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 4 19-MAY-21 5J5E 1 JRNL
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 L.SUI,A.GANDHI,H.C.GUO
JRNL TITL CRYSTAL STRUCTURE OF A POLYPEPTIDE'S C-TERMINUS IN COMPLEX
JRNL TITL 2 WITH THE REGULATORY DOMAIN OF ER AMINOPEPTIDASE 1.
JRNL REF MOL.IMMUNOL. V. 80 41 2016
JRNL REFN ISSN 0161-5890
JRNL PMID 27825049
JRNL DOI 10.1016/J.MOLIMM.2016.10.012
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.GANDHI,D.LAKSHMINARASIMHAN,Y.SUN,H.-C.GUO
REMARK 1 TITL STRUCTURAL INSIGHTS INTO THE MOLECULAR RULER MECHANISM OF
REMARK 1 TITL 2 THE ENDOPLASMIC RETICULUM AMINOPEPTIDASE ERAP1.
REMARK 1 REF SCI REP V. 1 186 2011
REMARK 1 REFN ESSN 2045-2322
REMARK 1 PMID 22355701
REMARK 1 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
