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Database: PDB
Entry: 3HHP
LinkDB: 3HHP
Original site: 3HHP 
HEADER    OXIDOREDUCTASE                          15-MAY-09   3HHP              
TITLE     MALATE DEHYDROGENASE OPEN CONFORMATION                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MALATE DEHYDROGENASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.1.1.37;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 GENE: MDH, B3236, JW3205;                                            
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    MALATE DEHYDROGENASE, MDH, CITRIC ACID CYCLE, TCA CYCLE, NAD,         
KEYWDS   2 OXIDOREDUCTASE, TRICARBOXYLIC ACID CYCLE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZAITSEVA,K.M.MENEELY,A.L.LAMB                                       
REVDAT   2   21-FEB-24 3HHP    1       REMARK                                   
REVDAT   1   22-SEP-09 3HHP    0                                                
JRNL        AUTH   J.ZAITSEVA,K.M.MENEELY,A.L.LAMB                              
JRNL        TITL   STRUCTURE OF ESCHERICHIA COLI MALATE DEHYDROGENASE AT 1.45 A 
JRNL        TITL 2 RESOLUTION.                                                  
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  65   866 2009              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   19724119                                                     
JRNL        DOI    10.1107/S1744309109032217                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 215852                         
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 21468                           
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 13842                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3390                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1512                         
REMARK   3   BIN FREE R VALUE                    : 0.3630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8978                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 525                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.071         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.073         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.048         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.253         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9654 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 13198 ; 2.065 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1379 ; 5.290 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   363 ;36.441 ;26.336       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1711 ;12.961 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;21.454 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1594 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7225 ; 0.012 ; 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):  6391 ; 1.315 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10333 ; 2.077 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3263 ; 3.433 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2811 ; 5.613 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 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 3HHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053147.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.25                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 215865                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.971                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ADA, 0.2 M SODIUM ACETATE, 30%    
REMARK 280  PEG MME 5000, 5% GLYCEROL, PH 6.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       73.01300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.98600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       73.01300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.98600            
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: 3070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 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: 3000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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     ALA B    80                                                      
REMARK 465     ARG B    81                                                      
REMARK 465     LYS B    82                                                      
REMARK 465     PRO B    83                                                      
REMARK 465     GLY B    84                                                      
REMARK 465     MET B    85                                                      
REMARK 465     ASP B    86                                                      
REMARK 465     LYS B   312                                                      
REMARK 465     ALA D    80                                                      
REMARK 465     ARG D    81                                                      
REMARK 465     LYS D    82                                                      
REMARK 465     PRO D    83                                                      
REMARK 465     GLY D    84                                                      
REMARK 465     LYS D   312                                                      
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   OD1  ASP B   297     O    HOH B   378              1.65            
REMARK 500   OD1  ASN B   119     O    HOH B   525              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 212   CB    GLU A 212   CG     -0.125                       
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 A   1   CG  -  SD  -  CE  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ASP A 257   CB  -  CG  -  OD1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG A 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG B 153   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ASP C  34   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP C 150   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG C 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG C 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU C 292   CB  -  CG  -  CD2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ASP D 139   CB  -  CG  -  OD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP D 257   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG D 262   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  59     -159.25   -130.82                                   
REMARK 500    SER B  59     -158.38   -128.40                                   
REMARK 500    SER B  59     -154.72   -129.53                                   
REMARK 500    SER B 222     -169.19   -120.73                                   
REMARK 500    SER C  59     -162.80   -123.91                                   
REMARK 500    SER D  59     -163.76   -126.26                                   
REMARK 500    SER D  59     -164.22   -126.04                                   
REMARK 500    THR D 224      -55.36   -125.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3HHP A    1   312  UNP    P61889   MDH_ECOLI        1    312             
DBREF  3HHP B    1   312  UNP    P61889   MDH_ECOLI        1    312             
DBREF  3HHP C    1   312  UNP    P61889   MDH_ECOLI        1    312             
DBREF  3HHP D    1   312  UNP    P61889   MDH_ECOLI        1    312             
SEQRES   1 A  312  MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY          
SEQRES   2 A  312  GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER          
SEQRES   3 A  312  GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR          
SEQRES   4 A  312  PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA          
SEQRES   5 A  312  VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO          
SEQRES   6 A  312  ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY          
SEQRES   7 A  312  VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE          
SEQRES   8 A  312  ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN          
SEQRES   9 A  312  VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE          
SEQRES  10 A  312  THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU          
SEQRES  11 A  312  VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU          
SEQRES  12 A  312  PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR          
SEQRES  13 A  312  PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL          
SEQRES  14 A  312  GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE          
SEQRES  15 A  312  LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR          
SEQRES  16 A  312  GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN          
SEQRES  17 A  312  ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY          
SEQRES  18 A  312  SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE          
SEQRES  19 A  312  GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY          
SEQRES  20 A  312  VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR          
SEQRES  21 A  312  ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN          
SEQRES  22 A  312  GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA          
SEQRES  23 A  312  PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU          
SEQRES  24 A  312  LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS          
SEQRES   1 B  312  MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY          
SEQRES   2 B  312  GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER          
SEQRES   3 B  312  GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR          
SEQRES   4 B  312  PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA          
SEQRES   5 B  312  VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO          
SEQRES   6 B  312  ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY          
SEQRES   7 B  312  VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE          
SEQRES   8 B  312  ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN          
SEQRES   9 B  312  VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE          
SEQRES  10 B  312  THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU          
SEQRES  11 B  312  VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU          
SEQRES  12 B  312  PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR          
SEQRES  13 B  312  PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL          
SEQRES  14 B  312  GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE          
SEQRES  15 B  312  LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR          
SEQRES  16 B  312  GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN          
SEQRES  17 B  312  ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY          
SEQRES  18 B  312  SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE          
SEQRES  19 B  312  GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY          
SEQRES  20 B  312  VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR          
SEQRES  21 B  312  ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN          
SEQRES  22 B  312  GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA          
SEQRES  23 B  312  PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU          
SEQRES  24 B  312  LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS          
SEQRES   1 C  312  MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY          
SEQRES   2 C  312  GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER          
SEQRES   3 C  312  GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR          
SEQRES   4 C  312  PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA          
SEQRES   5 C  312  VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO          
SEQRES   6 C  312  ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY          
SEQRES   7 C  312  VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE          
SEQRES   8 C  312  ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN          
SEQRES   9 C  312  VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE          
SEQRES  10 C  312  THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU          
SEQRES  11 C  312  VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU          
SEQRES  12 C  312  PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR          
SEQRES  13 C  312  PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL          
SEQRES  14 C  312  GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE          
SEQRES  15 C  312  LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR          
SEQRES  16 C  312  GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN          
SEQRES  17 C  312  ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY          
SEQRES  18 C  312  SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE          
SEQRES  19 C  312  GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY          
SEQRES  20 C  312  VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR          
SEQRES  21 C  312  ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN          
SEQRES  22 C  312  GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA          
SEQRES  23 C  312  PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU          
SEQRES  24 C  312  LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS          
SEQRES   1 D  312  MET LYS VAL ALA VAL LEU GLY ALA ALA GLY GLY ILE GLY          
SEQRES   2 D  312  GLN ALA LEU ALA LEU LEU LEU LYS THR GLN LEU PRO SER          
SEQRES   3 D  312  GLY SER GLU LEU SER LEU TYR ASP ILE ALA PRO VAL THR          
SEQRES   4 D  312  PRO GLY VAL ALA VAL ASP LEU SER HIS ILE PRO THR ALA          
SEQRES   5 D  312  VAL LYS ILE LYS GLY PHE SER GLY GLU ASP ALA THR PRO          
SEQRES   6 D  312  ALA LEU GLU GLY ALA ASP VAL VAL LEU ILE SER ALA GLY          
SEQRES   7 D  312  VAL ALA ARG LYS PRO GLY MET ASP ARG SER ASP LEU PHE          
SEQRES   8 D  312  ASN VAL ASN ALA GLY ILE VAL LYS ASN LEU VAL GLN GLN          
SEQRES   9 D  312  VAL ALA LYS THR CYS PRO LYS ALA CYS ILE GLY ILE ILE          
SEQRES  10 D  312  THR ASN PRO VAL ASN THR THR VAL ALA ILE ALA ALA GLU          
SEQRES  11 D  312  VAL LEU LYS LYS ALA GLY VAL TYR ASP LYS ASN LYS LEU          
SEQRES  12 D  312  PHE GLY VAL THR THR LEU ASP ILE ILE ARG SER ASN THR          
SEQRES  13 D  312  PHE VAL ALA GLU LEU LYS GLY LYS GLN PRO GLY GLU VAL          
SEQRES  14 D  312  GLU VAL PRO VAL ILE GLY GLY HIS SER GLY VAL THR ILE          
SEQRES  15 D  312  LEU PRO LEU LEU SER GLN VAL PRO GLY VAL SER PHE THR          
SEQRES  16 D  312  GLU GLN GLU VAL ALA ASP LEU THR LYS ARG ILE GLN ASN          
SEQRES  17 D  312  ALA GLY THR GLU VAL VAL GLU ALA LYS ALA GLY GLY GLY          
SEQRES  18 D  312  SER ALA THR LEU SER MET GLY GLN ALA ALA ALA ARG PHE          
SEQRES  19 D  312  GLY LEU SER LEU VAL ARG ALA LEU GLN GLY GLU GLN GLY          
SEQRES  20 D  312  VAL VAL GLU CYS ALA TYR VAL GLU GLY ASP GLY GLN TYR          
SEQRES  21 D  312  ALA ARG PHE PHE SER GLN PRO LEU LEU LEU GLY LYS ASN          
SEQRES  22 D  312  GLY VAL GLU GLU ARG LYS SER ILE GLY THR LEU SER ALA          
SEQRES  23 D  312  PHE GLU GLN ASN ALA LEU GLU GLY MET LEU ASP THR LEU          
SEQRES  24 D  312  LYS LYS ASP ILE ALA LEU GLY GLU GLU PHE VAL ASN LYS          
FORMUL   5  HOH   *525(H2 O)                                                    
HELIX    1   1 GLY A   10  LEU A   24  1                                  15    
HELIX    2   2 VAL A   38  HIS A   48  1                                  11    
HELIX    3   3 ALA A   63  GLU A   68  1                                   6    
HELIX    4   4 ASP A   86  CYS A  109  1                                  24    
HELIX    5   5 PRO A  120  ALA A  135  1                                  16    
HELIX    6   6 THR A  147  GLY A  163  1                                  17    
HELIX    7   7 GLN A  165  VAL A  169  5                                   5    
HELIX    8   8 SER A  178  VAL A  180  5                                   3    
HELIX    9   9 LEU A  186  VAL A  189  5                                   4    
HELIX   10  10 THR A  195  ASN A  208  1                                  14    
HELIX   11  11 ASN A  208  LYS A  217  1                                  10    
HELIX   12  12 THR A  224  GLN A  243  1                                  20    
HELIX   13  13 SER A  285  ASN A  311  1                                  27    
HELIX   14  14 GLY B   10  LEU B   24  1                                  15    
HELIX   15  15 VAL B   38  HIS B   48  1                                  11    
HELIX   16  16 ALA B   63  GLU B   68  1                                   6    
HELIX   17  17 ARG B   87  CYS B  109  1                                  23    
HELIX   18  18 PRO B  120  ALA B  135  1                                  16    
HELIX   19  19 THR B  147  GLY B  163  1                                  17    
HELIX   20  20 GLN B  165  VAL B  169  5                                   5    
HELIX   21  21 SER B  178  VAL B  180  5                                   3    
HELIX   22  22 LEU B  186  VAL B  189  5                                   4    
HELIX   23  23 THR B  195  LYS B  217  1                                  23    
HELIX   24  24 THR B  224  GLN B  243  1                                  20    
HELIX   25  25 SER B  285  ASN B  311  1                                  27    
HELIX   26  26 GLY C   10  LEU C   24  1                                  15    
HELIX   27  27 VAL C   38  HIS C   48  1                                  11    
HELIX   28  28 ALA C   63  GLU C   68  1                                   6    
HELIX   29  29 ASP C   86  CYS C  109  1                                  24    
HELIX   30  30 PRO C  120  ALA C  135  1                                  16    
HELIX   31  31 THR C  147  GLY C  163  1                                  17    
HELIX   32  32 GLN C  165  VAL C  169  5                                   5    
HELIX   33  33 SER C  178  VAL C  180  5                                   3    
HELIX   34  34 LEU C  186  VAL C  189  5                                   4    
HELIX   35  35 THR C  195  ALA C  218  1                                  24    
HELIX   36  36 THR C  224  GLN C  243  1                                  20    
HELIX   37  37 SER C  285  LYS C  312  1                                  28    
HELIX   38  38 GLY D   10  LEU D   24  1                                  15    
HELIX   39  39 VAL D   38  HIS D   48  1                                  11    
HELIX   40  40 ALA D   63  GLU D   68  1                                   6    
HELIX   41  41 ASP D   86  CYS D  109  1                                  24    
HELIX   42  42 PRO D  120  ALA D  135  1                                  16    
HELIX   43  43 THR D  147  GLY D  163  1                                  17    
HELIX   44  44 GLN D  165  VAL D  169  5                                   5    
HELIX   45  45 SER D  178  VAL D  180  5                                   3    
HELIX   46  46 LEU D  186  VAL D  189  5                                   4    
HELIX   47  47 THR D  195  ASN D  208  1                                  14    
HELIX   48  48 ASN D  208  ALA D  218  1                                  11    
HELIX   49  49 THR D  224  GLN D  243  1                                  20    
HELIX   50  50 SER D  285  ASN D  311  1                                  27    
SHEET    1   A 6 VAL A  53  PHE A  58  0                                        
SHEET    2   A 6 SER A  28  TYR A  33  1  N  LEU A  30   O  LYS A  54           
SHEET    3   A 6 LYS A   2  LEU A   6  1  N  VAL A   3   O  GLU A  29           
SHEET    4   A 6 VAL A  72  ILE A  75  1  O  LEU A  74   N  ALA A   4           
SHEET    5   A 6 CYS A 113  ILE A 116  1  O  GLY A 115   N  VAL A  73           
SHEET    6   A 6 LEU A 143  GLY A 145  1  O  PHE A 144   N  ILE A 116           
SHEET    1   B 2 VAL A 173  GLY A 175  0                                        
SHEET    2   B 2 ILE A 182  PRO A 184 -1  O  LEU A 183   N  ILE A 174           
SHEET    1   C 3 VAL A 249  GLU A 255  0                                        
SHEET    2   C 3 PHE A 263  GLY A 271 -1  O  PHE A 264   N  VAL A 254           
SHEET    3   C 3 GLY A 274  ARG A 278 -1  O  GLU A 276   N  LEU A 269           
SHEET    1   D 6 VAL B  53  PHE B  58  0                                        
SHEET    2   D 6 SER B  28  TYR B  33  1  N  LEU B  30   O  LYS B  54           
SHEET    3   D 6 LYS B   2  LEU B   6  1  N  VAL B   5   O  SER B  31           
SHEET    4   D 6 VAL B  72  ILE B  75  1  O  LEU B  74   N  ALA B   4           
SHEET    5   D 6 CYS B 113  ILE B 116  1  O  GLY B 115   N  VAL B  73           
SHEET    6   D 6 LEU B 143  GLY B 145  1  O  PHE B 144   N  ILE B 116           
SHEET    1   E 2 VAL B 173  GLY B 175  0                                        
SHEET    2   E 2 ILE B 182  PRO B 184 -1  O  LEU B 183   N  ILE B 174           
SHEET    1   F 3 VAL B 249  GLU B 255  0                                        
SHEET    2   F 3 PHE B 263  GLY B 271 -1  O  PHE B 264   N  VAL B 254           
SHEET    3   F 3 GLY B 274  ARG B 278 -1  O  GLU B 276   N  LEU B 269           
SHEET    1   G 6 VAL C  53  PHE C  58  0                                        
SHEET    2   G 6 SER C  28  TYR C  33  1  N  LEU C  30   O  LYS C  54           
SHEET    3   G 6 LYS C   2  LEU C   6  1  N  VAL C   3   O  SER C  31           
SHEET    4   G 6 VAL C  72  ILE C  75  1  O  VAL C  72   N  ALA C   4           
SHEET    5   G 6 CYS C 113  ILE C 116  1  O  GLY C 115   N  ILE C  75           
SHEET    6   G 6 LEU C 143  GLY C 145  1  O  PHE C 144   N  ILE C 116           
SHEET    1   H 2 VAL C 173  GLY C 175  0                                        
SHEET    2   H 2 ILE C 182  PRO C 184 -1  O  LEU C 183   N  ILE C 174           
SHEET    1   I 3 VAL C 249  GLU C 255  0                                        
SHEET    2   I 3 PHE C 263  GLY C 271 -1  O  PHE C 264   N  VAL C 254           
SHEET    3   I 3 GLY C 274  ARG C 278 -1  O  GLU C 276   N  LEU C 269           
SHEET    1   J 6 VAL D  53  PHE D  58  0                                        
SHEET    2   J 6 SER D  28  TYR D  33  1  N  LEU D  30   O  LYS D  54           
SHEET    3   J 6 LYS D   2  LEU D   6  1  N  VAL D   5   O  SER D  31           
SHEET    4   J 6 VAL D  72  ILE D  75  1  O  LEU D  74   N  ALA D   4           
SHEET    5   J 6 CYS D 113  ILE D 116  1  O  GLY D 115   N  VAL D  73           
SHEET    6   J 6 LEU D 143  GLY D 145  1  O  PHE D 144   N  ILE D 116           
SHEET    1   K 2 VAL D 173  GLY D 175  0                                        
SHEET    2   K 2 ILE D 182  PRO D 184 -1  O  LEU D 183   N  ILE D 174           
SHEET    1   L 3 VAL D 249  GLU D 255  0                                        
SHEET    2   L 3 PHE D 263  GLY D 271 -1  O  PHE D 264   N  VAL D 254           
SHEET    3   L 3 GLY D 274  ARG D 278 -1  O  GLU D 276   N  LEU D 269           
CISPEP   1 ASN A  119    PRO A  120          0         3.99                     
CISPEP   2 ASN B  119    PRO B  120          0         0.71                     
CISPEP   3 ASN B  119    PRO B  120          0        -0.30                     
CISPEP   4 ASN C  119    PRO C  120          0         5.52                     
CISPEP   5 ASN D  119    PRO D  120          0         7.95                     
CRYST1  146.026   51.972  168.980  90.00 102.23  90.00 C 1 2 1      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      0.006848  0.000000  0.001484        0.00000                         
SCALE2      0.000000  0.019241  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006055        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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