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Database: PDB
Entry: 6QF7
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Original site: 6QF7 
HEADER    BLOOD CLOTTING                          09-JAN-19   6QF7              
TITLE     CRYSTAL STRUCTURES OF THE RECOMBINANT BETA-FACTOR XIIA PROTEASE WITH  
TITLE    2 BOUND THR-ARG AND PRO-ARG SUBSTRATE MIMETICS                         
CAVEAT     6QF7    NAG E 2 HAS WRONG CHIRALITY AT ATOM C1 NAG B 701 HAS WRONG   
CAVEAT   2 6QF7    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALTODEXTRIN-BINDING PROTEIN;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: COAGULATION FACTOR XII;                                    
COMPND   7 CHAIN: B, D;                                                         
COMPND   8 SYNONYM: HAGEMAN FACTOR,HAF;                                         
COMPND   9 EC: 3.4.21.38;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: MALE, NCTC8450_00456, NCTC9775_03059;                          
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 GENE: F12;                                                           
SOURCE  12 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 7227                                        
KEYWDS    COAGULATION FACTOR XII; SERINE PROTEASE; CRYSTAL STRUCTURE; INHIBITOR 
KEYWDS   2 COMPLEX, BLOOD CLOTTING                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.PATHAK,R.MANNAL,C.LI,G.K.BUBACARR,K.H.BADRALDIN,B.D.BELVISO,        
AUTHOR   2 R.B.CAMILA,I.DREVENY,P.M.FISCHER,L.V.DEKKER,M.L.V.OLIVA,J.EMSLEY     
REVDAT   4   29-JUL-20 6QF7    1       CAVEAT COMPND REMARK HET                 
REVDAT   4 2                   1       HETNAM FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   31-JUL-19 6QF7    1       REMARK                                   
REVDAT   2   26-JUN-19 6QF7    1       JRNL                                     
REVDAT   1   05-JUN-19 6QF7    0                                                
JRNL        AUTH   M.PATHAK,R.MANNA,C.LI,B.G.KAIRA,B.K.HAMAD,B.D.BELVISO,       
JRNL        AUTH 2 C.R.BONTURI,I.DREVENY,P.M.FISCHER,L.V.DEKKER,M.L.V.OLIVA,    
JRNL        AUTH 3 J.EMSLEY                                                     
JRNL        TITL   CRYSTAL STRUCTURES OF THE RECOMBINANT BETA-FACTOR XIIA       
JRNL        TITL 2 PROTEASE WITH BOUND THR-ARG AND PRO-ARG SUBSTRATE MIMETICS.  
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  75   578 2019              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   31205020                                                     
JRNL        DOI    10.1107/S2059798319006910                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 115.11                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 15371                          
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) : 0.303                           
REMARK   3   R VALUE            (WORKING SET) : 0.297                           
REMARK   3   FREE R VALUE                     : 0.356                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1708                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1134                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3680                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 126                          
REMARK   3   BIN FREE R VALUE                    : 0.4010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9347                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 148                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.10000                                              
REMARK   3    B22 (A**2) : 0.10000                                              
REMARK   3    B33 (A**2) : -0.20000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 1.191         
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      : 0.736                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.579                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9785 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8909 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13325 ; 1.471 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20732 ; 3.882 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1227 ; 6.055 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   414 ;38.088 ;24.807       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1510 ;20.252 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    38 ;22.300 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1467 ; 0.091 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10937 ; 0.016 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1943 ; 0.030 ; 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):  4914 ; 1.064 ; 3.913       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4914 ; 1.064 ; 3.913       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6127 ; 1.997 ; 5.862       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6128 ; 1.996 ; 5.861       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4871 ; 1.421 ; 3.887       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4872 ; 1.421 ; 3.887       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  7195 ; 1.519 ; 5.807       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10791 ; 4.006 ;44.826       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10792 ; 4.005 ;44.823       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : D B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     D    339       D     711      1                      
REMARK   3           1     B    339       B     711      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT THERMAL      1    D (A**2):   3521 ;  7.60 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 6QF7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-JAN-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292100057.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17015                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 115.110                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 2.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.6 WITH 10%    
REMARK 280  PEG 4000 AND 0.15 M MGCL2, EVAPORATION, TEMPERATURE 292K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      119.17500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       65.72500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       65.72500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.58750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       65.72500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       65.72500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      178.76250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       65.72500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.72500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.58750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       65.72500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.72500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      178.76250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      119.17500            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F                               
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     ALA A   370                                                      
REMARK 465     ALA A   371                                                      
REMARK 465     SER A   372                                                      
REMARK 465     ALA B   330                                                      
REMARK 465     ALA B   331                                                      
REMARK 465     ALA B   332                                                      
REMARK 465     ALA B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     GLU B   335                                                      
REMARK 465     PHE B   336                                                      
REMARK 465     GLY B   337                                                      
REMARK 465     PRO B   338                                                      
REMARK 465     LEU B   339                                                      
REMARK 465     ARG C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     ALA C   371                                                      
REMARK 465     SER C   372                                                      
REMARK 465     ALA D   329                                                      
REMARK 465     ALA D   330                                                      
REMARK 465     ALA D   331                                                      
REMARK 465     ALA D   332                                                      
REMARK 465     SER D   333                                                      
REMARK 465     GLU D   334                                                      
REMARK 465     PHE D   335                                                      
REMARK 465     GLY D   336                                                      
REMARK 465     PRO D   337                                                      
REMARK 465     LEU D   338                                                      
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     TYR B  372   CG   CD1  CD2                                       
REMARK 480     GLU D  494   CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN D   414     C1   NAG E     1              1.66            
REMARK 500   NH2  ARG B   426     OE2  GLU B   450              1.93            
REMARK 500   OG   SER B   544     C3   0G6 B   702              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ALA B 360   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    PRO B 469   C   -  N   -  CA  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    PHE B 499   CB  -  CA  -  C   ANGL. DEV. =  14.2 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    ASN A 100       64.47     65.92                                   
REMARK 500    ILE A 104       -6.82   -140.70                                   
REMARK 500    LYS A 142       21.19   -140.28                                   
REMARK 500    ALA A 146      -76.22    -69.66                                   
REMARK 500    ASN A 150      106.76    -51.19                                   
REMARK 500    ASP A 209     -161.69    -77.02                                   
REMARK 500    ASN A 218       -8.15    -57.20                                   
REMARK 500    ALA A 239       31.19     79.25                                   
REMARK 500    THR A 245     -166.75   -161.14                                   
REMARK 500    LYS A 256       78.95   -108.55                                   
REMARK 500    ASN A 272       47.45   -108.29                                   
REMARK 500    CYS B 341       47.68   -150.34                                   
REMARK 500    GLN B 343     -154.73   -123.68                                   
REMARK 500    LEU B 358     -163.09   -126.37                                   
REMARK 500    LEU B 361     -124.68     50.23                                   
REMARK 500    ARG B 362      172.70    177.70                                   
REMARK 500    ALA B 364       46.46   -108.03                                   
REMARK 500    HIS B 365       28.12   -151.85                                   
REMARK 500    PRO B 366       39.17    -87.14                                   
REMARK 500    LEU B 395       61.18   -101.75                                   
REMARK 500    ASP B 451     -166.47    -79.75                                   
REMARK 500    ALA B 452      -74.74    -39.53                                   
REMARK 500    ASP B 453      -11.35    -47.97                                   
REMARK 500    CYS B 456      -74.13    -74.20                                   
REMARK 500    PRO B 465     -173.96    -55.40                                   
REMARK 500    VAL B 466       90.45   -161.88                                   
REMARK 500    ARG B 474      128.49    -34.38                                   
REMARK 500    GLU B 491      124.55    -31.51                                   
REMARK 500    GLU B 495      144.69    174.08                                   
REMARK 500    ALA B 497     -161.13   -104.00                                   
REMARK 500    SER B 498      -68.39   -128.72                                   
REMARK 500    LEU B 500      130.42    -32.98                                   
REMARK 500    VAL B 518      -57.54   -142.04                                   
REMARK 500    HIS B 519       79.37   -151.42                                   
REMARK 500    SER B 521       24.14   -143.45                                   
REMARK 500    ALA B 530      119.29   -161.09                                   
REMARK 500    CYS B 540     -168.61   -122.57                                   
REMARK 500    PRO B 547      169.67    -45.71                                   
REMARK 500    ARG B 558      -74.30    -78.45                                   
REMARK 500    ALA B 581      -34.25    -34.59                                   
REMARK 500    TYR B 583       31.27    -94.19                                   
REMARK 500    ASP C  14       60.28   -113.41                                   
REMARK 500    PHE C  67      -47.44    -27.06                                   
REMARK 500    TRP C 158      -38.91    -32.44                                   
REMARK 500    ALA C 168      -70.83    -87.70                                   
REMARK 500    PRO C 229      -34.42    -39.40                                   
REMARK 500    LYS C 256       66.42   -119.27                                   
REMARK 500    SER C 270      122.43    -39.72                                   
REMARK 500    LYS C 313       41.92    -83.95                                   
REMARK 500    ARG D 362      177.41    -54.34                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG E    1                                                       
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)METHYL]    
REMARK 630 AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-PROLINAMIDE                   
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     0G6 B   702                                                      
REMARK 630     0G6 D   703                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    DPN PRO AR7 0QE                                          
REMARK 630 DETAILS: NULL                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6GT6   RELATED DB: PDB                                   
DBREF1 6QF7 A    0   367  UNP                  A0A376KDN7_ECOLX                 
DBREF2 6QF7 A     A0A376KDN7                         26         393             
DBREF  6QF7 B  334   593  UNP    P00748   FA12_HUMAN     352    615             
DBREF1 6QF7 C    0   367  UNP                  A0A376KDN7_ECOLX                 
DBREF2 6QF7 C     A0A376KDN7                         26         393             
DBREF  6QF7 D  333   593  UNP    P00748   FA12_HUMAN     352    615             
SEQADV 6QF7 ARG A   -1  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 SER A    0  UNP  A0A376KDN ALA    26 CONFLICT                       
SEQADV 6QF7 ALA A   82  UNP  A0A376KDN ASP   108 CONFLICT                       
SEQADV 6QF7 ALA A   83  UNP  A0A376KDN LYS   109 CONFLICT                       
SEQADV 6QF7 ALA A  172  UNP  A0A376KDN GLU   198 CONFLICT                       
SEQADV 6QF7 ALA A  173  UNP  A0A376KDN ASN   199 CONFLICT                       
SEQADV 6QF7 ALA A  239  UNP  A0A376KDN LYS   265 CONFLICT                       
SEQADV 6QF7 ALA A  362  UNP  A0A376KDN LYS   388 CONFLICT                       
SEQADV 6QF7 ALA A  363  UNP  A0A376KDN ASP   389 CONFLICT                       
SEQADV 6QF7 ASN A  367  UNP  A0A376KDN ARG   393 CONFLICT                       
SEQADV 6QF7 ALA A  368  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA A  369  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA A  370  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA A  371  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 SER A  372  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA B  330  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA B  331  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA B  332  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA B  333  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 SER B  334  UNP  P00748    THR   352 CONFLICT                       
SEQADV 6QF7 GLU B  335  UNP  P00748    ARG   353 CONFLICT                       
SEQADV 6QF7 PHE B  336  UNP  P00748    ASN   354 CONFLICT                       
SEQADV 6QF7     B       UNP  P00748    LEU   363 DELETION                       
SEQADV 6QF7     B       UNP  P00748    ARG   364 DELETION                       
SEQADV 6QF7     B       UNP  P00748    LYS   365 DELETION                       
SEQADV 6QF7     B       UNP  P00748    SER   366 DELETION                       
SEQADV 6QF7     B       UNP  P00748    LEU   367 DELETION                       
SEQADV 6QF7     B       UNP  P00748    SER   368 DELETION                       
SEQADV 6QF7     B       UNP  P00748    SER   369 DELETION                       
SEQADV 6QF7     B       UNP  P00748    MET   370 DELETION                       
SEQADV 6QF7     B       UNP  P00748    THR   371 DELETION                       
SEQADV 6QF7     B       UNP  P00748    ARG   372 DELETION                       
SEQADV 6QF7     B       UNP  P00748    GLN   572 DELETION                       
SEQADV 6QF7     B       UNP  P00748    ALA   573 DELETION                       
SEQADV 6QF7     B       UNP  P00748    ALA   574 DELETION                       
SEQADV 6QF7     B       UNP  P00748    GLU   575 DELETION                       
SEQADV 6QF7 ARG C   -1  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 SER C    0  UNP  A0A376KDN ALA    26 CONFLICT                       
SEQADV 6QF7 ALA C   82  UNP  A0A376KDN ASP   108 CONFLICT                       
SEQADV 6QF7 ALA C   83  UNP  A0A376KDN LYS   109 CONFLICT                       
SEQADV 6QF7 ALA C  172  UNP  A0A376KDN GLU   198 CONFLICT                       
SEQADV 6QF7 ALA C  173  UNP  A0A376KDN ASN   199 CONFLICT                       
SEQADV 6QF7 ALA C  239  UNP  A0A376KDN LYS   265 CONFLICT                       
SEQADV 6QF7 ALA C  362  UNP  A0A376KDN LYS   388 CONFLICT                       
SEQADV 6QF7 ALA C  363  UNP  A0A376KDN ASP   389 CONFLICT                       
SEQADV 6QF7 ASN C  367  UNP  A0A376KDN ARG   393 CONFLICT                       
SEQADV 6QF7 ALA C  368  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA C  369  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA C  370  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA C  371  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 SER C  372  UNP  A0A376KDN           EXPRESSION TAG                 
SEQADV 6QF7 ALA D  329  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA D  330  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA D  331  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 ALA D  332  UNP  P00748              EXPRESSION TAG                 
SEQADV 6QF7 SER D  333  UNP  P00748    THR   352 CONFLICT                       
SEQADV 6QF7 GLU D  334  UNP  P00748    ARG   353 CONFLICT                       
SEQADV 6QF7 PHE D  335  UNP  P00748    ASN   354 CONFLICT                       
SEQADV 6QF7     D       UNP  P00748    LEU   363 DELETION                       
SEQADV 6QF7     D       UNP  P00748    ARG   364 DELETION                       
SEQADV 6QF7     D       UNP  P00748    LYS   365 DELETION                       
SEQADV 6QF7     D       UNP  P00748    SER   366 DELETION                       
SEQADV 6QF7     D       UNP  P00748    LEU   367 DELETION                       
SEQADV 6QF7     D       UNP  P00748    SER   368 DELETION                       
SEQADV 6QF7     D       UNP  P00748    SER   369 DELETION                       
SEQADV 6QF7     D       UNP  P00748    MET   370 DELETION                       
SEQADV 6QF7     D       UNP  P00748    THR   371 DELETION                       
SEQADV 6QF7     D       UNP  P00748    ARG   372 DELETION                       
SEQADV 6QF7     D       UNP  P00748    GLN   572 DELETION                       
SEQADV 6QF7     D       UNP  P00748    ALA   573 DELETION                       
SEQADV 6QF7     D       UNP  P00748    ALA   574 DELETION                       
SEQADV 6QF7     D       UNP  P00748    GLU   575 DELETION                       
SEQRES   1 A  374  ARG SER LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE          
SEQRES   2 A  374  ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY          
SEQRES   3 A  374  LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL          
SEQRES   4 A  374  GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL          
SEQRES   5 A  374  ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA          
SEQRES   6 A  374  HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU          
SEQRES   7 A  374  ALA GLU ILE THR PRO ALA ALA ALA PHE GLN ASP LYS LEU          
SEQRES   8 A  374  TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS          
SEQRES   9 A  374  LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU          
SEQRES  10 A  374  ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR          
SEQRES  11 A  374  TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA          
SEQRES  12 A  374  LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO          
SEQRES  13 A  374  TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR          
SEQRES  14 A  374  ALA PHE LYS TYR ALA ALA GLY LYS TYR ASP ILE LYS ASP          
SEQRES  15 A  374  VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR          
SEQRES  16 A  374  PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA          
SEQRES  17 A  374  ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS          
SEQRES  18 A  374  GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP          
SEQRES  19 A  374  SER ASN ILE ASP THR SER ALA VAL ASN TYR GLY VAL THR          
SEQRES  20 A  374  VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE          
SEQRES  21 A  374  VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO          
SEQRES  22 A  374  ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU          
SEQRES  23 A  374  LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS          
SEQRES  24 A  374  PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU          
SEQRES  25 A  374  LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN          
SEQRES  26 A  374  ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET          
SEQRES  27 A  374  SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN          
SEQRES  28 A  374  ALA ALA SER GLY ARG GLN THR VAL ASP ALA ALA LEU ALA          
SEQRES  29 A  374  ALA ALA GLN THR ASN ALA ALA ALA ALA SER                      
SEQRES   1 B  254  ALA ALA ALA ALA SER GLU PHE GLY PRO LEU SER CYS GLY          
SEQRES   2 B  254  GLN ARG VAL VAL GLY GLY LEU VAL ALA LEU ARG GLY ALA          
SEQRES   3 B  254  HIS PRO TYR ILE ALA ALA LEU TYR TRP GLY HIS SER PHE          
SEQRES   4 B  254  CYS ALA GLY SER LEU ILE ALA PRO CYS TRP VAL LEU THR          
SEQRES   5 B  254  ALA ALA HIS CYS LEU GLN ASP ARG PRO ALA PRO GLU ASP          
SEQRES   6 B  254  LEU THR VAL VAL LEU GLY GLN GLU ARG ARG ASN HIS SER          
SEQRES   7 B  254  CYS GLU PRO CYS GLN THR LEU ALA VAL ARG SER TYR ARG          
SEQRES   8 B  254  LEU HIS GLU ALA PHE SER PRO VAL SER TYR GLN HIS ASP          
SEQRES   9 B  254  LEU ALA LEU LEU ARG LEU GLN GLU ASP ALA ASP GLY SER          
SEQRES  10 B  254  CYS ALA LEU LEU SER PRO TYR VAL GLN PRO VAL CYS LEU          
SEQRES  11 B  254  PRO SER GLY ALA ALA ARG PRO SER GLU THR THR LEU CYS          
SEQRES  12 B  254  GLN VAL ALA GLY TRP GLY HIS GLN PHE GLU GLY ALA GLU          
SEQRES  13 B  254  GLU TYR ALA SER PHE LEU GLN GLU ALA GLN VAL PRO PHE          
SEQRES  14 B  254  LEU SER LEU GLU ARG CYS SER ALA PRO ASP VAL HIS GLY          
SEQRES  15 B  254  SER SER ILE LEU PRO GLY MET LEU CYS ALA GLY PHE LEU          
SEQRES  16 B  254  GLU GLY GLY THR ASP ALA CYS GLN GLY ASP SER GLY GLY          
SEQRES  17 B  254  PRO LEU VAL CYS GLU ASP ARG ARG LEU THR LEU GLN GLY          
SEQRES  18 B  254  ILE ILE SER TRP GLY SER GLY CYS GLY ASP ARG ASN LYS          
SEQRES  19 B  254  PRO GLY VAL TYR THR ASP VAL ALA TYR TYR LEU ALA TRP          
SEQRES  20 B  254  ILE ARG GLU HIS THR VAL SER                                  
SEQRES   1 C  374  ARG SER LYS ILE GLU GLU GLY LYS LEU VAL ILE TRP ILE          
SEQRES   2 C  374  ASN GLY ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY          
SEQRES   3 C  374  LYS LYS PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL          
SEQRES   4 C  374  GLU HIS PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL          
SEQRES   5 C  374  ALA ALA THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA          
SEQRES   6 C  374  HIS ASP ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU          
SEQRES   7 C  374  ALA GLU ILE THR PRO ALA ALA ALA PHE GLN ASP LYS LEU          
SEQRES   8 C  374  TYR PRO PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS          
SEQRES   9 C  374  LEU ILE ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU          
SEQRES  10 C  374  ILE TYR ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR          
SEQRES  11 C  374  TRP GLU GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA          
SEQRES  12 C  374  LYS GLY LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO          
SEQRES  13 C  374  TYR PHE THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR          
SEQRES  14 C  374  ALA PHE LYS TYR ALA ALA GLY LYS TYR ASP ILE LYS ASP          
SEQRES  15 C  374  VAL GLY VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR          
SEQRES  16 C  374  PHE LEU VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA          
SEQRES  17 C  374  ASP THR ASP TYR SER ILE ALA GLU ALA ALA PHE ASN LYS          
SEQRES  18 C  374  GLY GLU THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP          
SEQRES  19 C  374  SER ASN ILE ASP THR SER ALA VAL ASN TYR GLY VAL THR          
SEQRES  20 C  374  VAL LEU PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE          
SEQRES  21 C  374  VAL GLY VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO          
SEQRES  22 C  374  ASN LYS GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU          
SEQRES  23 C  374  LEU THR ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS          
SEQRES  24 C  374  PRO LEU GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU          
SEQRES  25 C  374  LEU ALA LYS ASP PRO ARG ILE ALA ALA THR MET GLU ASN          
SEQRES  26 C  374  ALA GLN LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET          
SEQRES  27 C  374  SER ALA PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN          
SEQRES  28 C  374  ALA ALA SER GLY ARG GLN THR VAL ASP ALA ALA LEU ALA          
SEQRES  29 C  374  ALA ALA GLN THR ASN ALA ALA ALA ALA SER                      
SEQRES   1 D  254  ALA ALA ALA ALA SER GLU PHE GLY PRO LEU SER CYS GLY          
SEQRES   2 D  254  GLN ARG VAL VAL GLY GLY LEU VAL ALA LEU ARG GLY ALA          
SEQRES   3 D  254  HIS PRO TYR ILE ALA ALA LEU TYR TRP GLY HIS SER PHE          
SEQRES   4 D  254  CYS ALA GLY SER LEU ILE ALA PRO CYS TRP VAL LEU THR          
SEQRES   5 D  254  ALA ALA HIS CYS LEU GLN ASP ARG PRO ALA PRO GLU ASP          
SEQRES   6 D  254  LEU THR VAL VAL LEU GLY GLN GLU ARG ARG ASN HIS SER          
SEQRES   7 D  254  CYS GLU PRO CYS GLN THR LEU ALA VAL ARG SER TYR ARG          
SEQRES   8 D  254  LEU HIS GLU ALA PHE SER PRO VAL SER TYR GLN HIS ASP          
SEQRES   9 D  254  LEU ALA LEU LEU ARG LEU GLN GLU ASP ALA ASP GLY SER          
SEQRES  10 D  254  CYS ALA LEU LEU SER PRO TYR VAL GLN PRO VAL CYS LEU          
SEQRES  11 D  254  PRO SER GLY ALA ALA ARG PRO SER GLU THR THR LEU CYS          
SEQRES  12 D  254  GLN VAL ALA GLY TRP GLY HIS GLN PHE GLU GLY ALA GLU          
SEQRES  13 D  254  GLU TYR ALA SER PHE LEU GLN GLU ALA GLN VAL PRO PHE          
SEQRES  14 D  254  LEU SER LEU GLU ARG CYS SER ALA PRO ASP VAL HIS GLY          
SEQRES  15 D  254  SER SER ILE LEU PRO GLY MET LEU CYS ALA GLY PHE LEU          
SEQRES  16 D  254  GLU GLY GLY THR ASP ALA CYS GLN GLY ASP SER GLY GLY          
SEQRES  17 D  254  PRO LEU VAL CYS GLU ASP ARG ARG LEU THR LEU GLN GLY          
SEQRES  18 D  254  ILE ILE SER TRP GLY SER GLY CYS GLY ASP ARG ASN LYS          
SEQRES  19 D  254  PRO GLY VAL TYR THR ASP VAL ALA TYR TYR LEU ALA TRP          
SEQRES  20 D  254  ILE ARG GLU HIS THR VAL SER                                  
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    GLC  F   1      12                                                       
HET    GLC  F   2      11                                                       
HET    GLC  G   1      12                                                       
HET    GLC  G   2      11                                                       
HET    NAG  B 701      14                                                       
HET    0G6  B 702      30                                                       
HET    0G6  D 703      30                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     0G6 D-PHENYLALANYL-N-[(2S,3S)-6-{[AMINO(IMINIO)                      
HETNAM   2 0G6  METHYL]AMINO}-1-CHLORO-2-HYDROXYHEXAN-3-YL]-L-                  
HETNAM   3 0G6  PROLINAMIDE                                                     
HETSYN     0G6 PPACK                                                            
FORMUL   5  NAG    3(C8 H15 N O6)                                               
FORMUL   6  GLC    4(C6 H12 O6)                                                 
FORMUL   9  0G6    2(C21 H34 CL N6 O3 1+)                                       
HELIX    1 AA1 ASN A   18  THR A   31  1                                  14    
HELIX    2 AA2 LYS A   42  ALA A   51  1                                  10    
HELIX    3 AA3 ALA A   52  GLY A   54  5                                   3    
HELIX    4 AA4 ARG A   66  GLY A   74  1                                   9    
HELIX    5 AA5 ALA A   82  ASP A   87  1                                   6    
HELIX    6 AA6 LYS A   88  LEU A   89  5                                   2    
HELIX    7 AA7 TYR A   90  TRP A   94  5                                   5    
HELIX    8 AA8 GLU A  131  ALA A  141  1                                  11    
HELIX    9 AA9 GLU A  153  ASP A  164  1                                  12    
HELIX   10 AB1 ASN A  185  ASN A  201  1                                  17    
HELIX   11 AB2 ASP A  209  GLY A  220  1                                  12    
HELIX   12 AB3 GLY A  228  TRP A  230  5                                   3    
HELIX   13 AB4 ALA A  231  SER A  238  1                                   8    
HELIX   14 AB5 ASN A  272  TYR A  283  1                                  12    
HELIX   15 AB6 GLU A  288  LYS A  297  1                                  10    
HELIX   16 AB7 LEU A  304  GLU A  309  1                                   6    
HELIX   17 AB8 ASP A  314  GLY A  327  1                                  14    
HELIX   18 AB9 GLN A  335  GLY A  353  1                                  19    
HELIX   19 AC1 THR A  356  ALA A  368  1                                  13    
HELIX   20 AC2 ALA B  392  ASP B  397  5                                   6    
HELIX   21 AC3 SER B  509  SER B  514  1                                   6    
HELIX   22 AC4 VAL B  580  TYR B  582  5                                   3    
HELIX   23 AC5 TYR B  583  THR B  591  1                                   9    
HELIX   24 AC6 GLY C   16  GLY C   32  1                                  17    
HELIX   25 AC7 LYS C   42  ALA C   51  1                                  10    
HELIX   26 AC8 ARG C   66  GLY C   74  1                                   9    
HELIX   27 AC9 TYR C   90  ARG C   98  1                                   9    
HELIX   28 AD1 GLU C  131  LYS C  140  1                                  10    
HELIX   29 AD2 GLU C  153  ALA C  163  1                                  11    
HELIX   30 AD3 ASN C  185  ASN C  201  1                                  17    
HELIX   31 AD4 ASP C  209  LYS C  219  1                                  11    
HELIX   32 AD5 GLY C  228  TRP C  230  5                                   3    
HELIX   33 AD6 ALA C  231  SER C  238  1                                   8    
HELIX   34 AD7 ASN C  272  GLU C  281  1                                  10    
HELIX   35 AD8 GLU C  288  LYS C  297  1                                  10    
HELIX   36 AD9 LEU C  304  GLU C  309  1                                   6    
HELIX   37 AE1 ARG C  316  GLY C  327  1                                  12    
HELIX   38 AE2 PRO C  334  SER C  352  1                                  19    
HELIX   39 AE3 THR C  356  ALA C  369  1                                  14    
HELIX   40 AE4 ALA D  392  ASP D  397  5                                   6    
HELIX   41 AE5 ASP D  451  SER D  455  5                                   5    
HELIX   42 AE6 SER D  509  SER D  514  1                                   6    
HELIX   43 AE7 VAL D  580  TYR D  582  5                                   3    
HELIX   44 AE8 TYR D  583  THR D  591  1                                   9    
SHEET    1 AA1 6 VAL A  35  GLU A  38  0                                        
SHEET    2 AA1 6 LEU A   7  TRP A  10  1  N  ILE A   9   O  THR A  36           
SHEET    3 AA1 6 ILE A  59  ALA A  63  1  O  ILE A  59   N  TRP A  10           
SHEET    4 AA1 6 VAL A 261  ILE A 266 -1  O  SER A 263   N  TRP A  62           
SHEET    5 AA1 6 TYR A 106  VAL A 110 -1  N  TYR A 106   O  ALA A 264           
SHEET    6 AA1 6 ALA A 301  VAL A 302 -1  O  ALA A 301   N  VAL A 110           
SHEET    1 AA2 4 SER A 145  LEU A 147  0                                        
SHEET    2 AA2 4 THR A 222  ASN A 227  1  O  ALA A 223   N  SER A 145           
SHEET    3 AA2 4 SER A 114  ASN A 118 -1  N  ASN A 118   O  ALA A 223           
SHEET    4 AA2 4 TYR A 242  THR A 245 -1  O  THR A 245   N  LEU A 115           
SHEET    1 AA3 2 TYR A 167  LYS A 170  0                                        
SHEET    2 AA3 2 ASP A 177  GLY A 182 -1  O  ASP A 177   N  LYS A 170           
SHEET    1 AA4 2 PHE A 258  VAL A 259  0                                        
SHEET    2 AA4 2 GLU A 328  ILE A 329  1  O  GLU A 328   N  VAL A 259           
SHEET    1 AA5 8 LEU B 358  VAL B 359  0                                        
SHEET    2 AA5 8 GLN B 501  LEU B 508 -1  O  GLU B 502   N  LEU B 358           
SHEET    3 AA5 8 LEU B 528  ALA B 530 -1  O  CYS B 529   N  LEU B 508           
SHEET    4 AA5 8 LYS B 573  THR B 578 -1  O  TYR B 577   N  LEU B 528           
SHEET    5 AA5 8 LEU B 559  ASP B 570 -1  N  TRP B 564   O  VAL B 576           
SHEET    6 AA5 8 PRO B 547  GLU B 551 -1  N  CYS B 550   O  THR B 560           
SHEET    7 AA5 8 LEU B 480  GLY B 485 -1  N  GLN B 482   O  VAL B 549           
SHEET    8 AA5 8 GLN B 501  LEU B 508 -1  O  GLN B 501   N  GLY B 485           
SHEET    1 AA6 7 SER B 376  ALA B 379  0                                        
SHEET    2 AA6 7 ALA B 369  TRP B 373 -1  N  LEU B 371   O  CYS B 378           
SHEET    3 AA6 7 THR B 405  LEU B 408 -1  O  VAL B 407   N  ALA B 370           
SHEET    4 AA6 7 LEU B 423  LEU B 430 -1  O  LEU B 423   N  VAL B 406           
SHEET    5 AA6 7 ALA B 444  LEU B 448 -1  O  LEU B 445   N  ARG B 429           
SHEET    6 AA6 7 TRP B 387  THR B 390 -1  N  THR B 390   O  ALA B 444           
SHEET    7 AA6 7 LEU B 382  ALA B 384 -1  N  ILE B 383   O  TRP B 387           
SHEET    1 AA7 5 VAL C  35  GLU C  38  0                                        
SHEET    2 AA7 5 LEU C   7  TRP C  10  1  N  ILE C   9   O  GLU C  38           
SHEET    3 AA7 5 ILE C  59  ALA C  63  1  O  PHE C  61   N  TRP C  10           
SHEET    4 AA7 5 LEU C 262  ILE C 266 -1  O  SER C 263   N  TRP C  62           
SHEET    5 AA7 5 TYR C 106  PRO C 107 -1  N  TYR C 106   O  ALA C 264           
SHEET    1 AA8 2 ALA C 109  VAL C 110  0                                        
SHEET    2 AA8 2 ALA C 301  VAL C 302 -1  O  ALA C 301   N  VAL C 110           
SHEET    1 AA9 3 MET C 224  ASN C 227  0                                        
SHEET    2 AA9 3 SER C 114  ASN C 118 -1  N  SER C 114   O  ASN C 227           
SHEET    3 AA9 3 TYR C 242  THR C 245 -1  O  GLY C 243   N  TYR C 117           
SHEET    1 AB1 2 LYS C 170  ALA C 172  0                                        
SHEET    2 AB1 2 LYS C 175  ASP C 177 -1  O  ASP C 177   N  LYS C 170           
SHEET    1 AB2 2 PHE C 258  VAL C 259  0                                        
SHEET    2 AB2 2 GLU C 328  ILE C 329  1  O  GLU C 328   N  VAL C 259           
SHEET    1 AB3 8 LEU D 358  VAL D 359  0                                        
SHEET    2 AB3 8 GLN D 501  LEU D 508 -1  O  GLU D 502   N  LEU D 358           
SHEET    3 AB3 8 LEU D 528  ALA D 530 -1  O  CYS D 529   N  LEU D 508           
SHEET    4 AB3 8 LYS D 573  THR D 578 -1  O  TYR D 577   N  LEU D 528           
SHEET    5 AB3 8 LEU D 559  ASP D 570 -1  N  TRP D 564   O  VAL D 576           
SHEET    6 AB3 8 PRO D 547  GLU D 551 -1  N  LEU D 548   O  GLY D 561B          
SHEET    7 AB3 8 LEU D 480  GLY D 485 -1  N  LEU D 480   O  GLU D 551           
SHEET    8 AB3 8 GLN D 501  LEU D 508 -1  O  GLN D 501   N  GLY D 485           
SHEET    1 AB4 7 SER D 376  ALA D 379  0                                        
SHEET    2 AB4 7 ALA D 369  TRP D 373 -1  N  TRP D 373   O  SER D 376           
SHEET    3 AB4 7 THR D 405  LEU D 408 -1  O  VAL D 407   N  ALA D 370           
SHEET    4 AB4 7 LEU D 423  LEU D 430 -1  O  LEU D 423   N  VAL D 406           
SHEET    5 AB4 7 ALA D 444  LEU D 448 -1  O  LEU D 445   N  ARG D 429           
SHEET    6 AB4 7 TRP D 387  THR D 390 -1  N  THR D 390   O  ALA D 444           
SHEET    7 AB4 7 LEU D 382  ALA D 384 -1  N  ILE D 383   O  TRP D 387           
SSBOND   1 CYS B  341    CYS B  467                          1555   1555  1.83  
SSBOND   2 CYS B  378    CYS B  394                          1555   1555  2.03  
SSBOND   3 CYS B  386    CYS B  456                          1555   1555  2.03  
SSBOND   4 CYS B  417    CYS B  420                          1555   1555  2.05  
SSBOND   5 CYS B  481    CYS B  550                          1555   1555  2.12  
SSBOND   6 CYS B  513    CYS B  529                          1555   1555  2.03  
SSBOND   7 CYS B  540    CYS B  568                          1555   1555  2.03  
SSBOND   8 CYS D  340    CYS D  467                          1555   1555  2.06  
SSBOND   9 CYS D  378    CYS D  394                          1555   1555  2.03  
SSBOND  10 CYS D  386    CYS D  456                          1555   1555  2.04  
SSBOND  11 CYS D  417    CYS D  420                          1555   1555  2.04  
SSBOND  12 CYS D  481    CYS D  550                          1555   1555  2.04  
SSBOND  13 CYS D  513    CYS D  529                          1555   1555  2.04  
SSBOND  14 CYS D  540    CYS D  568                          1555   1555  2.03  
LINK         NE2 HIS B 393                 C3  0G6 B 702     1555   1555  1.52  
LINK         ND2 ASN B 414                 C1  NAG B 701     1555   1555  1.44  
LINK         OG  SER B 544                 C2  0G6 B 702     1555   1555  1.53  
LINK         NE2 HIS D 393                 C3  0G6 D 703     1555   1555  1.43  
LINK         OG  SER D 544                 C2  0G6 D 703     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.43  
LINK         O4  GLC F   1                 C1  GLC F   2     1555   1555  1.43  
LINK         O4  GLC G   1                 C1  GLC G   2     1555   1555  1.43  
CRYST1  131.450  131.450  238.350  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007607  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007607  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004196        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.341905  0.939444 -0.023348      -54.94065    1                    
MTRIX2   2  0.938833 -0.342560 -0.035295       98.26934    1                    
MTRIX3   2 -0.041156 -0.009852 -0.999104      578.46246    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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