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Database: PDB
Entry: 1VJ1
LinkDB: 1VJ1
Original site: 1VJ1 
HEADER    UNKNOWN FUNCTION                        03-DEC-03   1VJ1              
TITLE     CRYSTAL STRUCTURE OF PUTATIVE NADPH-DEPENDENT OXIDOREDUCTASE FROM MUS 
TITLE    2 MUSCULUS AT 2.10 A RESOLUTION                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE NADPH-DEPENDENT OXIDOREDUCTASE;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ZADH1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    PUTATIVE NADPH-DEPENDENT OXIDOREDUCTASE, STRUCTURAL GENOMICS, JCSG,   
KEYWDS   2 PSI, PROTEIN STRUCTURE INITIATIVE, JOINT CENTER FOR STRUCTURAL       
KEYWDS   3 GENOMICS, UNKNOWN FUNCTION                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   6   13-JUL-11 1VJ1    1       VERSN                                    
REVDAT   5   24-FEB-09 1VJ1    1       VERSN                                    
REVDAT   4   20-SEP-05 1VJ1    1       JRNL                                     
REVDAT   3   18-JAN-05 1VJ1    1       AUTHOR KEYWDS REMARK                     
REVDAT   2   03-AUG-04 1VJ1    1       JRNL   TITLE  KEYWDS COMPND              
REVDAT   1   09-DEC-03 1VJ1    0                                                
JRNL        AUTH   I.LEVIN,R.SCHWARZENBACHER,D.MCMULLAN,P.ABDUBEK,E.AMBING,     
JRNL        AUTH 2 T.BIORAC,J.CAMBELL,J.M.CANAVES,H.J.CHIU,X.DAI,A.M.DEACON,    
JRNL        AUTH 3 M.DIDONATO,M.A.ELSLIGER,A.GODZIK,C.GRITTINI,S.K.GRZECHNIK,   
JRNL        AUTH 4 E.HAMPTON,L.JAROSZEWSKI,C.KARLAK,H.E.KLOCK,E.KOESEMA,        
JRNL        AUTH 5 A.KREUSCH,P.KUHN,S.A.LESLEY,T.M.MCPHILLIPS,M.D.MILLER,       
JRNL        AUTH 6 A.MORSE,K.MOY,J.OUYANG,R.PAGE,K.QUIJANO,R.REYES,A.ROBB,      
JRNL        AUTH 7 E.SIMS,G.SPRAGGON,R.C.STEVENS,H.VAN DEN BEDEM,J.VELASQUEZ,   
JRNL        AUTH 8 J.VINCENT,F.VON DELFT,X.WANG,B.WEST,G.WOLF,Q.XU,K.O.HODGSON, 
JRNL        AUTH 9 J.WOOLEY,I.A.WILSON                                          
JRNL        TITL   CRYSTAL STRUCTURE OF A PUTATIVE NADPH-DEPENDENT              
JRNL        TITL 2 OXIDOREDUCTASE (GI: 18204011) FROM MOUSE AT 2.10 A           
JRNL        TITL 3 RESOLUTION                                                   
JRNL        REF    PROTEINS                      V.  56   629 2004              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   15229897                                                     
JRNL        DOI    10.1002/PROT.20163                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.9999                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21310                          
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1123                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1211                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2555                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 41.59                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : -0.72000                                             
REMARK   3    B33 (A**2) : 0.35000                                              
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): 0.200         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.168         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.520         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2615 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2376 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3540 ; 1.473 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5542 ; 0.824 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   341 ; 6.660 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   109 ;42.504 ;25.321       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   442 ;14.852 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;21.759 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   399 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2947 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   491 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   530 ; 0.201 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2528 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1630 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   124 ; 0.128 ; 0.200       
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):    14 ; 0.149 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    59 ; 0.297 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.267 ; 0.200       
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):  1780 ; 2.368 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   710 ; 0.533 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2693 ; 3.254 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1008 ; 6.205 ; 8.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   846 ; 7.828 ;11.000       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -1        A   131                          
REMARK   3    RESIDUE RANGE :   A   315        A   351                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.1800  64.3100  15.4230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1940 T22:   0.0816                                     
REMARK   3      T33:   0.0197 T12:   0.0081                                     
REMARK   3      T13:  -0.0252 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0267 L22:   3.5314                                     
REMARK   3      L33:   1.9826 L12:   0.3164                                     
REMARK   3      L13:  -0.2337 L23:   0.4615                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0308 S12:  -0.0792 S13:   0.0053                       
REMARK   3      S21:   0.2789 S22:  -0.0217 S23:   0.0342                       
REMARK   3      S31:  -0.0426 S32:  -0.1305 S33:  -0.0091                       
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 :   A   132        A   314                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3540  47.1410  39.4000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2070 T22:   0.0971                                     
REMARK   3      T33:   0.1045 T12:  -0.0121                                     
REMARK   3      T13:   0.0355 T23:   0.0531                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3515 L22:   1.8092                                     
REMARK   3      L33:   3.2123 L12:  -0.1933                                     
REMARK   3      L13:   1.0833 L23:  -0.0665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0451 S12:  -0.0745 S13:   0.0338                       
REMARK   3      S21:   0.0493 S22:   0.1324 S23:   0.0278                       
REMARK   3      S31:  -0.1994 S32:  -0.1416 S33:  -0.0873                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1VJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB001912.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAY-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.10                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97950, 0.9793, 0.9567            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22460                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.560                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.10                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.43100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE/RESOLVE                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CITRATE PH 5.1, 0.2M NH4OAC, 15%    
REMARK 280  PEG-4000 , VAPOR DIFFUSION,SITTING DROP,NANODROP, TEMPERATURE       
REMARK 280  277K, PH 5.10                                                       
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       21.19300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.28250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.90250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.28250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.19300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.90250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     ASP A    -8                                                      
REMARK 465     LYS A    -7                                                      
REMARK 465     ILE A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     GLN A   255                                                      
REMARK 465     ILE A   256                                                      
REMARK 465     SER A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     TYR A   259                                                      
REMARK 465     ASN A   260                                                      
REMARK 465     LYS A   261                                                      
REMARK 465     ASP A   262                                                      
REMARK 465     VAL A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A  32    CG   OD1  OD2                                       
REMARK 470     TYR A  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 115    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 191    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 212    CG   OD1                                            
REMARK 470     ARG A 286    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 297    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 320    CE   NZ                                             
REMARK 470     GLU A 347    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   421     O    HOH A   503     2564     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 187   CB    CYS A 187   SG     -0.103                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  24   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A  24   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP A  49   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A  75   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 230   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 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    ASN A 212       53.50   -113.46                                   
REMARK 500    VAL A 232     -158.67   -121.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 354739   RELATED DB: TARGETDB                            
DBREF  1VJ1 A    1   351  UNP    Q8VDQ1   ZADH1_MOUSE      1    351             
SEQADV 1VJ1 GLY A  -10  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 SER A   -9  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 ASP A   -8  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 LYS A   -7  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 ILE A   -6  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A   -5  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A   -4  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A   -3  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A   -2  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A   -1  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 HIS A    0  UNP  Q8VDQ1              LEADER SEQUENCE                
SEQADV 1VJ1 MSE A    1  UNP  Q8VDQ1    MET     1 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A   52  UNP  Q8VDQ1    MET    52 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A   56  UNP  Q8VDQ1    MET    56 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  135  UNP  Q8VDQ1    MET   135 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  158  UNP  Q8VDQ1    MET   158 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  244  UNP  Q8VDQ1    MET   244 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  325  UNP  Q8VDQ1    MET   325 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  332  UNP  Q8VDQ1    MET   332 MODIFIED RESIDUE               
SEQADV 1VJ1 MSE A  333  UNP  Q8VDQ1    MET   333 MODIFIED RESIDUE               
SEQRES   1 A  363  MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MSE          
SEQRES   2 A  363  ILE ILE GLN ARG VAL VAL LEU ASN SER ARG PRO GLY LYS          
SEQRES   3 A  363  ASN GLY ASN PRO VAL ALA GLU ASN PHE ARG VAL GLU GLU          
SEQRES   4 A  363  PHE SER LEU LEU ASP ALA LEU ASN GLU GLY GLN VAL GLN          
SEQRES   5 A  363  VAL ARG THR LEU TYR LEU SER VAL ASP PRO TYR MSE ARG          
SEQRES   6 A  363  CYS LYS MSE ASN GLU ASP THR GLY THR ASP TYR LEU ALA          
SEQRES   7 A  363  PRO TRP GLN LEU ALA GLN VAL ALA ASP GLY GLY GLY ILE          
SEQRES   8 A  363  GLY ILE VAL GLU GLU SER LYS HIS GLN LYS LEU ALA LYS          
SEQRES   9 A  363  GLY ASP PHE VAL THR SER PHE TYR TRP PRO TRP GLN THR          
SEQRES  10 A  363  LYS ALA ILE LEU ASP GLY ASN GLY LEU GLU LYS VAL ASP          
SEQRES  11 A  363  PRO GLN LEU VAL ASP GLY HIS LEU SER TYR PHE LEU GLY          
SEQRES  12 A  363  ALA ILE GLY MSE PRO GLY LEU THR SER LEU ILE GLY VAL          
SEQRES  13 A  363  GLN GLU LYS GLY HIS ILE SER ALA GLY SER ASN GLN THR          
SEQRES  14 A  363  MSE VAL VAL SER GLY ALA ALA GLY ALA CYS GLY SER LEU          
SEQRES  15 A  363  ALA GLY GLN ILE GLY HIS LEU LEU GLY CYS SER ARG VAL          
SEQRES  16 A  363  VAL GLY ILE CYS GLY THR GLN GLU LYS CYS LEU PHE LEU          
SEQRES  17 A  363  THR SER GLU LEU GLY PHE ASP ALA ALA VAL ASN TYR LYS          
SEQRES  18 A  363  THR GLY ASN VAL ALA GLU GLN LEU ARG GLU ALA CYS PRO          
SEQRES  19 A  363  GLY GLY VAL ASP VAL TYR PHE ASP ASN VAL GLY GLY ASP          
SEQRES  20 A  363  ILE SER ASN THR VAL ILE SER GLN MSE ASN GLU ASN SER          
SEQRES  21 A  363  HIS ILE ILE LEU CYS GLY GLN ILE SER GLN TYR ASN LYS          
SEQRES  22 A  363  ASP VAL PRO TYR PRO PRO PRO LEU PRO PRO ALA VAL GLU          
SEQRES  23 A  363  ALA ILE ARG LYS GLU ARG ASN ILE THR ARG GLU ARG PHE          
SEQRES  24 A  363  THR VAL LEU ASN TYR LYS ASP LYS PHE GLU PRO GLY ILE          
SEQRES  25 A  363  LEU GLN LEU SER GLN TRP PHE LYS GLU GLY LYS LEU LYS          
SEQRES  26 A  363  VAL LYS GLU THR VAL ALA LYS GLY LEU GLU ASN MSE GLY          
SEQRES  27 A  363  VAL ALA PHE GLN SER MSE MSE THR GLY GLY ASN VAL GLY          
SEQRES  28 A  363  LYS GLN ILE VAL CYS ILE SER GLU ASP SER SER LEU              
MODRES 1VJ1 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A   52  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A   56  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  135  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  158  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  244  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  325  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  332  MET  SELENOMETHIONINE                                   
MODRES 1VJ1 MSE A  333  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  52       8                                                       
HET    MSE  A  56       8                                                       
HET    MSE  A 135       8                                                       
HET    MSE  A 158       8                                                       
HET    MSE  A 244       8                                                       
HET    MSE  A 325       8                                                       
HET    MSE  A 332       8                                                       
HET    MSE  A 333       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    9(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *153(H2 O)                                                    
HELIX    1   1 VAL A   19  GLU A   21  5                                   3    
HELIX    2   2 ASP A   49  ASN A   57  5                                   9    
HELIX    3   3 ASN A  112  LEU A  114  5                                   3    
HELIX    4   4 ASP A  118  ASP A  123  5                                   6    
HELIX    5   5 HIS A  125  GLY A  131  5                                   7    
HELIX    6   6 GLY A  134  GLY A  148  1                                  15    
HELIX    7   7 CYS A  167  SER A  169  5                                   3    
HELIX    8   8 LEU A  170  LEU A  178  1                                   9    
HELIX    9   9 THR A  189  LEU A  200  1                                  12    
HELIX   10  10 ASN A  212  CYS A  221  1                                  10    
HELIX   11  11 GLY A  233  SER A  242  1                                  10    
HELIX   12  12 PRO A  270  ARG A  280  1                                  11    
HELIX   13  13 THR A  288  ASP A  294  5                                   7    
HELIX   14  14 LYS A  295  GLU A  309  1                                  15    
HELIX   15  15 ASN A  324  THR A  334  1                                  11    
SHEET    1   A 2 HIS A   0  LEU A   8  0                                        
SHEET    2   A 2 PHE A  23  LEU A  31 -1  O  LEU A  30   N  MSE A   1           
SHEET    1   B 5 LYS A 106  ASP A 110  0                                        
SHEET    2   B 5 GLN A  38  VAL A  48 -1  N  VAL A  41   O  ALA A 107           
SHEET    3   B 5 ASP A  75  SER A  85 -1  O  GLU A  83   N  GLN A  40           
SHEET    4   B 5 PHE A  95  PRO A 102 -1  O  TRP A 101   N  GLY A  76           
SHEET    5   B 5 GLU A 115  VAL A 117 -1  O  VAL A 117   N  PHE A  95           
SHEET    1   C 4 LYS A 106  ASP A 110  0                                        
SHEET    2   C 4 GLN A  38  VAL A  48 -1  N  VAL A  41   O  ALA A 107           
SHEET    3   C 4 LYS A 340  CYS A 344 -1  O  VAL A 343   N  LEU A  46           
SHEET    4   C 4 GLU A 316  LYS A 320  1  N  ALA A 319   O  CYS A 344           
SHEET    1   D 6 ALA A 204  ASN A 207  0                                        
SHEET    2   D 6 ARG A 182  CYS A 187  1  N  GLY A 185   O  VAL A 206           
SHEET    3   D 6 THR A 157  VAL A 160  1  N  MSE A 158   O  VAL A 184           
SHEET    4   D 6 VAL A 225  ASP A 230  1  O  PHE A 229   N  VAL A 159           
SHEET    5   D 6 MSE A 244  LEU A 252  1  O  ILE A 251   N  TYR A 228           
SHEET    6   D 6 THR A 283  ARG A 286  1  O  THR A 283   N  ILE A 250           
LINK         C   HIS A   0                 N   MSE A   1     1555   1555  1.32  
LINK         C   MSE A   1                 N   ILE A   2     1555   1555  1.32  
LINK         C   TYR A  51                 N   MSE A  52     1555   1555  1.32  
LINK         C   MSE A  52                 N   ARG A  53     1555   1555  1.33  
LINK         C   LYS A  55                 N   MSE A  56     1555   1555  1.33  
LINK         C   MSE A  56                 N   ASN A  57     1555   1555  1.33  
LINK         C   GLY A 134                 N   MSE A 135     1555   1555  1.32  
LINK         C   MSE A 135                 N   PRO A 136     1555   1555  1.32  
LINK         C   THR A 157                 N   MSE A 158     1555   1555  1.32  
LINK         C   MSE A 158                 N   VAL A 159     1555   1555  1.33  
LINK         C   GLN A 243                 N   MSE A 244     1555   1555  1.34  
LINK         C   MSE A 244                 N   ASN A 245     1555   1555  1.33  
LINK         C   ASN A 324                 N   MSE A 325     1555   1555  1.33  
LINK         C   MSE A 325                 N   GLY A 326     1555   1555  1.33  
LINK         C   SER A 331                 N   MSE A 332     1555   1555  1.32  
LINK         C   MSE A 332                 N   MSE A 333     1555   1555  1.33  
LINK         C   MSE A 333                 N   THR A 334     1555   1555  1.33  
CRYST1   42.386   91.805  100.565  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.023593  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009944        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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