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Database: PDB
Entry: 5J5E
LinkDB: 5J5E
Original site: 5J5E 
HEADER    HYDROLASE                               02-APR-16   5J5E              
TITLE     CRYSTAL STRUCTURE OF ANTIGEN-ERAP1 DOMAIN COMPLEX                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 529-941;                                      
COMPND   5 SYNONYM: ARTS-1,ADIPOCYTE-DERIVED LEUCINE AMINOPEPTIDASE,A-LAP,      
COMPND   6 AMINOPEPTIDASE PILS,PUROMYCIN-INSENSITIVE LEUCYL-SPECIFIC            
COMPND   7 AMINOPEPTIDASE,PILS-AP,TYPE 1 TUMOR NECROSIS FACTOR RECEPTOR SHEDDING
COMPND   8 AMINOPEPTIDASE REGULATOR;                                            
COMPND   9 EC: 3.4.11.-;                                                        
COMPND  10 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: ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154;                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    HYDROLASE, AMINOPEPTIDASE                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.SUI,A.GANDHI,H.-C.GUO                                               
REVDAT   3   11-DEC-19 5J5E    1       REMARK                                   
REVDAT   2   20-SEP-17 5J5E    1       SPRSDE REMARK                            
REVDAT   1   12-APR-17 5J5E    0                                                
SPRSDE     20-SEP-17 5J5E      5J48 5J5E                                        
JRNL        AUTH   A.GANDHI,D.LAKSHMINARASIMHAN,Y.SUN,H.-C.GUO                  
JRNL        TITL   STRUCTURAL INSIGHTS INTO THE MOLECULAR RULER MECHANISM OF    
JRNL        TITL 2 THE ENDOPLASMIC RETICULUM AMINOPEPTIDASE ERAP1.              
JRNL        REF    SCI REP                       V.   1   186 2011              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   22355701                                                     
JRNL        DOI    10.1038/SREP00186                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0124                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.43                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 9400                           
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 500                             
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 722                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 80.11                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 39                           
REMARK   3   BIN FREE R VALUE                    : 0.3700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.22000                                              
REMARK   3    B22 (A**2) : -0.48000                                             
REMARK   3    B33 (A**2) : 0.14000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12000                                              
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): 0.502         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.300         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.211        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.905                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.848                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3405 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3280 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4593 ; 1.610 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7533 ; 1.022 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   404 ; 7.009 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   160 ;37.657 ;24.438       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   636 ;17.236 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;19.680 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   510 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3783 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   805 ; 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):  1631 ; 1.623 ; 2.765       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1630 ; 1.622 ; 2.764       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2032 ; 2.773 ; 4.139       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2033 ; 2.772 ; 4.140       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1774 ; 1.573 ; 2.925       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1774 ; 1.569 ; 2.925       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2561 ; 2.697 ; 4.315       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3793 ; 4.260 ;21.583       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3794 ; 4.259 ;21.588       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 5J5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219985.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.2.0, XIA2                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10114                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.430                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.0                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3RJO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, PH 8.5 AND 16% PEG8000,     
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       33.42500            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     LYS A   551                                                      
REMARK 465     GLY A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     ASP A   554                                                      
REMARK 465     GLY A   555                                                      
REMARK 465     ALA A   556                                                      
REMARK 465     PRO A   557                                                      
REMARK 465     ASP A   558                                                      
REMARK 465     THR A   559                                                      
REMARK 465     GLY A   560                                                      
REMARK 465     GLY A   902                                                      
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     TYR A 561    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 615    CG   OD1  OD2                                       
REMARK 470     CYS A 743    CA                                                  
REMARK 470     LEU A 793    CG   CD1  CD2                                       
REMARK 470     ARG A 885    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 899    CG   CD   CE   NZ                                   
REMARK 470     GLU A 900    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 904    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 910    CG   CD   OE1  NE2                                  
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   OH   TYR A   684     OXT  LEU A   948     2645     2.14            
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    ASP A 575   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    HIS A 611   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    TYR A 740   N   -  CA  -  C   ANGL. DEV. = -19.8 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    ASP A 575      -71.52    -88.39                                   
REMARK 500    TYR A 612     -142.98     59.78                                   
REMARK 500    GLU A 613     -171.48   -176.25                                   
REMARK 500    THR A 627       75.45   -150.94                                   
REMARK 500    SER A 661       10.21    -68.17                                   
REMARK 500    ASP A 691       69.38   -100.40                                   
REMARK 500    MET A 692       44.03   -144.65                                   
REMARK 500    TRP A 716       63.64   -104.69                                   
REMARK 500    LEU A 793       35.32    -99.87                                   
REMARK 500    SER A 883       31.54   -142.15                                   
REMARK 500    SER A 897        1.03    -67.29                                   
REMARK 500    LYS A 899     -136.92     61.99                                   
REMARK 500    LYS A 947     -125.06     58.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5J5E A  529   941  UNP    Q9NZ08   ERAP1_HUMAN    529    941             
SEQADV 5J5E ILE A  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E ILE A  943  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E ASN A  944  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E PHE A  945  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E GLU A  946  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E LYS A  947  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 5J5E LEU A  948  UNP  Q9NZ08              EXPRESSION TAG                 
SEQRES   1 A  420  GLY PHE PRO LEU ILE THR ILE THR VAL ARG GLY ARG ASN          
SEQRES   2 A  420  VAL HIS MET LYS GLN GLU HIS TYR MET LYS GLY SER ASP          
SEQRES   3 A  420  GLY ALA PRO ASP THR GLY TYR LEU TRP HIS VAL PRO LEU          
SEQRES   4 A  420  THR PHE ILE THR SER LYS SER ASP MET VAL HIS ARG PHE          
SEQRES   5 A  420  LEU LEU LYS THR LYS THR ASP VAL LEU ILE LEU PRO GLU          
SEQRES   6 A  420  GLU VAL GLU TRP ILE LYS PHE ASN VAL GLY MET ASN GLY          
SEQRES   7 A  420  TYR TYR ILE VAL HIS TYR GLU ASP ASP GLY TRP ASP SER          
SEQRES   8 A  420  LEU THR GLY LEU LEU LYS GLY THR HIS THR ALA VAL SER          
SEQRES   9 A  420  SER ASN ASP ARG ALA SER LEU ILE ASN ASN ALA PHE GLN          
SEQRES  10 A  420  LEU VAL SER ILE GLY LYS LEU SER ILE GLU LYS ALA LEU          
SEQRES  11 A  420  ASP LEU SER LEU TYR LEU LYS HIS GLU THR GLU ILE MET          
SEQRES  12 A  420  PRO VAL PHE GLN GLY LEU ASN GLU LEU ILE PRO MET TYR          
SEQRES  13 A  420  LYS LEU MET GLU LYS ARG ASP MET ASN GLU VAL GLU THR          
SEQRES  14 A  420  GLN PHE LYS ALA PHE LEU ILE ARG LEU LEU ARG ASP LEU          
SEQRES  15 A  420  ILE ASP LYS GLN THR TRP THR ASP GLU GLY SER VAL SER          
SEQRES  16 A  420  GLU ARG MET LEU ARG SER GLN LEU LEU LEU LEU ALA CYS          
SEQRES  17 A  420  VAL HIS ASN TYR GLN PRO CYS VAL GLN ARG ALA GLU GLY          
SEQRES  18 A  420  TYR PHE ARG LYS TRP LYS GLU SER ASN GLY ASN LEU SER          
SEQRES  19 A  420  LEU PRO VAL ASP VAL THR LEU ALA VAL PHE ALA VAL GLY          
SEQRES  20 A  420  ALA GLN SER THR GLU GLY TRP ASP PHE LEU TYR SER LYS          
SEQRES  21 A  420  TYR GLN PHE SER LEU SER SER THR GLU LYS SER GLN ILE          
SEQRES  22 A  420  GLU PHE ALA LEU CYS ARG THR GLN ASN LYS GLU LYS LEU          
SEQRES  23 A  420  GLN TRP LEU LEU ASP GLU SER PHE LYS GLY ASP LYS ILE          
SEQRES  24 A  420  LYS THR GLN GLU PHE PRO GLN ILE LEU THR LEU ILE GLY          
SEQRES  25 A  420  ARG ASN PRO VAL GLY TYR PRO LEU ALA TRP GLN PHE LEU          
SEQRES  26 A  420  ARG LYS ASN TRP ASN LYS LEU VAL GLN LYS PHE GLU LEU          
SEQRES  27 A  420  GLY SER SER SER ILE ALA HIS MET VAL MET GLY THR THR          
SEQRES  28 A  420  ASN GLN PHE SER THR ARG THR ARG LEU GLU GLU VAL LYS          
SEQRES  29 A  420  GLY PHE PHE SER SER LEU LYS GLU ASN GLY SER GLN LEU          
SEQRES  30 A  420  ARG CYS VAL GLN GLN THR ILE GLU THR ILE GLU GLU ASN          
SEQRES  31 A  420  ILE GLY TRP MET ASP LYS ASN PHE ASP LYS ILE ARG VAL          
SEQRES  32 A  420  TRP LEU GLN SER GLU LYS LEU GLU ARG MET ILE ILE ASN          
SEQRES  33 A  420  PHE GLU LYS LEU                                              
HELIX    1 AA1 GLU A  613  THR A  627  1                                  15    
HELIX    2 AA2 HIS A  628  VAL A  631  5                                   4    
HELIX    3 AA3 SER A  632  ILE A  649  1                                  18    
HELIX    4 AA4 SER A  653  SER A  661  1                                   9    
HELIX    5 AA5 LEU A  662  HIS A  666  5                                   5    
HELIX    6 AA6 GLU A  669  GLU A  688  1                                  20    
HELIX    7 AA7 MET A  692  LEU A  707  1                                  16    
HELIX    8 AA8 LEU A  707  LYS A  713  1                                   7    
HELIX    9 AA9 SER A  721  HIS A  738  1                                  18    
HELIX   10 AB1 TYR A  740  SER A  757  1                                  18    
HELIX   11 AB2 VAL A  767  ALA A  776  1                                  10    
HELIX   12 AB3 SER A  778  SER A  792  1                                  15    
HELIX   13 AB4 SER A  794  ARG A  807  1                                  14    
HELIX   14 AB5 ASN A  810  GLY A  824  1                                  15    
HELIX   15 AB6 LYS A  828  GLN A  830  5                                   3    
HELIX   16 AB7 GLU A  831  ARG A  841  1                                  11    
HELIX   17 AB8 GLY A  845  ASN A  856  1                                  12    
HELIX   18 AB9 ASN A  856  PHE A  864  1                                   9    
HELIX   19 AC1 SER A  868  ASN A  880  1                                  13    
HELIX   20 AC2 THR A  884  SER A  897  1                                  14    
HELIX   21 AC3 LEU A  905  ILE A  942  1                                  38    
SHEET    1 AA1 4 THR A 586  ILE A 590  0                                        
SHEET    2 AA1 4 ASN A 541  TYR A 549 -1  N  VAL A 542   O  LEU A 589           
SHEET    3 AA1 4 PHE A 530  ARG A 538 -1  N  THR A 536   O  HIS A 543           
SHEET    4 AA1 4 ILE A 609  VAL A 610  1  O  ILE A 609   N  ILE A 533           
SHEET    1 AA2 3 HIS A 578  LEU A 582  0                                        
SHEET    2 AA2 3 VAL A 565  THR A 571 -1  N  PHE A 569   O  HIS A 578           
SHEET    3 AA2 3 ILE A 598  VAL A 602 -1  O  ASN A 601   N  THR A 568           
CRYST1   64.260   66.850   66.500  90.00 110.16  90.00 P 1 21 1      2          
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      0.015562  0.000000  0.005713        0.00000                         
SCALE2      0.000000  0.014959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016019        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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