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LongText Report for: 7avr-pdb

Name Class
7avr-pdb
HEADER    HYDROLASE                               05-NOV-20   7AVR              
TITLE     THE TETRAMERIC STRUCTURE OF HALOALKANE DEHALOGENASE DPAA FROM         
TITLE    2 PARAGLACIECOLA AGARILYTICA NO2                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE 1;                                 
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: HALOALKANE DEHALOGENASE DPAA;                               
COMPND   5 EC: 3.8.1.5;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PARAGLACIECOLA AGARILYTICA NO2;                 
SOURCE   3 ORGANISM_TAXID: 1125747;                                             
SOURCE   4 GENE: DHMA1, GAGA_3124;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    HALOALKANE DEHALOGENASE, ENZYME, TETRAMER, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MAZUR,P.KOLENKO,T.PRUDNIKOVA,P.GRINKEVICH,I.KUTA SMATANOVA          
REVDAT   1   17-MAR-21 7AVR    0                                                
JRNL        AUTH   A.MAZUR,T.PRUDNIKOVA,P.GRINKEVICH,J.R.MESTERS,D.MRAZOVA,     
JRNL        AUTH 2 R.CHALOUPKOVA,J.DAMBORSKY,M.KUTY,P.KOLENKO,I.KUTA SMATANOVA  
JRNL        TITL   THE TETRAMERIC STRUCTURE OF THE NOVEL HALOALKANE             
JRNL        TITL 2 DEHALOGENASE DPAA FROM PARAGLACIECOLA AGARILYTICA NO2.       
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  77   347 2021              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   33645538                                                     
JRNL        DOI    10.1107/S2059798321000486                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0189                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 182376                         
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9496                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13173                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.0880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 673                          
REMARK   3   BIN FREE R VALUE                    : 0.1180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18745                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 2008                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.06000                                             
REMARK   3    B22 (A**2) : 0.25000                                              
REMARK   3    B33 (A**2) : -0.18000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.035         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.030         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 19269 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 17587 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26149 ; 1.769 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 40893 ; 3.875 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2395 ; 6.127 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   899 ;35.803 ;24.839       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3181 ;13.557 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    80 ;21.643 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2808 ; 0.122 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 21591 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  3917 ; 0.017 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  9562 ; 3.290 ; 2.666       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  9561 ; 3.290 ; 2.665       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 11945 ; 4.119 ; 3.988       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 11946 ; 4.119 ; 3.989       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  9707 ; 3.454 ; 2.816       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  9708 ; 3.453 ; 2.816       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 14199 ; 4.353 ; 4.160       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 22958 ; 6.242 ;32.170       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 22267 ; 6.038 ;31.793       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 28                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     3    299       B     3    299   19296  0.10  0.05     
REMARK   3    2     A     3    299       C     3    299   19400  0.10  0.05     
REMARK   3    3     A     3    298       D     3    298   19352  0.09  0.05     
REMARK   3    4     A     3    299       E     3    299   19278  0.10  0.05     
REMARK   3    5     A     3    298       F     3    298   19324  0.10  0.05     
REMARK   3    6     A     3    299       G     3    299   19414  0.09  0.05     
REMARK   3    7     A     3    301       H     3    301   19752  0.08  0.05     
REMARK   3    8     B     3    299       C     3    299   19246  0.10  0.05     
REMARK   3    9     B     3    298       D     3    298   19100  0.10  0.05     
REMARK   3   10     B     3    300       E     3    300   19672  0.08  0.05     
REMARK   3   11     B     3    298       F     3    298   19076  0.10  0.05     
REMARK   3   12     B     3    299       G     3    299   19374  0.09  0.05     
REMARK   3   13     B     3    299       H     3    299   19092  0.10  0.05     
REMARK   3   14     C     3    298       D     3    298   19358  0.09  0.05     
REMARK   3   15     C     3    299       E     3    299   19324  0.10  0.05     
REMARK   3   16     C     2    298       F     2    298   19330  0.10  0.05     
REMARK   3   17     C     2    300       G     2    300   19794  0.08  0.05     
REMARK   3   18     C     3    299       H     3    299   19194  0.10  0.05     
REMARK   3   19     D     3    298       E     3    298   19216  0.09  0.05     
REMARK   3   20     D     3    298       F     3    298   19780  0.06  0.05     
REMARK   3   21     D     3    298       G     3    298   19350  0.08  0.05     
REMARK   3   22     D     3    298       H     3    298   19260  0.09  0.05     
REMARK   3   23     E     3    298       F     3    298   19248  0.09  0.05     
REMARK   3   24     E     3    299       G     3    299   19426  0.09  0.05     
REMARK   3   25     E     3    299       H     3    299   19200  0.10  0.05     
REMARK   3   26     F     2    298       G     2    298   19314  0.09  0.05     
REMARK   3   27     F     3    298       H     3    298   19270  0.10  0.05     
REMARK   3   28     G     3    299       H     3    299   19280  0.10  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 7AVR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292112003.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918409                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 191831                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.440                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 1.790                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2XT0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NA HEPES, 4% W/V PEG 400, 2 M      
REMARK 280  (NH4)2SO4, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE       
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       58.69250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       77.75300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.69250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       77.75300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7150 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 42210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH F 682  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     HIS A   302                                                      
REMARK 465     HIS A   303                                                      
REMARK 465     HIS A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ILE B   301                                                      
REMARK 465     HIS B   302                                                      
REMARK 465     HIS B   303                                                      
REMARK 465     HIS B   304                                                      
REMARK 465     HIS B   305                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     HIS B   307                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ILE C   301                                                      
REMARK 465     HIS C   302                                                      
REMARK 465     HIS C   303                                                      
REMARK 465     HIS C   304                                                      
REMARK 465     HIS C   305                                                      
REMARK 465     HIS C   306                                                      
REMARK 465     HIS C   307                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     MET D   300                                                      
REMARK 465     ILE D   301                                                      
REMARK 465     HIS D   302                                                      
REMARK 465     HIS D   303                                                      
REMARK 465     HIS D   304                                                      
REMARK 465     HIS D   305                                                      
REMARK 465     HIS D   306                                                      
REMARK 465     HIS D   307                                                      
REMARK 465     MET E     1                                                      
REMARK 465     THR E     2                                                      
REMARK 465     ILE E   301                                                      
REMARK 465     HIS E   302                                                      
REMARK 465     HIS E   303                                                      
REMARK 465     HIS E   304                                                      
REMARK 465     HIS E   305                                                      
REMARK 465     HIS E   306                                                      
REMARK 465     HIS E   307                                                      
REMARK 465     MET F     1                                                      
REMARK 465     MET F   300                                                      
REMARK 465     ILE F   301                                                      
REMARK 465     HIS F   302                                                      
REMARK 465     HIS F   303                                                      
REMARK 465     HIS F   304                                                      
REMARK 465     HIS F   305                                                      
REMARK 465     HIS F   306                                                      
REMARK 465     HIS F   307                                                      
REMARK 465     MET G     1                                                      
REMARK 465     ILE G   301                                                      
REMARK 465     HIS G   302                                                      
REMARK 465     HIS G   303                                                      
REMARK 465     HIS G   304                                                      
REMARK 465     HIS G   305                                                      
REMARK 465     HIS G   306                                                      
REMARK 465     HIS G   307                                                      
REMARK 465     MET H     1                                                      
REMARK 465     THR H     2                                                      
REMARK 465     HIS H   302                                                      
REMARK 465     HIS H   303                                                      
REMARK 465     HIS H   304                                                      
REMARK 465     HIS H   305                                                      
REMARK 465     HIS H   306                                                      
REMARK 465     HIS H   307                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER F  34    OG                                                  
REMARK 470     ASP H  46    CG   OD1  OD2                                       
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASP C   28   CG                                                  
REMARK 480     ASP D  140   CG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP E 140   CB  -  CG  -  OD1 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    ASP E 140   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  20       45.20    -90.39                                   
REMARK 500    SER A  34      -12.87     78.60                                   
REMARK 500    PRO A  58       56.87   -103.74                                   
REMARK 500    THR A  59     -166.65   -107.27                                   
REMARK 500    ASP A 125     -137.20     52.31                                   
REMARK 500    MET A 138       63.38   -162.60                                   
REMARK 500    ASN A 149      101.62    -36.16                                   
REMARK 500    ASN A 238      -35.27   -131.74                                   
REMARK 500    MET A 300       38.29    -90.25                                   
REMARK 500    PRO B  20       44.58    -89.76                                   
REMARK 500    GLU B  33     -136.29     47.92                                   
REMARK 500    PRO B  58       57.19   -105.08                                   
REMARK 500    THR B  59     -164.53   -106.96                                   
REMARK 500    ASN B 118       75.89   -104.17                                   
REMARK 500    ASP B 125     -136.66     54.01                                   
REMARK 500    MET B 138       49.30   -151.77                                   
REMARK 500    ASN B 149      100.11    -19.33                                   
REMARK 500    PRO C  20       43.58    -88.95                                   
REMARK 500    SER C  34      -12.88     79.11                                   
REMARK 500    PRO C  58       54.85   -103.11                                   
REMARK 500    THR C  59     -165.01   -106.98                                   
REMARK 500    ASP C 125     -137.96     53.80                                   
REMARK 500    MET C 138       49.52   -153.09                                   
REMARK 500    ASN C 149      106.38    -36.47                                   
REMARK 500    TRP C 240      128.63    -36.68                                   
REMARK 500    PRO D  20       45.72    -91.04                                   
REMARK 500    SER D  34      -15.39     79.58                                   
REMARK 500    PRO D  58       57.89   -103.74                                   
REMARK 500    THR D  59     -167.64   -108.76                                   
REMARK 500    ASP D 125     -136.81     53.04                                   
REMARK 500    MET D 138       53.76   -153.29                                   
REMARK 500    ASN D 149      100.87    -22.39                                   
REMARK 500    PRO E  20       43.80    -89.15                                   
REMARK 500    GLU E  33     -132.84     50.36                                   
REMARK 500    GLU E  33     -131.65     50.36                                   
REMARK 500    PRO E  58       57.79   -104.32                                   
REMARK 500    THR E  59     -164.21   -108.40                                   
REMARK 500    ASP E 125     -138.46     54.29                                   
REMARK 500    MET E 138       49.67   -152.27                                   
REMARK 500    ASN E 149      100.53    -24.35                                   
REMARK 500    PRO F  20       46.02    -91.49                                   
REMARK 500    SER F  34      -15.84     78.96                                   
REMARK 500    PRO F  58       56.87   -104.37                                   
REMARK 500    THR F  59     -164.62   -109.53                                   
REMARK 500    ASP F 125     -138.88     55.49                                   
REMARK 500    MET F 138       48.99   -151.28                                   
REMARK 500    ASN F 149       98.72    -19.19                                   
REMARK 500    PRO G  20       43.28    -86.99                                   
REMARK 500    SER G  34      -10.61     76.54                                   
REMARK 500    PRO G  58       56.33   -105.89                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      62 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 756        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A 757        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A 758        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A 759        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A 760        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A 761        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH A 762        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH A 763        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH A 764        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH B 732        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B 733        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B 734        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B 735        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH B 736        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 737        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 738        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH B 739        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH B 740        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH B 741        DISTANCE =  6.97 ANGSTROMS                       
REMARK 525    HOH B 742        DISTANCE =  7.00 ANGSTROMS                       
REMARK 525    HOH B 743        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH B 744        DISTANCE =  8.90 ANGSTROMS                       
REMARK 525    HOH C 766        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C 767        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C 768        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH C 769        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH C 770        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH C 771        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH C 772        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH C 773        DISTANCE =  6.47 ANGSTROMS                       
REMARK 525    HOH C 774        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH C 775        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH C 776        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH C 777        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH C 778        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH C 779        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH C 780        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH C 781        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH C 782        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH C 783        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH C 784        DISTANCE =  7.78 ANGSTROMS                       
REMARK 525    HOH C 785        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH C 786        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH C 787        DISTANCE =  8.69 ANGSTROMS                       
REMARK 525    HOH C 788        DISTANCE =  8.75 ANGSTROMS                       
REMARK 525    HOH C 789        DISTANCE =  9.55 ANGSTROMS                       
REMARK 525    HOH C 790        DISTANCE = 10.67 ANGSTROMS                       
REMARK 525    HOH C 791        DISTANCE = 15.76 ANGSTROMS                       
REMARK 525    HOH D 710        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH D 711        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH D 712        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH D 713        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH D 714        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH D 715        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH D 716        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH D 717        DISTANCE =  9.65 ANGSTROMS                       
REMARK 525    HOH E 736        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH E 737        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH E 738        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH E 739        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH E 740        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH E 741        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH E 742        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH E 743        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH E 744        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH E 745        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH E 746        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH E 747        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH E 748        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH E 749        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH E 750        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH E 751        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH E 752        DISTANCE =  6.72 ANGSTROMS                       
REMARK 525    HOH E 753        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH E 754        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH E 755        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH E 756        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH E 757        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH E 758        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH E 759        DISTANCE =  7.81 ANGSTROMS                       
REMARK 525    HOH E 760        DISTANCE =  7.84 ANGSTROMS                       
REMARK 525    HOH E 761        DISTANCE =  7.97 ANGSTROMS                       
REMARK 525    HOH E 762        DISTANCE =  8.44 ANGSTROMS                       
REMARK 525    HOH E 763        DISTANCE =  8.62 ANGSTROMS                       
REMARK 525    HOH E 764        DISTANCE =  9.12 ANGSTROMS                       
REMARK 525    HOH F 777        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH F 778        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH F 779        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH F 780        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH F 781        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH F 782        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH F 783        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH F 784        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH F 785        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH F 786        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH F 787        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH F 788        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH F 789        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH F 790        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH F 791        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH F 792        DISTANCE =  7.53 ANGSTROMS                       
REMARK 525    HOH F 793        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH F 794        DISTANCE =  7.92 ANGSTROMS                       
REMARK 525    HOH F 795        DISTANCE =  8.04 ANGSTROMS                       
REMARK 525    HOH F 796        DISTANCE =  8.48 ANGSTROMS                       
REMARK 525    HOH F 797        DISTANCE =  8.60 ANGSTROMS                       
REMARK 525    HOH F 798        DISTANCE = 11.19 ANGSTROMS                       
REMARK 525    HOH G 714        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH G 715        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH G 716        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH G 717        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH G 718        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH G 719        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH G 720        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH G 721        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH G 722        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH G 723        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH G 724        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH G 725        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH G 726        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH G 727        DISTANCE =  7.73 ANGSTROMS                       
REMARK 525    HOH G 728        DISTANCE =  8.01 ANGSTROMS                       
REMARK 525    HOH G 729        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH G 730        DISTANCE =  9.45 ANGSTROMS                       
REMARK 525    HOH G 731        DISTANCE =  9.90 ANGSTROMS                       
REMARK 525    HOH H 687        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH H 688        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH H 689        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH H 690        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH H 691        DISTANCE =  6.69 ANGSTROMS                       
REMARK 525    HOH H 692        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH H 693        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH H 694        DISTANCE =  8.03 ANGSTROMS                       
REMARK 525    HOH H 695        DISTANCE =  8.10 ANGSTROMS                       
REMARK 525    HOH H 696        DISTANCE =  8.42 ANGSTROMS                       
REMARK 525    HOH H 697        DISTANCE =  9.44 ANGSTROMS                       
REMARK 525    HOH H 698        DISTANCE = 10.03 ANGSTROMS                       
REMARK 525    HOH H 699        DISTANCE = 10.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 401                  
DBREF  7AVR A    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR B    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR C    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR D    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR E    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR F    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR G    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
DBREF  7AVR H    3   301  UNP    K6XNL5   K6XNL5_9ALTE     3    301             
SEQADV 7AVR MET A    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR A    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS A  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET B    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR B    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS B  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET C    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR C    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS C  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET D    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR D    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS D  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET E    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR E    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS E  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET F    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR F    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS F  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET G    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR G    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS G  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR MET H    1  UNP  K6XNL5              INITIATING METHIONINE          
SEQADV 7AVR THR H    2  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  302  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  303  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  304  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  305  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  306  UNP  K6XNL5              EXPRESSION TAG                 
SEQADV 7AVR HIS H  307  UNP  K6XNL5              EXPRESSION TAG                 
SEQRES   1 A  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 A  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 A  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 A  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 A  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 A  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 A  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 A  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 A  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 A  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 A  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 A  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 A  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 A  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 A  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 A  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 A  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 A  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 A  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 A  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 A  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 A  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 A  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 A  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 B  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 B  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 B  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 B  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 B  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 B  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 B  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 B  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 B  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 B  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 B  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 B  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 B  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 B  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 B  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 B  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 B  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 B  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 B  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 B  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 B  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 B  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 B  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 C  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 C  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 C  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 C  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 C  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 C  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 C  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 C  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 C  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 C  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 C  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 C  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 C  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 C  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 C  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 C  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 C  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 C  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 C  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 C  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 C  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 C  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 C  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 D  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 D  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 D  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 D  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 D  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 D  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 D  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 D  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 D  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 D  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 D  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 D  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 D  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 D  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 D  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 D  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 D  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 D  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 D  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 D  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 D  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 D  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 D  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 E  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 E  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 E  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 E  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 E  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 E  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 E  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 E  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 E  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 E  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 E  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 E  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 E  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 E  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 E  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 E  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 E  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 E  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 E  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 E  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 E  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 E  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 E  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 E  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 F  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 F  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 F  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 F  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 F  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 F  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 F  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 F  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 F  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 F  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 F  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 F  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 F  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 F  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 F  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 F  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 F  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 F  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 F  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 F  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 F  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 F  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 F  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 F  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 G  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 G  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 G  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 G  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 G  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 G  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 G  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 G  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 G  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 G  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 G  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 G  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 G  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 G  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 G  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 G  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 G  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 G  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 G  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 G  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 G  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 G  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 G  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 G  307  MET ILE HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  307  MET THR ILE LYS ALA LEU ARG THR PRO GLU GLU ARG PHE          
SEQRES   2 H  307  SER VAL LEU PRO ALA PHE PRO TYR GLN PRO ASN TYR VAL          
SEQRES   3 H  307  ASP ASP LEU GLY GLY TYR GLU SER LEU ARG MET ALA TYR          
SEQRES   4 H  307  ILE ASP GLU GLY ASP LYS ASP SER GLU TYR THR PHE LEU          
SEQRES   5 H  307  CYS LEU HIS GLY GLU PRO THR TRP SER TYR LEU TYR ARG          
SEQRES   6 H  307  LYS MET ILE PRO VAL PHE THR ASP ALA GLY HIS ARG VAL          
SEQRES   7 H  307  VAL ALA PRO ASP LEU PHE GLY PHE GLY ARG SER ASP LYS          
SEQRES   8 H  307  PRO ILE GLU ASP SER VAL TYR ASN PHE GLU PHE HIS ARG          
SEQRES   9 H  307  ASN SER LEU ILE GLN LEU ILE GLU HIS LEU ASP LEU LYS          
SEQRES  10 H  307  ASN ILE VAL LEU VAL CYS GLN ASP TRP GLY GLY GLY LEU          
SEQRES  11 H  307  GLY LEU THR ILE PRO MET ASP MET GLN ASP ARG PHE LYS          
SEQRES  12 H  307  LYS LEU ILE VAL MET ASN THR THR ILE SER ASN GLY GLU          
SEQRES  13 H  307  PRO LEU ALA GLU ALA ALA VAL GLN TRP MET ALA PHE ASN          
SEQRES  14 H  307  GLU THR ILE SER GLU LEU PRO VAL ALA GLY LEU VAL ALA          
SEQRES  15 H  307  CYS ASP ALA GLY ALA ALA VAL ASN VAL MET ASP ALA LEU          
SEQRES  16 H  307  ALA TYR ASP ALA PRO PHE PRO ASN LYS ASN TYR LYS VAL          
SEQRES  17 H  307  GLY VAL LYS ARG PHE PRO GLN MET ILE PRO THR ASN ALA          
SEQRES  18 H  307  ASP ASP ASP ALA VAL LYS TYR GLY LEU ARG ALA ILE GLU          
SEQRES  19 H  307  PHE TRP SER ASN GLU TRP SER GLY GLU SER PHE MET ALA          
SEQRES  20 H  307  ILE GLY MET LYS ASP ALA VAL LEU GLY GLU ALA ALA MET          
SEQRES  21 H  307  MET GLN LEU LYS THR VAL ILE LYS GLY CYS PRO GLU PRO          
SEQRES  22 H  307  MET LYS ILE GLU GLU ALA GLY HIS PHE VAL GLN GLU TYR          
SEQRES  23 H  307  GLY VAL GLU VAL ALA GLU GLN ALA LEU ALA SER PHE THR          
SEQRES  24 H  307  MET ILE HIS HIS HIS HIS HIS HIS                              
HET     CL  A 401       1                                                       
HET     CL  B 401       1                                                       
HET     CL  C 401       1                                                       
HET     CL  C 402       1                                                       
HET     CL  C 403       1                                                       
HET     CL  D 401       1                                                       
HET     CL  E 401       1                                                       
HET     CL  E 402       1                                                       
HET     CL  F 401       1                                                       
HET     CL  F 402       1                                                       
HET     CL  F 403       1                                                       
HET     CL  F 404       1                                                       
HET     CL  F 405       1                                                       
HET     CL  F 406       1                                                       
HET     CL  G 401       1                                                       
HET     CL  G 402       1                                                       
HET     CL  G 403       1                                                       
HET     CL  H 401       1                                                       
HETNAM      CL CHLORIDE ION                                                     
FORMUL   9   CL    18(CL 1-)                                                    
FORMUL  27  HOH   *2008(H2 O)                                                   
HELIX    1 AA1 PRO A    9  SER A   14  5                                   6    
HELIX    2 AA2 TRP A   60  ARG A   65  5                                   6    
HELIX    3 AA3 MET A   67  ASP A   73  1                                   7    
HELIX    4 AA4 GLU A   94  TYR A   98  5                                   5    
HELIX    5 AA5 ASN A   99  LEU A  114  1                                  16    
HELIX    6 AA6 ASP A  125  LEU A  132  1                                   8    
HELIX    7 AA7 THR A  133  MET A  138  5                                   6    
HELIX    8 AA8 ALA A  159  GLU A  170  1                                  12    
HELIX    9 AA9 PRO A  176  GLY A  186  1                                  11    
HELIX   10 AB1 ALA A  187  VAL A  189  5                                   3    
HELIX   11 AB2 ASN A  190  ALA A  199  1                                  10    
HELIX   12 AB3 ASN A  203  TYR A  206  5                                   4    
HELIX   13 AB4 LYS A  207  MET A  216  1                                  10    
HELIX   14 AB5 ASP A  223  GLU A  239  1                                  17    
HELIX   15 AB6 GLY A  256  THR A  265  1                                  10    
HELIX   16 AB7 PHE A  282  GLU A  285  5                                   4    
HELIX   17 AB8 TYR A  286  PHE A  298  1                                  13    
HELIX   18 AB9 PRO B    9  SER B   14  5                                   6    
HELIX   19 AC1 TRP B   60  ARG B   65  5                                   6    
HELIX   20 AC2 MET B   67  ALA B   74  1                                   8    
HELIX   21 AC3 GLU B   94  TYR B   98  5                                   5    
HELIX   22 AC4 ASN B   99  LEU B  114  1                                  16    
HELIX   23 AC5 ASP B  125  LEU B  132  1                                   8    
HELIX   24 AC6 THR B  133  ASP B  140  5                                   8    
HELIX   25 AC7 ALA B  159  ILE B  172  1                                  14    
HELIX   26 AC8 PRO B  176  GLY B  186  1                                  11    
HELIX   27 AC9 ALA B  187  VAL B  189  5                                   3    
HELIX   28 AD1 ASN B  190  ALA B  199  1                                  10    
HELIX   29 AD2 ASN B  203  TYR B  206  5                                   4    
HELIX   30 AD3 LYS B  207  ILE B  217  1                                  11    
HELIX   31 AD4 ASP B  223  GLU B  239  1                                  17    
HELIX   32 AD5 GLY B  256  THR B  265  1                                  10    
HELIX   33 AD6 PHE B  282  GLU B  285  5                                   4    
HELIX   34 AD7 TYR B  286  PHE B  298  1                                  13    
HELIX   35 AD8 PRO C    9  SER C   14  5                                   6    
HELIX   36 AD9 TRP C   60  ARG C   65  5                                   6    
HELIX   37 AE1 MET C   67  ALA C   74  1                                   8    
HELIX   38 AE2 GLU C   94  TYR C   98  5                                   5    
HELIX   39 AE3 ASN C   99  LEU C  114  1                                  16    
HELIX   40 AE4 ASP C  125  LEU C  132  1                                   8    
HELIX   41 AE5 THR C  133  MET C  138  5                                   6    
HELIX   42 AE6 ALA C  159  ILE C  172  1                                  14    
HELIX   43 AE7 PRO C  176  GLY C  186  1                                  11    
HELIX   44 AE8 ALA C  187  VAL C  189  5                                   3    
HELIX   45 AE9 ASN C  190  ALA C  199  1                                  10    
HELIX   46 AF1 ASN C  203  TYR C  206  5                                   4    
HELIX   47 AF2 LYS C  207  ILE C  217  1                                  11    
HELIX   48 AF3 ASP C  223  GLU C  239  1                                  17    
HELIX   49 AF4 GLY C  256  THR C  265  1                                  10    
HELIX   50 AF5 PHE C  282  GLU C  285  5                                   4    
HELIX   51 AF6 TYR C  286  PHE C  298  1                                  13    
HELIX   52 AF7 PRO D    9  SER D   14  5                                   6    
HELIX   53 AF8 TRP D   60  ARG D   65  5                                   6    
HELIX   54 AF9 MET D   67  ALA D   74  1                                   8    
HELIX   55 AG1 GLU D   94  TYR D   98  5                                   5    
HELIX   56 AG2 ASN D   99  LEU D  114  1                                  16    
HELIX   57 AG3 ASP D  125  LEU D  132  1                                   8    
HELIX   58 AG4 THR D  133  ASP D  140  5                                   8    
HELIX   59 AG5 ALA D  159  ILE D  172  1                                  14    
HELIX   60 AG6 PRO D  176  GLY D  186  1                                  11    
HELIX   61 AG7 ALA D  187  VAL D  189  5                                   3    
HELIX   62 AG8 ASN D  190  ALA D  199  1                                  10    
HELIX   63 AG9 ASN D  203  TYR D  206  5                                   4    
HELIX   64 AH1 LYS D  207  ILE D  217  1                                  11    
HELIX   65 AH2 ASP D  223  GLU D  239  1                                  17    
HELIX   66 AH3 GLY D  256  THR D  265  1                                  10    
HELIX   67 AH4 PHE D  282  TYR D  286  5                                   5    
HELIX   68 AH5 GLY D  287  PHE D  298  1                                  12    
HELIX   69 AH6 PRO E    9  SER E   14  5                                   6    
HELIX   70 AH7 TRP E   60  ARG E   65  5                                   6    
HELIX   71 AH8 MET E   67  ALA E   74  1                                   8    
HELIX   72 AH9 GLU E   94  TYR E   98  5                                   5    
HELIX   73 AI1 ASN E   99  LEU E  114  1                                  16    
HELIX   74 AI2 ASP E  125  LEU E  132  1                                   8    
HELIX   75 AI3 THR E  133  ASP E  140  5                                   8    
HELIX   76 AI4 ALA E  159  ILE E  172  1                                  14    
HELIX   77 AI5 PRO E  176  GLY E  186  1                                  11    
HELIX   78 AI6 ALA E  187  VAL E  189  5                                   3    
HELIX   79 AI7 ASN E  190  ALA E  199  1                                  10    
HELIX   80 AI8 ASN E  203  TYR E  206  5                                   4    
HELIX   81 AI9 LYS E  207  ILE E  217  1                                  11    
HELIX   82 AJ1 ASP E  223  GLU E  239  1                                  17    
HELIX   83 AJ2 GLY E  256  THR E  265  1                                  10    
HELIX   84 AJ3 PHE E  282  GLU E  285  5                                   4    
HELIX   85 AJ4 TYR E  286  PHE E  298  1                                  13    
HELIX   86 AJ5 PRO F    9  SER F   14  5                                   6    
HELIX   87 AJ6 TRP F   60  ARG F   65  5                                   6    
HELIX   88 AJ7 MET F   67  ALA F   74  1                                   8    
HELIX   89 AJ8 GLU F   94  TYR F   98  5                                   5    
HELIX   90 AJ9 ASN F   99  ASP F  115  1                                  17    
HELIX   91 AK1 ASP F  125  LEU F  132  1                                   8    
HELIX   92 AK2 THR F  133  ASP F  140  5                                   8    
HELIX   93 AK3 ALA F  159  ILE F  172  1                                  14    
HELIX   94 AK4 PRO F  176  GLY F  186  1                                  11    
HELIX   95 AK5 ALA F  187  VAL F  189  5                                   3    
HELIX   96 AK6 ASN F  190  ALA F  199  1                                  10    
HELIX   97 AK7 ASN F  203  TYR F  206  5                                   4    
HELIX   98 AK8 LYS F  207  ILE F  217  1                                  11    
HELIX   99 AK9 ASP F  223  GLU F  239  1                                  17    
HELIX  100 AL1 GLY F  256  THR F  265  1                                  10    
HELIX  101 AL2 PHE F  282  TYR F  286  5                                   5    
HELIX  102 AL3 GLY F  287  PHE F  298  1                                  12    
HELIX  103 AL4 PRO G    9  SER G   14  5                                   6    
HELIX  104 AL5 TRP G   60  ARG G   65  5                                   6    
HELIX  105 AL6 MET G   67  ALA G   74  1                                   8    
HELIX  106 AL7 GLU G   94  TYR G   98  5                                   5    
HELIX  107 AL8 ASN G   99  ASP G  115  1                                  17    
HELIX  108 AL9 ASP G  125  LEU G  132  1                                   8    
HELIX  109 AM1 THR G  133  MET G  138  5                                   6    
HELIX  110 AM2 ALA G  159  ILE G  172  1                                  14    
HELIX  111 AM3 PRO G  176  GLY G  186  1                                  11    
HELIX  112 AM4 ALA G  187  VAL G  189  5                                   3    
HELIX  113 AM5 ASN G  190  ALA G  199  1                                  10    
HELIX  114 AM6 ASN G  203  TYR G  206  5                                   4    
HELIX  115 AM7 LYS G  207  MET G  216  1                                  10    
HELIX  116 AM8 ASP G  223  GLU G  239  1                                  17    
HELIX  117 AM9 GLY G  256  THR G  265  1                                  10    
HELIX  118 AN1 PHE G  282  TYR G  286  5                                   5    
HELIX  119 AN2 GLY G  287  PHE G  298  1                                  12    
HELIX  120 AN3 PRO H    9  SER H   14  5                                   6    
HELIX  121 AN4 TRP H   60  ARG H   65  5                                   6    
HELIX  122 AN5 MET H   67  ALA H   74  1                                   8    
HELIX  123 AN6 GLU H   94  TYR H   98  5                                   5    
HELIX  124 AN7 ASN H   99  LEU H  114  1                                  16    
HELIX  125 AN8 ASP H  125  LEU H  132  1                                   8    
HELIX  126 AN9 THR H  133  ASP H  140  5                                   8    
HELIX  127 AO1 ALA H  159  ILE H  172  1                                  14    
HELIX  128 AO2 PRO H  176  GLY H  186  1                                  11    
HELIX  129 AO3 ALA H  187  VAL H  189  5                                   3    
HELIX  130 AO4 ASN H  190  ALA H  199  1                                  10    
HELIX  131 AO5 ASN H  203  TYR H  206  5                                   4    
HELIX  132 AO6 LYS H  207  ILE H  217  1                                  11    
HELIX  133 AO7 ASP H  223  GLU H  239  1                                  17    
HELIX  134 AO8 GLY H  256  THR H  265  1                                  10    
HELIX  135 AO9 PHE H  282  GLU H  285  5                                   4    
HELIX  136 AP1 TYR H  286  PHE H  298  1                                  13    
SHEET    1 AA1 2 ALA A   5  LEU A   6  0                                        
SHEET    2 AA1 2 LYS A  91  PRO A  92 -1  O  LYS A  91   N  LEU A   6           
SHEET    1 AA2 8 ASN A  24  VAL A  26  0                                        
SHEET    2 AA2 8 MET A  37  GLU A  42 -1  O  TYR A  39   N  ASN A  24           
SHEET    3 AA2 8 ARG A  77  PRO A  81 -1  O  VAL A  78   N  GLU A  42           
SHEET    4 AA2 8 THR A  50  LEU A  54  1  N  PHE A  51   O  ARG A  77           
SHEET    5 AA2 8 ILE A 119  CYS A 123  1  O  VAL A 122   N  LEU A  52           
SHEET    6 AA2 8 PHE A 142  VAL A 147  1  O  ILE A 146   N  LEU A 121           
SHEET    7 AA2 8 GLU A 243  LYS A 251  1  O  PHE A 245   N  VAL A 147           
SHEET    8 AA2 8 MET A 274  GLY A 280  1  O  ILE A 276   N  ILE A 248           
SHEET    1 AA3 2 ALA B   5  LEU B   6  0                                        
SHEET    2 AA3 2 LYS B  91  PRO B  92 -1  O  LYS B  91   N  LEU B   6           
SHEET    1 AA4 8 ASN B  24  VAL B  26  0                                        
SHEET    2 AA4 8 MET B  37  GLU B  42 -1  O  TYR B  39   N  ASN B  24           
SHEET    3 AA4 8 ARG B  77  PRO B  81 -1  O  ALA B  80   N  ILE B  40           
SHEET    4 AA4 8 THR B  50  LEU B  54  1  N  PHE B  51   O  ARG B  77           
SHEET    5 AA4 8 ILE B 119  CYS B 123  1  O  VAL B 122   N  LEU B  52           
SHEET    6 AA4 8 PHE B 142  MET B 148  1  O  ILE B 146   N  LEU B 121           
SHEET    7 AA4 8 GLU B 243  LYS B 251  1  O  ALA B 247   N  VAL B 147           
SHEET    8 AA4 8 MET B 274  GLY B 280  1  O  ILE B 276   N  ILE B 248           
SHEET    1 AA5 2 ALA C   5  LEU C   6  0                                        
SHEET    2 AA5 2 LYS C  91  PRO C  92 -1  O  LYS C  91   N  LEU C   6           
SHEET    1 AA6 8 ASN C  24  VAL C  26  0                                        
SHEET    2 AA6 8 MET C  37  GLU C  42 -1  O  TYR C  39   N  ASN C  24           
SHEET    3 AA6 8 ARG C  77  PRO C  81 -1  O  VAL C  78   N  GLU C  42           
SHEET    4 AA6 8 THR C  50  LEU C  54  1  N  PHE C  51   O  ARG C  77           
SHEET    5 AA6 8 ILE C 119  CYS C 123  1  O  VAL C 122   N  LEU C  52           
SHEET    6 AA6 8 PHE C 142  VAL C 147  1  O  ILE C 146   N  LEU C 121           
SHEET    7 AA6 8 GLU C 243  LYS C 251  1  O  ALA C 247   N  VAL C 147           
SHEET    8 AA6 8 MET C 274  GLY C 280  1  O  ILE C 276   N  ILE C 248           
SHEET    1 AA7 2 ALA D   5  LEU D   6  0                                        
SHEET    2 AA7 2 LYS D  91  PRO D  92 -1  O  LYS D  91   N  LEU D   6           
SHEET    1 AA8 8 ASN D  24  VAL D  26  0                                        
SHEET    2 AA8 8 MET D  37  GLU D  42 -1  O  TYR D  39   N  ASN D  24           
SHEET    3 AA8 8 ARG D  77  PRO D  81 -1  O  VAL D  78   N  GLU D  42           
SHEET    4 AA8 8 THR D  50  LEU D  54  1  N  PHE D  51   O  ARG D  77           
SHEET    5 AA8 8 ILE D 119  CYS D 123  1  O  VAL D 122   N  LEU D  52           
SHEET    6 AA8 8 PHE D 142  MET D 148  1  O  ILE D 146   N  LEU D 121           
SHEET    7 AA8 8 GLU D 243  LYS D 251  1  O  PHE D 245   N  VAL D 147           
SHEET    8 AA8 8 MET D 274  GLY D 280  1  O  ILE D 276   N  ILE D 248           
SHEET    1 AA9 2 ALA E   5  LEU E   6  0                                        
SHEET    2 AA9 2 LYS E  91  PRO E  92 -1  O  LYS E  91   N  LEU E   6           
SHEET    1 AB1 8 ASN E  24  VAL E  26  0                                        
SHEET    2 AB1 8 MET E  37  GLU E  42 -1  O  TYR E  39   N  ASN E  24           
SHEET    3 AB1 8 ARG E  77  PRO E  81 -1  O  VAL E  78   N  GLU E  42           
SHEET    4 AB1 8 THR E  50  LEU E  54  1  N  PHE E  51   O  ARG E  77           
SHEET    5 AB1 8 ILE E 119  CYS E 123  1  O  VAL E 122   N  LEU E  52           
SHEET    6 AB1 8 PHE E 142  MET E 148  1  O  ILE E 146   N  LEU E 121           
SHEET    7 AB1 8 GLU E 243  LYS E 251  1  O  PHE E 245   N  VAL E 147           
SHEET    8 AB1 8 MET E 274  GLY E 280  1  O  ILE E 276   N  ILE E 248           
SHEET    1 AB2 2 ALA F   5  LEU F   6  0                                        
SHEET    2 AB2 2 LYS F  91  PRO F  92 -1  O  LYS F  91   N  LEU F   6           
SHEET    1 AB3 8 ASN F  24  VAL F  26  0                                        
SHEET    2 AB3 8 MET F  37  GLU F  42 -1  O  TYR F  39   N  ASN F  24           
SHEET    3 AB3 8 ARG F  77  PRO F  81 -1  O  VAL F  78   N  GLU F  42           
SHEET    4 AB3 8 THR F  50  LEU F  54  1  N  PHE F  51   O  ARG F  77           
SHEET    5 AB3 8 ILE F 119  CYS F 123  1  O  VAL F 122   N  LEU F  52           
SHEET    6 AB3 8 PHE F 142  MET F 148  1  O  ILE F 146   N  LEU F 121           
SHEET    7 AB3 8 GLU F 243  LYS F 251  1  O  PHE F 245   N  VAL F 147           
SHEET    8 AB3 8 MET F 274  GLY F 280  1  O  ILE F 276   N  ILE F 248           
SHEET    1 AB4 2 ALA G   5  LEU G   6  0                                        
SHEET    2 AB4 2 LYS G  91  PRO G  92 -1  O  LYS G  91   N  LEU G   6           
SHEET    1 AB5 8 ASN G  24  VAL G  26  0                                        
SHEET    2 AB5 8 MET G  37  GLU G  42 -1  O  TYR G  39   N  ASN G  24           
SHEET    3 AB5 8 ARG G  77  PRO G  81 -1  O  VAL G  78   N  GLU G  42           
SHEET    4 AB5 8 THR G  50  LEU G  54  1  N  PHE G  51   O  ARG G  77           
SHEET    5 AB5 8 ILE G 119  CYS G 123  1  O  VAL G 122   N  LEU G  52           
SHEET    6 AB5 8 PHE G 142  MET G 148  1  O  ILE G 146   N  LEU G 121           
SHEET    7 AB5 8 GLU G 243  LYS G 251  1  O  ALA G 247   N  VAL G 147           
SHEET    8 AB5 8 MET G 274  GLY G 280  1  O  ILE G 276   N  ILE G 248           
SHEET    1 AB6 2 ALA H   5  LEU H   6  0                                        
SHEET    2 AB6 2 LYS H  91  PRO H  92 -1  O  LYS H  91   N  LEU H   6           
SHEET    1 AB7 8 ASN H  24  VAL H  26  0                                        
SHEET    2 AB7 8 MET H  37  GLU H  42 -1  O  TYR H  39   N  ASN H  24           
SHEET    3 AB7 8 ARG H  77  PRO H  81 -1  O  VAL H  78   N  GLU H  42           
SHEET    4 AB7 8 THR H  50  LEU H  54  1  N  PHE H  51   O  ARG H  77           
SHEET    5 AB7 8 ILE H 119  CYS H 123  1  O  VAL H 122   N  LEU H  52           
SHEET    6 AB7 8 PHE H 142  MET H 148  1  O  ILE H 146   N  LEU H 121           
SHEET    7 AB7 8 GLU H 243  LYS H 251  1  O  PHE H 245   N  VAL H 147           
SHEET    8 AB7 8 MET H 274  GLY H 280  1  O  ILE H 276   N  ILE H 248           
CISPEP   1 GLU A   57    PRO A   58          0       -22.48                     
CISPEP   2 GLU B   57    PRO B   58          0       -20.84                     
CISPEP   3 GLU C   57    PRO C   58          0       -21.29                     
CISPEP   4 GLU D   57    PRO D   58          0       -22.44                     
CISPEP   5 GLU E   57    PRO E   58          0       -21.85                     
CISPEP   6 GLU F   57    PRO F   58          0       -22.01                     
CISPEP   7 GLU G   57    PRO G   58          0       -18.86                     
CISPEP   8 GLU H   57    PRO H   58          0       -21.16                     
SITE     1 AC1  6 GLU A  57  TRP A 126  TRP A 165  PHE A 213                    
SITE     2 AC1  6 PRO A 214  HOH A 596                                          
SITE     1 AC2  5 GLU B  57  TRP B 126  TRP B 165  PHE B 213                    
SITE     2 AC2  5 PRO B 214                                                     
SITE     1 AC3  5 GLU C  57  TRP C 126  TRP C 165  PRO C 214                    
SITE     2 AC3  5 HOH C 643                                                     
SITE     1 AC4  2 LEU C   6  ARG C   7                                          
SITE     1 AC5  6 ARG C   7  THR C   8  ARG C  88  SER C  89                    
SITE     2 AC5  6 LYS C  91  HOH C 650                                          
SITE     1 AC6  4 TRP D 126  TRP D 165  PHE D 213  PRO D 214                    
SITE     1 AC7  4 GLU E  57  TRP E 126  TRP E 165  PRO E 214                    
SITE     1 AC8  4 SER E  47  GLU E  48  GLY E  75  HOH E 534                    
SITE     1 AC9  5 HOH E 536  MET F 136  ASP F 137  MET F 138                    
SITE     2 AC9  5 GLN F 139                                                     
SITE     1 AD1  6 GLU F  57  TRP F 126  TRP F 165  PHE F 213                    
SITE     2 AD1  6 PRO F 214  HOH F 629                                          
SITE     1 AD2  6 SER F 153  ASN F 154  GLY F 155  PRO F 218                    
SITE     2 AD2  6 HOH F 541  HOH F 581                                          
SITE     1 AD3  2 PRO F 157  LEU F 158                                          
SITE     1 AD4  3 GLY F 186  ALA F 187  TYR F 286                               
SITE     1 AD5  2 GLU F 272  HOH H 637                                          
SITE     1 AD6  3 TRP G 126  TRP G 165  PRO G 214                               
SITE     1 AD7  3 LEU G   6  ARG G   7  HOH G 564                               
SITE     1 AD8  6 ARG G   7  THR G   8  ARG G  88  SER G  89                    
SITE     2 AD8  6 LYS G  91  HOH G 604                                          
SITE     1 AD9  6 GLU H  57  TRP H 126  TRP H 165  PHE H 213                    
SITE     2 AD9  6 PRO H 214  HOH H 567                                          
CRYST1  117.385  155.506  155.611  90.00  90.00  90.00 P 21 21 2    32          
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      0.008519  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006431  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006426        0.00000                         
TER    2356      ILE A 301                                                      
TER    4698      MET B 300                                                      
TER    7053      MET C 300                                                      
TER    9387      THR D 299                                                      
TER   11746      MET E 300                                                      
TER   14095      THR F 299                                                      
TER   16450      MET G 300                                                      
TER   18803      ILE H 301                                                      
MASTER      695    0   18  136   80    0   27    620771    8    0  192          
END                                                                             

Send your questions or comments to :
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.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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