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Database: PDB
Entry: 3RJO
LinkDB: 3RJO
Original site: 3RJO 
HEADER    HYDROLASE                               15-APR-11   3RJO              
TITLE     CRYSTAL STRUCTURE OF ERAP1 PEPTIDE BINDING DOMAIN                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1;                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ERAP1, RESIDUES 530-941;                                   
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       
COMPND   8 SHEDDING 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_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    ERAP1, AMINOPEPTIDASE, HYDROLASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-C.GUO,D.LAKSHMINARASIMHAN,A.GANDHI                                 
REVDAT   2   07-MAR-12 3RJO    1       JRNL                                     
REVDAT   1   21-DEC-11 3RJO    0                                                
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.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22138                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.262                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1199                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1672                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.83                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 71                           
REMARK   3   BIN FREE R VALUE                    : 0.3450                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3336                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 145                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.33000                                             
REMARK   3    B22 (A**2) : -0.26000                                             
REMARK   3    B33 (A**2) : 0.42000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.23000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.295         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.244         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.159         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.492         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3421 ; 0.047 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4615 ; 2.113 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   405 ; 6.336 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   163 ;37.927 ;24.233       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   629 ;20.129 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.005 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   507 ; 0.138 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2537 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2027 ; 0.975 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3277 ; 1.896 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1394 ; 3.353 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1338 ; 5.337 ; 4.500       
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   : 1.40                                          
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 3RJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB065014.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-06                          
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                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23337                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.10400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.2M MGCL, PH 8.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       33.65500            
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     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     GLN A 910    CG   CD   OE1  NE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     CYS A  743   CA                                                  
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 736   CB    CYS A 736   SG      0.203                       
REMARK 500    CYS A 743   CA    CYS A 743   CB     -0.251                       
REMARK 500    CYS A 743   CB    CYS A 743   SG      0.403                       
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 587   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    CYS A 743   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES          
REMARK 500    CYS A 743   N   -  CA  -  CB  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    CYS A 743   CA  -  CB  -  SG  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    ARG A 854   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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      -75.99    -94.80                                   
REMARK 500    GLU A 613      168.95     68.86                                   
REMARK 500    MET A 692       35.18   -146.64                                   
REMARK 500    GLU A 865      138.15     92.55                                   
REMARK 500    SER A 883       31.97   -147.81                                   
REMARK 500    LYS A 899     -114.15     56.22                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 931        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2                   
DBREF  3RJO A  529   941  UNP    Q9NZ08   ERAP1_HUMAN    529    941             
SEQADV 3RJO HIS A  942  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3RJO HIS A  943  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3RJO HIS A  944  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3RJO HIS A  945  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3RJO HIS A  946  UNP  Q9NZ08              EXPRESSION TAG                 
SEQADV 3RJO HIS A  947  UNP  Q9NZ08              EXPRESSION TAG                 
SEQRES   1 A  419  GLY PHE PRO LEU ILE THR ILE THR VAL ARG GLY ARG ASN          
SEQRES   2 A  419  VAL HIS MET LYS GLN GLU HIS TYR MET LYS GLY SER ASP          
SEQRES   3 A  419  GLY ALA PRO ASP THR GLY TYR LEU TRP HIS VAL PRO LEU          
SEQRES   4 A  419  THR PHE ILE THR SER LYS SER ASP MET VAL HIS ARG PHE          
SEQRES   5 A  419  LEU LEU LYS THR LYS THR ASP VAL LEU ILE LEU PRO GLU          
SEQRES   6 A  419  GLU VAL GLU TRP ILE LYS PHE ASN VAL GLY MET ASN GLY          
SEQRES   7 A  419  TYR TYR ILE VAL HIS TYR GLU ASP ASP GLY TRP ASP SER          
SEQRES   8 A  419  LEU THR GLY LEU LEU LYS GLY THR HIS THR ALA VAL SER          
SEQRES   9 A  419  SER ASN ASP ARG ALA SER LEU ILE ASN ASN ALA PHE GLN          
SEQRES  10 A  419  LEU VAL SER ILE GLY LYS LEU SER ILE GLU LYS ALA LEU          
SEQRES  11 A  419  ASP LEU SER LEU TYR LEU LYS HIS GLU THR GLU ILE MET          
SEQRES  12 A  419  PRO VAL PHE GLN GLY LEU ASN GLU LEU ILE PRO MET TYR          
SEQRES  13 A  419  LYS LEU MET GLU LYS ARG ASP MET ASN GLU VAL GLU THR          
SEQRES  14 A  419  GLN PHE LYS ALA PHE LEU ILE ARG LEU LEU ARG ASP LEU          
SEQRES  15 A  419  ILE ASP LYS GLN THR TRP THR ASP GLU GLY SER VAL SER          
SEQRES  16 A  419  GLU ARG MET LEU ARG SER GLN LEU LEU LEU LEU ALA CYS          
SEQRES  17 A  419  VAL HIS ASN TYR GLN PRO CYS VAL GLN ARG ALA GLU GLY          
SEQRES  18 A  419  TYR PHE ARG LYS TRP LYS GLU SER ASN GLY ASN LEU SER          
SEQRES  19 A  419  LEU PRO VAL ASP VAL THR LEU ALA VAL PHE ALA VAL GLY          
SEQRES  20 A  419  ALA GLN SER THR GLU GLY TRP ASP PHE LEU TYR SER LYS          
SEQRES  21 A  419  TYR GLN PHE SER LEU SER SER THR GLU LYS SER GLN ILE          
SEQRES  22 A  419  GLU PHE ALA LEU CYS ARG THR GLN ASN LYS GLU LYS LEU          
SEQRES  23 A  419  GLN TRP LEU LEU ASP GLU SER PHE LYS GLY ASP LYS ILE          
SEQRES  24 A  419  LYS THR GLN GLU PHE PRO GLN ILE LEU THR LEU ILE GLY          
SEQRES  25 A  419  ARG ASN PRO VAL GLY TYR PRO LEU ALA TRP GLN PHE LEU          
SEQRES  26 A  419  ARG LYS ASN TRP ASN LYS LEU VAL GLN LYS PHE GLU LEU          
SEQRES  27 A  419  GLY SER SER SER ILE ALA HIS MET VAL MET GLY THR THR          
SEQRES  28 A  419  ASN GLN PHE SER THR ARG THR ARG LEU GLU GLU VAL LYS          
SEQRES  29 A  419  GLY PHE PHE SER SER LEU LYS GLU ASN GLY SER GLN LEU          
SEQRES  30 A  419  ARG CYS VAL GLN GLN THR ILE GLU THR ILE GLU GLU ASN          
SEQRES  31 A  419  ILE GLY TRP MET ASP LYS ASN PHE ASP LYS ILE ARG VAL          
SEQRES  32 A  419  TRP LEU GLN SER GLU LYS LEU GLU ARG MET HIS HIS HIS          
SEQRES  33 A  419  HIS HIS HIS                                                  
HET    EDO  A   1       4                                                       
HET    EDO  A   2       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    2(C2 H6 O2)                                                  
FORMUL   4  HOH   *145(H2 O)                                                    
HELIX    1   1 TYR A  612  HIS A  628  1                                  17    
HELIX    2   2 THR A  629  VAL A  631  5                                   3    
HELIX    3   3 SER A  632  ILE A  649  1                                  18    
HELIX    4   4 SER A  653  LEU A  662  1                                  10    
HELIX    5   5 TYR A  663  GLU A  667  5                                   5    
HELIX    6   6 GLU A  669  GLU A  688  1                                  20    
HELIX    7   7 MET A  692  GLN A  714  1                                  23    
HELIX    8   8 SER A  721  HIS A  738  1                                  18    
HELIX    9   9 TYR A  740  SER A  757  1                                  18    
HELIX   10  10 PRO A  764  ASP A  766  5                                   3    
HELIX   11  11 VAL A  767  ALA A  776  1                                  10    
HELIX   12  12 SER A  778  SER A  792  1                                  15    
HELIX   13  13 SER A  794  CYS A  806  1                                  13    
HELIX   14  14 ASN A  810  GLY A  824  1                                  15    
HELIX   15  15 LYS A  828  GLN A  830  5                                   3    
HELIX   16  16 GLU A  831  ARG A  841  1                                  11    
HELIX   17  17 GLY A  845  GLU A  865  1                                  21    
HELIX   18  18 SER A  868  THR A  878  1                                  11    
HELIX   19  19 THR A  884  SER A  897  1                                  14    
HELIX   20  20 LEU A  905  HIS A  942  1                                  38    
HELIX   21  21 HIS A  943  HIS A  947  5                                   5    
SHEET    1   A 4 THR A 586  ILE A 590  0                                        
SHEET    2   A 4 ASN A 541  TYR A 549 -1  N  MET A 544   O  ASP A 587           
SHEET    3   A 4 PHE A 530  ARG A 538 -1  N  THR A 536   O  HIS A 543           
SHEET    4   A 4 ILE A 609  HIS A 611  1  O  HIS A 611   N  ILE A 533           
SHEET    1   B 3 HIS A 578  LEU A 582  0                                        
SHEET    2   B 3 VAL A 565  THR A 571 -1  N  VAL A 565   O  LEU A 582           
SHEET    3   B 3 ILE A 598  VAL A 602 -1  O  ASN A 601   N  THR A 568           
SSBOND   1 CYS A  736    CYS A  743                          1555   1555  2.08  
SITE     1 AC1  2 ASN A 918  TRP A 921                                          
SITE     1 AC2  5 ASP A 659  TRP A 932  SER A 935  GLU A 936                    
SITE     2 AC2  5 GLU A 939                                                     
CRYST1   63.840   67.310   65.920  90.00 110.25  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      0.015664  0.000000  0.005779        0.00000                         
SCALE2      0.000000  0.014857  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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