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HEADER HYDROLASE 23-AUG-18 6HGW
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH 2-(4-FLUOROPHENYL)-N-(4-
TITLE 2 PHENOXYBENZYL)ETHANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIFUNCTIONAL EPOXIDE HYDROLASE 2;
COMPND 3 CHAIN: A;
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_TAXID: 9606;
SOURCE 4 GENE: EPHX2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS INHIBITOR, COMPLEX, SEH, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.KRAMER,D.POGORYELOV,K.HIESINGER,E.PROSCHAK
REVDAT 1 07-AUG-19 6HGW 0
JRNL AUTH J.S.KRAMER,D.POGORYELOV,K.HIESINGER,E.PROSCHAK
JRNL TITL SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH
JRNL TITL 2 2-(4-FLUOROPHENYL)-N-(4-PHENOXYBENZYL)ETHANAMINE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 15694
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1569
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 53.2780 - 5.3517 1.00 1370 151 0.1845 0.2602
REMARK 3 2 5.3517 - 4.2484 1.00 1309 146 0.1474 0.1748
REMARK 3 3 4.2484 - 3.7115 1.00 1287 143 0.1568 0.2151
REMARK 3 4 3.7115 - 3.3722 1.00 1282 142 0.1659 0.2259
REMARK 3 5 3.3722 - 3.1305 1.00 1282 143 0.1898 0.2536
REMARK 3 6 3.1305 - 2.9460 1.00 1286 143 0.2048 0.2680
REMARK 3 7 2.9460 - 2.7985 1.00 1237 136 0.2076 0.2550
REMARK 3 8 2.7985 - 2.6766 1.00 1282 143 0.2135 0.3352
REMARK 3 9 2.6766 - 2.5736 1.00 1279 142 0.2092 0.2617
REMARK 3 10 2.5736 - 2.4848 1.00 1243 138 0.2532 0.2807
REMARK 3 11 2.4848 - 2.4071 1.00 1268 142 0.2910 0.3587
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.980
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.87
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.05
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 : 0.005 2675
REMARK 3 ANGLE : 0.741 3631
REMARK 3 CHIRALITY : 0.047 375
REMARK 3 PLANARITY : 0.006 469
REMARK 3 DIHEDRAL : 23.352 988
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5553 -6.6033 -36.5311
REMARK 3 T TENSOR
REMARK 3 T11: 0.3120 T22: 0.2994
REMARK 3 T33: 0.3418 T12: -0.0268
REMARK 3 T13: 0.0235 T23: 0.0134
REMARK 3 L TENSOR
REMARK 3 L11: 3.5096 L22: 5.4890
REMARK 3 L33: 4.1958 L12: 2.6935
REMARK 3 L13: 0.7184 L23: 0.5731
REMARK 3 S TENSOR
REMARK 3 S11: -0.1468 S12: 0.0843 S13: 0.1783
REMARK 3 S21: -0.4274 S22: 0.1302 S23: 0.1462
REMARK 3 S31: -0.0817 S32: 0.0654 S33: -0.0347
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 271 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3719 -16.5968 -31.5347
REMARK 3 T TENSOR
REMARK 3 T11: 0.2922 T22: 0.3241
REMARK 3 T33: 0.3730 T12: -0.0057
REMARK 3 T13: 0.0235 T23: 0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 2.6656 L22: 3.1143
REMARK 3 L33: 2.0529 L12: 0.4063
REMARK 3 L13: -0.4938 L23: -0.2957
REMARK 3 S TENSOR
REMARK 3 S11: -0.0658 S12: -0.1734 S13: -0.2685
REMARK 3 S21: -0.0916 S22: 0.0071 S23: -0.2835
REMARK 3 S31: 0.2389 S32: 0.0838 S33: 0.0744
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 399 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.1756 -31.4450 -44.9697
REMARK 3 T TENSOR
REMARK 3 T11: 0.9369 T22: 0.6594
REMARK 3 T33: 0.8724 T12: -0.1415
REMARK 3 T13: 0.1553 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 2.2582 L22: 2.1746
REMARK 3 L33: 5.6506 L12: -2.0209
REMARK 3 L13: -0.3948 L23: -0.4458
REMARK 3 S TENSOR
REMARK 3 S11: -0.8117 S12: 0.0194 S13: -1.3983
REMARK 3 S21: -0.1826 S22: 0.3024 S23: 0.3725
REMARK 3 S31: 1.0722 S32: -0.4068 S33: 0.3255
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 400 THROUGH 435 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.8149 -23.1807 -45.9599
REMARK 3 T TENSOR
REMARK 3 T11: 0.5928 T22: 0.5897
REMARK 3 T33: 0.6980 T12: -0.0990
REMARK 3 T13: -0.1155 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 5.5955 L22: 4.2611
REMARK 3 L33: 7.0307 L12: 0.1862
REMARK 3 L13: -3.1027 L23: 4.5798
REMARK 3 S TENSOR
REMARK 3 S11: -0.5381 S12: 0.2521 S13: -0.9475
REMARK 3 S21: -0.4196 S22: 0.2548 S23: 0.5073
REMARK 3 S31: 0.7034 S32: -0.6383 S33: 0.2587
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 436 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.0713 -20.1936 -30.4202
REMARK 3 T TENSOR
REMARK 3 T11: 0.3580 T22: 0.3149
REMARK 3 T33: 0.3469 T12: -0.0633
REMARK 3 T13: 0.0439 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 3.2676 L22: 3.8781
REMARK 3 L33: 3.0797 L12: -0.4778
REMARK 3 L13: 0.0843 L23: -0.3985
REMARK 3 S TENSOR
REMARK 3 S11: -0.0430 S12: -0.1225 S13: -0.1928
REMARK 3 S21: -0.1664 S22: 0.0930 S23: 0.0692
REMARK 3 S31: 0.1443 S32: -0.1018 S33: -0.0549
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 6HGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011631.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-6.55
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15705
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.407
REMARK 200 RESOLUTION RANGE LOW (A) : 53.265
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.92
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.84
REMARK 200 R MERGE FOR SHELL (I) : 1.33100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.080
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: 6FR2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN SOLUTION PROTEIN (5-10
REMARK 280 MG/ML , 50 MM NACL, 50 MM SODIUM PHOSPHATE, 10% GLYCEROL (98%),
REMARK 280 2 MM DTT AT PH 7.4) WAS MIXED IN DIFFERENT RATIOS (2/1, 1/1, 1/2)
REMARK 280 WITH PRECIPITANT SOLUTION (23 %-28 % (W/V) POLYETHYLENGLYCOL
REMARK 280 (PEG) 6000, 70 MM AMMONIUM ACETAT, 200 MM MAGNESIUM ACETAT, 100
REMARK 280 MM SODIUM CACODYLATE AT PH 6.1-6.5), VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.21000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 53.26500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.21000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 53.26500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.21000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 53.26500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.09000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.21000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 53.26500
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 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 MET A 219
REMARK 465 ALA A 220
REMARK 465 SER A 221
REMARK 465 LEU A 222
REMARK 465 ASN A 223
REMARK 465 THR A 224
REMARK 465 PRO A 225
REMARK 465 ALA A 226
REMARK 465 PRO A 227
REMARK 465 LEU A 228
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 LEU A 556
REMARK 465 LEU A 557
REMARK 465 GLU A 558
REMARK 465 HIS A 559
REMARK 465 HIS A 560
REMARK 465 HIS A 561
REMARK 465 HIS A 562
REMARK 465 HIS A 563
REMARK 465 HIS A 564
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 LYS A 376 CG CD CE NZ
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 GLU A 424 CG CD OE1 OE2
REMARK 470 TRP A 510 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 510 CZ3 CH2
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 -160.71 -105.69
REMARK 500 GLU A 269 -137.82 -120.33
REMARK 500 SER A 270 161.39 176.56
REMARK 500 ASP A 335 -130.07 66.19
REMARK 500 ASN A 359 -51.20 72.72
REMARK 500 LYS A 376 20.65 -73.20
REMARK 500 ALA A 377 -69.09 -102.40
REMARK 500 MET A 419 0.52 -65.61
REMARK 500 LYS A 421 32.70 -79.37
REMARK 500 ALA A 425 64.66 -159.87
REMARK 500 VAL A 498 -60.94 -106.97
REMARK 500 HIS A 513 33.68 -98.99
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 G3W A 601
DBREF 6HGW A 222 555 UNP P34913 HYES_HUMAN 222 555
SEQADV 6HGV MET A 219 UNP P34913 INITIATING METHIONINE
SEQADV 6HGV ALA A 220 UNP P34913 EXPRESSION TAG
SEQADV 6HGV SER A 221 UNP P34913 EXPRESSION TAG
SEQADV 6HGV LEU A 556 UNP P34913 EXPRESSION TAG
SEQADV 6HGV LEU A 557 UNP P34913 EXPRESSION TAG
SEQADV 6HGV GLU A 558 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 559 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 560 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 561 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 562 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 563 UNP P34913 EXPRESSION TAG
SEQADV 6HGV HIS A 564 UNP P34913 EXPRESSION TAG
SEQRES 1 A 346 MET ALA SER LEU ASN THR PRO ALA PRO LEU PRO THR SER
SEQRES 2 A 346 CYS ASN PRO SER ASP MET SER HIS GLY TYR VAL THR VAL
SEQRES 3 A 346 LYS PRO ARG VAL ARG LEU HIS PHE VAL GLU LEU GLY SER
SEQRES 4 A 346 GLY PRO ALA VAL CYS LEU CYS HIS GLY PHE PRO GLU SER
SEQRES 5 A 346 TRP TYR SER TRP ARG TYR GLN ILE PRO ALA LEU ALA GLN
SEQRES 6 A 346 ALA GLY TYR ARG VAL LEU ALA MET ASP MET LYS GLY TYR
SEQRES 7 A 346 GLY GLU SER SER ALA PRO PRO GLU ILE GLU GLU TYR CYS
SEQRES 8 A 346 MET GLU VAL LEU CYS LYS GLU MET VAL THR PHE LEU ASP
SEQRES 9 A 346 LYS LEU GLY LEU SER GLN ALA VAL PHE ILE GLY HIS ASP
SEQRES 10 A 346 TRP GLY GLY MET LEU VAL TRP TYR MET ALA LEU PHE TYR
SEQRES 11 A 346 PRO GLU ARG VAL ARG ALA VAL ALA SER LEU ASN THR PRO
SEQRES 12 A 346 PHE ILE PRO ALA ASN PRO ASN MET SER PRO LEU GLU SER
SEQRES 13 A 346 ILE LYS ALA ASN PRO VAL PHE ASP TYR GLN LEU TYR PHE
SEQRES 14 A 346 GLN GLU PRO GLY VAL ALA GLU ALA GLU LEU GLU GLN ASN
SEQRES 15 A 346 LEU SER ARG THR PHE LYS SER LEU PHE ARG ALA SER ASP
SEQRES 16 A 346 GLU SER VAL LEU SER MET HIS LYS VAL CYS GLU ALA GLY
SEQRES 17 A 346 GLY LEU PHE VAL ASN SER PRO GLU GLU PRO SER LEU SER
SEQRES 18 A 346 ARG MET VAL THR GLU GLU GLU ILE GLN PHE TYR VAL GLN
SEQRES 19 A 346 GLN PHE LYS LYS SER GLY PHE ARG GLY PRO LEU ASN TRP
SEQRES 20 A 346 TYR ARG ASN MET GLU ARG ASN TRP LYS TRP ALA CYS LYS
SEQRES 21 A 346 SER LEU GLY ARG LYS ILE LEU ILE PRO ALA LEU MET VAL
SEQRES 22 A 346 THR ALA GLU LYS ASP PHE VAL LEU VAL PRO GLN MET SER
SEQRES 23 A 346 GLN HIS MET GLU ASP TRP ILE PRO HIS LEU LYS ARG GLY
SEQRES 24 A 346 HIS ILE GLU ASP CYS GLY HIS TRP THR GLN MET ASP LYS
SEQRES 25 A 346 PRO THR GLU VAL ASN GLN ILE LEU ILE LYS TRP LEU ASP
SEQRES 26 A 346 SER ASP ALA ARG ASN PRO PRO VAL VAL SER LYS MET LEU
SEQRES 27 A 346 LEU GLU HIS HIS HIS HIS HIS HIS
HET G3W A 601 24
HETNAM G3W 2-(4-FLUOROPHENYL)-~{N}-[(4-PHENOXYPHENYL)
HETNAM 2 G3W METHYL]ETHANAMINE
FORMUL 2 G3W C21 H20 F N O
FORMUL 3 HOH *28(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 GLN A 277 ALA A 284 1 8
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 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 GLN A 399 1 9
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 GLY A 458 1 16
HELIX 14 AB5 PHE A 459 ASN A 464 1 6
HELIX 15 AB6 TRP A 465 ARG A 467 5 3
HELIX 16 AB7 ASN A 468 LYS A 478 1 11
HELIX 17 AB8 VAL A 500 GLN A 505 5 6
HELIX 18 AB9 HIS A 506 TRP A 510 5 5
HELIX 19 AC1 TRP A 525 LYS A 530 1 6
HELIX 20 AC2 LYS A 530 ALA A 546 1 17
SHEET 1 AA1 8 SER A 238 LYS A 245 0
SHEET 2 AA1 8 VAL A 248 LEU A 255 -1 O LEU A 250 N VAL A 242
SHEET 3 AA1 8 ARG A 287 ASP A 292 -1 O ALA A 290 N VAL A 253
SHEET 4 AA1 8 ALA A 260 CYS A 264 1 N VAL A 261 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 ALA A 354 N PHE A 331
SHEET 7 AA1 8 ALA A 488 ALA A 493 1 O VAL A 491 N SER A 357
SHEET 8 AA1 8 LEU A 514 ILE A 519 1 O LYS A 515 N ALA A 488
CISPEP 1 PHE A 267 PRO A 268 0 -9.25
SITE 1 AC1 9 ASP A 335 TRP A 336 MET A 339 ILE A 375
SITE 2 AC1 9 PHE A 381 TYR A 383 GLN A 384 MET A 419
SITE 3 AC1 9 TYR A 466
CRYST1 80.180 92.420 106.530 90.00 90.00 90.00 I 2 2 2 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 0.012472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010820 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009387 0.00000
TER 2572 ARG A 547
MASTER 377 0 1 20 8 0 3 6 2600 1 24 27
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