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HEADER HYDROLASE 09-DEC-18 6IX2
TITLE STRUCTURE OF THE A214C/A250I MUTANT OF AN EPOXIDE HYDROLASE FROM
TITLE 2 ASPERGILLUS USAMII E001 (AUEH2) AT 1.48 ANGSTROMS RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROSOMAL EPOXIDE HYDDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.3.2.9;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS USAMII;
SOURCE 3 ORGANISM_TAXID: 186680;
SOURCE 4 GENE: EH2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA AND BETA PROTEINS, ALPHA/BETA-HYDROLASES, STYRENE OXIDE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.HU,B.C.HU,X.D.HOU,Y.J.RAO,M.C.WU
REVDAT 1 11-DEC-19 6IX2 0
JRNL AUTH D.HU,B.C.HU,X.D.HOU,Y.J.RAO,M.C.WU
JRNL TITL STRUCTURE OF THE A214C/A250I MUTANT OF AN EPOXIDE HYDROLASE
JRNL TITL 2 FROM ASPERGILLUS USAMII E001 (AUEH2) AT 1.48 ANGSTROMS
JRNL TITL 3 RESOLUTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 131108
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.178
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 6591
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 43.8859 - 4.5914 1.00 4373 194 0.1712 0.1742
REMARK 3 2 4.5914 - 3.6449 1.00 4226 234 0.1446 0.1730
REMARK 3 3 3.6449 - 3.1843 1.00 4169 238 0.1510 0.1675
REMARK 3 4 3.1843 - 2.8932 1.00 4173 235 0.1615 0.1709
REMARK 3 5 2.8932 - 2.6859 1.00 4184 227 0.1616 0.1805
REMARK 3 6 2.6859 - 2.5275 1.00 4211 225 0.1692 0.1920
REMARK 3 7 2.5275 - 2.4010 1.00 4172 218 0.1647 0.1770
REMARK 3 8 2.4010 - 2.2965 0.99 4134 198 0.1601 0.1742
REMARK 3 9 2.2965 - 2.2081 1.00 4145 206 0.1557 0.1649
REMARK 3 10 2.2081 - 2.1319 1.00 4160 256 0.1558 0.1610
REMARK 3 11 2.1319 - 2.0652 1.00 4168 214 0.1586 0.1944
REMARK 3 12 2.0652 - 2.0062 1.00 4183 208 0.1605 0.1902
REMARK 3 13 2.0062 - 1.9534 1.00 4180 203 0.1579 0.1745
REMARK 3 14 1.9534 - 1.9057 1.00 4123 230 0.1564 0.1828
REMARK 3 15 1.9057 - 1.8624 1.00 4153 195 0.1517 0.1790
REMARK 3 16 1.8624 - 1.8227 1.00 4156 228 0.1606 0.1722
REMARK 3 17 1.8227 - 1.7863 1.00 4110 225 0.1592 0.1810
REMARK 3 18 1.7863 - 1.7526 1.00 4133 271 0.1649 0.2005
REMARK 3 19 1.7526 - 1.7213 1.00 4110 198 0.1644 0.1853
REMARK 3 20 1.7213 - 1.6921 1.00 4161 230 0.1667 0.1850
REMARK 3 21 1.6921 - 1.6648 1.00 4152 224 0.1678 0.2002
REMARK 3 22 1.6648 - 1.6392 1.00 4073 249 0.1633 0.1862
REMARK 3 23 1.6392 - 1.6151 1.00 4128 227 0.1568 0.1900
REMARK 3 24 1.6151 - 1.5923 1.00 4136 233 0.1584 0.1965
REMARK 3 25 1.5923 - 1.5708 0.99 4120 198 0.1601 0.1800
REMARK 3 26 1.5708 - 1.5504 0.99 4099 210 0.1578 0.1931
REMARK 3 27 1.5504 - 1.5310 1.00 4204 201 0.1610 0.1769
REMARK 3 28 1.5310 - 1.5126 1.00 4105 222 0.1637 0.1830
REMARK 3 29 1.5126 - 1.4950 1.00 4160 184 0.1608 0.1864
REMARK 3 30 1.4950 - 1.4782 0.95 3916 210 0.1655 0.1874
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.110
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.610
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6IX2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-18.
REMARK 100 THE DEPOSITION ID IS D_1300009611.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-NOV-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 131152
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.20600
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: AMPLE
REMARK 200 STARTING MODEL: 1QO7
REMARK 200
REMARK 200 REMARK: TETRAGONAL CRYSTAL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE, PH 5.5, 18%(W/V) POLYETHYLENE GLYCOL 3,350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 25.96100
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 -35
REMARK 465 GLY A -34
REMARK 465 SER A -33
REMARK 465 SER A -32
REMARK 465 HIS A -31
REMARK 465 HIS A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 SER A -25
REMARK 465 SER A -24
REMARK 465 GLY A -23
REMARK 465 LEU A -22
REMARK 465 VAL A -21
REMARK 465 PRO A -20
REMARK 465 ARG A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 MET A -15
REMARK 465 ALA A -14
REMARK 465 SER A -13
REMARK 465 MET A -12
REMARK 465 THR A -11
REMARK 465 GLY A -10
REMARK 465 GLY A -9
REMARK 465 GLN A -8
REMARK 465 GLN A -7
REMARK 465 MET A -6
REMARK 465 GLY A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 THR A 226
REMARK 465 ALA A 227
REMARK 465 ILE A 228
REMARK 465 THR A 229
REMARK 465 GLU A 230
REMARK 465 GLU A 231
REMARK 465 ASP A 232
REMARK 465 LYS A 233
REMARK 465 ARG A 234
REMARK 465 ALA A 235
REMARK 465 LEU A 236
REMARK 465 ALA A 237
REMARK 465 ARG A 238
REMARK 465 ARG A 394
REMARK 465 LYS A 395
REMARK 465 MET B -35
REMARK 465 GLY B -34
REMARK 465 SER B -33
REMARK 465 SER B -32
REMARK 465 HIS B -31
REMARK 465 HIS B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 SER B -25
REMARK 465 SER B -24
REMARK 465 GLY B -23
REMARK 465 LEU B -22
REMARK 465 VAL B -21
REMARK 465 PRO B -20
REMARK 465 ARG B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 MET B -15
REMARK 465 ALA B -14
REMARK 465 SER B -13
REMARK 465 MET B -12
REMARK 465 THR B -11
REMARK 465 GLY B -10
REMARK 465 GLY B -9
REMARK 465 GLN B -8
REMARK 465 GLN B -7
REMARK 465 MET B -6
REMARK 465 GLY B -5
REMARK 465 ARG B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 GLU B -1
REMARK 465 PHE B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 221
REMARK 465 SER B 222
REMARK 465 ILE B 223
REMARK 465 PRO B 224
REMARK 465 ASP B 225
REMARK 465 THR B 226
REMARK 465 ALA B 227
REMARK 465 ILE B 228
REMARK 465 ARG B 394
REMARK 465 LYS B 395
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 OE2 GLU A 290 O HOH A 501 1.99
REMARK 500 O HOH A 501 O HOH A 819 1.99
REMARK 500 O HOH A 728 O HOH A 902 2.05
REMARK 500 OE1 GLU A 66 O HOH A 502 2.06
REMARK 500 O HOH A 1045 O HOH A 1050 2.09
REMARK 500 O HOH B 409 O HOH B 774 2.11
REMARK 500 OE1 GLU A 294 O HOH A 503 2.12
REMARK 500 OH TYR A 134 O HOH A 504 2.12
REMARK 500 O HOH A 674 O HOH A 943 2.13
REMARK 500 OE1 GLU A 290 O HOH A 505 2.13
REMARK 500 O HOH A 793 O HOH A 945 2.14
REMARK 500 O HOH B 409 O HOH B 791 2.15
REMARK 500 O HOH A 717 O HOH A 890 2.16
REMARK 500 O HOH B 463 O HOH B 566 2.16
REMARK 500 OD2 ASP A 378 O HOH A 506 2.17
REMARK 500 O HOH A 613 O HOH A 897 2.17
REMARK 500 O HOH A 523 O HOH A 984 2.17
REMARK 500 OE2 GLU B 325 O HOH B 401 2.18
REMARK 500 O HOH B 416 O HOH B 503 2.18
REMARK 500 OE1 GLU B 290 O HOH B 402 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 O HOH B 559 O HOH B 623 2656 2.19
REMARK 500 O HOH A 898 O HOH A 947 2655 2.19
REMARK 500 O HOH A 872 O HOH A 984 2645 2.19
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 PRO A 117 43.28 -98.74
REMARK 500 SER A 119 -177.54 -179.87
REMARK 500 THR A 152 -116.57 49.43
REMARK 500 ASP A 191 -135.26 49.11
REMARK 500 GLN A 240 74.63 61.34
REMARK 500 PRO B 117 43.83 -97.41
REMARK 500 SER B 119 -176.74 -179.72
REMARK 500 THR B 152 -116.96 45.55
REMARK 500 ASP B 191 -136.75 49.26
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 GLN A 240 TRP A 241 145.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1052 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH A1053 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH A1054 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A1055 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A1056 DISTANCE = 6.64 ANGSTROMS
REMARK 525 HOH A1057 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A1058 DISTANCE = 7.21 ANGSTROMS
REMARK 525 HOH A1059 DISTANCE = 7.60 ANGSTROMS
REMARK 525 HOH A1060 DISTANCE = 8.39 ANGSTROMS
REMARK 525 HOH A1061 DISTANCE = 8.87 ANGSTROMS
REMARK 525 HOH A1062 DISTANCE = 9.75 ANGSTROMS
REMARK 525 HOH A1063 DISTANCE = 9.99 ANGSTROMS
REMARK 525 HOH A1064 DISTANCE = 9.99 ANGSTROMS
REMARK 525 HOH B 877 DISTANCE = 7.16 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401
DBREF 6IX2 A 1 395 UNP T2B4K5 T2B4K5_9EURO 1 395
DBREF 6IX2 B 1 395 UNP T2B4K5 T2B4K5_9EURO 1 395
SEQADV 6IX2 MET A -35 UNP T2B4K5 INITIATING METHIONINE
SEQADV 6IX2 GLY A -34 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -33 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -32 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -31 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -30 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -29 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -28 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -27 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -26 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -25 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -24 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -23 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 LEU A -22 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 VAL A -21 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 PRO A -20 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ARG A -19 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -18 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -17 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS A -16 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET A -15 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ALA A -14 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -13 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET A -12 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 THR A -11 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -10 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -9 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLN A -8 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLN A -7 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET A -6 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -5 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ARG A -4 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY A -3 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER A -2 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLU A -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 PHE A 0 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 CYS A 214 UNP T2B4K5 ALA 214 ENGINEERED MUTATION
SEQADV 6IX2 ILE A 250 UNP T2B4K5 ALA 250 ENGINEERED MUTATION
SEQADV 6IX2 MET B -35 UNP T2B4K5 INITIATING METHIONINE
SEQADV 6IX2 GLY B -34 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -33 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -32 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -31 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -30 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -29 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -28 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -27 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -26 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -25 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -24 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -23 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 LEU B -22 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 VAL B -21 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 PRO B -20 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ARG B -19 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -18 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -17 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 HIS B -16 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET B -15 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ALA B -14 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -13 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET B -12 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 THR B -11 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -10 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -9 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLN B -8 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLN B -7 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 MET B -6 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -5 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 ARG B -4 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLY B -3 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 SER B -2 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 GLU B -1 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 PHE B 0 UNP T2B4K5 EXPRESSION TAG
SEQADV 6IX2 CYS B 214 UNP T2B4K5 ALA 214 ENGINEERED MUTATION
SEQADV 6IX2 ILE B 250 UNP T2B4K5 ALA 250 ENGINEERED MUTATION
SEQRES 1 A 431 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 431 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 431 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET ALA LEU
SEQRES 4 A 431 ALA TYR SER ASN ILE PRO LEU GLY ALA THR VAL ILE PRO
SEQRES 5 A 431 SER PRO PHE GLN VAL HIS ILE SER ASP GLU GLN ILE GLU
SEQRES 6 A 431 GLU LEU GLN LEU LEU VAL LYS LEU SER LYS LEU ALA PRO
SEQRES 7 A 431 PRO THR TYR GLU GLY LEU GLN GLN ASP ARG ARG TYR GLY
SEQRES 8 A 431 ILE THR ASN GLU TRP LEU ALA ASN ALA LYS GLU ALA TRP
SEQRES 9 A 431 LYS SER PHE ASP TRP ARG PRO ALA GLU SER ARG ILE ASN
SEQRES 10 A 431 SER PHE PRO GLN PHE THR TYR ASP ILE GLU GLY LEU THR
SEQRES 11 A 431 ILE HIS PHE VAL ALA LEU PHE SER GLU LYS LYS ASP ALA
SEQRES 12 A 431 ILE PRO ILE VAL LEU LEU HIS GLY TRP PRO GLY SER PHE
SEQRES 13 A 431 LEU GLU PHE LEU PRO VAL LEU THR SER ILE ARG ASP LYS
SEQRES 14 A 431 TYR SER PRO GLU THR LEU PRO TYR HIS ILE VAL VAL PRO
SEQRES 15 A 431 SER LEU PRO GLY TYR THR PHE SER SER GLY PRO PRO LEU
SEQRES 16 A 431 ASP VAL ASN PHE ASN GLY GLU ASP THR ALA ARG VAL ILE
SEQRES 17 A 431 ASN LYS VAL MET LEU ASN LEU GLY PHE GLU ASP GLY TYR
SEQRES 18 A 431 VAL ALA GLN GLY GLY ASP ILE GLY SER LYS ILE GLY ARG
SEQRES 19 A 431 ILE LEU ALA VAL ASP HIS ASP ALA CYS LYS ALA VAL HIS
SEQRES 20 A 431 LEU ASN CYS CYS TYR MET GLY LYS PRO SER SER ILE PRO
SEQRES 21 A 431 ASP THR ALA ILE THR GLU GLU ASP LYS ARG ALA LEU ALA
SEQRES 22 A 431 ARG ALA GLN TRP PHE ALA THR PHE GLY SER GLY TYR ILE
SEQRES 23 A 431 VAL GLU HIS GLY THR ARG PRO SER THR ILE GLY ASN ALA
SEQRES 24 A 431 LEU SER THR SER PRO VAL ALA LEU LEU SER TRP ILE GLY
SEQRES 25 A 431 GLU LYS PHE LEU ASP TRP ALA GLY GLU THR ILE PRO LEU
SEQRES 26 A 431 GLU THR ILE LEU GLU SER VAL THR LEU TYR TRP PHE THR
SEQRES 27 A 431 GLU THR PHE PRO ARG SER ILE TYR HIS TYR ARG GLU ASN
SEQRES 28 A 431 PHE PRO PRO PRO LYS LEU ARG HIS THR GLU ASP PRO ARG
SEQRES 29 A 431 TRP TYR ILE ARG LYS PRO PHE GLY PHE SER TYR TYR PRO
SEQRES 30 A 431 MET GLU LEU VAL PRO THR PRO ARG ALA TRP VAL GLU THR
SEQRES 31 A 431 THR GLY ASN LEU VAL PHE TRP GLN ALA HIS GLU LYS GLY
SEQRES 32 A 431 GLY HIS PHE ALA ALA LEU GLU ARG PRO GLN ASP TYR LEU
SEQRES 33 A 431 ASP ASP LEU THR ALA PHE CYS GLU GLN VAL TRP ALA GLY
SEQRES 34 A 431 ARG LYS
SEQRES 1 B 431 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 431 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 431 GLY GLN GLN MET GLY ARG GLY SER GLU PHE MET ALA LEU
SEQRES 4 B 431 ALA TYR SER ASN ILE PRO LEU GLY ALA THR VAL ILE PRO
SEQRES 5 B 431 SER PRO PHE GLN VAL HIS ILE SER ASP GLU GLN ILE GLU
SEQRES 6 B 431 GLU LEU GLN LEU LEU VAL LYS LEU SER LYS LEU ALA PRO
SEQRES 7 B 431 PRO THR TYR GLU GLY LEU GLN GLN ASP ARG ARG TYR GLY
SEQRES 8 B 431 ILE THR ASN GLU TRP LEU ALA ASN ALA LYS GLU ALA TRP
SEQRES 9 B 431 LYS SER PHE ASP TRP ARG PRO ALA GLU SER ARG ILE ASN
SEQRES 10 B 431 SER PHE PRO GLN PHE THR TYR ASP ILE GLU GLY LEU THR
SEQRES 11 B 431 ILE HIS PHE VAL ALA LEU PHE SER GLU LYS LYS ASP ALA
SEQRES 12 B 431 ILE PRO ILE VAL LEU LEU HIS GLY TRP PRO GLY SER PHE
SEQRES 13 B 431 LEU GLU PHE LEU PRO VAL LEU THR SER ILE ARG ASP LYS
SEQRES 14 B 431 TYR SER PRO GLU THR LEU PRO TYR HIS ILE VAL VAL PRO
SEQRES 15 B 431 SER LEU PRO GLY TYR THR PHE SER SER GLY PRO PRO LEU
SEQRES 16 B 431 ASP VAL ASN PHE ASN GLY GLU ASP THR ALA ARG VAL ILE
SEQRES 17 B 431 ASN LYS VAL MET LEU ASN LEU GLY PHE GLU ASP GLY TYR
SEQRES 18 B 431 VAL ALA GLN GLY GLY ASP ILE GLY SER LYS ILE GLY ARG
SEQRES 19 B 431 ILE LEU ALA VAL ASP HIS ASP ALA CYS LYS ALA VAL HIS
SEQRES 20 B 431 LEU ASN CYS CYS TYR MET GLY LYS PRO SER SER ILE PRO
SEQRES 21 B 431 ASP THR ALA ILE THR GLU GLU ASP LYS ARG ALA LEU ALA
SEQRES 22 B 431 ARG ALA GLN TRP PHE ALA THR PHE GLY SER GLY TYR ILE
SEQRES 23 B 431 VAL GLU HIS GLY THR ARG PRO SER THR ILE GLY ASN ALA
SEQRES 24 B 431 LEU SER THR SER PRO VAL ALA LEU LEU SER TRP ILE GLY
SEQRES 25 B 431 GLU LYS PHE LEU ASP TRP ALA GLY GLU THR ILE PRO LEU
SEQRES 26 B 431 GLU THR ILE LEU GLU SER VAL THR LEU TYR TRP PHE THR
SEQRES 27 B 431 GLU THR PHE PRO ARG SER ILE TYR HIS TYR ARG GLU ASN
SEQRES 28 B 431 PHE PRO PRO PRO LYS LEU ARG HIS THR GLU ASP PRO ARG
SEQRES 29 B 431 TRP TYR ILE ARG LYS PRO PHE GLY PHE SER TYR TYR PRO
SEQRES 30 B 431 MET GLU LEU VAL PRO THR PRO ARG ALA TRP VAL GLU THR
SEQRES 31 B 431 THR GLY ASN LEU VAL PHE TRP GLN ALA HIS GLU LYS GLY
SEQRES 32 B 431 GLY HIS PHE ALA ALA LEU GLU ARG PRO GLN ASP TYR LEU
SEQRES 33 B 431 ASP ASP LEU THR ALA PHE CYS GLU GLN VAL TRP ALA GLY
SEQRES 34 B 431 ARG LYS
HET GOL A 401 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *1041(H2 O)
HELIX 1 AA1 SER A 24 SER A 38 1 15
HELIX 2 AA2 TYR A 45 GLN A 49 5 5
HELIX 3 AA3 THR A 57 SER A 70 1 14
HELIX 4 AA4 ASP A 72 ASN A 81 1 10
HELIX 5 AA5 SER A 119 GLU A 122 5 4
HELIX 6 AA6 PHE A 123 TYR A 134 1 12
HELIX 7 AA7 ASN A 164 LEU A 179 1 16
HELIX 8 AA8 GLY A 180 GLY A 184 5 5
HELIX 9 AA9 ASP A 191 HIS A 204 1 14
HELIX 10 AB1 TRP A 241 GLY A 246 1 6
HELIX 11 AB2 SER A 247 ARG A 256 1 10
HELIX 12 AB3 ARG A 256 SER A 265 1 10
HELIX 13 AB4 SER A 267 ALA A 283 1 17
HELIX 14 AB5 PRO A 288 THR A 302 1 15
HELIX 15 AB6 THR A 304 ILE A 309 1 6
HELIX 16 AB7 TYR A 310 PHE A 316 5 7
HELIX 17 AB8 ARG A 322 TYR A 330 5 9
HELIX 18 AB9 PRO A 348 THR A 354 1 7
HELIX 19 AC1 PHE A 370 ARG A 375 1 6
HELIX 20 AC2 ARG A 375 TRP A 391 1 17
HELIX 21 AC3 SER B 24 SER B 38 1 15
HELIX 22 AC4 TYR B 45 GLN B 49 5 5
HELIX 23 AC5 THR B 57 SER B 70 1 14
HELIX 24 AC6 ASP B 72 SER B 82 1 11
HELIX 25 AC7 SER B 119 GLU B 122 5 4
HELIX 26 AC8 PHE B 123 TYR B 134 1 12
HELIX 27 AC9 ASN B 164 LEU B 179 1 16
HELIX 28 AD1 ASP B 191 HIS B 204 1 14
HELIX 29 AD2 GLU B 230 GLY B 246 1 17
HELIX 30 AD3 SER B 247 ARG B 256 1 10
HELIX 31 AD4 ARG B 256 THR B 266 1 11
HELIX 32 AD5 SER B 267 ALA B 283 1 17
HELIX 33 AD6 PRO B 288 THR B 302 1 15
HELIX 34 AD7 GLU B 303 ILE B 309 1 7
HELIX 35 AD8 TYR B 310 PHE B 316 5 7
HELIX 36 AD9 ARG B 322 TYR B 330 5 9
HELIX 37 AE1 PRO B 348 GLU B 353 1 6
HELIX 38 AE2 PHE B 370 ARG B 375 1 6
HELIX 39 AE3 ARG B 375 TRP B 391 1 17
SHEET 1 AA1 9 SER A 17 PRO A 18 0
SHEET 2 AA1 9 GLN A 85 ILE A 90 -1 O THR A 87 N SER A 17
SHEET 3 AA1 9 LEU A 93 LEU A 100 -1 O ILE A 95 N TYR A 88
SHEET 4 AA1 9 TYR A 141 PRO A 146 -1 O VAL A 145 N VAL A 98
SHEET 5 AA1 9 ILE A 108 LEU A 113 1 N ILE A 110 O HIS A 142
SHEET 6 AA1 9 TYR A 185 GLY A 189 1 O VAL A 186 N PRO A 109
SHEET 7 AA1 9 CYS A 207 LEU A 212 1 O LYS A 208 N TYR A 185
SHEET 8 AA1 9 ILE A 331 TYR A 339 1 O GLY A 336 N VAL A 210
SHEET 9 AA1 9 GLY A 356 ALA A 363 1 O ASN A 357 N ILE A 331
SHEET 1 AA2 9 SER B 17 PRO B 18 0
SHEET 2 AA2 9 GLN B 85 ILE B 90 -1 O THR B 87 N SER B 17
SHEET 3 AA2 9 LEU B 93 LEU B 100 -1 O ILE B 95 N TYR B 88
SHEET 4 AA2 9 TYR B 141 PRO B 146 -1 O VAL B 145 N VAL B 98
SHEET 5 AA2 9 ILE B 108 LEU B 113 1 N ILE B 110 O HIS B 142
SHEET 6 AA2 9 TYR B 185 GLY B 189 1 O VAL B 186 N PRO B 109
SHEET 7 AA2 9 CYS B 207 LEU B 212 1 O LYS B 208 N TYR B 185
SHEET 8 AA2 9 ILE B 331 TYR B 339 1 O GLY B 336 N LEU B 212
SHEET 9 AA2 9 GLY B 356 ALA B 363 1 O ASN B 357 N ILE B 331
CISPEP 1 TRP A 116 PRO A 117 0 5.72
CISPEP 2 GLY A 156 PRO A 157 0 -1.70
CISPEP 3 PHE A 316 PRO A 317 0 -0.20
CISPEP 4 TRP B 116 PRO B 117 0 5.33
CISPEP 5 GLY B 156 PRO B 157 0 -3.80
CISPEP 6 PHE B 316 PRO B 317 0 -0.62
SITE 1 AC1 6 ASP A 183 LYS A 208 TRP A 391 ALA A 392
SITE 2 AC1 6 GLY A 393 HOH A 591
CRYST1 57.365 51.922 133.488 90.00 90.97 90.00 P 1 21 1 4
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 0.017432 0.000000 0.000295 0.00000
SCALE2 0.000000 0.019260 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007492 0.00000
TER 3105 GLY A 393
TER 6194 GLY B 393
MASTER 437 0 1 39 18 0 2 6 7193 2 6 68
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