GenomeNet

Database: PDB
Entry: 5C1P
LinkDB: 5C1P
Original site: 5C1P 
HEADER    LIGASE                                  15-JUN-15   5C1P              
TITLE     CRYSTAL STRUCTURE OF ADP AND D-ALANYL-D-ALANINE COMPLEXED D-ALANINE-D-
TITLE    2 ALANINE LIGASE(DDL) FROM YERSINIA PESTIS                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE,D-ALANYLALANINE SYNTHETASE;              
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;                                
SOURCE   3 ORGANISM_TAXID: 632;                                                 
SOURCE   4 GENE: DDL, DDLB, YPO0557, Y3624, YP_3627;                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21-GOLD(DE3)PLYSS AG;          
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD(DE3)PLYSS AG                     
KEYWDS    D-ALANINE-D-ALANINE LIGASE, DDL, DRUG TARGET, BACTERIAL CELL WALL     
KEYWDS   2 SYNTHESIS, LIGASE                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.T.TRAN,L.W.KANG,M.K.HONG,H.P.T.NGO                                  
REVDAT   1   02-MAR-16 5C1P    0                                                
JRNL        AUTH   H.T.TRAN,M.K.HONG,H.P.NGO,K.H.HUYNH,Y.J.AHN,Z.WANG,L.W.KANG  
JRNL        TITL   STRUCTURE OF D-ALANINE-D-ALANINE LIGASE FROM YERSINIA        
JRNL        TITL 2 PESTIS: NUCLEOTIDE PHOSPHATE RECOGNITION BY THE SERINE LOOP. 
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72    12 2016              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   26894530                                                     
JRNL        DOI    10.1107/S2059798315021671                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 53293                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2846                            
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) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.46                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3855                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.39                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 193                          
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9108                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 143                                     
REMARK   3   SOLVENT ATOMS            : 218                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.377         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.163         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.019         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9440 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  9049 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12780 ; 1.617 ; 1.996       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20863 ; 1.319 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1188 ; 5.911 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   381 ;36.887 ;24.987       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1572 ;15.527 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;20.547 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1465 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10551 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1998 ; 0.007 ; 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):  4779 ; 3.638 ; 4.124       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4778 ; 3.636 ; 4.124       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5955 ; 5.319 ; 6.169       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5956 ; 5.319 ; 6.170       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4661 ; 4.799 ; 4.831       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4660 ; 4.798 ; 4.832       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6822 ; 7.266 ; 7.012       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10305 ; 9.279 ;33.719       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10302 ; 9.280 ;33.724       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 6                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     1    306       B     1    306   17106  0.09  0.05     
REMARK   3    2     A     1    306       C     1    306   17127  0.10  0.05     
REMARK   3    3     A     2    306       D     2    306   17109  0.09  0.05     
REMARK   3    4     B     1    306       C     1    306   17598  0.10  0.05     
REMARK   3    5     B     2    306       D     2    306   17454  0.10  0.05     
REMARK   3    6     C     2    306       D     2    306   17793  0.11  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5C1P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210609.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.997                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56216                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 32.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ORTHORHOMBIC SHAPED CRYSTAL                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE, 0.1M RIS PH7.0,     
REMARK 280  29% PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K       
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       31.33500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.55150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.27250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.55150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.33500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.27250            
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: 4260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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: 5010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25320 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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     GLU A   148                                                      
REMARK 465     GLY A   149                                                      
REMARK 465     SER A   150                                                      
REMARK 465     PRO A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     VAL A   208                                                      
REMARK 465     PHE A   209                                                      
REMARK 465     TYR A   210                                                      
REMARK 465     ASP A   211                                                      
REMARK 465     TYR A   212                                                      
REMARK 465     ASP A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     LYS A   215                                                      
REMARK 465     TYR A   216                                                      
REMARK 465     LEU A   217                                                      
REMARK 465     SER A   218                                                      
REMARK 465     ASP A   219                                                      
REMARK 465     GLU B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     SER B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     TYR B   216                                                      
REMARK 465     LEU B   217                                                      
REMARK 465     SER B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLY D   149                                                      
REMARK 465     SER D   150                                                      
REMARK 465     SER D   151                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ALA D   214     OG1  THR D   221              2.16            
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    ASP B 263   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 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    GLU B 128      -51.49    136.11                                   
REMARK 500    GLU C 148      129.29    -35.27                                   
REMARK 500    GLN D 172      -26.65    110.33                                   
REMARK 500    ASP D 211     -169.24   -122.31                                   
REMARK 500    ASP D 219       -3.42     80.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU D  217     SER D  218                 -148.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              NA A 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  68   O                                                      
REMARK 620 2 SER A  91   O    77.8                                              
REMARK 620 3 THR A  94   OG1 154.1  77.0                                        
REMARK 620 4 THR A 273   OG1  85.0 115.8 100.5                                  
REMARK 620 5 HOH A 517   O   106.3 161.7  99.6  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  68   O                                                      
REMARK 620 2 SER B  91   O    79.0                                              
REMARK 620 3 THR B  94   OG1 156.0  77.0                                        
REMARK 620 4 THR B 273   OG1  89.9 122.4 101.4                                  
REMARK 620 5 HOH B 512   O   108.8 150.8  93.2  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 402  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  68   O                                                      
REMARK 620 2 SER C  91   O    78.2                                              
REMARK 620 3 THR C  94   OG1 154.6  76.4                                        
REMARK 620 4 THR C 273   OG1  90.1 121.4 102.1                                  
REMARK 620 5 HOH C 543   O   113.6 157.4  90.8  79.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 404  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  68   O                                                      
REMARK 620 2 SER D  91   O    76.7                                              
REMARK 620 3 THR D  94   OG1 152.0  76.2                                        
REMARK 620 4 THR D 273   OG1  85.5 115.4  99.9                                  
REMARK 620 5 HOH D 508   O   110.9 159.3  97.1  84.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DAL D 402 and DAL D    
REMARK 800  403                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5C1P   RELATED DB: PDB                                   
DBREF  5C1P A    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5C1P B    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5C1P C    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  5C1P D    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
SEQRES   1 A  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 A  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 A  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 A  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 A  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 A  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 A  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 A  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 A  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 A  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 A  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 A  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 A  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 A  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 A  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 A  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 A  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 A  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 A  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 A  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 A  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 A  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 A  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 A  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 B  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 B  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 B  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 B  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 B  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 B  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 B  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 B  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 B  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 B  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 B  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 B  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 B  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 B  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 B  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 B  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 B  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 B  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 B  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 B  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 B  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 B  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 B  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 B  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 C  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 C  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 C  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 C  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 C  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 C  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 C  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 C  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 C  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 C  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 C  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 C  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 C  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 C  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 C  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 C  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 C  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 C  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 C  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 C  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 C  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 C  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 C  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 C  306  ARG ILE LEU MET LEU ALA ASP                                  
SEQRES   1 D  306  MET ALA GLU LYS VAL ALA VAL LEU LEU GLY GLY THR SER          
SEQRES   2 D  306  ALA GLU ARG GLU VAL SER LEU LEU SER GLY GLN ALA VAL          
SEQRES   3 D  306  LEU ALA GLY LEU LYS GLU ALA GLY ILE ASP ALA TYR GLY          
SEQRES   4 D  306  VAL ASP THR LYS ASP PHE PRO VAL THR GLN LEU LYS GLU          
SEQRES   5 D  306  GLN GLY PHE ASP LYS VAL PHE ILE ALA LEU HIS GLY ARG          
SEQRES   6 D  306  GLY GLY GLU ASP GLY THR LEU GLN GLY VAL LEU GLU PHE          
SEQRES   7 D  306  LEU GLN LEU PRO TYR THR GLY SER GLY VAL MET ALA SER          
SEQRES   8 D  306  ALA LEU THR MET ASP LYS LEU ARG THR LYS LEU VAL TRP          
SEQRES   9 D  306  GLN ALA LEU GLY LEU PRO ILE SER PRO TYR VAL ALA LEU          
SEQRES  10 D  306  ASN ARG GLN GLN PHE GLU THR LEU SER PRO GLU GLU LEU          
SEQRES  11 D  306  VAL ALA CYS VAL ALA LYS LEU GLY LEU PRO LEU ILE VAL          
SEQRES  12 D  306  LYS PRO SER HIS GLU GLY SER SER VAL GLY MET SER LYS          
SEQRES  13 D  306  VAL ASP HIS ALA SER GLU LEU GLN LYS ALA LEU VAL GLU          
SEQRES  14 D  306  ALA PHE GLN HIS ASP SER ASP VAL LEU ILE GLU LYS TRP          
SEQRES  15 D  306  LEU SER GLY PRO GLU PHE THR VAL ALA ILE LEU GLY ASP          
SEQRES  16 D  306  GLU VAL LEU PRO SER ILE ARG ILE GLN PRO PRO GLY VAL          
SEQRES  17 D  306  PHE TYR ASP TYR ASP ALA LYS TYR LEU SER ASP LYS THR          
SEQRES  18 D  306  GLN TYR PHE CYS PRO SER GLY LEU SER ASP GLU SER GLU          
SEQRES  19 D  306  GLN GLN LEU ALA ALA LEU ALA LEU GLN ALA TYR HIS ALA          
SEQRES  20 D  306  LEU ASP CYS SER GLY TRP GLY ARG VAL ASP VAL MET GLN          
SEQRES  21 D  306  ASP ARG ASP GLY HIS PHE TYR LEU LEU GLU VAL ASN THR          
SEQRES  22 D  306  SER PRO GLY MET THR SER HIS SER LEU VAL PRO MET ALA          
SEQRES  23 D  306  ALA ARG GLN TYR GLY LEU SER PHE SER GLN LEU VAL ALA          
SEQRES  24 D  306  ARG ILE LEU MET LEU ALA ASP                                  
HET     NA  A 401       1                                                       
HET    GOL  A 402       6                                                       
HET    GOL  A 403       6                                                       
HET    ADP  B 401      27                                                       
HET     NA  B 402       1                                                       
HET    GOL  B 403       6                                                       
HET    ADP  C 401      27                                                       
HET     NA  C 402       1                                                       
HET    ACT  C 403       4                                                       
HET    GOL  C 404       6                                                       
HET    GOL  C 405       6                                                       
HET    GOL  C 406       6                                                       
HET    GOL  C 407       6                                                       
HET     NA  C 408       1                                                       
HET    ADP  D 401      27                                                       
HET    DAL  D 402       5                                                       
HET    DAL  D 403       6                                                       
HET     NA  D 404       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM     DAL D-ALANINE                                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   NA    5(NA 1+)                                                     
FORMUL   6  GOL    7(C3 H8 O3)                                                  
FORMUL   8  ADP    3(C10 H15 N5 O10 P2)                                         
FORMUL  13  ACT    C2 H3 O2 1-                                                  
FORMUL  20  DAL    2(C3 H7 N O2)                                                
FORMUL  23  HOH   *218(H2 O)                                                    
HELIX    1 AA1 GLU A   15  ALA A   33  1                                  19    
HELIX    2 AA2 PRO A   46  LEU A   50  5                                   5    
HELIX    3 AA3 GLY A   70  GLN A   80  1                                  11    
HELIX    4 AA4 GLY A   87  THR A   94  1                                   8    
HELIX    5 AA5 ASP A   96  LEU A  107  1                                  12    
HELIX    6 AA6 ARG A  119  LEU A  125  1                                   7    
HELIX    7 AA7 SER A  126  ALA A  135  1                                  10    
HELIX    8 AA8 LYS A  136  GLY A  138  5                                   3    
HELIX    9 AA9 HIS A  159  SER A  161  5                                   3    
HELIX   10 AB1 GLU A  162  GLN A  172  1                                  11    
HELIX   11 AB2 SER A  230  LEU A  248  1                                  19    
HELIX   12 AB3 SER A  281  GLY A  291  1                                  11    
HELIX   13 AB4 SER A  293  LEU A  304  1                                  12    
HELIX   14 AB5 GLU B   15  ALA B   33  1                                  19    
HELIX   15 AB6 PRO B   46  LEU B   50  5                                   5    
HELIX   16 AB7 GLY B   70  GLN B   80  1                                  11    
HELIX   17 AB8 GLY B   87  THR B   94  1                                   8    
HELIX   18 AB9 ASP B   96  LEU B  107  1                                  12    
HELIX   19 AC1 ARG B  119  THR B  124  1                                   6    
HELIX   20 AC2 GLU B  128  ALA B  135  1                                   8    
HELIX   21 AC3 LYS B  136  GLY B  138  5                                   3    
HELIX   22 AC4 HIS B  159  SER B  161  5                                   3    
HELIX   23 AC5 GLU B  162  PHE B  171  1                                  10    
HELIX   24 AC6 SER B  230  LEU B  248  1                                  19    
HELIX   25 AC7 SER B  281  GLY B  291  1                                  11    
HELIX   26 AC8 SER B  293  LEU B  304  1                                  12    
HELIX   27 AC9 GLU C   15  ALA C   33  1                                  19    
HELIX   28 AD1 PRO C   46  LEU C   50  5                                   5    
HELIX   29 AD2 GLY C   70  GLN C   80  1                                  11    
HELIX   30 AD3 GLY C   87  THR C   94  1                                   8    
HELIX   31 AD4 ASP C   96  LEU C  107  1                                  12    
HELIX   32 AD5 ARG C  119  LEU C  125  1                                   7    
HELIX   33 AD6 SER C  126  ALA C  135  1                                  10    
HELIX   34 AD7 LYS C  136  GLY C  138  5                                   3    
HELIX   35 AD8 HIS C  159  SER C  161  5                                   3    
HELIX   36 AD9 GLU C  162  GLN C  172  1                                  11    
HELIX   37 AE1 ASP C  211  LEU C  217  1                                   7    
HELIX   38 AE2 SER C  230  LEU C  248  1                                  19    
HELIX   39 AE3 SER C  281  GLY C  291  1                                  11    
HELIX   40 AE4 SER C  293  LEU C  304  1                                  12    
HELIX   41 AE5 GLU D   15  ALA D   33  1                                  19    
HELIX   42 AE6 PRO D   46  LEU D   50  5                                   5    
HELIX   43 AE7 GLY D   70  GLN D   80  1                                  11    
HELIX   44 AE8 GLY D   87  THR D   94  1                                   8    
HELIX   45 AE9 ASP D   96  LEU D  107  1                                  12    
HELIX   46 AF1 ARG D  119  LEU D  125  1                                   7    
HELIX   47 AF2 SER D  126  ALA D  135  1                                  10    
HELIX   48 AF3 LYS D  136  GLY D  138  5                                   3    
HELIX   49 AF4 HIS D  159  SER D  161  5                                   3    
HELIX   50 AF5 GLU D  162  PHE D  171  1                                  10    
HELIX   51 AF6 ASP D  211  LEU D  217  1                                   7    
HELIX   52 AF7 SER D  230  LEU D  248  1                                  19    
HELIX   53 AF8 SER D  281  GLY D  291  1                                  11    
HELIX   54 AF9 SER D  293  LEU D  304  1                                  12    
SHEET    1 AA1 3 ALA A  37  ASP A  41  0                                        
SHEET    2 AA1 3 VAL A   5  LEU A   9  1  N  VAL A   7   O  TYR A  38           
SHEET    3 AA1 3 LYS A  57  ILE A  60  1  O  PHE A  59   N  ALA A   6           
SHEET    1 AA2 4 TYR A 114  ASN A 118  0                                        
SHEET    2 AA2 4 ASP A 176  LYS A 181 -1  O  ILE A 179   N  VAL A 115           
SHEET    3 AA2 4 LEU A 141  PRO A 145 -1  N  LYS A 144   O  LEU A 178           
SHEET    4 AA2 4 SER A 155  VAL A 157 -1  O  VAL A 157   N  LEU A 141           
SHEET    1 AA3 4 GLU A 196  VAL A 197  0                                        
SHEET    2 AA3 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3 AA3 4 ILE A 201  GLN A 204 -1  O  ILE A 203   N  GLU A 187           
SHEET    4 AA3 4 GLN A 222  PHE A 224 -1  O  GLN A 222   N  GLN A 204           
SHEET    1 AA4 4 GLU A 196  VAL A 197  0                                        
SHEET    2 AA4 4 GLU A 187  LEU A 193 -1  N  LEU A 193   O  GLU A 196           
SHEET    3 AA4 4 TRP A 253  GLN A 260 -1  O  VAL A 258   N  PHE A 188           
SHEET    4 AA4 4 PHE A 266  ASN A 272 -1  O  LEU A 269   N  ASP A 257           
SHEET    1 AA5 3 ASP B  36  ASP B  41  0                                        
SHEET    2 AA5 3 LYS B   4  LEU B   9  1  N  VAL B   7   O  TYR B  38           
SHEET    3 AA5 3 LYS B  57  ILE B  60  1  O  PHE B  59   N  ALA B   6           
SHEET    1 AA6 4 TYR B 114  ASN B 118  0                                        
SHEET    2 AA6 4 ASP B 176  LYS B 181 -1  O  ILE B 179   N  VAL B 115           
SHEET    3 AA6 4 LEU B 141  PRO B 145 -1  N  LYS B 144   O  LEU B 178           
SHEET    4 AA6 4 SER B 155  VAL B 157 -1  O  VAL B 157   N  LEU B 141           
SHEET    1 AA7 4 GLU B 196  VAL B 197  0                                        
SHEET    2 AA7 4 GLU B 187  LEU B 193 -1  N  LEU B 193   O  GLU B 196           
SHEET    3 AA7 4 ILE B 201  GLN B 204 -1  O  ILE B 203   N  GLU B 187           
SHEET    4 AA7 4 GLN B 222  PHE B 224 -1  O  GLN B 222   N  GLN B 204           
SHEET    1 AA8 4 GLU B 196  VAL B 197  0                                        
SHEET    2 AA8 4 GLU B 187  LEU B 193 -1  N  LEU B 193   O  GLU B 196           
SHEET    3 AA8 4 TRP B 253  GLN B 260 -1  O  VAL B 256   N  VAL B 190           
SHEET    4 AA8 4 PHE B 266  ASN B 272 -1  O  LEU B 269   N  ASP B 257           
SHEET    1 AA9 3 ALA C  37  ASP C  41  0                                        
SHEET    2 AA9 3 VAL C   5  LEU C   9  1  N  VAL C   7   O  TYR C  38           
SHEET    3 AA9 3 LYS C  57  ILE C  60  1  O  PHE C  59   N  ALA C   6           
SHEET    1 AB1 4 TYR C 114  ASN C 118  0                                        
SHEET    2 AB1 4 ASP C 176  LYS C 181 -1  O  ILE C 179   N  VAL C 115           
SHEET    3 AB1 4 LEU C 141  PRO C 145 -1  N  LYS C 144   O  LEU C 178           
SHEET    4 AB1 4 SER C 155  VAL C 157 -1  O  VAL C 157   N  LEU C 141           
SHEET    1 AB2 4 GLU C 196  VAL C 197  0                                        
SHEET    2 AB2 4 GLU C 187  LEU C 193 -1  N  LEU C 193   O  GLU C 196           
SHEET    3 AB2 4 ILE C 201  GLN C 204 -1  O  ILE C 203   N  GLU C 187           
SHEET    4 AB2 4 GLN C 222  PHE C 224 -1  O  GLN C 222   N  GLN C 204           
SHEET    1 AB3 4 GLU C 196  VAL C 197  0                                        
SHEET    2 AB3 4 GLU C 187  LEU C 193 -1  N  LEU C 193   O  GLU C 196           
SHEET    3 AB3 4 TRP C 253  GLN C 260 -1  O  VAL C 258   N  PHE C 188           
SHEET    4 AB3 4 PHE C 266  ASN C 272 -1  O  GLU C 270   N  ASP C 257           
SHEET    1 AB4 3 ASP D  36  ASP D  41  0                                        
SHEET    2 AB4 3 LYS D   4  LEU D   9  1  N  VAL D   7   O  TYR D  38           
SHEET    3 AB4 3 LYS D  57  ILE D  60  1  O  PHE D  59   N  ALA D   6           
SHEET    1 AB5 4 TYR D 114  ASN D 118  0                                        
SHEET    2 AB5 4 ASP D 176  LYS D 181 -1  O  ILE D 179   N  VAL D 115           
SHEET    3 AB5 4 LEU D 141  PRO D 145 -1  N  LYS D 144   O  LEU D 178           
SHEET    4 AB5 4 SER D 155  VAL D 157 -1  O  VAL D 157   N  LEU D 141           
SHEET    1 AB6 4 GLU D 196  VAL D 197  0                                        
SHEET    2 AB6 4 GLU D 187  LEU D 193 -1  N  LEU D 193   O  GLU D 196           
SHEET    3 AB6 4 ILE D 201  GLN D 204 -1  O  ILE D 203   N  GLU D 187           
SHEET    4 AB6 4 GLN D 222  PHE D 224 -1  O  GLN D 222   N  GLN D 204           
SHEET    1 AB7 4 GLU D 196  VAL D 197  0                                        
SHEET    2 AB7 4 GLU D 187  LEU D 193 -1  N  LEU D 193   O  GLU D 196           
SHEET    3 AB7 4 TRP D 253  GLN D 260 -1  O  VAL D 258   N  PHE D 188           
SHEET    4 AB7 4 PHE D 266  ASN D 272 -1  O  LEU D 269   N  ASP D 257           
LINK         O   GLU A  68                NA    NA A 401     1555   1555  2.27  
LINK         O   SER A  91                NA    NA A 401     1555   1555  2.32  
LINK         OG1 THR A  94                NA    NA A 401     1555   1555  2.26  
LINK         OG1 THR A 273                NA    NA A 401     1555   1555  2.30  
LINK         O   GLU B  68                NA    NA B 402     1555   1555  2.21  
LINK         O   SER B  91                NA    NA B 402     1555   1555  2.23  
LINK         OG1 THR B  94                NA    NA B 402     1555   1555  2.27  
LINK         OG1 THR B 273                NA    NA B 402     1555   1555  2.22  
LINK         O   GLU C  68                NA    NA C 402     1555   1555  2.22  
LINK         O   SER C  91                NA    NA C 402     1555   1555  2.29  
LINK         OG1 THR C  94                NA    NA C 402     1555   1555  2.29  
LINK         OG1 THR C 273                NA    NA C 402     1555   1555  2.22  
LINK         O   GLU D  68                NA    NA D 404     1555   1555  2.27  
LINK         O   SER D  91                NA    NA D 404     1555   1555  2.32  
LINK         OG1 THR D  94                NA    NA D 404     1555   1555  2.27  
LINK         OG1 THR D 273                NA    NA D 404     1555   1555  2.29  
LINK        NA    NA A 401                 O   HOH A 517     1555   1555  2.26  
LINK        NA    NA B 402                 O   HOH B 512     1555   1555  2.24  
LINK        NA    NA C 402                 O   HOH C 543     1555   1555  2.30  
LINK        NA    NA C 408                 O   HOH C 575     1555   1555  2.20  
LINK         C   DAL D 402                 N   DAL D 403     1555   1555  1.33  
LINK        NA    NA D 404                 O   HOH D 508     1555   1555  2.29  
CISPEP   1 LEU A  139    PRO A  140          0        -5.78                     
CISPEP   2 GLY A  185    PRO A  186          0        -6.37                     
CISPEP   3 CYS A  225    PRO A  226          0         3.01                     
CISPEP   4 LEU B  139    PRO B  140          0        -4.73                     
CISPEP   5 GLY B  185    PRO B  186          0        -0.11                     
CISPEP   6 CYS B  225    PRO B  226          0         6.30                     
CISPEP   7 LEU C  139    PRO C  140          0        -3.26                     
CISPEP   8 GLY C  185    PRO C  186          0         2.47                     
CISPEP   9 CYS C  225    PRO C  226          0         2.90                     
CISPEP  10 LEU D  139    PRO D  140          0        -7.57                     
CISPEP  11 GLY D  185    PRO D  186          0        -3.45                     
CISPEP  12 CYS D  225    PRO D  226          0         7.06                     
SITE     1 AC1  6 GLU A  68  SER A  91  THR A  94  MET A  95                    
SITE     2 AC1  6 THR A 273  HOH A 517                                          
SITE     1 AC2  4 GLY A  11  THR A  12  THR A  42  GLY A  66                    
SITE     1 AC3  5 GLU A  77  GLN A  80  LEU A  81  TYR A  83                    
SITE     2 AC3  5 ASP A 306                                                     
SITE     1 AC4 10 LYS B  97  ILE B 142  LYS B 144  GLU B 180                    
SITE     2 AC4 10 LYS B 181  LEU B 183  GLU B 187  TYR B 210                    
SITE     3 AC4 10 MET B 259  GLU B 270                                          
SITE     1 AC5  6 GLU B  68  SER B  91  THR B  94  MET B  95                    
SITE     2 AC5  6 THR B 273  HOH B 512                                          
SITE     1 AC6  4 GLY B  11  THR B  12  THR B  42  GLY B  66                    
SITE     1 AC7 15 LYS C  97  ILE C 142  LYS C 144  GLU C 148                    
SITE     2 AC7 15 SER C 151  MET C 154  GLU C 180  LYS C 181                    
SITE     3 AC7 15 LEU C 183  GLU C 187  PHE C 209  TYR C 210                    
SITE     4 AC7 15 LYS C 215  MET C 259  GLU C 270                               
SITE     1 AC8  6 GLU C  68  SER C  91  THR C  94  MET C  95                    
SITE     2 AC8  6 THR C 273  HOH C 543                                          
SITE     1 AC9  7 ARG C 255  GLY C 276  SER C 281  LEU C 282                    
SITE     2 AC9  7 HOH C 501  HOH C 519  HOH C 533                               
SITE     1 AD1  1 ALA C 247                                                     
SITE     1 AD2  4 ASP A 306  GLN C 296  ARG C 300  HOH C 547                    
SITE     1 AD3  5 LEU C  76  GLU C  77  LEU C  81  ASP C 306                    
SITE     2 AD3  5 GOL C 407                                                     
SITE     1 AD4  6 PRO C  82  TYR C  83  GLY C  85  GLY C  87                    
SITE     2 AD4  6 ASP C 306  GOL C 406                                          
SITE     1 AD5  4 HIS A 265  HOH A 507  HIS C 280  HOH C 575                    
SITE     1 AD6 14 LYS D  97  ILE D 142  LYS D 144  GLU D 148                    
SITE     2 AD6 14 GLU D 180  LYS D 181  TRP D 182  LEU D 183                    
SITE     3 AD6 14 GLU D 187  PHE D 209  TYR D 210  MET D 259                    
SITE     4 AD6 14 GLU D 270  HOH D 527                                          
SITE     1 AD7  6 GLU D  68  SER D  91  THR D  94  MET D  95                    
SITE     2 AD7  6 THR D 273  HOH D 508                                          
SITE     1 AD8 11 TYR D 210  LYS D 215  TYR D 216  ARG D 255                    
SITE     2 AD8 11 ASN D 272  PRO D 275  GLY D 276  SER D 281                    
SITE     3 AD8 11 LEU D 282  HOH D 505  HOH D 506                               
CRYST1   62.670  106.545  211.103  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      0.015957  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009386  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004737        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system