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HEADER HYDROLASE 13-NOV-18 6I5E
TITLE X-RAY STRUCTURE OF APO HUMAN SOLUBLE EPOXIDE HYDROLASE C-TERMINAL
TITLE 2 DOMAIN (HSEH CTD)
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, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.ABIS,J.KOPEC,W.W.YUE,M.R.CONTE
REVDAT 1 29-MAY-19 6I5E 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. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 21388
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.246
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1101
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1581
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3890
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.4300
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 : 0
REMARK 3 SOLVENT ATOMS : 13
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.08000
REMARK 3 B22 (A**2) : -3.20000
REMARK 3 B33 (A**2) : 6.95000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 1.475
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.358
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.393
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.645
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.910
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5238 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4864 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7104 ; 1.449 ; 1.947
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11232 ; 1.001 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 630 ; 5.804 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 244 ;35.732 ;23.934
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 880 ;15.291 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.764 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 736 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5886 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1234 ; 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): 2526 ; 2.784 ; 4.391
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2525 ; 2.778 ; 4.391
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3154 ; 4.618 ; 6.585
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3155 ; 4.618 ; 6.586
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2712 ; 2.789 ; 4.678
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2710 ; 2.785 ; 4.676
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3950 ; 4.708 ; 6.899
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22200 ; 8.989 ;40.944
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 22199 ; 8.989 ;40.945
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 6I5E 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_1200012689.
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 : I04
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 : 22492
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 70.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.077
REMARK 200 R MERGE (I) : 0.21000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 29.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.74100
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 (%): 47.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
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 39.19471
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.06950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.11654
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.19471
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.06950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 52.11654
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 O ILE A 375 N ALA A 377 2.06
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 -149.19 -123.90
REMARK 500 GLU A 269 -139.71 -113.35
REMARK 500 ASP A 335 -125.94 61.10
REMARK 500 ASN A 359 -43.22 78.78
REMARK 500 ILE A 375 -71.39 -87.89
REMARK 500 LYS A 376 3.58 -46.39
REMARK 500 GLU A 435 74.68 -117.08
REMARK 500 SER B 231 -144.38 -120.45
REMARK 500 PRO B 246 -50.17 -29.82
REMARK 500 GLU B 269 -148.44 -117.51
REMARK 500 ASP B 335 -123.75 58.53
REMARK 500 ASN B 359 -46.42 71.90
REMARK 500 LEU B 499 74.48 -100.99
REMARK 500 HIS B 513 42.49 -93.48
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 MET A 291 ASP A 292 146.11
REMARK 500 MET B 291 ASP B 292 148.95
REMARK 500
REMARK 500 REMARK: NULL
DBREF 6I5E A 230 555 UNP P34913 HYES_HUMAN 230 555
DBREF 6I5E B 230 555 UNP P34913 HYES_HUMAN 230 555
SEQADV 6I5E MET A 212 UNP P34913 INITIATING METHIONINE
SEQADV 6I5E HIS A 213 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS A 214 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS A 215 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS A 216 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS A 217 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS A 218 UNP P34913 EXPRESSION TAG
SEQADV 6I5E SER A 219 UNP P34913 EXPRESSION TAG
SEQADV 6I5E THR A 220 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLU A 221 UNP P34913 EXPRESSION TAG
SEQADV 6I5E ASN A 222 UNP P34913 EXPRESSION TAG
SEQADV 6I5E LEU A 223 UNP P34913 EXPRESSION TAG
SEQADV 6I5E TYR A 224 UNP P34913 EXPRESSION TAG
SEQADV 6I5E PHE A 225 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLN A 226 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLY A 227 UNP P34913 EXPRESSION TAG
SEQADV 6I5E SER A 228 UNP P34913 EXPRESSION TAG
SEQADV 6I5E SER A 229 UNP P34913 EXPRESSION TAG
SEQADV 6I5E MET B 212 UNP P34913 INITIATING METHIONINE
SEQADV 6I5E HIS B 213 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS B 214 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS B 215 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS B 216 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS B 217 UNP P34913 EXPRESSION TAG
SEQADV 6I5E HIS B 218 UNP P34913 EXPRESSION TAG
SEQADV 6I5E SER B 219 UNP P34913 EXPRESSION TAG
SEQADV 6I5E THR B 220 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLU B 221 UNP P34913 EXPRESSION TAG
SEQADV 6I5E ASN B 222 UNP P34913 EXPRESSION TAG
SEQADV 6I5E LEU B 223 UNP P34913 EXPRESSION TAG
SEQADV 6I5E TYR B 224 UNP P34913 EXPRESSION TAG
SEQADV 6I5E PHE B 225 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLN B 226 UNP P34913 EXPRESSION TAG
SEQADV 6I5E GLY B 227 UNP P34913 EXPRESSION TAG
SEQADV 6I5E SER B 228 UNP P34913 EXPRESSION TAG
SEQADV 6I5E 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
FORMUL 3 HOH *13(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 LEU A 324 1 16
HELIX 6 AA6 ASP A 335 TYR A 348 1 14
HELIX 7 AA7 SER A 370 LYS A 376 1 7
HELIX 8 AA8 ASN A 378 PHE A 381 5 4
HELIX 9 AA9 ASP A 382 PHE A 387 1 6
HELIX 10 AB1 GLY A 391 GLU A 398 1 8
HELIX 11 AB2 ASN A 400 PHE A 409 1 10
HELIX 12 AB3 ALA A 411 SER A 415 5 5
HELIX 13 AB4 THR A 443 LYS A 455 1 13
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 GLN B 277 ALA B 284 1 8
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 SER B 370 ASN B 378 1 9
HELIX 27 AC9 PRO B 379 PHE B 381 5 3
HELIX 28 AD1 ASP B 382 PHE B 387 1 6
HELIX 29 AD2 GLY B 391 ASN B 400 1 10
HELIX 30 AD3 ASN B 400 PHE B 409 1 10
HELIX 31 AD4 ALA B 411 SER B 415 5 5
HELIX 32 AD5 THR B 443 GLY B 458 1 16
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 ILE B 511 1 6
HELIX 37 AE1 TRP B 525 LYS B 530 1 6
HELIX 38 AE2 LYS B 530 ASP B 545 1 16
SHEET 1 AA116 LYS A 515 ILE A 519 0
SHEET 2 AA116 ALA A 488 ALA A 493 1 N ALA A 488 O LYS A 515
SHEET 3 AA116 VAL A 352 LEU A 358 1 N SER A 357 O VAL A 491
SHEET 4 AA116 ALA A 329 HIS A 334 1 N GLY A 333 O LEU A 358
SHEET 5 AA116 ALA A 260 CYS A 264 1 N CYS A 262 O VAL A 330
SHEET 6 AA116 ARG A 287 MET A 291 1 O ARG A 287 N VAL A 261
SHEET 7 AA116 VAL A 248 LEU A 255 -1 N LEU A 255 O VAL A 288
SHEET 8 AA116 SER A 238 LYS A 245 -1 N GLY A 240 O PHE A 252
SHEET 9 AA116 SER B 238 LYS B 245 -1 O TYR B 241 N HIS A 239
SHEET 10 AA116 VAL B 248 LEU B 255 -1 O VAL B 248 N LYS B 245
SHEET 11 AA116 ARG B 287 MET B 291 -1 O VAL B 288 N LEU B 255
SHEET 12 AA116 ALA B 260 CYS B 264 1 N VAL B 261 O LEU B 289
SHEET 13 AA116 ALA B 329 HIS B 334 1 O VAL B 330 N CYS B 262
SHEET 14 AA116 VAL B 352 LEU B 358 1 O ALA B 356 N PHE B 331
SHEET 15 AA116 ALA B 488 ALA B 493 1 O VAL B 491 N SER B 357
SHEET 16 AA116 LEU B 514 ILE B 519 1 O LYS B 515 N ALA B 488
CISPEP 1 PHE A 267 PRO A 268 0 -11.78
CISPEP 2 PHE B 267 PRO B 268 0 -10.14
CRYST1 88.224 80.139 104.696 90.00 95.39 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 0.011335 0.000000 0.001070 0.00000
SCALE2 0.000000 0.012478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009594 0.00000
TER 2544 ASP A 545
TER 5088 ASP B 545
MASTER 366 0 0 38 16 0 0 6 5099 2 0 54
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