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Database: PDB
Entry: 3HN2
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Original site: 3HN2 
HEADER    OXIDOREDUCTASE                          29-MAY-09   3HN2              
TITLE     CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM GEOBACTER     
TITLE    2 METALLIREDUCENS GS-15                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-DEHYDROPANTOATE 2-REDUCTASE;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.1.1.169;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GEOBACTER METALLIREDUCENS;                      
SOURCE   3 ORGANISM_TAXID: 269799;                                              
SOURCE   4 STRAIN: GS-15;                                                       
SOURCE   5 ATCC: 53774;                                                         
SOURCE   6 GENE: GMET_2643;                                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-CODON+RIL;                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)                              
KEYWDS    2-DEHYDROPANTOATE 2-REDUCTASE, PSI-2, NYSGXRC, STRUCTURAL GENOMICS,   
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR       
KEYWDS   3 STRUCTURAL GENOMICS, NADP, OXIDOREDUCTASE, PANTOTHENATE BIOSYNTHESIS 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,S.CHANG,J.M.SAUDER,S.K.BURLEY,  
AUTHOR   2 S.C.ALMO,NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS        
AUTHOR   3 (NYSGXRC)                                                            
REVDAT   6   21-FEB-24 3HN2    1       REMARK                                   
REVDAT   5   10-FEB-21 3HN2    1       AUTHOR JRNL   SEQADV                     
REVDAT   4   28-NOV-18 3HN2    1       REMARK                                   
REVDAT   3   21-NOV-18 3HN2    1       AUTHOR                                   
REVDAT   2   13-JUL-11 3HN2    1       VERSN                                    
REVDAT   1   09-JUN-09 3HN2    0                                                
JRNL        AUTH   Y.PATSKOVSKY,R.TORO,C.MORANO,M.RUTTER,S.CHANG,J.M.SAUDER,    
JRNL        AUTH 2 S.K.BURLEY,S.C.ALMO                                          
JRNL        TITL   CRYSTAL STRUCTURE OF 2-DEHYDROPANTOATE 2-REDUCTASE FROM      
JRNL        TITL 2 GEOBACTER METALLIREDUCENS                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0034                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 42815                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.292                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1371                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2749                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.03                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4310                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 97                           
REMARK   3   BIN FREE R VALUE                    : 0.4520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9301                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 7                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.97000                                             
REMARK   3    B22 (A**2) : -4.35000                                             
REMARK   3    B33 (A**2) : 8.32000                                              
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): 0.800         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.346         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.353         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 37.145        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9466 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12798 ; 1.233 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1205 ; 7.137 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   438 ;33.283 ;23.219       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1621 ;20.150 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    96 ;15.157 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1436 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7210 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4079 ; 0.131 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6248 ; 0.302 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   387 ; 0.154 ; 0.500       
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):    85 ; 0.105 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.109 ; 0.500       
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):  6136 ; 3.973 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9465 ; 5.907 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3732 ; 8.789 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3332 ;11.922 ; 6.000       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   303                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5300  22.5020  -7.7730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0210 T22:  -0.0268                                     
REMARK   3      T33:  -0.1380 T12:   0.0609                                     
REMARK   3      T13:   0.0089 T23:  -0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4573 L22:   0.4068                                     
REMARK   3      L33:   0.3906 L12:  -0.3505                                     
REMARK   3      L13:   0.1128 L23:  -0.3103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:   0.0522 S13:  -0.2002                       
REMARK   3      S21:   0.0096 S22:  -0.0929 S23:   0.1184                       
REMARK   3      S31:  -0.0635 S32:   0.0209 S33:   0.0951                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     3        B   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8310  21.6050 -40.1980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1043 T22:   0.0497                                     
REMARK   3      T33:  -0.0358 T12:   0.0894                                     
REMARK   3      T13:  -0.0784 T23:   0.0665                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6536 L22:   0.8913                                     
REMARK   3      L33:   1.2539 L12:  -0.8023                                     
REMARK   3      L13:   0.9063 L23:   0.1769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0662 S12:   0.4352 S13:   0.3377                       
REMARK   3      S21:   0.0254 S22:  -0.2513 S23:   0.0576                       
REMARK   3      S31:  -0.1024 S32:   0.2499 S33:   0.3176                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     3        C   302                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2660  57.1050  14.0500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0382 T22:  -0.0566                                     
REMARK   3      T33:  -0.0677 T12:  -0.1117                                     
REMARK   3      T13:   0.0147 T23:  -0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9516 L22:   1.5522                                     
REMARK   3      L33:   0.3592 L12:   0.3658                                     
REMARK   3      L13:  -0.0464 L23:  -0.0936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0189 S12:  -0.1432 S13:   0.3217                       
REMARK   3      S21:  -0.1864 S22:  -0.1014 S23:   0.0801                       
REMARK   3      S31:  -0.0010 S32:   0.0820 S33:   0.0826                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     3        D   301                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.4150  68.8350  36.8590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0325 T22:   0.0114                                     
REMARK   3      T33:   0.0035 T12:  -0.1581                                     
REMARK   3      T13:   0.0398 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9619 L22:   1.4244                                     
REMARK   3      L33:   0.9482 L12:   1.6448                                     
REMARK   3      L13:  -0.8796 L23:  -0.5789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1270 S12:  -0.3462 S13:  -0.1607                       
REMARK   3      S21:   0.1219 S22:  -0.2252 S23:   0.0269                       
REMARK   3      S31:   0.0446 S32:   0.0118 S33:   0.0982                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
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 3HN2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053335.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9790                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45333                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.14000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.94000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXDE, RESOLVE                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, PH 6.0, 20% PEG8000, 200MM    
REMARK 280  CALCIUM ACETATE, 10% GLYCEROL, TEMPERATURE 294K, VAPOR DIFFUSION,   
REMARK 280  SITTING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.65900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      100.64550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.08950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      100.64550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.65900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.08950            
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 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 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     MET A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     HIS A   305                                                      
REMARK 465     HIS A   306                                                      
REMARK 465     HIS A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     HIS A   309                                                      
REMARK 465     HIS A   310                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLU B   303                                                      
REMARK 465     GLY B   304                                                      
REMARK 465     HIS B   305                                                      
REMARK 465     HIS B   306                                                      
REMARK 465     HIS B   307                                                      
REMARK 465     HIS B   308                                                      
REMARK 465     HIS B   309                                                      
REMARK 465     HIS B   310                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 465     GLU C   303                                                      
REMARK 465     GLY C   304                                                      
REMARK 465     HIS C   305                                                      
REMARK 465     HIS C   306                                                      
REMARK 465     HIS C   307                                                      
REMARK 465     HIS C   308                                                      
REMARK 465     HIS C   309                                                      
REMARK 465     HIS C   310                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     SER D     0                                                      
REMARK 465     GLY D   302                                                      
REMARK 465     GLU D   303                                                      
REMARK 465     GLY D   304                                                      
REMARK 465     HIS D   305                                                      
REMARK 465     HIS D   306                                                      
REMARK 465     HIS D   307                                                      
REMARK 465     HIS D   308                                                      
REMARK 465     HIS D   309                                                      
REMARK 465     HIS D   310                                                      
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    PRO B 133   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO C 133   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO D 133   C   -  N   -  CA  ANGL. DEV. =  11.3 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    ARG A  31      -75.48   -130.77                                   
REMARK 500    ASN A  48       35.30    -92.86                                   
REMARK 500    GLU A  93      108.31    -58.35                                   
REMARK 500    PRO A 133       94.95    -11.10                                   
REMARK 500    ALA A 141     -143.17     53.68                                   
REMARK 500    PRO A 151       46.23    -80.14                                   
REMARK 500    ASP A 153      175.19    116.41                                   
REMARK 500    THR A 301       56.46   -115.40                                   
REMARK 500    ALA B   8     -139.16     55.43                                   
REMARK 500    ASP B  33       59.92   -113.95                                   
REMARK 500    ASN B  48       37.15    -95.62                                   
REMARK 500    ALA B  79       42.94   -104.06                                   
REMARK 500    PHE B 114      -37.88   -135.19                                   
REMARK 500    PRO B 133       93.08    -10.81                                   
REMARK 500    ALA B 141     -139.82     48.91                                   
REMARK 500    ASP B 153      149.19    179.80                                   
REMARK 500    ALA B 228       66.95   -113.65                                   
REMARK 500    GLU B 252       54.58    -93.48                                   
REMARK 500    ALA C   8       59.65    -95.09                                   
REMARK 500    ARG C  31      -70.22   -116.75                                   
REMARK 500    ASN C  48       38.21    -90.73                                   
REMARK 500    GLU C  93       95.72    -53.62                                   
REMARK 500    PRO C 133       84.36    -21.74                                   
REMARK 500    ALA C 141     -139.44     50.77                                   
REMARK 500    PRO C 151       36.47    -91.04                                   
REMARK 500    ASP C 153      -90.66    -95.16                                   
REMARK 500    THR C 154      -81.99   -127.46                                   
REMARK 500    ASP C 170       98.37    -67.99                                   
REMARK 500    GLN C 199       63.21     35.60                                   
REMARK 500    GLU C 268       49.17    -85.15                                   
REMARK 500    MET C 287       67.79   -119.37                                   
REMARK 500    ALA D   8     -128.77     53.38                                   
REMARK 500    ARG D  31      -32.31   -140.91                                   
REMARK 500    PHE D  45       76.63   -104.18                                   
REMARK 500    GLU D  93       96.45    -57.92                                   
REMARK 500    PHE D 114      -67.10   -127.60                                   
REMARK 500    PRO D 133       73.40    -17.37                                   
REMARK 500    THR D 154      -64.35    -97.71                                   
REMARK 500    GLU D 252       54.87    -96.96                                   
REMARK 500    GLU D 268       48.02    -97.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B  130     GLY B  131                  144.17                    
REMARK 500 GLY B  131     GLU B  132                  138.24                    
REMARK 500 LEU B  150     PRO B  151                 -149.10                    
REMARK 500 ARG B  152     ASP B  153                  130.75                    
REMARK 500 LEU C  150     PRO C  151                 -144.58                    
REMARK 500 ARG C  152     ASP C  153                  -48.92                    
REMARK 500 ASP C  153     THR C  154                 -143.11                    
REMARK 500 LEU D  150     PRO D  151                 -147.49                    
REMARK 500 ARG D  152     ASP D  153                 -133.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-11135A   RELATED DB: TARGETDB                    
DBREF  3HN2 A    2   302  UNP    Q39SB2   Q39SB2_GEOMG     2    302             
DBREF  3HN2 B    2   302  UNP    Q39SB2   Q39SB2_GEOMG     2    302             
DBREF  3HN2 C    2   302  UNP    Q39SB2   Q39SB2_GEOMG     2    302             
DBREF  3HN2 D    2   302  UNP    Q39SB2   Q39SB2_GEOMG     2    302             
SEQADV 3HN2 MET A   -1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 SER A    0  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 LEU A    1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLU A  303  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLY A  304  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  305  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  306  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  307  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  308  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  309  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS A  310  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 MET B   -1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 SER B    0  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 LEU B    1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLU B  303  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLY B  304  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  305  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  306  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  307  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  308  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  309  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS B  310  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 MET C   -1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 SER C    0  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 LEU C    1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLU C  303  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLY C  304  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  305  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  306  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  307  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  308  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  309  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS C  310  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 MET D   -1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 SER D    0  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 LEU D    1  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLU D  303  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 GLY D  304  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  305  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  306  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  307  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  308  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  309  UNP  Q39SB2              EXPRESSION TAG                 
SEQADV 3HN2 HIS D  310  UNP  Q39SB2              EXPRESSION TAG                 
SEQRES   1 A  312  MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU          
SEQRES   2 A  312  GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU          
SEQRES   3 A  312  ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE          
SEQRES   4 A  312  ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP          
SEQRES   5 A  312  PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU          
SEQRES   6 A  312  GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS          
SEQRES   7 A  312  THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO          
SEQRES   8 A  312  LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN          
SEQRES   9 A  312  GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY          
SEQRES  10 A  312  ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER          
SEQRES  11 A  312  ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA          
SEQRES  12 A  312  GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR          
SEQRES  13 A  312  GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA          
SEQRES  14 A  312  GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA          
SEQRES  15 A  312  ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY          
SEQRES  16 A  312  LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU          
SEQRES  17 A  312  ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET          
SEQRES  18 A  312  LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA          
SEQRES  19 A  312  THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU          
SEQRES  20 A  312  PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU          
SEQRES  21 A  312  ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA          
SEQRES  22 A  312  ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY          
SEQRES  23 A  312  ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU          
SEQRES  24 A  312  GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  312  MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU          
SEQRES   2 B  312  GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU          
SEQRES   3 B  312  ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE          
SEQRES   4 B  312  ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP          
SEQRES   5 B  312  PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU          
SEQRES   6 B  312  GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS          
SEQRES   7 B  312  THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO          
SEQRES   8 B  312  LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN          
SEQRES   9 B  312  GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY          
SEQRES  10 B  312  ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER          
SEQRES  11 B  312  ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA          
SEQRES  12 B  312  GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR          
SEQRES  13 B  312  GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA          
SEQRES  14 B  312  GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA          
SEQRES  15 B  312  ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY          
SEQRES  16 B  312  LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU          
SEQRES  17 B  312  ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET          
SEQRES  18 B  312  LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA          
SEQRES  19 B  312  THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU          
SEQRES  20 B  312  PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU          
SEQRES  21 B  312  ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA          
SEQRES  22 B  312  ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY          
SEQRES  23 B  312  ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU          
SEQRES  24 B  312  GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  312  MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU          
SEQRES   2 C  312  GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU          
SEQRES   3 C  312  ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE          
SEQRES   4 C  312  ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP          
SEQRES   5 C  312  PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU          
SEQRES   6 C  312  GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS          
SEQRES   7 C  312  THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO          
SEQRES   8 C  312  LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN          
SEQRES   9 C  312  GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY          
SEQRES  10 C  312  ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER          
SEQRES  11 C  312  ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA          
SEQRES  12 C  312  GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR          
SEQRES  13 C  312  GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA          
SEQRES  14 C  312  GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA          
SEQRES  15 C  312  ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY          
SEQRES  16 C  312  LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU          
SEQRES  17 C  312  ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET          
SEQRES  18 C  312  LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA          
SEQRES  19 C  312  THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU          
SEQRES  20 C  312  PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU          
SEQRES  21 C  312  ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA          
SEQRES  22 C  312  ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY          
SEQRES  23 C  312  ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU          
SEQRES  24 C  312  GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  312  MET SER LEU ARG ILE ALA ILE VAL GLY ALA GLY ALA LEU          
SEQRES   2 D  312  GLY LEU TYR TYR GLY ALA LEU LEU GLN ARG SER GLY GLU          
SEQRES   3 D  312  ASP VAL HIS PHE LEU LEU ARG ARG ASP TYR GLU ALA ILE          
SEQRES   4 D  312  ALA GLY ASN GLY LEU LYS VAL PHE SER ILE ASN GLY ASP          
SEQRES   5 D  312  PHE THR LEU PRO HIS VAL LYS GLY TYR ARG ALA PRO GLU          
SEQRES   6 D  312  GLU ILE GLY PRO MET ASP LEU VAL LEU VAL GLY LEU LYS          
SEQRES   7 D  312  THR PHE ALA ASN SER ARG TYR GLU GLU LEU ILE ARG PRO          
SEQRES   8 D  312  LEU VAL GLU GLU GLY THR GLN ILE LEU THR LEU GLN ASN          
SEQRES   9 D  312  GLY LEU GLY ASN GLU GLU ALA LEU ALA THR LEU PHE GLY          
SEQRES  10 D  312  ALA GLU ARG ILE ILE GLY GLY VAL ALA PHE LEU CYS SER          
SEQRES  11 D  312  ASN ARG GLY GLU PRO GLY GLU VAL HIS HIS LEU GLY ALA          
SEQRES  12 D  312  GLY ARG ILE ILE LEU GLY GLU PHE LEU PRO ARG ASP THR          
SEQRES  13 D  312  GLY ARG ILE GLU GLU LEU ALA ALA MET PHE ARG GLN ALA          
SEQRES  14 D  312  GLY VAL ASP CYS ARG THR THR ASP ASP LEU LYS ARG ALA          
SEQRES  15 D  312  ARG TRP GLU LYS LEU VAL TRP ASN ILE PRO PHE ASN GLY          
SEQRES  16 D  312  LEU CYS ALA LEU LEU GLN GLN PRO VAL ASN LEU ILE LEU          
SEQRES  17 D  312  ALA ARG ASP VAL SER ARG LYS LEU VAL ARG GLY ILE MET          
SEQRES  18 D  312  LEU GLU VAL ILE ALA GLY ALA ASN ALA GLN GLY LEU ALA          
SEQRES  19 D  312  THR PHE ILE ALA ASP GLY TYR VAL ASP ASP MET LEU GLU          
SEQRES  20 D  312  PHE THR ASP ALA MET GLY GLU TYR LYS PRO SER MET GLU          
SEQRES  21 D  312  ILE ASP ARG GLU GLU GLY ARG PRO LEU GLU ILE ALA ALA          
SEQRES  22 D  312  ILE PHE ARG THR PRO LEU ALA TYR GLY ALA ARG GLU GLY          
SEQRES  23 D  312  ILE ALA MET PRO ARG VAL GLU MET LEU ALA THR LEU LEU          
SEQRES  24 D  312  GLU GLN ALA THR GLY GLU GLY HIS HIS HIS HIS HIS HIS          
FORMUL   5  HOH   *7(H2 O)                                                      
HELIX    1   1 LEU A   11  SER A   22  1                                  12    
HELIX    2   2 ASP A   33  ASN A   40  1                                   8    
HELIX    3   3 ALA A   61  GLY A   66  1                                   6    
HELIX    4   4 LYS A   76  SER A   81  5                                   6    
HELIX    5   5 ARG A   82  ARG A   88  1                                   7    
HELIX    6   6 PRO A   89  VAL A   91  5                                   3    
HELIX    7   7 GLY A  105  PHE A  114  1                                  10    
HELIX    8   8 GLY A  115  GLU A  117  5                                   3    
HELIX    9   9 THR A  154  ALA A  167  1                                  14    
HELIX   10  10 ASP A  176  GLN A  199  1                                  24    
HELIX   11  11 PRO A  201  LEU A  206  1                                   6    
HELIX   12  12 ARG A  208  ALA A  228  1                                  21    
HELIX   13  13 GLY A  238  ASP A  248  1                                  11    
HELIX   14  14 PRO A  255  GLU A  263  1                                   9    
HELIX   15  15 GLU A  268  PHE A  273  1                                   6    
HELIX   16  16 PHE A  273  GLU A  283  1                                  11    
HELIX   17  17 MET A  287  THR A  301  1                                  15    
HELIX   18  18 ALA B    8  SER B   22  1                                  15    
HELIX   19  19 TYR B   34  GLY B   39  1                                   6    
HELIX   20  20 ALA B   61  GLY B   66  1                                   6    
HELIX   21  21 LYS B   76  ASN B   80  5                                   5    
HELIX   22  22 ARG B   82  ARG B   88  1                                   7    
HELIX   23  23 PRO B   89  VAL B   91  5                                   3    
HELIX   24  24 GLY B  105  PHE B  114  1                                  10    
HELIX   25  25 GLY B  115  GLU B  117  5                                   3    
HELIX   26  26 ASP B  153  ALA B  167  1                                  15    
HELIX   27  27 ASP B  176  GLN B  199  1                                  24    
HELIX   28  28 PRO B  201  LEU B  206  1                                   6    
HELIX   29  29 ARG B  208  ALA B  228  1                                  21    
HELIX   30  30 GLY B  238  ASP B  248  1                                  11    
HELIX   31  31 PRO B  255  GLY B  264  1                                  10    
HELIX   32  32 GLU B  268  PHE B  273  1                                   6    
HELIX   33  33 PHE B  273  GLU B  283  1                                  11    
HELIX   34  34 MET B  287  GLY B  302  1                                  16    
HELIX   35  35 LEU C   11  SER C   22  1                                  12    
HELIX   36  36 ASP C   33  ALA C   38  1                                   6    
HELIX   37  37 ALA C   61  ILE C   65  5                                   5    
HELIX   38  38 LYS C   76  SER C   81  5                                   6    
HELIX   39  39 ARG C   82  ARG C   88  1                                   7    
HELIX   40  40 PRO C   89  VAL C   91  5                                   3    
HELIX   41  41 GLY C  105  GLY C  115  1                                  11    
HELIX   42  42 THR C  154  GLN C  166  1                                  13    
HELIX   43  43 ASP C  176  ILE C  189  1                                  14    
HELIX   44  44 ILE C  189  GLN C  199  1                                  11    
HELIX   45  45 PRO C  201  LEU C  206  1                                   6    
HELIX   46  46 ARG C  208  ASN C  227  1                                  20    
HELIX   47  47 GLY C  238  ALA C  249  1                                  12    
HELIX   48  48 PRO C  255  GLY C  264  1                                  10    
HELIX   49  49 GLU C  268  PHE C  273  1                                   6    
HELIX   50  50 PHE C  273  ARG C  282  1                                  10    
HELIX   51  51 MET C  287  THR C  301  1                                  15    
HELIX   52  52 ALA D    8  SER D   22  1                                  15    
HELIX   53  53 TYR D   34  GLY D   39  1                                   6    
HELIX   54  54 ALA D   61  GLY D   66  1                                   6    
HELIX   55  55 LYS D   76  SER D   81  5                                   6    
HELIX   56  56 ARG D   82  ARG D   88  1                                   7    
HELIX   57  57 PRO D   89  VAL D   91  5                                   3    
HELIX   58  58 GLY D  105  PHE D  114  1                                  10    
HELIX   59  59 THR D  154  ALA D  167  1                                  14    
HELIX   60  60 ASP D  176  ASN D  192  1                                  17    
HELIX   61  61 GLY D  193  GLN D  199  1                                   7    
HELIX   62  62 PRO D  201  LEU D  206  1                                   6    
HELIX   63  63 ARG D  208  ALA D  228  1                                  21    
HELIX   64  64 GLY D  238  MET D  250  1                                  13    
HELIX   65  65 PRO D  255  GLU D  263  1                                   9    
HELIX   66  66 GLU D  268  PHE D  273  1                                   6    
HELIX   67  67 PHE D  273  GLU D  283  1                                  11    
HELIX   68  68 MET D  287  THR D  301  1                                  15    
SHEET    1   A 8 GLY A  58  TYR A  59  0                                        
SHEET    2   A 8 VAL A  26  LEU A  29  1  N  PHE A  28   O  TYR A  59           
SHEET    3   A 8 ILE A   3  VAL A   6  1  N  ILE A   5   O  HIS A  27           
SHEET    4   A 8 LEU A  70  VAL A  73  1  O  LEU A  72   N  VAL A   6           
SHEET    5   A 8 GLN A  96  THR A  99  1  O  LEU A  98   N  VAL A  73           
SHEET    6   A 8 ILE A 119  CYS A 127  1  O  ILE A 120   N  ILE A  97           
SHEET    7   A 8 GLY A 140  GLU A 148 -1  O  GLY A 147   N  GLY A 121           
SHEET    8   A 8 CYS A 171  THR A 173  1  O  ARG A 172   N  ILE A 144           
SHEET    1   B 3 PHE A  51  LEU A  53  0                                        
SHEET    2   B 3 LEU A  42  SER A  46 -1  N  VAL A  44   O  PHE A  51           
SHEET    3   B 3 GLU A 135  HIS A 138  1  O  VAL A 136   N  PHE A  45           
SHEET    1   C 9 PHE B  51  LEU B  53  0                                        
SHEET    2   C 9 LEU B  42  PHE B  45 -1  N  VAL B  44   O  PHE B  51           
SHEET    3   C 9 GLU B 135  GLU B 148  1  O  VAL B 136   N  PHE B  45           
SHEET    4   C 9 ILE B 119  ARG B 130 -1  N  GLY B 121   O  GLY B 147           
SHEET    5   C 9 GLN B  96  THR B  99  1  N  ILE B  97   O  ILE B 120           
SHEET    6   C 9 LEU B  70  VAL B  73  1  N  VAL B  73   O  LEU B  98           
SHEET    7   C 9 ARG B   2  VAL B   6  1  N  ALA B   4   O  LEU B  72           
SHEET    8   C 9 ASP B  25  LEU B  29  1  O  HIS B  27   N  ILE B   3           
SHEET    9   C 9 GLY B  58  TYR B  59  1  O  TYR B  59   N  PHE B  28           
SHEET    1   D 4 PHE B  51  LEU B  53  0                                        
SHEET    2   D 4 LEU B  42  PHE B  45 -1  N  VAL B  44   O  PHE B  51           
SHEET    3   D 4 GLU B 135  GLU B 148  1  O  VAL B 136   N  PHE B  45           
SHEET    4   D 4 CYS B 171  THR B 173  1  O  ARG B 172   N  LEU B 146           
SHEET    1   E 9 PHE C  51  LEU C  53  0                                        
SHEET    2   E 9 LEU C  42  PHE C  45 -1  N  VAL C  44   O  PHE C  51           
SHEET    3   E 9 GLU C 135  GLU C 148  1  O  VAL C 136   N  PHE C  45           
SHEET    4   E 9 ILE C 119  GLU C 132 -1  N  GLY C 121   O  GLY C 147           
SHEET    5   E 9 GLN C  96  THR C  99  1  N  ILE C  97   O  ILE C 120           
SHEET    6   E 9 LEU C  70  VAL C  73  1  N  VAL C  71   O  LEU C  98           
SHEET    7   E 9 ARG C   2  VAL C   6  1  N  ALA C   4   O  LEU C  72           
SHEET    8   E 9 ASP C  25  LEU C  29  1  O  ASP C  25   N  ILE C   3           
SHEET    9   E 9 GLY C  58  TYR C  59  1  O  TYR C  59   N  PHE C  28           
SHEET    1   F 4 PHE C  51  LEU C  53  0                                        
SHEET    2   F 4 LEU C  42  PHE C  45 -1  N  VAL C  44   O  PHE C  51           
SHEET    3   F 4 GLU C 135  GLU C 148  1  O  VAL C 136   N  PHE C  45           
SHEET    4   F 4 CYS C 171  THR C 173  1  O  ARG C 172   N  LEU C 146           
SHEET    1   G 9 ASP D  50  LEU D  53  0                                        
SHEET    2   G 9 LEU D  42  PHE D  45 -1  N  VAL D  44   O  PHE D  51           
SHEET    3   G 9 GLU D 135  GLU D 148  1  O  VAL D 136   N  PHE D  45           
SHEET    4   G 9 ILE D 119  ARG D 130 -1  N  CYS D 127   O  LEU D 139           
SHEET    5   G 9 GLN D  96  THR D  99  1  N  ILE D  97   O  ILE D 120           
SHEET    6   G 9 LEU D  70  VAL D  73  1  N  VAL D  73   O  LEU D  98           
SHEET    7   G 9 ARG D   2  VAL D   6  1  N  ALA D   4   O  LEU D  72           
SHEET    8   G 9 ASP D  25  LEU D  29  1  O  HIS D  27   N  ILE D   3           
SHEET    9   G 9 LYS D  57  TYR D  59  1  O  LYS D  57   N  PHE D  28           
SHEET    1   H 4 ASP D  50  LEU D  53  0                                        
SHEET    2   H 4 LEU D  42  PHE D  45 -1  N  VAL D  44   O  PHE D  51           
SHEET    3   H 4 GLU D 135  GLU D 148  1  O  VAL D 136   N  PHE D  45           
SHEET    4   H 4 CYS D 171  THR D 173  1  O  ARG D 172   N  LEU D 146           
CRYST1   77.318   82.179  201.291  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012934  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012169  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004968        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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