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Database: PDB
Entry: 5J07
LinkDB: 5J07
Original site: 5J07 
HEADER    OXIDOREDUCTASE                          27-MAR-16   5J07              
TITLE     MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE, LOOPS IV AND VII DELETED, 
TITLE    2 APO FORM, CIRCULAR PERMUTANT P1/2                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN],SUPEROXIDE DISMUTASE [CU-ZN], 
COMPND   3 SUPEROXIDE DISMUTASE [CU-ZN],SUPEROXIDE DISMUTASE [CU-ZN];           
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: SUPEROXIDE DISMUTASE 1,HSOD1,SUPEROXIDE DISMUTASE 1,HSOD1,  
COMPND   6 SUPEROXIDE DISMUTASE 1,HSOD1,SUPEROXIDE DISMUTASE 1,HSOD1;           
COMPND   7 EC: 1.15.1.1,1.15.1.1,1.15.1.1,1.15.1.1;                             
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333                                       
KEYWDS    SOD1, OXIDOREDUCTASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.WANG,L.LANG,D.LOGAN,J.DANIELSSON,M.OLIVEBERG                        
REVDAT   2   17-JAN-18 5J07    1       REMARK                                   
REVDAT   1   01-FEB-17 5J07    0                                                
JRNL        AUTH   H.WANG,L.LANG,D.T.LOGAN,J.DANIELSSON,M.OLIVEBERG             
JRNL        TITL   TRICKING A PROTEIN TO SWAP STRANDS.                          
JRNL        REF    J. AM. CHEM. SOC.             V. 138 15571 2016              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   27783493                                                     
JRNL        DOI    10.1021/JACS.6B05151                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 12221                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 644                             
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 896                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 45                           
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1594                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 85                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.96000                                              
REMARK   3    B22 (A**2) : 0.96000                                              
REMARK   3    B33 (A**2) : -3.11000                                             
REMARK   3    B12 (A**2) : 0.96000                                              
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): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.183         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.047        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1615 ; 0.004 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  1582 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2182 ; 0.880 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3638 ; 0.801 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   228 ; 4.755 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;36.771 ;25.714       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   252 ;11.253 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     4 ; 9.748 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   253 ; 0.056 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1904 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   336 ; 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):   918 ; 3.174 ; 4.119       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   917 ; 3.169 ; 4.111       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1144 ; 4.112 ; 6.155       
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):  3197 ; 7.113 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    36 ;49.725 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  3226 ;32.341 ; 5.000       
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  : 2                                          
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     1        A   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6882 -18.2236  -0.1497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0634 T22:   0.0362                                     
REMARK   3      T33:   0.1485 T12:   0.0039                                     
REMARK   3      T13:  -0.0055 T23:   0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1297 L22:   0.1762                                     
REMARK   3      L33:   0.1055 L12:  -0.0288                                     
REMARK   3      L13:  -0.0658 L23:   0.0813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0203 S12:  -0.0301 S13:  -0.0115                       
REMARK   3      S21:  -0.0426 S22:  -0.0201 S23:  -0.0228                       
REMARK   3      S31:   0.0219 S32:   0.0004 S33:  -0.0001                       
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     1        B   115                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.2713 -12.6403 -22.2038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0523 T22:   0.0520                                     
REMARK   3      T33:   0.1613 T12:  -0.0026                                     
REMARK   3      T13:   0.0108 T23:  -0.0129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5686 L22:   0.5358                                     
REMARK   3      L33:   0.1174 L12:   0.3770                                     
REMARK   3      L13:  -0.1451 L23:  -0.2458                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0807 S12:   0.0211 S13:  -0.0923                       
REMARK   3      S21:  -0.0710 S22:   0.0427 S23:  -0.0608                       
REMARK   3      S31:   0.0228 S32:  -0.0139 S33:   0.0380                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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 U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5J07 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219742.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12893                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.20                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61800                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 4BCZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MIB BUFFER PH 5.0 25 % W/V PEG     
REMARK 280  1500, EVAPORATION, TEMPERATURE 293K                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
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       39.34000            
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       19.67000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.50500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        9.83500            
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       49.17500            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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    ALA B  39      109.36    -59.49                                   
REMARK 500    SER B  57       74.02   -157.81                                   
REMARK 500    ASP B 114      -61.75   -142.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5J07 A    2    37  UNP    P00441   SODC_HUMAN      14     49             
DBREF  5J07 A   42    82  UNP    P00441   SODC_HUMAN      84    124             
DBREF  5J07 A   86    99  UNP    P00441   SODC_HUMAN     141    154             
DBREF  5J07 A  104   115  UNP    P00441   SODC_HUMAN       2     13             
DBREF  5J07 B    2    37  UNP    P00441   SODC_HUMAN      14     49             
DBREF  5J07 B   42    82  UNP    P00441   SODC_HUMAN      84    124             
DBREF  5J07 B   86    99  UNP    P00441   SODC_HUMAN     141    154             
DBREF  5J07 B  104   115  UNP    P00441   SODC_HUMAN       2     13             
SEQADV 5J07 ALA A    1  UNP  P00441              EXPRESSION TAG                 
SEQADV 5J07 GLY A   38  UNP  P00441              LINKER                         
SEQADV 5J07 ALA A   39  UNP  P00441              LINKER                         
SEQADV 5J07 GLY A   40  UNP  P00441              LINKER                         
SEQADV 5J07 GLY A   41  UNP  P00441              LINKER                         
SEQADV 5J07 SER A   70  UNP  P00441    CYS   112 CONFLICT                       
SEQADV 5J07 GLY A   83  UNP  P00441              LINKER                         
SEQADV 5J07 ALA A   84  UNP  P00441              LINKER                         
SEQADV 5J07 GLY A   85  UNP  P00441              LINKER                         
SEQADV 5J07 SER A   92  UNP  P00441    CYS   147 CONFLICT                       
SEQADV 5J07 ALA A  100  UNP  P00441              LINKER                         
SEQADV 5J07 GLY A  101  UNP  P00441              LINKER                         
SEQADV 5J07 ALA A  102  UNP  P00441              LINKER                         
SEQADV 5J07 GLY A  103  UNP  P00441              LINKER                         
SEQADV 5J07 ALA A  104  UNP  P00441    ALA     2 LINKER                         
SEQADV 5J07 ALA A  109  UNP  P00441    CYS     7 CONFLICT                       
SEQADV 5J07 ALA B    1  UNP  P00441              EXPRESSION TAG                 
SEQADV 5J07 GLY B   38  UNP  P00441              LINKER                         
SEQADV 5J07 ALA B   39  UNP  P00441              LINKER                         
SEQADV 5J07 GLY B   40  UNP  P00441              LINKER                         
SEQADV 5J07 GLY B   41  UNP  P00441              LINKER                         
SEQADV 5J07 SER B   70  UNP  P00441    CYS   112 CONFLICT                       
SEQADV 5J07 GLY B   83  UNP  P00441              LINKER                         
SEQADV 5J07 ALA B   84  UNP  P00441              LINKER                         
SEQADV 5J07 GLY B   85  UNP  P00441              LINKER                         
SEQADV 5J07 SER B   92  UNP  P00441    CYS   147 CONFLICT                       
SEQADV 5J07 ALA B  100  UNP  P00441              LINKER                         
SEQADV 5J07 GLY B  101  UNP  P00441              LINKER                         
SEQADV 5J07 ALA B  102  UNP  P00441              LINKER                         
SEQADV 5J07 GLY B  103  UNP  P00441              LINKER                         
SEQADV 5J07 ALA B  104  UNP  P00441    ALA     2 LINKER                         
SEQADV 5J07 ALA B  109  UNP  P00441    CYS     7 CONFLICT                       
SEQRES   1 A  115  ALA PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU          
SEQRES   2 A  115  SER ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY          
SEQRES   3 A  115  LEU THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLY ALA          
SEQRES   4 A  115  GLY GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASP GLY          
SEQRES   5 A  115  VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SER LEU          
SEQRES   6 A  115  SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU VAL VAL          
SEQRES   7 A  115  HIS GLU LYS ALA GLY ALA GLY ALA GLY SER ARG LEU ALA          
SEQRES   8 A  115  SER GLY VAL ILE GLY ILE ALA GLN ALA GLY ALA GLY ALA          
SEQRES   9 A  115  THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY                  
SEQRES   1 B  115  ALA PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU          
SEQRES   2 B  115  SER ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY          
SEQRES   3 B  115  LEU THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLY ALA          
SEQRES   4 B  115  GLY GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASP GLY          
SEQRES   5 B  115  VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE SER LEU          
SEQRES   6 B  115  SER GLY ASP HIS SER ILE ILE GLY ARG THR LEU VAL VAL          
SEQRES   7 B  115  HIS GLU LYS ALA GLY ALA GLY ALA GLY SER ARG LEU ALA          
SEQRES   8 B  115  SER GLY VAL ILE GLY ILE ALA GLN ALA GLY ALA GLY ALA          
SEQRES   9 B  115  THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY                  
FORMUL   3  HOH   *85(H2 O)                                                     
SHEET    1 AA1 8 ASP A  42  ALA A  48  0                                        
SHEET    2 AA1 8 GLY A  30  VAL A  36 -1  N  GLY A  30   O  ALA A  48           
SHEET    3 AA1 8 THR A  75  HIS A  79 -1  O  VAL A  77   N  HIS A  35           
SHEET    4 AA1 8 LEU A  90  ALA A 100 -1  O  GLY A  93   N  LEU A  76           
SHEET    5 AA1 8 THR A 105  LYS A 112 -1  O  LYS A 106   N  ALA A  98           
SHEET    6 AA1 8 GLN A   4  GLN A  11 -1  N  GLN A  11   O  THR A 105           
SHEET    7 AA1 8 VAL A  18  LYS A  25 -1  O  LYS A  25   N  GLN A   4           
SHEET    8 AA1 8 ALA A  54  ASP A  60 -1  O  ILE A  58   N  VAL A  20           
SHEET    1 AA2 8 ASP B  42  ALA B  48  0                                        
SHEET    2 AA2 8 GLY B  30  VAL B  36 -1  N  GLY B  30   O  ALA B  48           
SHEET    3 AA2 8 THR B  75  HIS B  79 -1  O  HIS B  79   N  GLY B  33           
SHEET    4 AA2 8 LEU B  90  GLN B  99 -1  O  GLY B  93   N  LEU B  76           
SHEET    5 AA2 8 THR B 105  LYS B 112 -1  O  VAL B 108   N  GLY B  96           
SHEET    6 AA2 8 GLN B   4  GLN B  11 -1  N  PHE B   9   O  ALA B 107           
SHEET    7 AA2 8 VAL B  18  LYS B  25 -1  O  TRP B  21   N  ASN B   8           
SHEET    8 AA2 8 ALA B  54  ASP B  60 -1  O  ILE B  58   N  VAL B  20           
CISPEP   1 GLY A  101    ALA A  102          0        -2.94                     
CISPEP   2 GLY B  101    ALA B  102          0         2.70                     
CISPEP   3 ALA B  102    GLY B  103          0        -6.67                     
CRYST1   75.040   75.040   59.010  90.00  90.00 120.00 P 65         12          
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      0.013326  0.007694  0.000000        0.00000                         
SCALE2      0.000000  0.015388  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016946        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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