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Database: PDB
Entry: 3Q1K
LinkDB: 3Q1K
Original site: 3Q1K 
HEADER    LIGASE                                  17-DEC-10   3Q1K              
TITLE     THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A FROM       
TITLE    2 SALMONELLA ENTERICA TYPHIMURIUM COMPLEXED WITH ADP                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE A;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE A, D-ALANYLALANINE SYNTHETASE A;         
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR     
SOURCE   3 TYPHIMURIUM;                                                         
SOURCE   4 ORGANISM_TAXID: 90371;                                               
SOURCE   5 STRAIN: LT2;                                                         
SOURCE   6 GENE: DDL, DDLA, STM0380;                                            
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21MAGIC;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG19C                                  
KEYWDS    STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   2 DISEASES, CSGID, ALPHA BETA SANDWICH, CYTOSOL, LIGASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK,CENTER FOR      
AUTHOR   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)                   
REVDAT   1   12-JAN-11 3Q1K    0                                                
JRNL        AUTH   R.ZHANG,N.MALTSEVA,L.PAPAZISI,W.ANDERSON,A.JOACHIMIAK,       
JRNL        AUTH 2 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 3 (CSGID)                                                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE D-ALANYL-ALANINE SYNTHETASE A   
JRNL        TITL 2 FROM SALMONELLA ENTERICA TYPHIMURIUM COMPLEXED WITH ADP      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.4_486)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 86401                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4332                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.5478 -  4.7418    1.00     8589   453  0.1671 0.1937        
REMARK   3     2  4.7418 -  3.7642    1.00     8313   461  0.1373 0.1717        
REMARK   3     3  3.7642 -  3.2885    1.00     8243   412  0.1846 0.2124        
REMARK   3     4  3.2885 -  2.9879    1.00     8231   436  0.1995 0.2588        
REMARK   3     5  2.9879 -  2.7737    1.00     8165   412  0.1978 0.2782        
REMARK   3     6  2.7737 -  2.6102    1.00     8196   398  0.1866 0.2646        
REMARK   3     7  2.6102 -  2.4795    1.00     8102   465  0.1863 0.2553        
REMARK   3     8  2.4795 -  2.3716    1.00     8092   424  0.1894 0.2556        
REMARK   3     9  2.3716 -  2.2803    1.00     8129   431  0.2052 0.2708        
REMARK   3    10  2.2803 -  2.2016    0.99     8009   440  0.2217 0.2940        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 42.05                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.76840                                             
REMARK   3    B22 (A**2) : -0.34450                                             
REMARK   3    B33 (A**2) : 4.11290                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010          11080                                  
REMARK   3   ANGLE     :  1.274          15084                                  
REMARK   3   CHIRALITY :  0.083           1758                                  
REMARK   3   PLANARITY :  0.006           1975                                  
REMARK   3   DIHEDRAL  : 17.727           4036                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  44.0114  26.5054  49.0764              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2707 T22:   0.1289                                     
REMARK   3      T33:   0.1965 T12:  -0.0092                                     
REMARK   3      T13:   0.0620 T23:   0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6308 L22:   0.7241                                     
REMARK   3      L33:   1.0930 L12:   0.2758                                     
REMARK   3      L13:  -0.2423 L23:  -0.7609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0542 S12:  -0.0045 S13:  -0.0690                       
REMARK   3      S21:  -0.0704 S22:   0.0971 S23:   0.0545                       
REMARK   3      S31:   0.2053 S32:  -0.0372 S33:  -0.0022                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  62.9416  43.6485  36.7297              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2105 T22:   0.1760                                     
REMARK   3      T33:   0.2130 T12:  -0.0292                                     
REMARK   3      T13:   0.0469 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5030 L22:   0.1737                                     
REMARK   3      L33:   0.5381 L12:   0.1167                                     
REMARK   3      L13:   0.3700 L23:  -0.0874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0895 S12:   0.1349 S13:   0.2229                       
REMARK   3      S21:  -0.0224 S22:   0.0673 S23:   0.0269                       
REMARK   3      S31:   0.0344 S32:   0.1024 S33:   0.0423                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  92.2790  34.3914   2.7117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2295 T22:   0.2337                                     
REMARK   3      T33:   0.2732 T12:   0.0161                                     
REMARK   3      T13:   0.0225 T23:  -0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7424 L22:   0.4704                                     
REMARK   3      L33:   1.1184 L12:   0.0557                                     
REMARK   3      L13:  -0.5724 L23:  -0.1150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0410 S12:   0.0593 S13:  -0.1330                       
REMARK   3      S21:  -0.0826 S22:  -0.1190 S23:   0.0632                       
REMARK   3      S31:   0.1731 S32:  -0.1083 S33:   0.1474                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 108.4227  57.3503   5.5026              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1479 T22:   0.2740                                     
REMARK   3      T33:   0.3148 T12:   0.0295                                     
REMARK   3      T13:   0.0206 T23:   0.0740                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5320 L22:   0.5888                                     
REMARK   3      L33:   0.5392 L12:   0.4628                                     
REMARK   3      L13:  -0.1272 L23:  -0.2049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:   0.0658 S13:   0.2103                       
REMARK   3      S21:  -0.0170 S22:  -0.1134 S23:  -0.0024                       
REMARK   3      S31:  -0.0114 S32:   0.1043 S33:   0.0450                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3Q1K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063078.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-DEC-08                          
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               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86501                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.79900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000, MOLREP                                      
REMARK 200 STARTING MODEL: PDBID 3I12                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000, PH 7.5, VAPOR DIFFUSION,    
REMARK 280  SITTING DROP, TEMPERATURE 289K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       42.57650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.44650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.90650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.44650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       42.57650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.90650            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6670 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     TYR A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     TYR A   256                                                      
REMARK 465     ASP A   257                                                      
REMARK 465     THR A   258                                                      
REMARK 465     MSE A   364                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     SER B   251                                                      
REMARK 465     GLU B   252                                                      
REMARK 465     PHE B   253                                                      
REMARK 465     TYR B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     TYR B   256                                                      
REMARK 465     ASP B   257                                                      
REMARK 465     THR B   258                                                      
REMARK 465     LYS B   259                                                      
REMARK 465     TYR B   260                                                      
REMARK 465     ILE B   261                                                      
REMARK 465     ASP B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     ASN B   264                                                      
REMARK 465     GLY B   265                                                      
REMARK 465     MSE B   364                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     ASN C    -1                                                      
REMARK 465     ALA C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     ASN C   250                                                      
REMARK 465     SER C   251                                                      
REMARK 465     GLU C   252                                                      
REMARK 465     PHE C   253                                                      
REMARK 465     TYR C   254                                                      
REMARK 465     ALA C   255                                                      
REMARK 465     TYR C   256                                                      
REMARK 465     ASP C   257                                                      
REMARK 465     THR C   258                                                      
REMARK 465     LYS C   259                                                      
REMARK 465     TYR C   260                                                      
REMARK 465     ILE C   261                                                      
REMARK 465     ASP C   262                                                      
REMARK 465     ASP C   263                                                      
REMARK 465     ASN C   264                                                      
REMARK 465     GLY C   265                                                      
REMARK 465     ALA C   266                                                      
REMARK 465     GLN C   267                                                      
REMARK 465     SER D    -2                                                      
REMARK 465     ASN D    -1                                                      
REMARK 465     ALA D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     TYR D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     TYR D   256                                                      
REMARK 465     ASP D   257                                                      
REMARK 465     THR D   258                                                      
REMARK 465     LYS D   259                                                      
REMARK 465     MSE D   364                                                      
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   CE   LYS A    33     O    HOH A   435              2.14            
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    ILE A 105       30.55   -141.35                                   
REMARK 500    LEU A 110      -56.83     73.23                                   
REMARK 500    SER A 192        0.54     80.09                                   
REMARK 500    ASN A 236      -82.98   -111.90                                   
REMARK 500    ASP B  32       95.94    -67.87                                   
REMARK 500    ASN B  56       78.68   -157.75                                   
REMARK 500    HIS B  66      -16.48     98.50                                   
REMARK 500    ILE B 105       25.93   -142.14                                   
REMARK 500    LEU B 110      -54.64     74.79                                   
REMARK 500    ASN B 236      -95.57   -111.31                                   
REMARK 500    ASN B 324       -5.75    -59.44                                   
REMARK 500    ASN C  56       86.92   -162.94                                   
REMARK 500    HIS C  66        0.10     91.32                                   
REMARK 500    ASN C  92       -1.26   -147.17                                   
REMARK 500    THR C 109      -74.26    -90.75                                   
REMARK 500    SER C 192        5.96     81.86                                   
REMARK 500    ASN C 236      -95.51   -110.50                                   
REMARK 500    ALA C 299      147.68   -170.66                                   
REMARK 500    LEU D  41       79.64   -104.49                                   
REMARK 500    ASN D  56       80.61   -156.80                                   
REMARK 500    HIS D  66       -9.26     77.62                                   
REMARK 500    ILE D 105       28.13   -142.19                                   
REMARK 500    LEU D 110      -60.18     74.26                                   
REMARK 500    SER D 191        5.47     84.10                                   
REMARK 500    ASN D 236      -79.31   -112.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 458        DISTANCE =  5.00 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 372  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP D 370   O1B                                                    
REMARK 620 2 ADP D 370   O1A  75.4                                              
REMARK 620 3 GLU D 315   OE1  91.0  93.9                                        
REMARK 620 4 HOH D 470   O    96.0  91.1 172.2                                  
REMARK 620 5 HOH D 472   O   164.4  89.1  87.7  86.4                            
REMARK 620 6 HOH D 471   O   111.6 168.2  95.4  79.0  84.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 372  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 370   O1B                                                    
REMARK 620 2 ADP A 370   O1A  76.0                                              
REMARK 620 3 GLU A 315   OE2  85.2  60.8                                        
REMARK 620 4 HOH A 494   O    89.0  81.8 142.5                                  
REMARK 620 5 HOH A 495   O   162.6  86.7  87.9  86.8                            
REMARK 620 6 HOH A 493   O   102.5 178.2 118.2  99.3  94.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 371  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 370   O1A                                                    
REMARK 620 2 GLU B 315   OE1 109.2                                              
REMARK 620 3 ADP B 370   O3B  66.8  76.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 372                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 371                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 373                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 374                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 375                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 376                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 372                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3I12   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITHOUT LIGAND                                          
REMARK 900 RELATED ID: IDP00919   RELATED DB: TARGETDB                          
DBREF  3Q1K A    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3Q1K B    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3Q1K C    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
DBREF  3Q1K D    1   364  UNP    P0A1F0   DDLA_SALTY       1    364             
SEQADV 3Q1K SER A   -2  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ASN A   -1  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ALA A    0  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K SER B   -2  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ASN B   -1  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ALA B    0  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K SER C   -2  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ASN C   -1  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ALA C    0  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K SER D   -2  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ASN D   -1  UNP  P0A1F0              EXPRESSION TAG                 
SEQADV 3Q1K ALA D    0  UNP  P0A1F0              EXPRESSION TAG                 
SEQRES   1 A  367  SER ASN ALA MSE ALA LYS LEU ARG VAL GLY ILE VAL PHE          
SEQRES   2 A  367  GLY GLY LYS SER ALA GLU HIS GLU VAL SER LEU GLN SER          
SEQRES   3 A  367  ALA LYS ASN ILE VAL ASP ALA ILE ASP LYS THR ARG PHE          
SEQRES   4 A  367  ASP VAL VAL LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP          
SEQRES   5 A  367  HIS VAL ASN ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP          
SEQRES   6 A  367  ASP PRO ALA HIS ILE ALA LEU ARG PRO SER ALA ILE SER          
SEQRES   7 A  367  LEU ALA GLN VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE          
SEQRES   8 A  367  ASN ALA GLN ASN GLY GLN PRO LEU PRO THR VAL ASP VAL          
SEQRES   9 A  367  ILE PHE PRO ILE VAL HIS GLY THR LEU GLY GLU ASP GLY          
SEQRES  10 A  367  SER LEU GLN GLY MSE LEU ARG VAL ALA ASN LEU PRO PHE          
SEQRES  11 A  367  VAL GLY SER ASP VAL LEU SER SER ALA ALA CYS MSE ASP          
SEQRES  12 A  367  LYS ASP VAL ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU          
SEQRES  13 A  367  ASN ILE ALA PRO PHE ILE THR LEU THR ARG THR ASN ARG          
SEQRES  14 A  367  HIS ALA PHE SER PHE ALA GLU VAL GLU SER ARG LEU GLY          
SEQRES  15 A  367  LEU PRO LEU PHE VAL LYS PRO ALA ASN GLN GLY SER SER          
SEQRES  16 A  367  VAL GLY VAL SER LYS VAL ALA ASN GLU ALA GLN TYR GLN          
SEQRES  17 A  367  GLN ALA VAL ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL          
SEQRES  18 A  367  VAL VAL GLU GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS          
SEQRES  19 A  367  ALA VAL LEU GLY ASN ASP ASN PRO GLN ALA SER THR CYS          
SEQRES  20 A  367  GLY GLU ILE VAL LEU ASN SER GLU PHE TYR ALA TYR ASP          
SEQRES  21 A  367  THR LYS TYR ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL          
SEQRES  22 A  367  PRO ALA GLN ILE PRO SER GLU VAL ASN ASP LYS ILE ARG          
SEQRES  23 A  367  ALA ILE ALA ILE GLN ALA TYR GLN THR LEU GLY CYS ALA          
SEQRES  24 A  367  GLY MSE ALA ARG VAL ASP VAL PHE LEU THR ALA ASP ASN          
SEQRES  25 A  367  GLU VAL VAL ILE ASN GLU ILE ASN THR LEU PRO GLY PHE          
SEQRES  26 A  367  THR ASN ILE SER MSE TYR PRO LYS LEU TRP GLN ALA SER          
SEQRES  27 A  367  GLY LEU GLY TYR THR ASP LEU ILE SER ARG LEU ILE GLU          
SEQRES  28 A  367  LEU ALA LEU GLU ARG HIS THR ALA ASN ASN ALA LEU LYS          
SEQRES  29 A  367  THR THR MSE                                                  
SEQRES   1 B  367  SER ASN ALA MSE ALA LYS LEU ARG VAL GLY ILE VAL PHE          
SEQRES   2 B  367  GLY GLY LYS SER ALA GLU HIS GLU VAL SER LEU GLN SER          
SEQRES   3 B  367  ALA LYS ASN ILE VAL ASP ALA ILE ASP LYS THR ARG PHE          
SEQRES   4 B  367  ASP VAL VAL LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP          
SEQRES   5 B  367  HIS VAL ASN ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP          
SEQRES   6 B  367  ASP PRO ALA HIS ILE ALA LEU ARG PRO SER ALA ILE SER          
SEQRES   7 B  367  LEU ALA GLN VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE          
SEQRES   8 B  367  ASN ALA GLN ASN GLY GLN PRO LEU PRO THR VAL ASP VAL          
SEQRES   9 B  367  ILE PHE PRO ILE VAL HIS GLY THR LEU GLY GLU ASP GLY          
SEQRES  10 B  367  SER LEU GLN GLY MSE LEU ARG VAL ALA ASN LEU PRO PHE          
SEQRES  11 B  367  VAL GLY SER ASP VAL LEU SER SER ALA ALA CYS MSE ASP          
SEQRES  12 B  367  LYS ASP VAL ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU          
SEQRES  13 B  367  ASN ILE ALA PRO PHE ILE THR LEU THR ARG THR ASN ARG          
SEQRES  14 B  367  HIS ALA PHE SER PHE ALA GLU VAL GLU SER ARG LEU GLY          
SEQRES  15 B  367  LEU PRO LEU PHE VAL LYS PRO ALA ASN GLN GLY SER SER          
SEQRES  16 B  367  VAL GLY VAL SER LYS VAL ALA ASN GLU ALA GLN TYR GLN          
SEQRES  17 B  367  GLN ALA VAL ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL          
SEQRES  18 B  367  VAL VAL GLU GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS          
SEQRES  19 B  367  ALA VAL LEU GLY ASN ASP ASN PRO GLN ALA SER THR CYS          
SEQRES  20 B  367  GLY GLU ILE VAL LEU ASN SER GLU PHE TYR ALA TYR ASP          
SEQRES  21 B  367  THR LYS TYR ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL          
SEQRES  22 B  367  PRO ALA GLN ILE PRO SER GLU VAL ASN ASP LYS ILE ARG          
SEQRES  23 B  367  ALA ILE ALA ILE GLN ALA TYR GLN THR LEU GLY CYS ALA          
SEQRES  24 B  367  GLY MSE ALA ARG VAL ASP VAL PHE LEU THR ALA ASP ASN          
SEQRES  25 B  367  GLU VAL VAL ILE ASN GLU ILE ASN THR LEU PRO GLY PHE          
SEQRES  26 B  367  THR ASN ILE SER MSE TYR PRO LYS LEU TRP GLN ALA SER          
SEQRES  27 B  367  GLY LEU GLY TYR THR ASP LEU ILE SER ARG LEU ILE GLU          
SEQRES  28 B  367  LEU ALA LEU GLU ARG HIS THR ALA ASN ASN ALA LEU LYS          
SEQRES  29 B  367  THR THR MSE                                                  
SEQRES   1 C  367  SER ASN ALA MSE ALA LYS LEU ARG VAL GLY ILE VAL PHE          
SEQRES   2 C  367  GLY GLY LYS SER ALA GLU HIS GLU VAL SER LEU GLN SER          
SEQRES   3 C  367  ALA LYS ASN ILE VAL ASP ALA ILE ASP LYS THR ARG PHE          
SEQRES   4 C  367  ASP VAL VAL LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP          
SEQRES   5 C  367  HIS VAL ASN ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP          
SEQRES   6 C  367  ASP PRO ALA HIS ILE ALA LEU ARG PRO SER ALA ILE SER          
SEQRES   7 C  367  LEU ALA GLN VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE          
SEQRES   8 C  367  ASN ALA GLN ASN GLY GLN PRO LEU PRO THR VAL ASP VAL          
SEQRES   9 C  367  ILE PHE PRO ILE VAL HIS GLY THR LEU GLY GLU ASP GLY          
SEQRES  10 C  367  SER LEU GLN GLY MSE LEU ARG VAL ALA ASN LEU PRO PHE          
SEQRES  11 C  367  VAL GLY SER ASP VAL LEU SER SER ALA ALA CYS MSE ASP          
SEQRES  12 C  367  LYS ASP VAL ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU          
SEQRES  13 C  367  ASN ILE ALA PRO PHE ILE THR LEU THR ARG THR ASN ARG          
SEQRES  14 C  367  HIS ALA PHE SER PHE ALA GLU VAL GLU SER ARG LEU GLY          
SEQRES  15 C  367  LEU PRO LEU PHE VAL LYS PRO ALA ASN GLN GLY SER SER          
SEQRES  16 C  367  VAL GLY VAL SER LYS VAL ALA ASN GLU ALA GLN TYR GLN          
SEQRES  17 C  367  GLN ALA VAL ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL          
SEQRES  18 C  367  VAL VAL GLU GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS          
SEQRES  19 C  367  ALA VAL LEU GLY ASN ASP ASN PRO GLN ALA SER THR CYS          
SEQRES  20 C  367  GLY GLU ILE VAL LEU ASN SER GLU PHE TYR ALA TYR ASP          
SEQRES  21 C  367  THR LYS TYR ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL          
SEQRES  22 C  367  PRO ALA GLN ILE PRO SER GLU VAL ASN ASP LYS ILE ARG          
SEQRES  23 C  367  ALA ILE ALA ILE GLN ALA TYR GLN THR LEU GLY CYS ALA          
SEQRES  24 C  367  GLY MSE ALA ARG VAL ASP VAL PHE LEU THR ALA ASP ASN          
SEQRES  25 C  367  GLU VAL VAL ILE ASN GLU ILE ASN THR LEU PRO GLY PHE          
SEQRES  26 C  367  THR ASN ILE SER MSE TYR PRO LYS LEU TRP GLN ALA SER          
SEQRES  27 C  367  GLY LEU GLY TYR THR ASP LEU ILE SER ARG LEU ILE GLU          
SEQRES  28 C  367  LEU ALA LEU GLU ARG HIS THR ALA ASN ASN ALA LEU LYS          
SEQRES  29 C  367  THR THR MSE                                                  
SEQRES   1 D  367  SER ASN ALA MSE ALA LYS LEU ARG VAL GLY ILE VAL PHE          
SEQRES   2 D  367  GLY GLY LYS SER ALA GLU HIS GLU VAL SER LEU GLN SER          
SEQRES   3 D  367  ALA LYS ASN ILE VAL ASP ALA ILE ASP LYS THR ARG PHE          
SEQRES   4 D  367  ASP VAL VAL LEU LEU GLY ILE ASP LYS ALA GLY GLN TRP          
SEQRES   5 D  367  HIS VAL ASN ASP ALA GLU ASN TYR LEU GLN ASN ALA ASP          
SEQRES   6 D  367  ASP PRO ALA HIS ILE ALA LEU ARG PRO SER ALA ILE SER          
SEQRES   7 D  367  LEU ALA GLN VAL PRO GLY LYS HIS GLN HIS GLN LEU ILE          
SEQRES   8 D  367  ASN ALA GLN ASN GLY GLN PRO LEU PRO THR VAL ASP VAL          
SEQRES   9 D  367  ILE PHE PRO ILE VAL HIS GLY THR LEU GLY GLU ASP GLY          
SEQRES  10 D  367  SER LEU GLN GLY MSE LEU ARG VAL ALA ASN LEU PRO PHE          
SEQRES  11 D  367  VAL GLY SER ASP VAL LEU SER SER ALA ALA CYS MSE ASP          
SEQRES  12 D  367  LYS ASP VAL ALA LYS ARG LEU LEU ARG ASP ALA GLY LEU          
SEQRES  13 D  367  ASN ILE ALA PRO PHE ILE THR LEU THR ARG THR ASN ARG          
SEQRES  14 D  367  HIS ALA PHE SER PHE ALA GLU VAL GLU SER ARG LEU GLY          
SEQRES  15 D  367  LEU PRO LEU PHE VAL LYS PRO ALA ASN GLN GLY SER SER          
SEQRES  16 D  367  VAL GLY VAL SER LYS VAL ALA ASN GLU ALA GLN TYR GLN          
SEQRES  17 D  367  GLN ALA VAL ALA LEU ALA PHE GLU PHE ASP HIS LYS VAL          
SEQRES  18 D  367  VAL VAL GLU GLN GLY ILE LYS GLY ARG GLU ILE GLU CYS          
SEQRES  19 D  367  ALA VAL LEU GLY ASN ASP ASN PRO GLN ALA SER THR CYS          
SEQRES  20 D  367  GLY GLU ILE VAL LEU ASN SER GLU PHE TYR ALA TYR ASP          
SEQRES  21 D  367  THR LYS TYR ILE ASP ASP ASN GLY ALA GLN VAL VAL VAL          
SEQRES  22 D  367  PRO ALA GLN ILE PRO SER GLU VAL ASN ASP LYS ILE ARG          
SEQRES  23 D  367  ALA ILE ALA ILE GLN ALA TYR GLN THR LEU GLY CYS ALA          
SEQRES  24 D  367  GLY MSE ALA ARG VAL ASP VAL PHE LEU THR ALA ASP ASN          
SEQRES  25 D  367  GLU VAL VAL ILE ASN GLU ILE ASN THR LEU PRO GLY PHE          
SEQRES  26 D  367  THR ASN ILE SER MSE TYR PRO LYS LEU TRP GLN ALA SER          
SEQRES  27 D  367  GLY LEU GLY TYR THR ASP LEU ILE SER ARG LEU ILE GLU          
SEQRES  28 D  367  LEU ALA LEU GLU ARG HIS THR ALA ASN ASN ALA LEU LYS          
SEQRES  29 D  367  THR THR MSE                                                  
MODRES 3Q1K MSE A  119  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE A  298  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE A  327  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE B  119  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE B  139  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE B  298  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE B  327  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE C  119  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE C  139  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE C  298  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE C  327  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE C  364  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE D  119  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE D  139  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE D  298  MET  SELENOMETHIONINE                                   
MODRES 3Q1K MSE D  327  MET  SELENOMETHIONINE                                   
HET    MSE  A 119       8                                                       
HET    MSE  A 139      16                                                       
HET    MSE  A 298       8                                                       
HET    MSE  A 327       8                                                       
HET    MSE  B 119       8                                                       
HET    MSE  B 139      16                                                       
HET    MSE  B 298       8                                                       
HET    MSE  B 327       8                                                       
HET    MSE  C 119       8                                                       
HET    MSE  C 139       8                                                       
HET    MSE  C 298      16                                                       
HET    MSE  C 327       8                                                       
HET    MSE  C 364       8                                                       
HET    MSE  D 119       8                                                       
HET    MSE  D 139       8                                                       
HET    MSE  D 298       8                                                       
HET    MSE  D 327       8                                                       
HET    ADP  A 370      27                                                       
HET    FMT  A 371       3                                                       
HET     MG  A 372       1                                                       
HET    GOL  A 373       6                                                       
HET    ADP  B 370      27                                                       
HET     MG  B 371       1                                                       
HET    FMT  B 372       3                                                       
HET    FMT  B 373       3                                                       
HET    FMT  B 374       3                                                       
HET    SO4  B 375       5                                                       
HET    GOL  B 376       6                                                       
HET    ADP  C 370      27                                                       
HET    GOL  C 371       6                                                       
HET    GOL  C 372       6                                                       
HET    ADP  D 370      27                                                       
HET    FMT  D 371       3                                                       
HET     MG  D 372       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     FMT FORMIC ACID                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    17(C5 H11 N O2 SE)                                           
FORMUL   5  ADP    4(C10 H15 N5 O10 P2)                                         
FORMUL   6  FMT    5(C H2 O2)                                                   
FORMUL   7   MG    3(MG 2+)                                                     
FORMUL   8  GOL    4(C3 H8 O3)                                                  
FORMUL  14  SO4    O4 S 2-                                                      
FORMUL  22  HOH   *481(H2 O)                                                    
HELIX    1   1 GLU A   16  ILE A   31  1                                  16    
HELIX    2   2 GLY A  114  ALA A  123  1                                  10    
HELIX    3   3 ASP A  131  ASP A  140  1                                  10    
HELIX    4   4 ASP A  140  ALA A  151  1                                  12    
HELIX    5   5 SER A  170  GLY A  179  1                                  10    
HELIX    6   6 ASN A  200  PHE A  212  1                                  13    
HELIX    7   7 ILE A  261  ALA A  266  5                                   6    
HELIX    8   8 PRO A  275  LEU A  293  1                                  19    
HELIX    9   9 SER A  326  ALA A  334  1                                   9    
HELIX   10  10 GLY A  338  LEU A  360  1                                  23    
HELIX   11  11 GLU B   16  ILE B   31  1                                  16    
HELIX   12  12 GLY B  114  ALA B  123  1                                  10    
HELIX   13  13 ASP B  131  ASP B  140  1                                  10    
HELIX   14  14 ASP B  140  ALA B  151  1                                  12    
HELIX   15  15 SER B  170  GLY B  179  1                                  10    
HELIX   16  16 ASN B  200  PHE B  212  1                                  13    
HELIX   17  17 PRO B  275  LEU B  293  1                                  19    
HELIX   18  18 SER B  326  ALA B  334  1                                   9    
HELIX   19  19 GLY B  338  ALA B  359  1                                  22    
HELIX   20  20 GLU C   16  ILE C   31  1                                  16    
HELIX   21  21 GLY C  114  ALA C  123  1                                  10    
HELIX   22  22 ASP C  131  ASP C  140  1                                  10    
HELIX   23  23 ASP C  140  ALA C  151  1                                  12    
HELIX   24  24 SER C  170  GLY C  179  1                                  10    
HELIX   25  25 ASN C  200  PHE C  212  1                                  13    
HELIX   26  26 PRO C  275  LEU C  293  1                                  19    
HELIX   27  27 SER C  326  ALA C  334  1                                   9    
HELIX   28  28 GLY C  338  ALA C  359  1                                  22    
HELIX   29  29 GLU D   16  ILE D   31  1                                  16    
HELIX   30  30 GLY D  114  ALA D  123  1                                  10    
HELIX   31  31 ASP D  131  ASP D  140  1                                  10    
HELIX   32  32 ASP D  140  ALA D  151  1                                  12    
HELIX   33  33 SER D  170  GLY D  179  1                                  10    
HELIX   34  34 ASN D  200  PHE D  212  1                                  13    
HELIX   35  35 ILE D  261  ALA D  266  5                                   6    
HELIX   36  36 PRO D  275  LEU D  293  1                                  19    
HELIX   37  37 SER D  326  ALA D  334  1                                   9    
HELIX   38  38 GLY D  338  LEU D  360  1                                  23    
SHEET    1   A 4 TRP A  49  ASN A  52  0                                        
SHEET    2   A 4 PHE A  36  ILE A  43 -1  N  LEU A  40   O  ASN A  52           
SHEET    3   A 4 LEU A   4  GLY A  11  1  N  PHE A  10   O  ILE A  43           
SHEET    4   A 4 VAL A 101  PRO A 104  1  O  PHE A 103   N  GLY A   7           
SHEET    1   B 2 LEU A  58  GLN A  59  0                                        
SHEET    2   B 2 ALA A  68  LEU A  69 -1  O  ALA A  68   N  GLN A  59           
SHEET    1   C 2 LEU A  76  GLN A  78  0                                        
SHEET    2   C 2 LEU A  87  ASN A  89 -1  O  ILE A  88   N  ALA A  77           
SHEET    1   D 4 PHE A 158  LEU A 161  0                                        
SHEET    2   D 4 VAL A 218  GLN A 222 -1  O  VAL A 218   N  LEU A 161           
SHEET    3   D 4 LEU A 182  PRO A 186 -1  N  LYS A 185   O  VAL A 219           
SHEET    4   D 4 SER A 196  VAL A 198 -1  O  VAL A 198   N  LEU A 182           
SHEET    1   E 5 GLN A 267  VAL A 269  0                                        
SHEET    2   E 5 GLN A 240  VAL A 248 -1  N  GLU A 246   O  VAL A 269           
SHEET    3   E 5 ARG A 227  GLY A 235 -1  N  LEU A 234   O  GLN A 240           
SHEET    4   E 5 GLY A 297  LEU A 305 -1  O  VAL A 303   N  ILE A 229           
SHEET    5   E 5 VAL A 311  ASN A 317 -1  O  VAL A 312   N  PHE A 304           
SHEET    1   F 4 TRP B  49  ASN B  52  0                                        
SHEET    2   F 4 PHE B  36  ILE B  43 -1  N  LEU B  40   O  ASN B  52           
SHEET    3   F 4 LEU B   4  GLY B  11  1  N  PHE B  10   O  ILE B  43           
SHEET    4   F 4 VAL B 101  PRO B 104  1  O  PHE B 103   N  GLY B   7           
SHEET    1   G 2 LEU B  58  GLN B  59  0                                        
SHEET    2   G 2 ALA B  68  LEU B  69 -1  O  ALA B  68   N  GLN B  59           
SHEET    1   H 2 LEU B  76  GLN B  78  0                                        
SHEET    2   H 2 LEU B  87  ASN B  89 -1  O  ILE B  88   N  ALA B  77           
SHEET    1   I 4 PHE B 158  THR B 162  0                                        
SHEET    2   I 4 LYS B 217  GLN B 222 -1  O  VAL B 218   N  LEU B 161           
SHEET    3   I 4 LEU B 182  PRO B 186 -1  N  PHE B 183   O  GLU B 221           
SHEET    4   I 4 SER B 196  VAL B 198 -1  O  VAL B 198   N  LEU B 182           
SHEET    1   J 5 GLN B 267  VAL B 269  0                                        
SHEET    2   J 5 GLN B 240  VAL B 248 -1  N  VAL B 248   O  GLN B 267           
SHEET    3   J 5 ARG B 227  GLY B 235 -1  N  ALA B 232   O  SER B 242           
SHEET    4   J 5 GLY B 297  LEU B 305 -1  O  ALA B 299   N  VAL B 233           
SHEET    5   J 5 VAL B 311  ASN B 317 -1  O  VAL B 312   N  PHE B 304           
SHEET    1   K 4 TRP C  49  ASN C  52  0                                        
SHEET    2   K 4 PHE C  36  ILE C  43 -1  N  LEU C  40   O  ASN C  52           
SHEET    3   K 4 LEU C   4  GLY C  11  1  N  VAL C   6   O  ASP C  37           
SHEET    4   K 4 VAL C 101  PRO C 104  1  O  VAL C 101   N  GLY C   7           
SHEET    1   L 2 LEU C  58  GLN C  59  0                                        
SHEET    2   L 2 ALA C  68  LEU C  69 -1  O  ALA C  68   N  GLN C  59           
SHEET    1   M 2 LEU C  76  GLN C  78  0                                        
SHEET    2   M 2 LEU C  87  ASN C  89 -1  O  ILE C  88   N  ALA C  77           
SHEET    1   N 4 PHE C 158  THR C 162  0                                        
SHEET    2   N 4 LYS C 217  GLN C 222 -1  O  VAL C 218   N  LEU C 161           
SHEET    3   N 4 LEU C 182  PRO C 186 -1  N  LYS C 185   O  VAL C 219           
SHEET    4   N 4 SER C 196  VAL C 198 -1  O  VAL C 198   N  LEU C 182           
SHEET    1   O 4 GLN C 240  ILE C 247  0                                        
SHEET    2   O 4 ARG C 227  LEU C 234 -1  N  ALA C 232   O  SER C 242           
SHEET    3   O 4 MSE C 298  LEU C 305 -1  O  VAL C 301   N  CYS C 231           
SHEET    4   O 4 VAL C 311  ASN C 317 -1  O  VAL C 312   N  PHE C 304           
SHEET    1   P 4 TRP D  49  ASN D  52  0                                        
SHEET    2   P 4 PHE D  36  ILE D  43 -1  N  LEU D  40   O  ASN D  52           
SHEET    3   P 4 LEU D   4  GLY D  11  1  N  VAL D   6   O  ASP D  37           
SHEET    4   P 4 VAL D 101  PRO D 104  1  O  VAL D 101   N  GLY D   7           
SHEET    1   Q 2 LEU D  58  GLN D  59  0                                        
SHEET    2   Q 2 ALA D  68  LEU D  69 -1  O  ALA D  68   N  GLN D  59           
SHEET    1   R 2 LEU D  76  GLN D  78  0                                        
SHEET    2   R 2 LEU D  87  ASN D  89 -1  O  ILE D  88   N  ALA D  77           
SHEET    1   S 4 PHE D 158  THR D 162  0                                        
SHEET    2   S 4 LYS D 217  GLN D 222 -1  O  VAL D 218   N  LEU D 161           
SHEET    3   S 4 LEU D 182  PRO D 186 -1  N  LYS D 185   O  VAL D 219           
SHEET    4   S 4 SER D 196  VAL D 198 -1  O  VAL D 198   N  LEU D 182           
SHEET    1   T 5 GLN D 267  VAL D 269  0                                        
SHEET    2   T 5 GLN D 240  VAL D 248 -1  N  GLU D 246   O  VAL D 269           
SHEET    3   T 5 ARG D 227  GLY D 235 -1  N  GLU D 230   O  GLY D 245           
SHEET    4   T 5 GLY D 297  LEU D 305 -1  O  LEU D 305   N  ARG D 227           
SHEET    5   T 5 VAL D 311  ASN D 317 -1  O  GLU D 315   N  ASP D 302           
LINK         C   GLY A 118                 N   MSE A 119     1555   1555  1.33  
LINK         C   MSE A 119                 N   LEU A 120     1555   1555  1.33  
LINK         C   CYS A 138                 N  AMSE A 139     1555   1555  1.34  
LINK         C   CYS A 138                 N  BMSE A 139     1555   1555  1.33  
LINK         C  AMSE A 139                 N   ASP A 140     1555   1555  1.32  
LINK         C  BMSE A 139                 N   ASP A 140     1555   1555  1.32  
LINK         C   GLY A 297                 N   MSE A 298     1555   1555  1.32  
LINK         C   MSE A 298                 N   ALA A 299     1555   1555  1.33  
LINK         C   SER A 326                 N   MSE A 327     1555   1555  1.33  
LINK         C   MSE A 327                 N   TYR A 328     1555   1555  1.34  
LINK         C   GLY B 118                 N   MSE B 119     1555   1555  1.33  
LINK         C   MSE B 119                 N   LEU B 120     1555   1555  1.33  
LINK         C   CYS B 138                 N  AMSE B 139     1555   1555  1.33  
LINK         C   CYS B 138                 N  CMSE B 139     1555   1555  1.33  
LINK         C  AMSE B 139                 N   ASP B 140     1555   1555  1.33  
LINK         C  CMSE B 139                 N   ASP B 140     1555   1555  1.33  
LINK         C   GLY B 297                 N   MSE B 298     1555   1555  1.33  
LINK         C   MSE B 298                 N   ALA B 299     1555   1555  1.33  
LINK         C   SER B 326                 N   MSE B 327     1555   1555  1.34  
LINK         C   MSE B 327                 N   TYR B 328     1555   1555  1.32  
LINK         C   GLY C 118                 N   MSE C 119     1555   1555  1.32  
LINK         C   MSE C 119                 N   LEU C 120     1555   1555  1.33  
LINK         C   CYS C 138                 N   MSE C 139     1555   1555  1.33  
LINK         C   MSE C 139                 N   ASP C 140     1555   1555  1.33  
LINK         C   GLY C 297                 N  AMSE C 298     1555   1555  1.33  
LINK         C   GLY C 297                 N  BMSE C 298     1555   1555  1.33  
LINK         C  AMSE C 298                 N   ALA C 299     1555   1555  1.32  
LINK         C  BMSE C 298                 N   ALA C 299     1555   1555  1.33  
LINK         C   SER C 326                 N   MSE C 327     1555   1555  1.33  
LINK         C   MSE C 327                 N   TYR C 328     1555   1555  1.34  
LINK         C   THR C 363                 N   MSE C 364     1555   1555  1.33  
LINK         C   GLY D 118                 N   MSE D 119     1555   1555  1.33  
LINK         C   MSE D 119                 N   LEU D 120     1555   1555  1.32  
LINK         C   CYS D 138                 N   MSE D 139     1555   1555  1.32  
LINK         C   MSE D 139                 N   ASP D 140     1555   1555  1.33  
LINK         C   GLY D 297                 N   MSE D 298     1555   1555  1.33  
LINK         C   MSE D 298                 N   ALA D 299     1555   1555  1.32  
LINK         C   SER D 326                 N   MSE D 327     1555   1555  1.33  
LINK         C   MSE D 327                 N   TYR D 328     1555   1555  1.34  
LINK         O1B ADP D 370                MG    MG D 372     1555   1555  2.07  
LINK         O1B ADP A 370                MG    MG A 372     1555   1555  2.20  
LINK         O1A ADP B 370                MG    MG B 371     1555   1555  2.36  
LINK         O1A ADP D 370                MG    MG D 372     1555   1555  2.38  
LINK         O1A ADP A 370                MG    MG A 372     1555   1555  2.40  
LINK         OE1 GLU D 315                MG    MG D 372     1555   1555  2.54  
LINK         OE1 GLU B 315                MG    MG B 371     1555   1555  2.68  
LINK         OE2 GLU A 315                MG    MG A 372     1555   1555  2.85  
LINK         O3B ADP B 370                MG    MG B 371     1555   1555  2.95  
LINK        MG    MG A 372                 O   HOH A 494     1555   1555  2.27  
LINK        MG    MG A 372                 O   HOH A 495     1555   1555  2.33  
LINK        MG    MG D 372                 O   HOH D 470     1555   1555  2.44  
LINK        MG    MG D 372                 O   HOH D 472     1555   1555  2.49  
LINK        MG    MG A 372                 O   HOH A 493     1555   1555  2.49  
LINK        MG    MG D 372                 O   HOH D 471     1555   1555  2.59  
CISPEP   1 LEU A  180    PRO A  181          0        -0.33                     
CISPEP   2 VAL A  270    PRO A  271          0         1.10                     
CISPEP   3 LEU B  180    PRO B  181          0        -3.13                     
CISPEP   4 VAL B  270    PRO B  271          0        -3.40                     
CISPEP   5 LEU C  180    PRO C  181          0        -5.76                     
CISPEP   6 VAL C  270    PRO C  271          0        -4.33                     
CISPEP   7 LEU D  180    PRO D  181          0        -2.13                     
CISPEP   8 VAL D  270    PRO D  271          0         0.29                     
SITE     1 AC1 17 LYS A 141  PHE A 183  LYS A 185  GLY A 190                    
SITE     2 AC1 17 SER A 191  SER A 192  GLU A 221  GLN A 222                    
SITE     3 AC1 17 GLY A 223  ILE A 224  GLU A 228  LEU A 249                    
SITE     4 AC1 17 PHE A 304  ASN A 314  GLU A 315   MG A 372                    
SITE     5 AC1 17 HOH A 494                                                     
SITE     1 AC2  5 PRO A 126  PHE A 127  ALA A 350  ARG A 353                    
SITE     2 AC2  5 HIS A 354                                                     
SITE     1 AC3  5 GLU A 315  ADP A 370  HOH A 493  HOH A 494                    
SITE     2 AC3  5 HOH A 495                                                     
SITE     1 AC4  7 ASN A 236  ASP A 237  CYS A 295  ALA A 296                    
SITE     2 AC4  7 ARG A 353  HOH A 375  HOH A 383                               
SITE     1 AC5 15 LYS B 141  PHE B 183  LYS B 185  GLY B 190                    
SITE     2 AC5 15 SER B 191  SER B 192  GLU B 221  GLN B 222                    
SITE     3 AC5 15 GLY B 223  ILE B 224  GLU B 228  PHE B 304                    
SITE     4 AC5 15 ASN B 314  GLU B 315   MG B 371                               
SITE     1 AC6  3 ASP B 302  GLU B 315  ADP B 370                               
SITE     1 AC7  2 GLN B 240  ARG B 345                                          
SITE     1 AC8  7 HIS B  85  GLN B  86  LEU B  87  LEU B  96                    
SITE     2 AC8  7 PRO B  97  THR B  98  VAL B  99                               
SITE     1 AC9  3 ASN B 236  CYS B 295  ALA B 296                               
SITE     1 BC1  6 ARG B 300  GLY B 321  SER B 326  MSE B 327                    
SITE     2 BC1  6 HOH B 365  HOH B 415                                          
SITE     1 BC2  9 CYS B 138  MSE B 139  LYS B 141  ALA B 187                    
SITE     2 BC2  9 GLN B 189  GLU B 315  ILE B 316  ASN B 317                    
SITE     3 BC2  9 HOH B 386                                                     
SITE     1 BC3 13 PHE C 183  LYS C 185  GLY C 190  SER C 191                    
SITE     2 BC3 13 SER C 192  GLU C 221  GLN C 222  GLY C 223                    
SITE     3 BC3 13 ILE C 224  GLU C 228  PHE C 304  ASN C 314                    
SITE     4 BC3 13 GLU C 315                                                     
SITE     1 BC4  5 ARG C 300  GLY C 321  SER C 326  MSE C 327                    
SITE     2 BC4  5 HOH C 416                                                     
SITE     1 BC5  6 PRO C 126  PHE C 127  ALA C 350  ARG C 353                    
SITE     2 BC5  6 HIS C 354  HOH C 397                                          
SITE     1 BC6 18 LYS D 141  PHE D 183  LYS D 185  GLN D 189                    
SITE     2 BC6 18 GLY D 190  SER D 191  SER D 192  GLU D 221                    
SITE     3 BC6 18 GLN D 222  GLY D 223  ILE D 224  GLU D 228                    
SITE     4 BC6 18 LEU D 249  PHE D 304  ASN D 314  GLU D 315                    
SITE     5 BC6 18  MG D 372  HOH D 470                                          
SITE     1 BC7  6 PRO D 126  PHE D 127  ALA D 350  ARG D 353                    
SITE     2 BC7  6 HIS D 354  HOH D 469                                          
SITE     1 BC8  5 GLU D 315  ADP D 370  HOH D 470  HOH D 471                    
SITE     2 BC8  5 HOH D 472                                                     
CRYST1   85.153   85.813  230.893  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011744  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004331        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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