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Database: PDB
Entry: 4ND5
LinkDB: 4ND5
Original site: 4ND5 
HEADER    OXIDOREDUCTASE                          25-OCT-13   4ND5              
TITLE     CRYSTAL STRUCTURE OF THE LACTATE DEHYDROGENASE FROM CRYPTOSPORIDIUM   
TITLE    2 PARVUM                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LACTATE DEHYDROGENASE, ADJACENT GENE ENCODES PREDICTED     
COMPND   3 MALATE DEHYDROGENASE;                                                
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 EC: 1.1.1.27;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;                         
SOURCE   3 ORGANISM_TAXID: 353152;                                              
SOURCE   4 STRAIN: IOWA II;                                                     
SOURCE   5 GENE: CGD7_480, LDH1;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3)PLYSS;                         
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    APOENZYME STRUCTURE, OXIDOREDUCTASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.CHATTOPADHYAY,W.J.COOK                                              
REVDAT   4   20-SEP-23 4ND5    1       REMARK                                   
REVDAT   3   17-JUL-19 4ND5    1       REMARK LINK                              
REVDAT   2   11-MAR-15 4ND5    1       JRNL                                     
REVDAT   1   17-DEC-14 4ND5    0                                                
SPRSDE     17-DEC-14 4ND5      2FRM                                             
JRNL        AUTH   W.J.COOK,O.SENKOVICH,A.HERNANDEZ,H.SPEED,D.CHATTOPADHYAY     
JRNL        TITL   BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF               
JRNL        TITL 2 CRYPTOSPORIDIUM PARVUM LACTATE DEHYDROGENASE.                
JRNL        REF    INT.J.BIOL.MACROMOL.          V. 74C   608 2014              
JRNL        REFN                   ISSN 0141-8130                               
JRNL        PMID   25542170                                                     
JRNL        DOI    10.1016/J.IJBIOMAC.2014.12.019                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 91538                          
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) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4880                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3948                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 54.24                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 191                          
REMARK   3   BIN FREE R VALUE                    : 0.3260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8905                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.37000                                              
REMARK   3    B22 (A**2) : 1.37000                                              
REMARK   3    B33 (A**2) : -4.44000                                             
REMARK   3    B12 (A**2) : 1.37000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.294         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9049 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8906 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12254 ; 0.844 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20507 ; 0.650 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1193 ; 4.607 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   333 ;35.918 ;25.435       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1544 ;11.179 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;14.519 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1463 ; 0.048 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10247 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1893 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4ND5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-OCT-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9998                             
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 100051                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.17                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 2EWD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16.5% PEG 2000, 0.1 M TRIS-HCL, 0.08%    
REMARK 280  B-D-GLYCOPYRANOSIDE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 1 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -Y,-X,-Z+1/3                                            
REMARK 290       5555   -X+Y,Y,-Z+2/3                                           
REMARK 290       6555   X,X-Y,-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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.48000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.74000            
REMARK 290   SMTRY1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000       56.74000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      113.48000            
REMARK 290   SMTRY1   6  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14600 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 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   BIOMT1   2  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       56.74000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000      272.98000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      113.48000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   100                                                      
REMARK 465     ILE A   101                                                      
REMARK 465     PRO A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     PRO A   105                                                      
REMARK 465     LYS A   106                                                      
REMARK 465     ASP A   107                                                      
REMARK 465     ASP A   108                                                      
REMARK 465     ARG A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     GLU A   111                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     ALA A   332                                                      
REMARK 465     PRO A   333                                                      
REMARK 465     ALA A   334                                                      
REMARK 465     ALA A   335                                                      
REMARK 465     GLY A   336                                                      
REMARK 465     ALA A   337                                                      
REMARK 465     SER B   100                                                      
REMARK 465     ILE B   101                                                      
REMARK 465     PRO B   102                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     ARG B   104                                                      
REMARK 465     PRO B   105                                                      
REMARK 465     LYS B   106                                                      
REMARK 465     ASP B   107                                                      
REMARK 465     ASP B   108                                                      
REMARK 465     ARG B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     GLU B   111                                                      
REMARK 465     ASP B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ALA B   332                                                      
REMARK 465     PRO B   333                                                      
REMARK 465     ALA B   334                                                      
REMARK 465     ALA B   335                                                      
REMARK 465     GLY B   336                                                      
REMARK 465     ALA B   337                                                      
REMARK 465     MET C    17                                                      
REMARK 465     SER C   100                                                      
REMARK 465     ILE C   101                                                      
REMARK 465     PRO C   102                                                      
REMARK 465     GLY C   103                                                      
REMARK 465     ARG C   104                                                      
REMARK 465     PRO C   105                                                      
REMARK 465     LYS C   106                                                      
REMARK 465     ASP C   107                                                      
REMARK 465     ASP C   108                                                      
REMARK 465     ARG C   109                                                      
REMARK 465     SER C   110                                                      
REMARK 465     GLU C   111                                                      
REMARK 465     ASP C   330                                                      
REMARK 465     ASN C   331                                                      
REMARK 465     ALA C   332                                                      
REMARK 465     PRO C   333                                                      
REMARK 465     ALA C   334                                                      
REMARK 465     ALA C   335                                                      
REMARK 465     GLY C   336                                                      
REMARK 465     ALA C   337                                                      
REMARK 465     MET D    17                                                      
REMARK 465     SER D   100                                                      
REMARK 465     ILE D   101                                                      
REMARK 465     PRO D   102                                                      
REMARK 465     GLY D   103                                                      
REMARK 465     ARG D   104                                                      
REMARK 465     PRO D   105                                                      
REMARK 465     LYS D   106                                                      
REMARK 465     ASP D   107                                                      
REMARK 465     ASP D   108                                                      
REMARK 465     ARG D   109                                                      
REMARK 465     SER D   110                                                      
REMARK 465     GLU D   111                                                      
REMARK 465     VAL D   328                                                      
REMARK 465     LEU D   329                                                      
REMARK 465     ASP D   330                                                      
REMARK 465     ASN D   331                                                      
REMARK 465     ALA D   332                                                      
REMARK 465     PRO D   333                                                      
REMARK 465     ALA D   334                                                      
REMARK 465     ALA D   335                                                      
REMARK 465     GLY D   336                                                      
REMARK 465     ALA D   337                                                      
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    CYS A 131       63.38   -153.18                                   
REMARK 500    ALA A 164      -52.73   -159.35                                   
REMARK 500    ALA A 202       93.22    -68.46                                   
REMARK 500    LYS A 244A     -54.03     74.71                                   
REMARK 500    TYR A 247      -26.81   -149.44                                   
REMARK 500    VAL A 328       98.66    -65.52                                   
REMARK 500    LEU A 329       80.31   -159.86                                   
REMARK 500    SER B  29       30.65    -99.06                                   
REMARK 500    CYS B 131       64.28   -155.14                                   
REMARK 500    ALA B 164      -52.98   -149.19                                   
REMARK 500    LYS B 244A     -42.11     71.59                                   
REMARK 500    TYR B 247      -22.91   -142.69                                   
REMARK 500    ALA C 164      -54.06   -154.45                                   
REMARK 500    LYS C 244A     -68.39     71.63                                   
REMARK 500    SER D  29       37.26    -98.94                                   
REMARK 500    ALA D 164      -54.68   -163.21                                   
REMARK 500    LYS D 244A     -63.89     71.83                                   
REMARK 500    TYR D 247      -29.45   -154.40                                   
REMARK 500    ASN D 277       50.49   -161.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ND1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ND2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ND3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ND4   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PEPTIDE SEQUENCE FOR THIS ENTRY WAS TRANSLATED FROM DNA SEQUENCING   
REMARK 999 OF ACTUAL CLONE USED FOR PROTEIN EXPRESSION. AUTHORS DO NOT KNOW IF  
REMARK 999 THE SEQUENCE DIFFERENCES ARE PCR ERRORS OR MUTATIONS CORRESPONDING   
REMARK 999 DNA POLYMORPHISM OR THERE WERE ERRORS IN PROTEIN DATABASE.           
DBREF  4ND5 A   17   337  UNP    Q5CYZ2   Q5CYZ2_CRYPI    17    337             
DBREF  4ND5 B   17   337  UNP    Q5CYZ2   Q5CYZ2_CRYPI    17    337             
DBREF  4ND5 C   17   337  UNP    Q5CYZ2   Q5CYZ2_CRYPI    17    337             
DBREF  4ND5 D   17   337  UNP    Q5CYZ2   Q5CYZ2_CRYPI    17    337             
SEQADV 4ND5 ALA A  202  UNP  Q5CYZ2    VAL   200 SEE REMARK 999                 
SEQADV 4ND5 ALA B  202  UNP  Q5CYZ2    VAL   200 SEE REMARK 999                 
SEQADV 4ND5 ALA C  202  UNP  Q5CYZ2    VAL   200 SEE REMARK 999                 
SEQADV 4ND5 ALA D  202  UNP  Q5CYZ2    VAL   200 SEE REMARK 999                 
SEQRES   1 A  321  MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY          
SEQRES   2 A  321  GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP          
SEQRES   3 A  321  ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY          
SEQRES   4 A  321  ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET          
SEQRES   5 A  321  VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN          
SEQRES   6 A  321  ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE          
SEQRES   7 A  321  THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER          
SEQRES   8 A  321  GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL          
SEQRES   9 A  321  ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL          
SEQRES  10 A  321  ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS          
SEQRES  11 A  321  PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS          
SEQRES  12 A  321  GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR          
SEQRES  13 A  321  PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL          
SEQRES  14 A  321  SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL          
SEQRES  15 A  321  PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU          
SEQRES  16 A  321  SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN          
SEQRES  17 A  321  ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS          
SEQRES  18 A  321  GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE          
SEQRES  19 A  321  ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR          
SEQRES  20 A  321  LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE          
SEQRES  21 A  321  CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY          
SEQRES  22 A  321  VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE          
SEQRES  23 A  321  LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU          
SEQRES  24 A  321  GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL          
SEQRES  25 A  321  LEU ASP ASN ALA PRO ALA ALA GLY ALA                          
SEQRES   1 B  321  MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY          
SEQRES   2 B  321  GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP          
SEQRES   3 B  321  ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY          
SEQRES   4 B  321  ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET          
SEQRES   5 B  321  VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN          
SEQRES   6 B  321  ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE          
SEQRES   7 B  321  THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER          
SEQRES   8 B  321  GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL          
SEQRES   9 B  321  ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL          
SEQRES  10 B  321  ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS          
SEQRES  11 B  321  PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS          
SEQRES  12 B  321  GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR          
SEQRES  13 B  321  PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL          
SEQRES  14 B  321  SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL          
SEQRES  15 B  321  PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU          
SEQRES  16 B  321  SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN          
SEQRES  17 B  321  ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS          
SEQRES  18 B  321  GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE          
SEQRES  19 B  321  ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR          
SEQRES  20 B  321  LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE          
SEQRES  21 B  321  CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY          
SEQRES  22 B  321  VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE          
SEQRES  23 B  321  LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU          
SEQRES  24 B  321  GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL          
SEQRES  25 B  321  LEU ASP ASN ALA PRO ALA ALA GLY ALA                          
SEQRES   1 C  321  MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY          
SEQRES   2 C  321  GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP          
SEQRES   3 C  321  ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY          
SEQRES   4 C  321  ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET          
SEQRES   5 C  321  VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN          
SEQRES   6 C  321  ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE          
SEQRES   7 C  321  THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER          
SEQRES   8 C  321  GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL          
SEQRES   9 C  321  ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL          
SEQRES  10 C  321  ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS          
SEQRES  11 C  321  PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS          
SEQRES  12 C  321  GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR          
SEQRES  13 C  321  PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL          
SEQRES  14 C  321  SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL          
SEQRES  15 C  321  PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU          
SEQRES  16 C  321  SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN          
SEQRES  17 C  321  ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS          
SEQRES  18 C  321  GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE          
SEQRES  19 C  321  ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR          
SEQRES  20 C  321  LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE          
SEQRES  21 C  321  CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY          
SEQRES  22 C  321  VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE          
SEQRES  23 C  321  LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU          
SEQRES  24 C  321  GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL          
SEQRES  25 C  321  LEU ASP ASN ALA PRO ALA ALA GLY ALA                          
SEQRES   1 D  321  MET ILE GLU ARG ARG LYS ILE ALA VAL ILE GLY SER GLY          
SEQRES   2 D  321  GLN ILE GLY GLY ASN ILE ALA TYR ILE VAL GLY LYS ASP          
SEQRES   3 D  321  ASN LEU ALA ASP VAL VAL LEU PHE ASP ILE ALA GLU GLY          
SEQRES   4 D  321  ILE PRO GLN GLY LYS ALA LEU ASP ILE THR HIS SER MET          
SEQRES   5 D  321  VAL MET PHE GLY SER THR SER LYS VAL ILE GLY THR ASN          
SEQRES   6 D  321  ASP TYR ALA ASP ILE SER GLY SER ASP VAL VAL ILE ILE          
SEQRES   7 D  321  THR ALA SER ILE PRO GLY ARG PRO LYS ASP ASP ARG SER          
SEQRES   8 D  321  GLU LEU LEU PHE GLY ASN ALA ARG ILE LEU ASP SER VAL          
SEQRES   9 D  321  ALA GLU GLY VAL LYS LYS TYR CYS PRO ASN ALA PHE VAL          
SEQRES  10 D  321  ILE CYS ILE THR ASN PRO LEU ASP VAL MET VAL SER HIS          
SEQRES  11 D  321  PHE GLN LYS VAL SER GLY LEU PRO HIS ASN LYS VAL CYS          
SEQRES  12 D  321  GLY MET ALA GLY VAL LEU ASP SER SER ARG PHE ARG THR          
SEQRES  13 D  321  PHE ILE ALA GLN HIS PHE GLY VAL ASN ALA SER ASP VAL          
SEQRES  14 D  321  SER ALA ASN VAL ILE GLY GLY HIS GLY ASP GLY MET VAL          
SEQRES  15 D  321  PRO ALA THR SER SER VAL SER VAL GLY GLY VAL PRO LEU          
SEQRES  16 D  321  SER SER PHE ILE LYS GLN GLY LEU ILE THR GLN GLU GLN          
SEQRES  17 D  321  ILE ASP GLU ILE VAL CYS HIS THR ARG ILE ALA TRP LYS          
SEQRES  18 D  321  GLU VAL ALA ASP ASN LEU LYS THR GLY THR ALA TYR PHE          
SEQRES  19 D  321  ALA PRO ALA ALA ALA ALA VAL LYS MET ALA GLU ALA TYR          
SEQRES  20 D  321  LEU LYS ASP LYS LYS ALA VAL VAL PRO CYS SER ALA PHE          
SEQRES  21 D  321  CYS SER ASN HIS TYR GLY VAL LYS GLY ILE TYR MET GLY          
SEQRES  22 D  321  VAL PRO THR ILE ILE GLY LYS ASN GLY VAL GLU ASP ILE          
SEQRES  23 D  321  LEU GLU LEU ASP LEU THR PRO LEU GLU GLN LYS LEU LEU          
SEQRES  24 D  321  GLY GLU SER ILE ASN GLU VAL ASN THR ILE SER LYS VAL          
SEQRES  25 D  321  LEU ASP ASN ALA PRO ALA ALA GLY ALA                          
FORMUL   5  HOH   *194(H2 O)                                                    
HELIX    1   1 GLY A   30  ASN A   44  1                                  15    
HELIX    2   2 GLY A   57  GLY A   73B 1                                  18    
HELIX    3   3 ASP A   84  SER A   89  5                                   6    
HELIX    4   4 LEU A  113  CYS A  131  1                                  19    
HELIX    5   5 PRO A  141  GLY A  154  1                                  14    
HELIX    6   6 PRO A  156  ASN A  158  5                                   3    
HELIX    7   7 ALA A  164  GLY A  181  1                                  18    
HELIX    8   8 ASN A  183  SER A  185  5                                   3    
HELIX    9   9 HIS A  195  ASP A  197  5                                   3    
HELIX   10  10 LEU A  212  GLN A  218A 1                                   7    
HELIX   11  11 THR A  221  LYS A  244A 1                                  24    
HELIX   12  12 TYR A  247  LYS A  263  1                                  17    
HELIX   13  13 THR A  308  VAL A  328  1                                  21    
HELIX   14  14 GLY B   30  ASN B   44  1                                  15    
HELIX   15  15 GLY B   57  MET B   70  1                                  14    
HELIX   16  16 ASP B   84  SER B   89  5                                   6    
HELIX   17  17 LEU B  113  CYS B  131  1                                  19    
HELIX   18  18 PRO B  141  GLY B  154  1                                  14    
HELIX   19  19 PRO B  156  ASN B  158  5                                   3    
HELIX   20  20 ALA B  164  GLY B  181  1                                  18    
HELIX   21  21 ASN B  183  SER B  185  5                                   3    
HELIX   22  22 HIS B  195  ASP B  197  5                                   3    
HELIX   23  23 THR B  203  SER B  205  5                                   3    
HELIX   24  24 LEU B  212  GLN B  218A 1                                   7    
HELIX   25  25 THR B  221  LYS B  244A 1                                  24    
HELIX   26  26 TYR B  247  LYS B  263  1                                  17    
HELIX   27  27 THR B  308  LEU B  329  1                                  22    
HELIX   28  28 GLY C   30  ASP C   43  1                                  14    
HELIX   29  29 GLY C   57  GLY C   73B 1                                  18    
HELIX   30  30 ASP C   84  SER C   89  5                                   6    
HELIX   31  31 LEU C  113  CYS C  131  1                                  19    
HELIX   32  32 PRO C  141  GLY C  154  1                                  14    
HELIX   33  33 PRO C  156  ASN C  158  5                                   3    
HELIX   34  34 ALA C  164  GLY C  181  1                                  18    
HELIX   35  35 ASN C  183  SER C  185  5                                   3    
HELIX   36  36 HIS C  195  ASP C  197  5                                   3    
HELIX   37  37 THR C  203  SER C  205  5                                   3    
HELIX   38  38 LEU C  212  GLN C  218A 1                                   7    
HELIX   39  39 THR C  221  LYS C  244A 1                                  24    
HELIX   40  40 TYR C  247  LYS C  263  1                                  17    
HELIX   41  41 THR C  308  LEU C  329  1                                  22    
HELIX   42  42 GLY D   30  ASN D   44  1                                  15    
HELIX   43  43 GLY D   57  GLY D   73B 1                                  18    
HELIX   44  44 ASP D   84  SER D   89  5                                   6    
HELIX   45  45 LEU D  113  CYS D  131  1                                  19    
HELIX   46  46 PRO D  141  GLY D  154  1                                  14    
HELIX   47  47 PRO D  156  ASN D  158  5                                   3    
HELIX   48  48 ALA D  164  GLY D  181  1                                  18    
HELIX   49  49 ASN D  183  SER D  185  5                                   3    
HELIX   50  50 HIS D  195  ASP D  197  5                                   3    
HELIX   51  51 THR D  203  VAL D  206  5                                   4    
HELIX   52  52 PRO D  210B GLN D  218A 1                                   8    
HELIX   53  53 THR D  221  LYS D  244A 1                                  24    
HELIX   54  54 TYR D  247  LYS D  263  1                                  17    
HELIX   55  55 THR D  308  SER D  326  1                                  19    
SHEET    1   A 6 VAL A  78  THR A  81  0                                        
SHEET    2   A 6 ASP A  48  PHE A  52  1  N  LEU A  51   O  ILE A  79           
SHEET    3   A 6 LYS A  23  ILE A  27  1  N  VAL A  26   O  PHE A  52           
SHEET    4   A 6 VAL A  93  ILE A  96  1  O  ILE A  95   N  ILE A  27           
SHEET    5   A 6 PHE A 134  CYS A 137  1  O  ILE A 136   N  VAL A  94           
SHEET    6   A 6 VAL A 160  GLY A 162  1  O  CYS A 161   N  CYS A 137           
SHEET    1   B 3 VAL A 187  GLY A 193  0                                        
SHEET    2   B 3 MET A 199  VAL A 208 -1  O  SER A 207   N  SER A 188           
SHEET    3   B 3 VAL A 210A PRO A 210B-1  O  VAL A 210A  N  VAL A 208           
SHEET    1   C 3 ALA A 267  CYS A 275  0                                        
SHEET    2   C 3 ILE A 285  GLY A 294 -1  O  ILE A 285   N  CYS A 275           
SHEET    3   C 3 GLY A 297  ILE A 302 -1  O  GLU A 299   N  ILE A 292           
SHEET    1   D 6 VAL B  78  THR B  81  0                                        
SHEET    2   D 6 ASP B  48  PHE B  52  1  N  LEU B  51   O  ILE B  79           
SHEET    3   D 6 LYS B  23  ILE B  27  1  N  VAL B  26   O  VAL B  50           
SHEET    4   D 6 VAL B  93  ILE B  96  1  O  ILE B  95   N  ILE B  27           
SHEET    5   D 6 PHE B 134  CYS B 137  1  O  ILE B 136   N  VAL B  94           
SHEET    6   D 6 VAL B 160  GLY B 162  1  O  CYS B 161   N  CYS B 137           
SHEET    1   E 3 VAL B 187  SER B 188  0                                        
SHEET    2   E 3 SER B 207  VAL B 208 -1  O  SER B 207   N  SER B 188           
SHEET    3   E 3 VAL B 210A PRO B 210B-1  O  VAL B 210A  N  VAL B 208           
SHEET    1   F 2 VAL B 191  GLY B 193  0                                        
SHEET    2   F 2 MET B 199  PRO B 201 -1  O  VAL B 200   N  ILE B 192           
SHEET    1   G 3 ALA B 267  CYS B 275  0                                        
SHEET    2   G 3 ILE B 285  GLY B 294 -1  O  ILE B 285   N  CYS B 275           
SHEET    3   G 3 GLY B 297  ILE B 302 -1  O  GLU B 299   N  ILE B 292           
SHEET    1   H 6 VAL C  78  THR C  81  0                                        
SHEET    2   H 6 ASP C  48  PHE C  52  1  N  LEU C  51   O  ILE C  79           
SHEET    3   H 6 LYS C  23  ILE C  27  1  N  VAL C  26   O  PHE C  52           
SHEET    4   H 6 VAL C  93  ILE C  96  1  O  ILE C  95   N  ALA C  25           
SHEET    5   H 6 PHE C 134  CYS C 137  1  O  ILE C 136   N  VAL C  94           
SHEET    6   H 6 VAL C 160  GLY C 162  1  O  CYS C 161   N  CYS C 137           
SHEET    1   I 3 VAL C 187  SER C 188  0                                        
SHEET    2   I 3 SER C 207  VAL C 208 -1  O  SER C 207   N  SER C 188           
SHEET    3   I 3 VAL C 210A PRO C 210B-1  O  VAL C 210A  N  VAL C 208           
SHEET    1   J 2 VAL C 191  GLY C 193  0                                        
SHEET    2   J 2 MET C 199  PRO C 201 -1  O  VAL C 200   N  ILE C 192           
SHEET    1   K 3 ALA C 267  CYS C 275  0                                        
SHEET    2   K 3 ILE C 285  GLY C 294 -1  O  THR C 291   N  VAL C 269           
SHEET    3   K 3 GLY C 297  ILE C 302 -1  O  GLU C 299   N  ILE C 292           
SHEET    1   L 6 VAL D  78  THR D  81  0                                        
SHEET    2   L 6 ASP D  48  PHE D  52  1  N  LEU D  51   O  ILE D  79           
SHEET    3   L 6 LYS D  23  ILE D  27  1  N  VAL D  26   O  PHE D  52           
SHEET    4   L 6 VAL D  93  ILE D  96  1  O  VAL D  93   N  ALA D  25           
SHEET    5   L 6 PHE D 134  CYS D 137  1  O  ILE D 136   N  VAL D  94           
SHEET    6   L 6 VAL D 160  GLY D 162  1  O  CYS D 161   N  CYS D 137           
SHEET    1   M 2 VAL D 187  SER D 188  0                                        
SHEET    2   M 2 SER D 207  VAL D 208 -1  O  SER D 207   N  SER D 188           
SHEET    1   N 2 VAL D 191  GLY D 193  0                                        
SHEET    2   N 2 MET D 199  PRO D 201 -1  O  VAL D 200   N  ILE D 192           
SHEET    1   O 3 ALA D 267  CYS D 275  0                                        
SHEET    2   O 3 ILE D 285  GLY D 294 -1  O  ILE D 285   N  CYS D 275           
SHEET    3   O 3 GLY D 297  ILE D 302 -1  O  GLU D 299   N  ILE D 292           
LINK         C   ARG A  20                 N   ARG A  22     1555   1555  1.33  
LINK         C   ALA A  46                 N   ASP A  48     1555   1555  1.33  
LINK         C   PHE A  73A                N   GLY A  73B    1555   1555  1.33  
LINK         C   THR A  81                 N   ASN A  83     1555   1555  1.33  
LINK         C   PRO A 132A                N   ASN A 132B    1555   1555  1.33  
LINK         C   GLY A 209A                N   GLY A 209B    1555   1555  1.33  
LINK         C   VAL A 210A                N   PRO A 210B    1555   1555  1.33  
LINK         C   PRO A 210B                N   LEU A 212     1555   1555  1.33  
LINK         C   GLN A 218A                N   GLY A 218B    1555   1555  1.33  
LINK         C   LYS A 244A                N   THR A 244B    1555   1555  1.33  
LINK         C   THR A 244B                N   GLY A 244C    1555   1555  1.33  
LINK         C   GLY A 283                 N   ILE A 285     1555   1555  1.33  
LINK         C   GLU A 299                 N   ASP A 301     1555   1555  1.33  
LINK         C   ARG B  20                 N   ARG B  22     1555   1555  1.33  
LINK         C   ALA B  46                 N   ASP B  48     1555   1555  1.33  
LINK         C   PHE B  73A                N   GLY B  73B    1555   1555  1.33  
LINK         C   THR B  81                 N   ASN B  83     1555   1555  1.33  
LINK         C   PRO B 132A                N   ASN B 132B    1555   1555  1.33  
LINK         C   GLY B 209A                N   GLY B 209B    1555   1555  1.33  
LINK         C   VAL B 210A                N   PRO B 210B    1555   1555  1.34  
LINK         C   PRO B 210B                N   LEU B 212     1555   1555  1.33  
LINK         C   GLN B 218A                N   GLY B 218B    1555   1555  1.33  
LINK         C   LYS B 244A                N   THR B 244B    1555   1555  1.33  
LINK         C   THR B 244B                N   GLY B 244C    1555   1555  1.33  
LINK         C   GLY B 283                 N   ILE B 285     1555   1555  1.33  
LINK         C   GLU B 299                 N   ASP B 301     1555   1555  1.33  
LINK         C   ARG C  20                 N   ARG C  22     1555   1555  1.33  
LINK         C   ALA C  46                 N   ASP C  48     1555   1555  1.33  
LINK         C   PHE C  73A                N   GLY C  73B    1555   1555  1.33  
LINK         C   THR C  81                 N   ASN C  83     1555   1555  1.33  
LINK         C   PRO C 132A                N   ASN C 132B    1555   1555  1.33  
LINK         C   GLY C 209A                N   GLY C 209B    1555   1555  1.33  
LINK         C   VAL C 210A                N   PRO C 210B    1555   1555  1.33  
LINK         C   PRO C 210B                N   LEU C 212     1555   1555  1.33  
LINK         C   GLN C 218A                N   GLY C 218B    1555   1555  1.33  
LINK         C   LYS C 244A                N   THR C 244B    1555   1555  1.33  
LINK         C   THR C 244B                N   GLY C 244C    1555   1555  1.33  
LINK         C   GLY C 283                 N   ILE C 285     1555   1555  1.33  
LINK         C   GLU C 299                 N   ASP C 301     1555   1555  1.33  
LINK         C   ARG D  20                 N   ARG D  22     1555   1555  1.33  
LINK         C   ALA D  46                 N   ASP D  48     1555   1555  1.33  
LINK         C   PHE D  73A                N   GLY D  73B    1555   1555  1.33  
LINK         C   THR D  81                 N   ASN D  83     1555   1555  1.33  
LINK         C   PRO D 132A                N   ASN D 132B    1555   1555  1.33  
LINK         C   GLY D 209A                N   GLY D 209B    1555   1555  1.33  
LINK         C   VAL D 210A                N   PRO D 210B    1555   1555  1.34  
LINK         C   PRO D 210B                N   LEU D 212     1555   1555  1.33  
LINK         C   GLN D 218A                N   GLY D 218B    1555   1555  1.33  
LINK         C   LYS D 244A                N   THR D 244B    1555   1555  1.33  
LINK         C   THR D 244B                N   GLY D 244C    1555   1555  1.33  
LINK         C   GLY D 283                 N   ILE D 285     1555   1555  1.33  
LINK         C   GLU D 299                 N   ASP D 301     1555   1555  1.33  
CISPEP   1 ASN A  140    PRO A  141          0        -4.53                     
CISPEP   2 ASN B  140    PRO B  141          0        -3.93                     
CISPEP   3 ASN C  140    PRO C  141          0        -3.59                     
CISPEP   4 ASN D  140    PRO D  141          0         0.22                     
CRYST1  136.490  136.490  170.220  90.00  90.00 120.00 P 32 1 2     24          
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      0.007327  0.004230  0.000000        0.00000                         
SCALE2      0.000000  0.008460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005875        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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