    
HELIX   58  58 ASP C  135  GLY C  141  1                                   7    
HELIX   59  59 ASP C  176  VAL C  192  1                                  17    
HELIX   60  60 ALA C  205  LEU C  216  1                                  12    
HELIX   61  61 GLY C  249  THR C  259  1                                  11    
HELIX   62  62 ASP C  273  GLY C  282  1                                  10    
HELIX   63  63 SER C  283  GLY C  292  1                                  10    
HELIX   64  64 LEU C  293  GLN C  295  5                                   3    
HELIX   65  65 TYR C  296  HIS C  305  1                                  10    
HELIX   66  66 ASP C  309  GLY C  314  1                                   6    
HELIX   67  67 ALA C  316  LYS C  325  1                                  10    
HELIX   68  68 TRP C  343  ALA C  355  1                                  13    
HELIX   69  69 SER C  371  TYR C  375  5                                   5    
HELIX   70  70 ASP C  388  VAL C  397  1                                  10    
HELIX   71  71 VAL C  397  LYS C  407  1                                  11    
HELIX   72  72 ASP C  453  HIS C  455  5                                   3    
HELIX   73  73 GLN C  489  LYS C  494  1                                   6    
HELIX   74  74 PRO C  495  GLN C  499  5                                   5    
HELIX   75  75 GLN C  501  SER C  506  1                                   6    
HELIX   76  76 ASP C  558  GLY C  562  5                                   5    
HELIX   77  77 ARG C  576  ARG C  578  5                                   3    
HELIX   78  78 ASN C  634  ALA C  638  5                                   5    
HELIX   79  79 LYS C  639  TYR C  643  5                                   5    
HELIX   80  80 GLY C  653  ALA C  657  5                                   5    
HELIX   81  81 MET D   67  GLN D   71  5                                   5    
HELIX   82  82 ASN D  113  ALA D  118  1                                   6    
HELIX   83  83 THR D  126  LEU D  131  1                                   6    
HELIX   84  84 PRO D  132  GLY D  134  5                                   3    
HELIX   85  85 ASP D  135  GLY D  141  1                                   7    
HELIX   86  86 ASP D  176  VAL D  192  1                                  17    
HELIX   87  87 ALA D  205  LEU D  215  1                                  11    
HELIX   88  88 GLY D  249  THR D  259  1                                  11    
HELIX   89  89 ASP D  273  GLY D  282  1                                  10    
HELIX   90  90 SER D  283  GLY D  292  1                                  10    
HELIX   91  91 LEU D  293  GLN D  295  5                                   3    
HELIX   92  92 TYR D  296  HIS D  305  1                                  10    
HELIX   93  93 ASP D  309  GLY D  314  1                                   6    
HELIX   94  94 ALA D  316  LYS D  325  1                                  10    
HELIX   95  95 TRP D  343  ALA D  355  1                                  13    
HELIX   96  96 SER D  371  TYR D  375  5                                   5    
HELIX   97  97 ASP D  388  VAL D  397  1                                  10    
HELIX   98  98 VAL D  397  LYS D  407  1                                  11    
HELIX   99  99 ASP D  453  HIS D  455  5                                   3    
HELIX  100 100 GLN D  489  LYS D  494  1                                   6    
HELIX  101 101 PRO D  495  GLN D  499  5                                   5    
HELIX  102 102 GLN D  501  SER D  506  1                                   6    
HELIX  103 103 ASP D  558  GLY D  562  5                                   5    
HELIX  104 104 ARG D  576  ARG D  578  5                                   3    
HELIX  105 105 ASN D  634  ALA D  638  5                                   5    
HELIX  106 106 LYS D  639  TYR D  643  5                                   5    
HELIX  107 107 GLY D  653  ALA D  657  5                                   5    
SHEET    1   A 6 TYR A  75  PRO A  83  0                                        
SHEET    2   A 6 LYS A  89  PRO A  97 -1  O  ILE A  94   N  ARG A  78           
SHEET    3   A 6 ILE A 144  ASP A 149 -1  O  ARG A 145   N  VAL A  95           
SHEET    4   A 6 ALA A 103  THR A 110  1  N  THR A 110   O  GLN A 148           
SHEET    5   A 6 SER A 195  SER A 204  1  O  GLY A 200   N  LEU A 107           
SHEET    6   A 6 LEU A 222  GLU A 228  1  O  GLU A 228   N  GLY A 203           
SHEET    1   B 2 PHE A 241  HIS A 242  0                                        
SHEET    2   B 2 ALA A 245  PHE A 246 -1  O  ALA A 245   N  HIS A 242           
SHEET    1   C 4 MET A 330  GLY A 335  0                                        
SHEET    2   C 4 ASN A 361  GLY A 366  1  O  VAL A 364   N  TRP A 332           
SHEET    3   C 4 ALA A 418  ASN A 422  1  O  ILE A 419   N  LEU A 363           
SHEET    4   C 4 LYS A 427  TYR A 431 -1  O  LYS A 427   N  ASN A 422           
SHEET    1   D 2 THR A 379  LEU A 380  0                                        
SHEET    2   D 2 LEU A 383  GLU A 384 -1  O  LEU A 383   N  LEU A 380           
SHEET    1   E 4 GLY A 466  SER A 472  0                                        
SHEET    2   E 4 ALA A 646  HIS A 652 -1  O  GLN A 648   N  TYR A 470           
SHEET    3   E 4 VAL A 529  THR A 536 -1  N  ALA A 535   O  SER A 649           
SHEET    4   E 4 LEU A 593  THR A 598 -1  O  TYR A 595   N  LEU A 532           
SHEET    1   F 6 GLY A 466  SER A 472  0                                        
SHEET    2   F 6 ALA A 646  HIS A 652 -1  O  GLN A 648   N  TYR A 470           
SHEET    3   F 6 VAL A 529  THR A 536 -1  N  ALA A 535   O  SER A 649           
SHEET    4   F 6 SER A 659  LEU A 662 -1  O  LEU A 661   N  VAL A 529           
SHEET    5   F 6 THR A 447  ALA A 452 -1  N  THR A 447   O  LEU A 662           
SHEET    6   F 6 GLY A 456  SER A 458 -1  O  GLY A 456   N  ALA A 452           
SHEET    1   G 4 VAL A 510  GLU A 514  0                                        
SHEET    2   G 4 ARG A 611  GLN A 617 -1  O  VAL A 614   N  TYR A 513           
SHEET    3   G 4 ASP A 542  VAL A 550 -1  N  ILE A 548   O  MET A 613           
SHEET    4   G 4 GLU A 565  ARG A 574 -1  O  LEU A 566   N  ASP A 549           
SHEET    1   H 2 VAL A 522  GLY A 526  0                                        
SHEET    2   H 2 VAL A 602  PHE A 606 -1  O  VAL A 602   N  GLY A 526           
SHEET    1   I 6 TYR B  75  PRO B  83  0                                        
SHEET    2   I 6 LYS B  89  PRO B  97 -1  O  ILE B  96   N  ILE B  76           
SHEET    3   I 6 ILE B 144  ASP B 149 -1  O  ARG B 145   N  VAL B  95           
SHEET    4   I 6 ALA B 103  THR B 110  1  N  THR B 110   O  GLN B 148           
SHEET    5   I 6 SER B 195  SER B 204  1  O  GLY B 200   N  LEU B 107           
SHEET    6   I 6 LEU B 222  GLU B 228  1  O  GLU B 228   N  GLY B 203           
SHEET    1   J 2 PHE B 241  HIS B 242  0                                        
SHEET    2   J 2 ALA B 245  PHE B 246 -1  O  ALA B 245   N  HIS B 242           
SHEET    1   K 4 MET B 330  GLY B 335  0                                        
SHEET    2   K 4 ASN B 361  GLY B 366  1  O  VAL B 364   N  TRP B 332           
SHEET    3   K 4 ALA B 418  ASN B 422  1  O  ILE B 419   N  LEU B 363           
SHEET    4   K 4 LYS B 427  TYR B 431 -1  O  LYS B 427   N  ASN B 422           
SHEET    1   L 2 THR B 379  LEU B 380  0                                        
SHEET    2   L 2 LEU B 383  GLU B 384 -1  O  LEU B 383   N  LEU B 380           
SHEET    1   M 4 GLY B 466  SER B 472  0                                        
SHEET    2   M 4 ALA B 646  HIS B 652 -1  O  GLN B 648   N  TYR B 470           
SHEET    3   M 4 VAL B 529  THR B 536 -1  N  ALA B 535   O  SER B 649           
SHEET    4   M 4 LEU B 593  THR B 598 -1  O  TYR B 595   N  LEU B 532           
SHEET    1   N 6 GLY B 466  SER B 472  0                                        
SHEET    2   N 6 ALA B 646  HIS B 652 -1  O  GLN B 648   N  TYR B 470           
SHEET    3   N 6 VAL B 529  THR B 536 -1  N  ALA B 535   O  SER B 649           
SHEET    4   N 6 SER B 659  LEU B 662 -1  O  LEU B 661   N  VAL B 529           
SHEET    5   N 6 THR B 447  ALA B 452 -1  N  THR B 447   O  LEU B 662           
SHEET    6   N 6 GLY B 456  SER B 458 -1  O  SER B 458   N  TYR B 450           
SHEET    1   O 4 VAL B 510  GLU B 514  0                                        
SHEET    2   O 4 ARG B 611  GLN B 617 -1  O  VAL B 614   N  TYR B 513           
SHEET    3   O 4 ASP B 542  VAL B 550 -1  N  ILE B 548   O  MET B 613           
SHEET    4   O 4 GLU B 565  ARG B 574 -1  O  LEU B 566   N  ASP B 549           
SHEET    1   P 2 VAL B 522  GLY B 526  0                                        
SHEET    2   P 2 VAL B 602  PHE B 606 -1  O  VAL B 602   N  GLY B 526           
SHEET    1   Q 6 TYR C  75  PRO C  83  0                                        
SHEET    2   Q 6 LYS C  89  PRO C  97 -1  O  ILE C  96   N  ILE C  76           
SHEET    3   Q 6 ILE C 144  ASP C 149 -1  O  ARG C 145   N  VAL C  95           
SHEET    4   Q 6 ALA C 103  THR C 110  1  N  THR C 110   O  GLN C 148           
SHEET    5   Q 6 SER C 195  SER C 204  1  O  GLY C 200   N  LEU C 107           
SHEET    6   Q 6 LEU C 222  GLU C 228  1  O  GLU C 228   N  GLY C 203           
SHEET    1   R 2 PHE C 241  HIS C 242  0                                        
SHEET    2   R 2 ALA C 245  PHE C 246 -1  O  ALA C 245   N  HIS C 242           
SHEET    1   S 4 MET C 330  GLY C 335  0                                        
SHEET    2   S 4 ASN C 361  GLY C 366  1  O  THR C 362   N  TRP C 332           
SHEET    3   S 4 ALA C 418  ASN C 422  1  O  ILE C 419   N  LEU C 363           
SHEET    4   S 4 LYS C 427  TYR C 431 -1  O  LYS C 427   N  ASN C 422           
SHEET    1   T 2 THR C 379  LEU C 380  0                                        
SHEET    2   T 2 LEU C 383  GLU C 384 -1  O  LEU C 383   N  LEU C 380           
SHEET    1   U 4 GLY C 466  SER C 472  0                                        
SHEET    2   U 4 ALA C 646  HIS C 652 -1  O  GLN C 648   N  TYR C 470           
SHEET    3   U 4 VAL C 529  THR C 536 -1  N  ALA C 535   O  SER C 649           
SHEET    4   U 4 LEU C 593  THR C 598 -1  O  TYR C 595   N  LEU C 532           
SHEET    1   V 6 GLY C 466  SER C 472  0                                        
SHEET    2   V 6 ALA C 646  HIS C 652 -1  O  GLN C 648   N  TYR C 470           
SHEET    3   V 6 VAL C 529  THR C 536 -1  N  ALA C 535   O  SER C 649           
SHEET    4   V 6 SER C 659  LEU C 662 -1  O  LEU C 661   N  VAL C 529           
SHEET    5   V 6 THR C 447  ALA C 452 -1  N  THR C 447   O  LEU C 662           
SHEET    6   V 6 GLY C 456  SER C 458 -1  O  GLY C 456   N  ALA C 452           
SHEET    1   W 4 VAL C 510  GLU C 514  0                                        
SHEET    2   W 4 ARG C 611  GLN C 617 -1  O  VAL C 614   N  TYR C 513           
SHEET    3   W 4 ASP C 542  VAL C 550 -1  N  ILE C 548   O  MET C 613           
SHEET    4   W 4 GLU C 565  ARG C 574 -1  O  LEU C 566   N  ASP C 549           
SHEET    1   X 3 VAL C 602  PHE C 606  0                                        
SHEET    2   X 3 VAL C 522  GLY C 526 -1  N  GLY C 526   O  VAL C 602           
SHEET    3   X 3 VAL C 664  VAL C 665 -1  O  VAL C 665   N  ARG C 523           
SHEET    1   Y 6 TYR D  75  PRO D  83  0                                        
SHEET    2   Y 6 LYS D  89  PRO D  97 -1  O  ILE D  96   N  ILE D  76           
SHEET    3   Y 6 ILE D 144  ASP D 149 -1  O  ARG D 145   N  VAL D  95           
SHEET    4   Y 6 ALA D 103  THR D 110  1  N  LEU D 106   O  ILE D 144           
SHEET    5   Y 6 SER D 195  SER D 204  1  O  GLY D 200   N  LEU D 107           
SHEET    6   Y 6 LEU D 222  GLU D 228  1  O  GLU D 228   N  GLY D 203           
SHEET    1   Z 2 PHE D 241  HIS D 242  0                                        
SHEET    2   Z 2 ALA D 245  PHE D 246 -1  O  ALA D 245   N  HIS D 242           
SHEET    1  AA 4 MET D 330  GLY D 335  0                                        
SHEET    2  AA 4 ASN D 361  GLY D 366  1  O  VAL D 364   N  TRP D 332           
SHEET    3  AA 4 ALA D 418  ASN D 422  1  O  ILE D 419   N  LEU D 363           
SHEET    4  AA 4 LYS D 427  TYR D 431 -1  O  LYS D 427   N  ASN D 422           
SHEET    1  AB 2 THR D 379  LEU D 380  0                                        
SHEET    2  AB 2 LEU D 383  GLU D 384 -1  O  LEU D 383   N  LEU D 380           
SHEET    1  AC 4 GLY D 466  SER D 472  0                                        
SHEET    2  AC 4 ALA D 646  HIS D 652 -1  O  GLN D 648   N  TYR D 470           
SHEET    3  AC 4 VAL D 529  THR D 536 -1  N  ALA D 535   O  SER D 649           
SHEET    4  AC 4 LEU D 593  THR D 598 -1  O  TYR D 595   N  LEU D 532           
SHEET    1  AD 6 GLY D 466  SER D 472  0                                        
SHEET    2  AD 6 ALA D 646  HIS D 652 -1  O  GLN D 648   N  TYR D 470           
SHEET    3  AD 6 VAL D 529  THR D 536 -1  N  ALA D 535   O  SER D 649           
SHEET    4  AD 6 SER D 659  LEU D 662 -1  O  LEU D 661   N  VAL D 529           
SHEET    5  AD 6 THR D 447  ALA D 452 -1  N  THR D 447   O  LEU D 662           
SHEET    6  AD 6 GLY D 456  SER D 458 -1  O  SER D 458   N  TYR D 450           
SHEET    1  AE 4 VAL D 510  GLU D 514  0                                        
SHEET    2  AE 4 ARG D 611  GLN D 617 -1  O  VAL D 614   N  TYR D 513           
SHEET    3  AE 4 ASP D 542  VAL D 550 -1  N  ILE D 548   O  MET D 613           
SHEET    4  AE 4 GLU D 565  ARG D 574 -1  O  LEU D 566   N  ASP D 549           
SHEET    1  AF 3 VAL D 602  PHE D 606  0                                        
SHEET    2  AF 3 VAL D 522  GLY D 526 -1  N  VAL D 522   O  PHE D 606           
SHEET    3  AF 3 VAL D 664  VAL D 665 -1  O  VAL D 665   N  ARG D 523           
CISPEP   1 TRP A  434    PRO A  435          0        -1.49                     
CISPEP   2 ARG A  483    PRO A  484          0        -1.50                     
CISPEP   3 PHE A  621    PRO A  622          0        -1.24                     
CISPEP   4 TRP B  434    PRO B  435          0        -2.16                     
CISPEP   5 ARG B  483    PRO B  484          0        -1.85                     
CISPEP   6 PHE B  621    PRO B  622          0        -0.92                     
CISPEP   7 TRP C  434    PRO C  435          0        -2.01                     
CISPEP   8 ARG C  483    PRO C  484          0        -2.54                     
CISPEP   9 PHE C  621    PRO C  622          0        -1.24                     
CISPEP  10 TRP D  434    PRO D  435          0        -1.27                     
CISPEP  11 ARG D  483    PRO D  484          0        -1.57                     
CISPEP  12 PHE D  621    PRO D  622          0        -0.95                     
CRYST1  341.828  341.828  341.828  90.00  90.00  90.00 I 2 3        96          
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      0.002925  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002925  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002925        0.00000                         
TER    4883      LYS A 666                                                      
TER    9766      LYS B 666                                                      
TER   14649      LYS C 666                                                      
TER   19532      LYS D 666                                                      
MASTER      552    0    8  107  122    0    0    621877    4  120  204          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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