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HEADER HYDROLASE 13-NOV-18 6I5G
TITLE X-RAY STRUCTURE OF HUMAN SOLUBLE EPOXIDE HYDROLASE C-TERMINAL DOMAIN
TITLE 2 (HSEH CTD)IN COMPLEX WITH 15D-PGJ2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.10,3.1.3.76;
COMPND 5 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: EPHX2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HSEH CTD, APOPROTEIN, ALPHA_BETA HYDROLASE FOLD, 15D-PGJ2, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.ABIS,J.KOPEC,W.W.YUE,M.R.CONTE
REVDAT 1 29-MAY-19 6I5G 0
JRNL AUTH G.ABIS,R.L.CHARLES,J.KOPEC,W.W.YUE,R.A.ATKINSON,T.T.T.BUI,
JRNL AUTH 2 S.LYNHAM,S.POPOVA,Y.-B.SUN,F.FRATERNALI,P.EATON,M.R.CONTE
JRNL TITL 15-DEOXY-DELTA12,14-PROSTAGLANDIN J2 INHIBITS HUMAN SOLUBLE
JRNL TITL 2 EPOXIDE HYDROLASE BY A DUAL ORTHOSTERIC AND ALLOSTERIC
JRNL TITL 3 MECHANISM
JRNL REF COMMUN BIOL 2019
JRNL REFN ESSN 2399-3642
JRNL DOI 10.1038/S42003-019-0426-2
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0107
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 71.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 46528
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2403
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.06
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3173
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5086
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 226
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : -2.17000
REMARK 3 B33 (A**2) : 1.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.164
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.125
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.594
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.940
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5341 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5007 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7220 ; 2.062 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11558 ; 1.212 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 638 ; 7.240 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;35.197 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 884 ;15.958 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;15.581 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 745 ; 0.147 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5962 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1254 ; 0.002 ; 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): 2534 ; 2.769 ; 3.135
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2535 ; 2.768 ; 3.136
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3166 ; 3.910 ; 4.687
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3167 ; 3.909 ; 4.688
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2807 ; 3.679 ; 3.551
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2808 ; 3.678 ; 3.553
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 4050 ; 5.546 ; 5.155
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 6240 ; 7.349 ;25.585
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 6241 ; 7.349 ;25.594
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 : NULL
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 6I5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1200012863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48933
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 71.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 4.990
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.70200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: REFMAC
REMARK 200 STARTING MODEL: 3ANS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22.5% PEG 3350, 0.2 M MALIC ACID, PH
REMARK 280 7.4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z+1/2
REMARK 290 4555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 38.57391
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.99600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.90645
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.57391
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 39.99600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 51.90645
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 SER A 219
REMARK 465 THR A 220
REMARK 465 GLU A 221
REMARK 465 ASN A 222
REMARK 465 LEU A 223
REMARK 465 TYR A 224
REMARK 465 PHE A 225
REMARK 465 GLN A 226
REMARK 465 GLY A 227
REMARK 465 SER A 228
REMARK 465 SER A 229
REMARK 465 ALA A 546
REMARK 465 ARG A 547
REMARK 465 ASN A 548
REMARK 465 PRO A 549
REMARK 465 PRO A 550
REMARK 465 VAL A 551
REMARK 465 VAL A 552
REMARK 465 SER A 553
REMARK 465 LYS A 554
REMARK 465 MET A 555
REMARK 465 MET B 212
REMARK 465 HIS B 213
REMARK 465 HIS B 214
REMARK 465 HIS B 215
REMARK 465 HIS B 216
REMARK 465 HIS B 217
REMARK 465 HIS B 218
REMARK 465 SER B 219
REMARK 465 THR B 220
REMARK 465 GLU B 221
REMARK 465 ASN B 222
REMARK 465 LEU B 223
REMARK 465 TYR B 224
REMARK 465 PHE B 225
REMARK 465 GLN B 226
REMARK 465 GLY B 227
REMARK 465 SER B 228
REMARK 465 SER B 229
REMARK 465 ALA B 546
REMARK 465 ARG B 547
REMARK 465 ASN B 548
REMARK 465 PRO B 549
REMARK 465 PRO B 550
REMARK 465 VAL B 551
REMARK 465 VAL B 552
REMARK 465 SER B 553
REMARK 465 LYS B 554
REMARK 465 MET B 555
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 THR A 230 OG1 CG2
REMARK 470 SER A 231 OG
REMARK 470 THR B 230 OG1 CG2
REMARK 470 SER B 231 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OH TYR B 466 O HOH B 701 1.92
REMARK 500 OG SER A 432 O HOH A 701 2.02
REMARK 500 O HOH A 706 O HOH A 764 2.15
REMARK 500 O TRP A 510 O HOH A 702 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 275 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 LEU A 428 CB - CG - CD1 ANGL. DEV. = 13.8 DEGREES
REMARK 500 ARG A 440 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 440 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 LEU B 340 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG B 440 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG B 440 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG B 440 NE - CZ - NH2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 MET B 528 CG - SD - CE ANGL. DEV. = 11.0 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 SER A 231 -169.39 -114.59
REMARK 500 GLU A 269 -143.26 -116.56
REMARK 500 ASP A 335 -126.75 60.05
REMARK 500 ASN A 359 -37.93 75.00
REMARK 500 ASN A 431 58.04 -117.29
REMARK 500 LEU A 499 79.76 -102.88
REMARK 500 HIS A 513 3.90 -64.47
REMARK 500 SER B 231 -157.40 -103.72
REMARK 500 GLU B 269 -143.92 -118.52
REMARK 500 ASP B 335 -124.88 61.94
REMARK 500 ASN B 359 -44.40 79.38
REMARK 500 ASN B 368 -67.48 -102.31
REMARK 500 PRO B 433 151.42 -47.69
REMARK 500 VAL B 498 -61.71 -109.17
REMARK 500 HIS B 513 41.81 -102.92
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ARG A 247 VAL A 248 -144.72
REMARK 500 MET A 291 ASP A 292 145.39
REMARK 500 MET B 291 ASP B 292 141.56
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 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTG A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PTG B 607
DBREF 6I5G A 230 555 UNP P34913 HYES_HUMAN 177 502
DBREF 6I5G B 230 555 UNP P34913 HYES_HUMAN 177 502
SEQADV 6I5G MET A 212 UNP P34913 INITIATING METHIONINE
SEQADV 6I5G HIS A 213 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS A 214 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS A 215 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS A 216 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS A 217 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS A 218 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER A 219 UNP P34913 EXPRESSION TAG
SEQADV 6I5G THR A 220 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLU A 221 UNP P34913 EXPRESSION TAG
SEQADV 6I5G ASN A 222 UNP P34913 EXPRESSION TAG
SEQADV 6I5G LEU A 223 UNP P34913 EXPRESSION TAG
SEQADV 6I5G TYR A 224 UNP P34913 EXPRESSION TAG
SEQADV 6I5G PHE A 225 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLN A 226 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLY A 227 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER A 228 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER A 229 UNP P34913 EXPRESSION TAG
SEQADV 6I5G MET B 212 UNP P34913 INITIATING METHIONINE
SEQADV 6I5G HIS B 213 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS B 214 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS B 215 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS B 216 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS B 217 UNP P34913 EXPRESSION TAG
SEQADV 6I5G HIS B 218 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER B 219 UNP P34913 EXPRESSION TAG
SEQADV 6I5G THR B 220 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLU B 221 UNP P34913 EXPRESSION TAG
SEQADV 6I5G ASN B 222 UNP P34913 EXPRESSION TAG
SEQADV 6I5G LEU B 223 UNP P34913 EXPRESSION TAG
SEQADV 6I5G TYR B 224 UNP P34913 EXPRESSION TAG
SEQADV 6I5G PHE B 225 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLN B 226 UNP P34913 EXPRESSION TAG
SEQADV 6I5G GLY B 227 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER B 228 UNP P34913 EXPRESSION TAG
SEQADV 6I5G SER B 229 UNP P34913 EXPRESSION TAG
SEQRES 1 A 344 MET HIS HIS HIS HIS HIS HIS SER THR GLU ASN LEU TYR
SEQRES 2 A 344 PHE GLN GLY SER SER THR SER CYS ASN PRO SER ASP MET
SEQRES 3 A 344 SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG LEU
SEQRES 4 A 344 HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS LEU
SEQRES 5 A 344 CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG TYR
SEQRES 6 A 344 GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL LEU
SEQRES 7 A 344 ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA PRO
SEQRES 8 A 344 PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS LYS
SEQRES 9 A 344 GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER GLN
SEQRES 10 A 344 ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU VAL
SEQRES 11 A 344 TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG ALA
SEQRES 12 A 344 VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN PRO
SEQRES 13 A 344 ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO VAL
SEQRES 14 A 344 PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL ALA
SEQRES 15 A 344 GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE LYS
SEQRES 16 A 344 SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER MET
SEQRES 17 A 344 HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN SER
SEQRES 18 A 344 PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU GLU
SEQRES 19 A 344 GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER GLY
SEQRES 20 A 344 PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU ARG
SEQRES 21 A 344 ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS ILE
SEQRES 22 A 344 LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP PHE
SEQRES 23 A 344 VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP TRP
SEQRES 24 A 344 ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS GLY
SEQRES 25 A 344 HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN GLN
SEQRES 26 A 344 ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN PRO
SEQRES 27 A 344 PRO VAL VAL SER LYS MET
SEQRES 1 B 344 MET HIS HIS HIS HIS HIS HIS SER THR GLU ASN LEU TYR
SEQRES 2 B 344 PHE GLN GLY SER SER THR SER CYS ASN PRO SER ASP MET
SEQRES 3 B 344 SER HIS GLY TYR VAL THR VAL LYS PRO ARG VAL ARG LEU
SEQRES 4 B 344 HIS PHE VAL GLU LEU GLY SER GLY PRO ALA VAL CYS LEU
SEQRES 5 B 344 CYS HIS GLY PHE PRO GLU SER TRP TYR SER TRP ARG TYR
SEQRES 6 B 344 GLN ILE PRO ALA LEU ALA GLN ALA GLY TYR ARG VAL LEU
SEQRES 7 B 344 ALA MET ASP MET LYS GLY TYR GLY GLU SER SER ALA PRO
SEQRES 8 B 344 PRO GLU ILE GLU GLU TYR CYS MET GLU VAL LEU CYS LYS
SEQRES 9 B 344 GLU MET VAL THR PHE LEU ASP LYS LEU GLY LEU SER GLN
SEQRES 10 B 344 ALA VAL PHE ILE GLY HIS ASP TRP GLY GLY MET LEU VAL
SEQRES 11 B 344 TRP TYR MET ALA LEU PHE TYR PRO GLU ARG VAL ARG ALA
SEQRES 12 B 344 VAL ALA SER LEU ASN THR PRO PHE ILE PRO ALA ASN PRO
SEQRES 13 B 344 ASN MET SER PRO LEU GLU SER ILE LYS ALA ASN PRO VAL
SEQRES 14 B 344 PHE ASP TYR GLN LEU TYR PHE GLN GLU PRO GLY VAL ALA
SEQRES 15 B 344 GLU ALA GLU LEU GLU GLN ASN LEU SER ARG THR PHE LYS
SEQRES 16 B 344 SER LEU PHE ARG ALA SER ASP GLU SER VAL LEU SER MET
SEQRES 17 B 344 HIS LYS VAL CYS GLU ALA GLY GLY LEU PHE VAL ASN SER
SEQRES 18 B 344 PRO GLU GLU PRO SER LEU SER ARG MET VAL THR GLU GLU
SEQRES 19 B 344 GLU ILE GLN PHE TYR VAL GLN GLN PHE LYS LYS SER GLY
SEQRES 20 B 344 PHE ARG GLY PRO LEU ASN TRP TYR ARG ASN MET GLU ARG
SEQRES 21 B 344 ASN TRP LYS TRP ALA CYS LYS SER LEU GLY ARG LYS ILE
SEQRES 22 B 344 LEU ILE PRO ALA LEU MET VAL THR ALA GLU LYS ASP PHE
SEQRES 23 B 344 VAL LEU VAL PRO GLN MET SER GLN HIS MET GLU ASP TRP
SEQRES 24 B 344 ILE PRO HIS LEU LYS ARG GLY HIS ILE GLU ASP CYS GLY
SEQRES 25 B 344 HIS TRP THR GLN MET ASP LYS PRO THR GLU VAL ASN GLN
SEQRES 26 B 344 ILE LEU ILE LYS TRP LEU ASP SER ASP ALA ARG ASN PRO
SEQRES 27 B 344 PRO VAL VAL SER LYS MET
HET EDO A 601 4
HET EDO A 602 4
HET EDO A 603 4
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET PTG A 607 23
HET EDO B 601 4
HET EDO B 602 4
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET EDO B 606 4
HET PTG B 607 23
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PTG (5E,14E)-11-OXOPROSTA-5,9,12,14-TETRAEN-1-OIC ACID
HETSYN EDO ETHYLENE GLYCOL
HETSYN PTG 15-DEOXY-DELTA(12,14)-PROSTAGLANDIN J2
FORMUL 3 EDO 12(C2 H6 O2)
FORMUL 9 PTG 2(C20 H28 O3)
FORMUL 17 HOH *226(H2 O)
HELIX 1 AA1 ASN A 233 MET A 237 5 5
HELIX 2 AA2 SER A 270 ARG A 275 5 6
HELIX 3 AA3 TYR A 276 ALA A 284 1 9
HELIX 4 AA4 GLU A 304 TYR A 308 5 5
HELIX 5 AA5 CYS A 309 GLY A 325 1 17
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 ASN A 378 1 9
HELIX 8 AA8 PHE A 381 PHE A 387 1 7
HELIX 9 AA9 GLY A 391 ASN A 400 1 10
HELIX 10 AB1 ASN A 400 PHE A 409 1 10
HELIX 11 AB2 ALA A 411 SER A 415 5 5
HELIX 12 AB3 LYS A 421 GLY A 426 1 6
HELIX 13 AB4 THR A 443 LYS A 456 1 14
HELIX 14 AB5 PHE A 459 TRP A 465 1 7
HELIX 15 AB6 ASN A 468 LYS A 478 1 11
HELIX 16 AB7 VAL A 500 GLN A 505 5 6
HELIX 17 AB8 HIS A 506 TRP A 510 5 5
HELIX 18 AB9 TRP A 525 LYS A 530 1 6
HELIX 19 AC1 LYS A 530 ASP A 545 1 16
HELIX 20 AC2 ASN B 233 MET B 237 5 5
HELIX 21 AC3 SER B 270 ARG B 275 5 6
HELIX 22 AC4 TYR B 276 ALA B 284 1 9
HELIX 23 AC5 GLU B 304 TYR B 308 5 5
HELIX 24 AC6 CYS B 309 GLY B 325 1 17
HELIX 25 AC7 ASP B 335 TYR B 348 1 14
HELIX 26 AC8 PRO B 371 ASN B 378 1 8
HELIX 27 AC9 PHE B 381 PHE B 387 1 7
HELIX 28 AD1 GLY B 391 ASN B 400 1 10
HELIX 29 AD2 ASN B 400 PHE B 409 1 10
HELIX 30 AD3 ALA B 411 SER B 415 5 5
HELIX 31 AD4 LYS B 421 GLY B 426 1 6
HELIX 32 AD5 THR B 443 LYS B 455 1 13
HELIX 33 AD6 PHE B 459 TRP B 465 1 7
HELIX 34 AD7 ASN B 468 LYS B 478 1 11
HELIX 35 AD8 VAL B 500 GLN B 505 5 6
HELIX 36 AD9 HIS B 506 TRP B 510 5 5
HELIX 37 AE1 TRP B 525 LYS B 530 1 6
HELIX 38 AE2 LYS B 530 ASP B 545 1 16
SHEET 1 AA1 8 SER A 238 LYS A 245 0
SHEET 2 AA1 8 VAL A 248 LEU A 255 -1 O PHE A 252 N GLY A 240
SHEET 3 AA1 8 ARG A 287 MET A 291 -1 O VAL A 288 N LEU A 255
SHEET 4 AA1 8 ALA A 260 CYS A 264 1 N LEU A 263 O LEU A 289
SHEET 5 AA1 8 ALA A 329 HIS A 334 1 O VAL A 330 N CYS A 262
SHEET 6 AA1 8 VAL A 352 LEU A 358 1 O LEU A 358 N GLY A 333
SHEET 7 AA1 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA1 8 LYS A 515 ILE A 519 1 O LYS A 515 N ALA A 488
SHEET 1 AA2 8 SER B 238 LYS B 245 0
SHEET 2 AA2 8 VAL B 248 LEU B 255 -1 O VAL B 248 N LYS B 245
SHEET 3 AA2 8 ARG B 287 MET B 291 -1 O VAL B 288 N LEU B 255
SHEET 4 AA2 8 ALA B 260 CYS B 264 1 N VAL B 261 O LEU B 289
SHEET 5 AA2 8 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 6 AA2 8 VAL B 352 LEU B 358 1 O LEU B 358 N GLY B 333
SHEET 7 AA2 8 ALA B 488 ALA B 493 1 O VAL B 491 N SER B 357
SHEET 8 AA2 8 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -8.87
CISPEP 2 PHE B 267 PRO B 268 0 -12.46
SITE 1 AC1 7 GLU A 269 SER A 273 HIS A 334 TRP A 525
SITE 2 AC1 7 THR A 526 GLN A 527 MET A 528
SITE 1 AC2 5 MET A 293 LYS A 294 LEU A 313 GLU A 316
SITE 2 AC2 5 MET A 317
SITE 1 AC3 8 GLU A 269 SER A 270 ASP A 292 TYR A 296
SITE 2 AC3 8 GLY A 297 GLN A 453 PHE A 454 HOH A 748
SITE 1 AC4 8 PRO A 390 GLY A 391 ARG A 460 HOH A 709
SITE 2 AC4 8 HOH A 758 PRO B 302 GLU B 304 GLU B 307
SITE 1 AC5 5 ASN A 468 MET A 469 GLU A 470 ARG A 471
SITE 2 AC5 5 HOH A 751
SITE 1 AC6 4 VAL A 318 GLU A 350 ARG A 351 HOH A 712
SITE 1 AC7 11 PHE A 387 LEU A 408 SER A 412 SER A 415
SITE 2 AC7 11 MET A 419 LYS A 495 ASP A 496 PHE A 497
SITE 3 AC7 11 VAL A 498 HIS A 524 HOH A 790
SITE 1 AC8 4 MET B 293 LYS B 294 LEU B 313 GLU B 316
SITE 1 AC9 8 SER A 238 GLY A 240 PHE A 252 GLU A 254
SITE 2 AC9 8 SER B 238 GLY B 240 PHE B 252 GLU B 254
SITE 1 AD1 8 ALA B 345 LEU B 346 PRO B 349 ASP B 413
SITE 2 AD1 8 LYS B 483 LEU B 485 HOH B 716 HOH B 737
SITE 1 AD2 7 HIS B 239 HIS B 251 TRP B 271 ASP B 292
SITE 2 AD2 7 GLU B 298 GLN B 453 HOH B 763
SITE 1 AD3 3 LYS B 315 THR B 319 GLU B 494
SITE 1 AD4 3 SER B 257 GLY B 258 GLY B 285
SITE 1 AD5 10 TYR B 383 PHE B 387 SER B 412 SER B 415
SITE 2 AD5 10 MET B 419 LYS B 495 ASP B 496 PHE B 497
SITE 3 AD5 10 VAL B 498 HIS B 524
CRYST1 89.490 79.992 104.544 90.00 96.78 90.00 I 1 2 1 8
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 0.011174 0.000000 0.001328 0.00000
SCALE2 0.000000 0.012501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009633 0.00000
TER 2548 ASP A 545
TER 5103 ASP B 545
MASTER 454 0 14 38 16 0 26 6 5406 2 94 54
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