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Database: PDB
Entry: 2Q13
LinkDB: 2Q13
Original site: 2Q13 
HEADER    PROTEIN TRANSPORT                       23-MAY-07   2Q13              
TITLE     CRYSTAL STRUCTURE OF BAR-PH DOMAIN OF APPL1                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DCC-INTERACTING PROTEIN 13 ALPHA;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 5-385, BAR AND PH DOMAINS;                        
COMPND   5 SYNONYM: DIP13 ALPHA, ADAPTER PROTEIN CONTAINING PH DOMAIN;          
COMPND   6 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: APPL1, APPL, DIP13A, KIAA1428;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B                                    
KEYWDS    APPL1, BAR DOMAIN, PH DOMAIN, BAR-PH DOMAIN, PROTEIN TRANSPORT        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.ZHU,X.C.ZHANG                                                       
REVDAT   3   13-JUL-11 2Q13    1       VERSN                                    
REVDAT   2   24-FEB-09 2Q13    1       VERSN                                    
REVDAT   1   14-AUG-07 2Q13    0                                                
JRNL        AUTH   G.ZHU,J.CHEN,J.LIU,J.S.BRUNZELLE,B.HUANG,N.WAKEHAM,          
JRNL        AUTH 2 S.TERZYAN,X.LI,Z.RAO,G.LI,X.C.ZHANG                          
JRNL        TITL   STRUCTURE OF THE APPL1 BAR-PH DOMAIN AND CHARACTERIZATION OF 
JRNL        TITL 2 ITS INTERACTION WITH RAB5.                                   
JRNL        REF    EMBO J.                       V.  26  3484 2007              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   17581628                                                     
JRNL        DOI    10.1038/SJ.EMBOJ.7601771                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 22082                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1200                            
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) : 2.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1319                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2060                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 67                           
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2943                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 38.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.72000                                             
REMARK   3    B22 (A**2) : 2.66000                                              
REMARK   3    B33 (A**2) : -0.94000                                             
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): 0.251         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.217         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.139         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.849         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
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):  2991 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4028 ; 1.302 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   361 ; 5.196 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   154 ;37.334 ;25.260       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   566 ;18.412 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;21.536 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   445 ; 0.089 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2248 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1265 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2081 ; 0.297 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   129 ; 0.152 ; 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):   126 ; 0.174 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.197 ; 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):  1885 ; 2.777 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2934 ; 4.047 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1262 ; 3.313 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1094 ; 4.848 ; 3.000       
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  : 1                                          
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     4        A   378                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8878  -0.0215   2.2490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0135 T22:  -0.0198                                     
REMARK   3      T33:  -0.0371 T12:  -0.0364                                     
REMARK   3      T13:  -0.0201 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6938 L22:   0.4750                                     
REMARK   3      L33:   0.0036 L12:   0.5707                                     
REMARK   3      L13:   0.0424 L23:   0.0372                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0115 S12:  -0.0352 S13:   0.1186                       
REMARK   3      S21:  -0.0395 S22:  -0.0120 S23:   0.0960                       
REMARK   3      S31:  -0.0197 S32:   0.0098 S33:   0.0235                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Q13 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043016.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE-CRYSTAL      
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23286                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG6000, 0.6M NACL, PH 8.0, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.86850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.83750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.86850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.83750            
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 300 REMARK: THE BIOLOGICAL DIMER IS GENERATED BY ASYMMETRIC UNIT AND     
REMARK 300 OPRATION: -X+1, -Y, Z                                                
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 12900 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 36450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
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   BIOMT1   2 -1.000000  0.000000  0.000000      103.73700            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     ASN A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     THR A   290                                                      
REMARK 465     GLY A   291                                                      
REMARK 465     LEU A   292                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     SER A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     LEU A   379                                                      
REMARK 465     SER A   380                                                      
REMARK 465     GLU A   381                                                      
REMARK 465     ASN A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     GLU A   384                                                      
REMARK 465     GLU A   385                                                      
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 121      -62.93   -101.00                                   
REMARK 500    ASN A 327       29.60     47.35                                   
REMARK 500    TYR A 340       38.61     74.83                                   
REMARK 500    PHE A 347       44.22    -76.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 492        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH A 534        DISTANCE =  6.02 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Q12   RELATED DB: PDB                                   
DBREF  2Q13 A    5   385  UNP    Q9UKG1   DP13A_HUMAN      5    385             
SEQADV 2Q13 GLY A    1  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q13 SER A    2  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q13 HIS A    3  UNP  Q9UKG1              EXPRESSION TAG                 
SEQADV 2Q13 MET A    4  UNP  Q9UKG1              EXPRESSION TAG                 
SEQRES   1 A  385  GLY SER HIS MET ASP LYS LEU PRO ILE GLU GLU THR LEU          
SEQRES   2 A  385  GLU ASP SER PRO GLN THR ARG SER LEU LEU GLY VAL PHE          
SEQRES   3 A  385  GLU GLU ASP ALA THR ALA ILE SER ASN TYR MET ASN GLN          
SEQRES   4 A  385  LEU TYR GLN ALA MET HIS ARG ILE TYR ASP ALA GLN ASN          
SEQRES   5 A  385  GLU LEU SER ALA ALA THR HIS LEU THR SER LYS LEU LEU          
SEQRES   6 A  385  LYS GLU TYR GLU LYS GLN ARG PHE PRO LEU GLY GLY ASP          
SEQRES   7 A  385  ASP GLU VAL MET SER SER THR LEU GLN GLN PHE SER LYS          
SEQRES   8 A  385  VAL ILE ASP GLU LEU SER SER CYS HIS ALA VAL LEU SER          
SEQRES   9 A  385  THR GLN LEU ALA ASP ALA MET MET PHE PRO ILE THR GLN          
SEQRES  10 A  385  PHE LYS GLU ARG ASP LEU LYS GLU ILE LEU THR LEU LYS          
SEQRES  11 A  385  GLU VAL PHE GLN ILE ALA SER ASN ASP HIS ASP ALA ALA          
SEQRES  12 A  385  ILE ASN ARG TYR SER ARG LEU SER LYS LYS ARG GLU ASN          
SEQRES  13 A  385  ASP LYS VAL LYS TYR GLU VAL THR GLU ASP VAL TYR THR          
SEQRES  14 A  385  SER ARG LYS LYS GLN HIS GLN THR MET MET HIS TYR PHE          
SEQRES  15 A  385  CYS ALA LEU ASN THR LEU GLN TYR LYS LYS LYS ILE ALA          
SEQRES  16 A  385  LEU LEU GLU PRO LEU LEU GLY TYR MET GLN ALA GLN ILE          
SEQRES  17 A  385  SER PHE PHE LYS MET GLY SER GLU ASN LEU ASN GLU GLN          
SEQRES  18 A  385  LEU GLU GLU PHE LEU ALA ASN ILE GLY THR SER VAL GLN          
SEQRES  19 A  385  ASN VAL ARG ARG GLU MET ASP SER ASP ILE GLU THR MET          
SEQRES  20 A  385  GLN GLN THR ILE GLU ASP LEU GLU VAL ALA SER ASP PRO          
SEQRES  21 A  385  LEU TYR VAL PRO ASP PRO ASP PRO THR LYS PHE PRO VAL          
SEQRES  22 A  385  ASN ARG ASN LEU THR ARG LYS ALA GLY TYR LEU ASN ALA          
SEQRES  23 A  385  ARG ASN LYS THR GLY LEU VAL SER SER THR TRP ASP ARG          
SEQRES  24 A  385  GLN PHE TYR PHE THR GLN GLY GLY ASN LEU MET SER GLN          
SEQRES  25 A  385  ALA ARG GLY ASP VAL ALA GLY GLY LEU ALA MET ASP ILE          
SEQRES  26 A  385  ASP ASN CYS SER VAL MET ALA VAL ASP CYS GLU ASP ARG          
SEQRES  27 A  385  ARG TYR CYS PHE GLN ILE THR SER PHE ASP GLY LYS LYS          
SEQRES  28 A  385  SER SER ILE LEU GLN ALA GLU SER LYS LYS ASP HIS GLU          
SEQRES  29 A  385  GLU TRP ILE CYS THR ILE ASN ASN ILE SER LYS GLN ILE          
SEQRES  30 A  385  TYR LEU SER GLU ASN PRO GLU GLU                              
FORMUL   2  HOH   *157(H2 O)                                                    
HELIX    1   1 PRO A    8  THR A   12  5                                   5    
HELIX    2   2 SER A   16  GLU A   67  1                                  52    
HELIX    3   3 GLU A   80  MET A  111  1                                  32    
HELIX    4   4 MET A  111  ARG A  121  1                                  11    
HELIX    5   5 ARG A  121  ARG A  149  1                                  29    
HELIX    6   6 ASN A  156  LEU A  218  1                                  63    
HELIX    7   7 ASN A  219  ASP A  259  1                                  41    
HELIX    8   8 PRO A  260  TYR A  262  5                                   3    
HELIX    9   9 SER A  359  LYS A  375  1                                  17    
SHEET    1   A 7 GLY A 320  ASP A 324  0                                        
SHEET    2   A 7 ASN A 308  GLN A 312 -1  N  LEU A 309   O  MET A 323           
SHEET    3   A 7 ASP A 298  GLN A 305 -1  N  GLN A 305   O  ASN A 308           
SHEET    4   A 7 ALA A 281  ALA A 286 -1  N  GLY A 282   O  TYR A 302           
SHEET    5   A 7 LEU A 355  GLN A 356 -1  O  GLN A 356   N  ASN A 285           
SHEET    6   A 7 CYS A 341  THR A 345 -1  N  PHE A 342   O  LEU A 355           
SHEET    7   A 7 SER A 329  VAL A 333 -1  N  SER A 329   O  THR A 345           
CRYST1  103.737  105.675   36.407  90.00  90.00  90.00 P 21 21 2     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      0.009640  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.027467        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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