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Database: PDB
Entry: 4ZQI
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Original site: 4ZQI 
HEADER    LIGASE                                  10-MAY-15   4ZQI              
TITLE     CRYSTAL STRUCTURE OF APO D-ALANINE-D-ALANINE LIGASE(DDL) FROM YERSINIA
TITLE    2 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;                                                     
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APO, LIGASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-T.TRAN,L.-W.KANG,M.-K.HONG,H.P.T.NGO,K.H.HUYNH,Y.J.AHN             
REVDAT   1   13-JAN-16 4ZQI    0                                                
JRNL        AUTH   H.-T.TRAN,M.-K.HONG,H.-P.-T.NGO,K.-H.HUYNH,Y.-J.AHN,Z.WANG,  
JRNL        AUTH 2 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.,SECT.D      V.  72    12 2016              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        DOI    10.1107/S2059798315021671                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.41                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 55129                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2970                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3864                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 212                          
REMARK   3   BIN FREE R VALUE                    : 0.3580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8970                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5                                       
REMARK   3   SOLVENT ATOMS            : 156                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.02000                                              
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): 0.346         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.245         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.154         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.261         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9157 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8844 ; 0.008 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12393 ; 1.570 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20390 ; 1.270 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1171 ; 5.956 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   371 ;36.570 ;25.040       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1551 ;15.553 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;21.497 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1427 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10320 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1932 ; 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):  4714 ; 3.880 ; 4.240       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4713 ; 3.879 ; 4.240       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5875 ; 5.498 ; 6.337       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5876 ; 5.498 ; 6.338       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4443 ; 5.077 ; 4.963       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4440 ; 5.078 ; 4.964       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6518 ; 7.776 ; 7.179       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  9798 ; 9.476 ;33.759       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9798 ; 9.476 ;33.760       
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   17220  0.09  0.05     
REMARK   3    2     A     1    306       C     1    306   17414  0.09  0.05     
REMARK   3    3     A     1    306       D     1    306   16969  0.10  0.05     
REMARK   3    4     B     1    306       C     1    306   17370  0.09  0.05     
REMARK   3    5     B     1    306       D     1    306   17384  0.09  0.05     
REMARK   3    6     C     1    306       D     1    306   17349  0.09  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 4ZQI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209682.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-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) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : DCM SI (111) CRYSTAL               
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   : 66609                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
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                : 14.60                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OBLIQUE-PILLAR SHAPED CRYSTAL                                
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM ACETATE, 0.1 M BIS-TRIS,    
REMARK 280  29% PEG 8000, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE    
REMARK 280  287.0K                                                              
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       31.49650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.50150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.51350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.50150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.49650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.51350            
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: 2430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 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: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26270 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 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     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     GLY B   149                                                      
REMARK 465     SER B   150                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     VAL B   208                                                      
REMARK 465     PHE B   209                                                      
REMARK 465     TYR B   210                                                      
REMARK 465     ASP B   211                                                      
REMARK 465     TYR B   212                                                      
REMARK 465     ASP B   213                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     LYS B   215                                                      
REMARK 465     TYR B   216                                                      
REMARK 465     LEU B   217                                                      
REMARK 465     SER B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     LYS B   220                                                      
REMARK 465     SER D   150                                                      
REMARK 465     SER D   151                                                      
REMARK 465     VAL D   208                                                      
REMARK 465     PHE D   209                                                      
REMARK 465     TYR D   210                                                      
REMARK 465     ASP D   211                                                      
REMARK 465     TYR D   212                                                      
REMARK 465     ASP D   213                                                      
REMARK 465     ALA D   214                                                      
REMARK 465     LYS D   215                                                      
REMARK 465     TYR D   216                                                      
REMARK 465     LEU D   217                                                      
REMARK 465     SER D   218                                                      
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    SER C 151        8.93     80.38                                   
REMARK 500    ASP C 211     -169.34   -104.18                                   
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    75.1                                              
REMARK 620 3 THR A  94   OG1 144.5  71.8                                        
REMARK 620 4 THR A 273   OG1  86.0 114.3  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  68   O                                                      
REMARK 620 2 SER B  91   O    78.9                                              
REMARK 620 3 THR B  94   OG1 153.0  75.5                                        
REMARK 620 4 THR B 273   OG1  85.7 118.5  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C  68   O                                                      
REMARK 620 2 SER C  91   O    79.8                                              
REMARK 620 3 THR C  94   OG1 156.8  78.0                                        
REMARK 620 4 THR C 273   OG1  87.4 122.2  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D 401  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D  68   O                                                      
REMARK 620 2 SER D  91   O    78.3                                              
REMARK 620 3 THR D  94   OG1 152.5  76.3                                        
REMARK 620 4 THR D 273   OG1  85.9 117.3  96.5                                  
REMARK 620 5 HOH D 508   O   116.4 155.9  91.0  84.1                            
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 NA B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 401                  
DBREF  4ZQI A    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  4ZQI B    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  4ZQI C    1   306  UNP    Q8ZIE7   DDL_YERPE        1    306             
DBREF  4ZQI 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     NA  B 401       1                                                       
HET     NA  B 402       1                                                       
HET     NA  C 401       1                                                       
HET     NA  D 401       1                                                       
HETNAM      NA SODIUM ION                                                       
FORMUL   5   NA    5(NA 1+)                                                     
FORMUL  10  HOH   *156(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  VAL A  134  1                                   9    
HELIX    8 AA8 ALA A  135  GLY A  138  5                                   4    
HELIX    9 AA9 HIS A  159  SER A  161  5                                   3    
HELIX   10 AB1 GLU A  162  PHE A  171  1                                  10    
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  LEU B  125  1                                   7    
HELIX   20 AC2 SER B  126  ALA B  135  1                                  10    
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  VAL C  134  1                                   9    
HELIX   34 AD7 ALA C  135  GLY C  138  5                                   4    
HELIX   35 AD8 HIS C  159  SER C  161  5                                   3    
HELIX   36 AD9 GLU C  162  PHE C  171  1                                  10    
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  VAL D  134  1                                   9    
HELIX   48 AF3 ALA D  135  GLY D  138  5                                   4    
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 SER D  230  LEU D  248  1                                  19    
HELIX   52 AF7 SER D  281  GLY D  291  1                                  11    
HELIX   53 AF8 SER D  293  LEU D  304  1                                  12    
SHEET    1 AA1 3 ASP A  36  ASP A  41  0                                        
SHEET    2 AA1 3 LYS A   4  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 256   N  VAL A 190           
SHEET    4 AA4 4 PHE A 266  ASN A 272 -1  O  GLU A 270   N  ASP A 257           
SHEET    1 AA5 3 ALA B  37  ASP B  41  0                                        
SHEET    2 AA5 3 VAL B   5  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  GLU B 270   N  ASP B 257           
SHEET    1 AA9 3 ASP C  36  ASP C  41  0                                        
SHEET    2 AA9 3 LYS C   4  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  ILE C 142   O  GLU C 180           
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  PHE C 224   N  ARG C 202           
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 256   N  VAL C 190           
SHEET    4 AB3 4 PHE C 266  ASN C 272 -1  O  GLU C 270   N  ASP C 257           
SHEET    1 AB4 3 ALA D  37  ASP D  41  0                                        
SHEET    2 AB4 3 VAL D   5  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 256   N  VAL D 190           
SHEET    4 AB7 4 PHE D 266  ASN D 272 -1  O  GLU D 270   N  ASP D 257           
LINK         O   GLU A  68                NA    NA A 401     1555   1555  2.25  
LINK         O   SER A  91                NA    NA A 401     1555   1555  2.33  
LINK         OG1 THR A  94                NA    NA A 401     1555   1555  2.31  
LINK         OG1 THR A 273                NA    NA A 401     1555   1555  2.27  
LINK         O   GLU B  68                NA    NA B 401     1555   1555  2.24  
LINK         O   SER B  91                NA    NA B 401     1555   1555  2.27  
LINK         OG1 THR B  94                NA    NA B 401     1555   1555  2.27  
LINK         OG1 THR B 273                NA    NA B 401     1555   1555  2.31  
LINK         O   GLU C  68                NA    NA C 401     1555   1555  2.23  
LINK         O   SER C  91                NA    NA C 401     1555   1555  2.21  
LINK         OG1 THR C  94                NA    NA C 401     1555   1555  2.26  
LINK         OG1 THR C 273                NA    NA C 401     1555   1555  2.27  
LINK         O   GLU D  68                NA    NA D 401     1555   1555  2.26  
LINK         O   SER D  91                NA    NA D 401     1555   1555  2.27  
LINK         OG1 THR D  94                NA    NA D 401     1555   1555  2.29  
LINK         OG1 THR D 273                NA    NA D 401     1555   1555  2.29  
LINK        NA    NA D 401                 O   HOH D 508     1555   1555  2.29  
CISPEP   1 LEU A  139    PRO A  140          0        -6.82                     
CISPEP   2 GLY A  185    PRO A  186          0         1.10                     
CISPEP   3 CYS A  225    PRO A  226          0         5.60                     
CISPEP   4 LEU B  139    PRO B  140          0        -9.70                     
CISPEP   5 GLY B  185    PRO B  186          0        -1.87                     
CISPEP   6 CYS B  225    PRO B  226          0         2.61                     
CISPEP   7 LEU C  139    PRO C  140          0        -3.97                     
CISPEP   8 GLY C  185    PRO C  186          0         0.19                     
CISPEP   9 CYS C  225    PRO C  226          0         3.73                     
CISPEP  10 LEU D  139    PRO D  140          0        -7.19                     
CISPEP  11 GLY D  185    PRO D  186          0        -0.80                     
CISPEP  12 CYS D  225    PRO D  226          0         4.13                     
SITE     1 AC1  5 GLU A  68  SER A  91  THR A  94  MET A  95                    
SITE     2 AC1  5 THR A 273                                                     
SITE     1 AC2  5 GLU B  68  SER B  91  THR B  94  MET B  95                    
SITE     2 AC2  5 THR B 273                                                     
SITE     1 AC3  2 HIS B 265  HIS C 280                                          
SITE     1 AC4  5 GLU C  68  SER C  91  THR C  94  MET C  95                    
SITE     2 AC4  5 THR C 273                                                     
SITE     1 AC5  6 GLU D  68  SER D  91  THR D  94  MET D  95                    
SITE     2 AC5  6 THR D 273  HOH D 508                                          
CRYST1   62.993  107.027  211.003  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      0.015875  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009343  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004739        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system