GenomeNet

Database: PDB
Entry: 5EWU
LinkDB: 5EWU
Original site: 5EWU 
HEADER    LIGASE                                  21-NOV-15   5EWU              
TITLE     CRYSTAL STRUCTURE OF THE ARABIDOPSIS THALIANA C-TERMINAL CHLH AT 1.25A
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAGNESIUM-CHELATASE SUBUNIT CHLH, CHLOROPLASTIC;           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 994-1381;                                     
COMPND   5 SYNONYM: MG-CHELATASE SUBUNIT H,ABA-BINDING PROTEIN,MG-PROTOPORPHYRIN
COMPND   6 IX CHELATASE SUBUNIT CHLH,PROTEIN CONDITIONAL CHLORINA,PROTEIN       
COMPND   7 GENOMES UNCOUPLED 5,PROTEIN RAPID TRANSPIRATION IN DETACHED LEAVES 1;
COMPND   8 EC: 6.6.1.1;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: CHLH, ABAR, CCH, GUN5, RTL1, AT5G13630, MSH12.9;               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    MG-CHELATASE, GUN5, METAL BINDING PROTEIN, MAGNESIUM-CHELATASE        
KEYWDS   2 SUBUNIT CHLH, ABAR, CCH, RTL1, LIGASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHEN,X.ZHANG,Y.LIU,L.JIANG                                          
REVDAT   3   20-MAR-24 5EWU    1       LINK                                     
REVDAT   2   19-FEB-20 5EWU    1       REMARK                                   
REVDAT   1   07-DEC-16 5EWU    0                                                
JRNL        AUTH   Z.CHEN,X.ZHANG,Y.LIU,L.JIANG                                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE ARABIDOPSIS THALIANA C-TERMINAL     
JRNL        TITL 2 CHLH AT 1.25A                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 159967                         
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) : 0.170                           
REMARK   3   R VALUE            (WORKING SET) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8308                            
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) : 1.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5972                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 45.38                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 310                          
REMARK   3   BIN FREE R VALUE                    : 0.3460                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5843                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 23                                      
REMARK   3   SOLVENT ATOMS            : 1228                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.20000                                              
REMARK   3    B22 (A**2) : 1.04000                                              
REMARK   3    B33 (A**2) : -0.67000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.85000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.061         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.051         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.029         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.458         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.962                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6026 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8178 ; 1.154 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   779 ; 5.363 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   262 ;34.233 ;24.771       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1039 ;11.684 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    37 ;16.331 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   934 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4529 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  3822 ; 0.882 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6144 ; 1.544 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2204 ; 2.183 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2024 ; 3.378 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  6026 ; 0.919 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
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   : 1.40                                          
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 5EWU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000215602.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : AR-NE3A                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 168362                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.250                              
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     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 45.0000                            
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 37.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, NACL, PH 7, VAPOR DIFFUSION,        
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.38800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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  1377                                                      
REMARK 465     GLY A  1378                                                      
REMARK 465     ILE A  1379                                                      
REMARK 465     ASP A  1380                                                      
REMARK 465     ARG A  1381                                                      
REMARK 465     GLN B   994                                                      
REMARK 465     PRO B  1186                                                      
REMARK 465     GLU B  1373                                                      
REMARK 465     ASP B  1374                                                      
REMARK 465     LYS B  1375                                                      
REMARK 465     ILE B  1376                                                      
REMARK 465     GLU B  1377                                                      
REMARK 465     GLY B  1378                                                      
REMARK 465     ILE B  1379                                                      
REMARK 465     ASP B  1380                                                      
REMARK 465     ARG B  1381                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 994    CD   OE1  NE2                                       
REMARK 470     GLU A1010    CD   OE1  OE2                                       
REMARK 470     ARG A1011    NH1  NH2                                            
REMARK 470     GLU A1014    CG   CD   OE1  OE2                                  
REMARK 470     ASN A1020    CG   OD1  ND2                                       
REMARK 470     GLU A1068    CD   OE1  OE2                                       
REMARK 470     GLU A1073    OE2                                                 
REMARK 470     GLU A1159    OE2                                                 
REMARK 470     ASN A1164    CG   OD1  ND2                                       
REMARK 470     LYS A1193    NZ                                                  
REMARK 470     GLU A1215    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1238    CG   CD   CE   NZ                                   
REMARK 470     LYS A1241    CG   CD   CE   NZ                                   
REMARK 470     ASN A1254    CG   OD1  ND2                                       
REMARK 470     GLN A1256    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1262    CD   OE1  OE2                                       
REMARK 470     LEU A1266    CD1  CD2                                            
REMARK 470     LYS A1276    CD   CE   NZ                                        
REMARK 470     ARG A1290    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A1326    OE1  OE2                                            
REMARK 470     ASN A1337    ND2                                                 
REMARK 470     ARG A1340    CZ   NH1  NH2                                       
REMARK 470     GLN A1344    CG   CD   OE1  NE2                                  
REMARK 470     GLU A1363    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1375    NZ                                                  
REMARK 470     ARG B1055    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1063    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B1068    CD   OE1  OE2                                       
REMARK 470     ARG B1103    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B1159    CG   CD   OE1  OE2                                  
REMARK 470     GLN B1195    CD   OE1  NE2                                       
REMARK 470     GLU B1215    CD   OE1  OE2                                       
REMARK 470     ARG B1269    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU B1287    CD   OE1  OE2                                       
REMARK 470     ARG B1290    NH2                                                 
REMARK 470     LYS B1294    CE   NZ                                             
REMARK 470     GLN B1323    CD   OE1  NE2                                       
REMARK 470     GLU B1325    CG   CD   OE1  OE2                                  
REMARK 470     GLU B1326    CG   CD   OE1  OE2                                  
REMARK 470     ASN B1329    OD1                                                 
REMARK 470     MET B1332    CG   SD   CE                                        
REMARK 470     ASN B1337    OD1  ND2                                            
REMARK 470     ARG B1340    CZ   NH1  NH2                                       
REMARK 470     GLN B1344    CG   CD   OE1  NE2                                  
REMARK 470     ASP B1356    CG   OD1  OD2                                       
REMARK 470     GLU B1360    CG   CD   OE1  OE2                                  
REMARK 470     ILE B1362    CG1  CD1                                            
REMARK 470     GLU B1363    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1364    CG   CD   CE   NZ                                   
REMARK 470     LYS B1366    CG   CD   CE   NZ                                   
REMARK 470     GLU B1367    CG   CD   OE1  OE2                                  
REMARK 470     LEU B1368    CG   CD1  CD2                                       
REMARK 470     SER B1370    OG                                                  
REMARK 470     GLN B1371    CG   CD   OE1  NE2                                  
REMARK 470     VAL B1372    CG1  CG2                                            
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    HOH A  1502     O    HOH B  1538              2.00            
REMARK 500   O    HOH A  2104     O    HOH A  2120              2.03            
REMARK 500   OD1  ASP A  1134     O    HOH A  1501              2.04            
REMARK 500   O    HOH A  2070     O    HOH A  2120              2.06            
REMARK 500   CE   MET B  1327     O    HOH B  1953              2.11            
REMARK 500   O    HOH A  2070     O    HOH A  2099              2.11            
REMARK 500   O    HOH A  1502     O    HOH A  1856              2.13            
REMARK 500   O    HOH A  1506     O    HOH A  1868              2.13            
REMARK 500   O    HOH A  1502     O    HOH B  1524              2.13            
REMARK 500   O    HOH A  1502     O    HOH B  1784              2.17            
REMARK 500   O    HOH A  1503     O    HOH A  1614              2.17            
REMARK 500   O    HOH B  1693     O    HOH B  1907              2.18            
REMARK 500   O    HOH B  1837     O    HOH B  1874              2.19            
REMARK 500   O    HOH B  1579     O    HOH B  1793              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    THR B  1060     NE2  GLN B  1168     2656     2.08            
REMARK 500   OE2  GLU A  1367     O    HOH A  1501     1455     2.11            
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    MET B1199   CG  -  SD  -  CE  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ASP B1324   N   -  CA  -  C   ANGL. DEV. = -18.9 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    SER A1151      165.11     76.37                                   
REMARK 500    ASN A1153       19.35     59.33                                   
REMARK 500    LYS A1271      -94.83   -118.44                                   
REMARK 500    ASN A1335       83.20   -151.92                                   
REMARK 500    ALA B1139       43.70    -84.39                                   
REMARK 500    SER B1151      165.42     77.12                                   
REMARK 500    ASN B1153       17.06     58.48                                   
REMARK 500    SER B1162       58.10    -95.44                                   
REMARK 500    LYS B1271      -94.82   -117.72                                   
REMARK 500    ASN B1335       83.08   -156.87                                   
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 GLN B 1323     ASP B 1324                  141.18                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2114        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A2115        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A2116        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH A2117        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A2118        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH A2119        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A2120        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH A2121        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH A2122        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH A2123        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A2124        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A2125        DISTANCE =  6.94 ANGSTROMS                       
REMARK 525    HOH A2126        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A2127        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH A2128        DISTANCE =  7.39 ANGSTROMS                       
REMARK 525    HOH A2129        DISTANCE =  7.45 ANGSTROMS                       
REMARK 525    HOH A2130        DISTANCE =  7.51 ANGSTROMS                       
REMARK 525    HOH A2131        DISTANCE =  7.82 ANGSTROMS                       
REMARK 525    HOH A2132        DISTANCE =  7.92 ANGSTROMS                       
REMARK 525    HOH A2133        DISTANCE =  8.76 ANGSTROMS                       
REMARK 525    HOH A2134        DISTANCE =  8.79 ANGSTROMS                       
REMARK 525    HOH B2062        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B2063        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH B2064        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH B2065        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH B2066        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH B2067        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B2068        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH B2069        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B2070        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH B2071        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH B2072        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH B2073        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH B2074        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH B2075        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH B2076        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH B2077        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH B2078        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH B2079        DISTANCE =  6.63 ANGSTROMS                       
REMARK 525    HOH B2080        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH B2081        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH B2082        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH B2083        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH B2084        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH B2085        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH B2086        DISTANCE =  7.74 ANGSTROMS                       
REMARK 525    HOH B2087        DISTANCE =  7.75 ANGSTROMS                       
REMARK 525    HOH B2088        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH B2089        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH B2090        DISTANCE =  8.48 ANGSTROMS                       
REMARK 525    HOH B2091        DISTANCE =  8.57 ANGSTROMS                       
REMARK 525    HOH B2092        DISTANCE =  9.49 ANGSTROMS                       
REMARK 525    HOH B2093        DISTANCE =  9.66 ANGSTROMS                       
REMARK 525    HOH B2094        DISTANCE =  9.97 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A1040   OG1                                                    
REMARK 620 2 SER A1044   OG  137.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1603   O                                                      
REMARK 620 2 HOH A1868   O   130.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ B 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 1404                 
DBREF  5EWU A  994  1381  UNP    Q9FNB0   CHLH_ARATH     994   1381             
DBREF  5EWU B  994  1381  UNP    Q9FNB0   CHLH_ARATH     994   1381             
SEQRES   1 A  388  GLN ALA ILE PRO THR THR ALA ALA MET ALA SER ALA LYS          
SEQRES   2 A  388  ILE VAL VAL GLU ARG LEU VAL GLU ARG GLN LYS LEU GLU          
SEQRES   3 A  388  ASN GLU GLY LYS TYR PRO GLU THR ILE ALA LEU VAL LEU          
SEQRES   4 A  388  TRP GLY THR ASP ASN ILE LYS THR TYR GLY GLU SER LEU          
SEQRES   5 A  388  GLY GLN VAL LEU TRP MET ILE GLY VAL ARG PRO ILE ALA          
SEQRES   6 A  388  ASP THR PHE GLY ARG VAL ASN ARG VAL GLU PRO VAL SER          
SEQRES   7 A  388  LEU GLU GLU LEU GLY ARG PRO ARG ILE ASP VAL VAL VAL          
SEQRES   8 A  388  ASN CYS SER GLY VAL PHE ARG ASP LEU PHE ILE ASN GLN          
SEQRES   9 A  388  MET ASN LEU LEU ASP ARG ALA ILE LYS MET VAL ALA GLU          
SEQRES  10 A  388  LEU ASP GLU PRO VAL GLU GLN ASN PHE VAL ARG LYS HIS          
SEQRES  11 A  388  ALA LEU GLU GLN ALA GLU ALA LEU GLY ILE ASP ILE ARG          
SEQRES  12 A  388  GLU ALA ALA THR ARG VAL PHE SER ASN ALA SER GLY SER          
SEQRES  13 A  388  TYR SER ALA ASN ILE SER LEU ALA VAL GLU ASN SER SER          
SEQRES  14 A  388  TRP ASN ASP GLU LYS GLN LEU GLN ASP MET TYR LEU SER          
SEQRES  15 A  388  ARG LYS SER PHE ALA PHE ASP SER ASP ALA PRO GLY ALA          
SEQRES  16 A  388  GLY MET ALA GLU LYS LYS GLN VAL PHE GLU MET ALA LEU          
SEQRES  17 A  388  SER THR ALA GLU VAL THR PHE GLN ASN LEU ASP SER SER          
SEQRES  18 A  388  GLU ILE SER LEU THR ASP VAL SER HIS TYR PHE ASP SER          
SEQRES  19 A  388  ASP PRO THR ASN LEU VAL GLN SER LEU ARG LYS ASP LYS          
SEQRES  20 A  388  LYS LYS PRO SER SER TYR ILE ALA ASP THR THR THR ALA          
SEQRES  21 A  388  ASN ALA GLN VAL ARG THR LEU SER GLU THR VAL ARG LEU          
SEQRES  22 A  388  ASP ALA ARG THR LYS LEU LEU ASN PRO LYS TRP TYR GLU          
SEQRES  23 A  388  GLY MET MET SER SER GLY TYR GLU GLY VAL ARG GLU ILE          
SEQRES  24 A  388  GLU LYS ARG LEU SER ASN THR VAL GLY TRP SER ALA THR          
SEQRES  25 A  388  SER GLY GLN VAL ASP ASN TRP VAL TYR GLU GLU ALA ASN          
SEQRES  26 A  388  SER THR PHE ILE GLN ASP GLU GLU MET LEU ASN ARG LEU          
SEQRES  27 A  388  MET ASN THR ASN PRO ASN SER PHE ARG LYS MET LEU GLN          
SEQRES  28 A  388  THR PHE LEU GLU ALA ASN GLY ARG GLY TYR TRP ASP THR          
SEQRES  29 A  388  SER ALA GLU ASN ILE GLU LYS LEU LYS GLU LEU TYR SER          
SEQRES  30 A  388  GLN VAL GLU ASP LYS ILE GLU GLY ILE ASP ARG                  
SEQRES   1 B  388  GLN ALA ILE PRO THR THR ALA ALA MET ALA SER ALA LYS          
SEQRES   2 B  388  ILE VAL VAL GLU ARG LEU VAL GLU ARG GLN LYS LEU GLU          
SEQRES   3 B  388  ASN GLU GLY LYS TYR PRO GLU THR ILE ALA LEU VAL LEU          
SEQRES   4 B  388  TRP GLY THR ASP ASN ILE LYS THR TYR GLY GLU SER LEU          
SEQRES   5 B  388  GLY GLN VAL LEU TRP MET ILE GLY VAL ARG PRO ILE ALA          
SEQRES   6 B  388  ASP THR PHE GLY ARG VAL ASN ARG VAL GLU PRO VAL SER          
SEQRES   7 B  388  LEU GLU GLU LEU GLY ARG PRO ARG ILE ASP VAL VAL VAL          
SEQRES   8 B  388  ASN CYS SER GLY VAL PHE ARG ASP LEU PHE ILE ASN GLN          
SEQRES   9 B  388  MET ASN LEU LEU ASP ARG ALA ILE LYS MET VAL ALA GLU          
SEQRES  10 B  388  LEU ASP GLU PRO VAL GLU GLN ASN PHE VAL ARG LYS HIS          
SEQRES  11 B  388  ALA LEU GLU GLN ALA GLU ALA LEU GLY ILE ASP ILE ARG          
SEQRES  12 B  388  GLU ALA ALA THR ARG VAL PHE SER ASN ALA SER GLY SER          
SEQRES  13 B  388  TYR SER ALA ASN ILE SER LEU ALA VAL GLU ASN SER SER          
SEQRES  14 B  388  TRP ASN ASP GLU LYS GLN LEU GLN ASP MET TYR LEU SER          
SEQRES  15 B  388  ARG LYS SER PHE ALA PHE ASP SER ASP ALA PRO GLY ALA          
SEQRES  16 B  388  GLY MET ALA GLU LYS LYS GLN VAL PHE GLU MET ALA LEU          
SEQRES  17 B  388  SER THR ALA GLU VAL THR PHE GLN ASN LEU ASP SER SER          
SEQRES  18 B  388  GLU ILE SER LEU THR ASP VAL SER HIS TYR PHE ASP SER          
SEQRES  19 B  388  ASP PRO THR ASN LEU VAL GLN SER LEU ARG LYS ASP LYS          
SEQRES  20 B  388  LYS LYS PRO SER SER TYR ILE ALA ASP THR THR THR ALA          
SEQRES  21 B  388  ASN ALA GLN VAL ARG THR LEU SER GLU THR VAL ARG LEU          
SEQRES  22 B  388  ASP ALA ARG THR LYS LEU LEU ASN PRO LYS TRP TYR GLU          
SEQRES  23 B  388  GLY MET MET SER SER GLY TYR GLU GLY VAL ARG GLU ILE          
SEQRES  24 B  388  GLU LYS ARG LEU SER ASN THR VAL GLY TRP SER ALA THR          
SEQRES  25 B  388  SER GLY GLN VAL ASP ASN TRP VAL TYR GLU GLU ALA ASN          
SEQRES  26 B  388  SER THR PHE ILE GLN ASP GLU GLU MET LEU ASN ARG LEU          
SEQRES  27 B  388  MET ASN THR ASN PRO ASN SER PHE ARG LYS MET LEU GLN          
SEQRES  28 B  388  THR PHE LEU GLU ALA ASN GLY ARG GLY TYR TRP ASP THR          
SEQRES  29 B  388  SER ALA GLU ASN ILE GLU LYS LEU LYS GLU LEU TYR SER          
SEQRES  30 B  388  GLN VAL GLU ASP LYS ILE GLU GLY ILE ASP ARG                  
HET    BEZ  A1401       9                                                       
HET     MG  A1402       1                                                       
HET     MG  A1403       1                                                       
HET    BEZ  B1401       9                                                       
HET     MG  B1402       1                                                       
HET     MG  B1403       1                                                       
HET     MG  B1404       1                                                       
HETNAM     BEZ BENZOIC ACID                                                     
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  BEZ    2(C7 H6 O2)                                                  
FORMUL   4   MG    5(MG 2+)                                                     
FORMUL  10  HOH   *1228(H2 O)                                                   
HELIX    1 AA1 THR A  998  ASN A 1020  1                                  23    
HELIX    2 AA2 TRP A 1033  TYR A 1041  1                                   9    
HELIX    3 AA3 GLY A 1042  GLY A 1053  1                                  12    
HELIX    4 AA4 SER A 1071  GLY A 1076  1                                   6    
HELIX    5 AA5 SER A 1087  PHE A 1094  1                                   8    
HELIX    6 AA6 PHE A 1094  GLU A 1110  1                                  17    
HELIX    7 AA7 PRO A 1114  GLN A 1117  5                                   4    
HELIX    8 AA8 ASN A 1118  GLY A 1132  1                                  15    
HELIX    9 AA9 ASP A 1134  ALA A 1139  1                                   6    
HELIX   10 AB1 ASN A 1153  SER A 1161  1                                   9    
HELIX   11 AB2 ASP A 1165  SER A 1178  1                                  14    
HELIX   12 AB3 ALA A 1185  GLY A 1189  5                                   5    
HELIX   13 AB4 LYS A 1193  THR A 1203  1                                  11    
HELIX   14 AB5 SER A 1222  ASP A 1228  1                                   7    
HELIX   15 AB6 PRO A 1229  ARG A 1237  1                                   9    
HELIX   16 AB7 LEU A 1260  LYS A 1271  1                                  12    
HELIX   17 AB8 ASN A 1274  SER A 1284  1                                  11    
HELIX   18 AB9 SER A 1284  GLY A 1307  1                                  24    
HELIX   19 AC1 ASP A 1310  ILE A 1322  1                                  13    
HELIX   20 AC2 ASP A 1324  ASN A 1335  1                                  12    
HELIX   21 AC3 ASN A 1335  ARG A 1352  1                                  18    
HELIX   22 AC4 SER A 1358  ILE A 1376  1                                  19    
HELIX   23 AC5 THR B  998  ASN B 1020  1                                  23    
HELIX   24 AC6 TRP B 1033  TYR B 1041  1                                   9    
HELIX   25 AC7 GLY B 1042  GLY B 1053  1                                  12    
HELIX   26 AC8 SER B 1071  GLY B 1076  1                                   6    
HELIX   27 AC9 SER B 1087  PHE B 1094  1                                   8    
HELIX   28 AD1 PHE B 1094  GLU B 1110  1                                  17    
HELIX   29 AD2 PRO B 1114  GLN B 1117  5                                   4    
HELIX   30 AD3 ASN B 1118  GLY B 1132  1                                  15    
HELIX   31 AD4 ASP B 1134  ALA B 1139  1                                   6    
HELIX   32 AD5 ASN B 1153  SER B 1161  1                                   9    
HELIX   33 AD6 ASP B 1165  LYS B 1177  1                                  13    
HELIX   34 AD7 LYS B 1193  THR B 1203  1                                  11    
HELIX   35 AD8 SER B 1222  SER B 1227  1                                   6    
HELIX   36 AD9 PRO B 1229  ARG B 1237  1                                   9    
HELIX   37 AE1 LEU B 1260  LYS B 1271  1                                  12    
HELIX   38 AE2 ASN B 1274  SER B 1283  1                                  10    
HELIX   39 AE3 GLY B 1285  GLY B 1307  1                                  23    
HELIX   40 AE4 ASP B 1310  ILE B 1322  1                                  13    
HELIX   41 AE5 GLU B 1325  ASN B 1335  1                                  11    
HELIX   42 AE6 ASN B 1335  ARG B 1352  1                                  18    
HELIX   43 AE7 SER B 1358  VAL B 1372  1                                  15    
SHEET    1 AA1 8 ALA A1191  GLU A1192  0                                        
SHEET    2 AA1 8 PHE A1179  ALA A1180 -1  N  ALA A1180   O  ALA A1191           
SHEET    3 AA1 8 VAL A1142  SER A1144 -1  N  SER A1144   O  PHE A1179           
SHEET    4 AA1 8 ASP A1081  CYS A1086  1  N  CYS A1086   O  PHE A1143           
SHEET    5 AA1 8 THR A1027  LEU A1032  1  N  LEU A1030   O  VAL A1083           
SHEET    6 AA1 8 VAL A1206  LEU A1211  1  O  VAL A1206   N  ALA A1029           
SHEET    7 AA1 8 SER A1244  ASP A1249  1  O  ALA A1248   N  LEU A1211           
SHEET    8 AA1 8 GLN A1256  THR A1259 -1  O  GLN A1256   N  ASP A1249           
SHEET    1 AA2 2 VAL A1054  ALA A1058  0                                        
SHEET    2 AA2 2 VAL A1064  PRO A1069 -1  O  GLU A1068   N  ARG A1055           
SHEET    1 AA3 8 ALA B1191  GLU B1192  0                                        
SHEET    2 AA3 8 PHE B1179  ALA B1180 -1  N  ALA B1180   O  ALA B1191           
SHEET    3 AA3 8 VAL B1142  SER B1144 -1  N  SER B1144   O  PHE B1179           
SHEET    4 AA3 8 ASP B1081  CYS B1086  1  N  CYS B1086   O  PHE B1143           
SHEET    5 AA3 8 THR B1027  LEU B1032  1  N  LEU B1030   O  VAL B1083           
SHEET    6 AA3 8 VAL B1206  LEU B1211  1  O  VAL B1206   N  ALA B1029           
SHEET    7 AA3 8 SER B1244  ASP B1249  1  O  ALA B1248   N  LEU B1211           
SHEET    8 AA3 8 GLN B1256  THR B1259 -1  O  GLN B1256   N  ASP B1249           
SHEET    1 AA4 2 VAL B1054  ALA B1058  0                                        
SHEET    2 AA4 2 VAL B1064  PRO B1069 -1  O  ARG B1066   N  ILE B1057           
LINK         OG1 THR A1040                MG    MG A1403     1555   1555  2.96  
LINK         OG  SER A1044                MG    MG A1403     1555   1555  2.99  
LINK        MG    MG A1402                 O   HOH A1603     1555   1555  2.99  
LINK        MG    MG A1402                 O   HOH A1868     1555   1555  2.41  
LINK         OG  SER B1044                MG    MG B1403     1555   1555  2.97  
LINK        MG    MG B1402                 O   HOH B1805     1555   1555  2.38  
LINK        MG    MG B1404                 O   HOH B1879     1555   1555  2.82  
CISPEP   1 ILE A  996    PRO A  997          0        -7.08                     
CISPEP   2 ILE B  996    PRO B  997          0         3.11                     
SITE     1 AC1  7 TRP A1033  GLY A1034  THR A1035  SER A1087                    
SITE     2 AC1  7 VAL A1089  HIS A1223  HOH A1506                               
SITE     1 AC2  4 GLY A1088  SER A1151  HOH A1603  HOH A1868                    
SITE     1 AC3  3 ASP A1036  THR A1040  SER A1044                               
SITE     1 AC4  8 TRP B1033  GLY B1034  THR B1035  SER B1087                    
SITE     2 AC4  8 VAL B1089  HIS B1223  HOH B1694  HOH B1805                    
SITE     1 AC5  5 GLY B1088  SER B1151  HOH B1563  HOH B1805                    
SITE     2 AC5  5 HOH B1920                                                     
SITE     1 AC6  3 ASP B1036  THR B1040  SER B1044                               
SITE     1 AC7  4 ARG B1015  ARG B1258  THR B1259  HOH B1879                    
CRYST1   69.099   72.776   72.911  90.00 109.76  90.00 P 1 21 1      4          
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      0.014472  0.000000  0.005200        0.00000                         
SCALE2      0.000000  0.013741  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014574        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system