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HEADER HYDROLASE 23-AUG-18 6HGX
TITLE SOLUBLE EPOXIDE HYDROLASE IN COMPLEX WITH 1-(4-((4-(TERT-BUTYL)
TITLE 2 MORPHOLIN-2-YL)METHOXY)PHENYL)-3-CYCLOHEXYLUREA
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 03-JUL-19 6HGX 0
JRNL AUTH K.HIESINGER,J.S.KRAMER,J.ACHENBACH,D.MOSER,J.WEBER,
JRNL AUTH 2 S.K.WITTMANN,C.MORISSEAU,C.ANGIONI,G.GEISSLINGER,A.S.KAHNT,
JRNL AUTH 3 A.KAISER,A.PROSCHAK,D.STEINHILBER,D.POGORYELOV,K.WAGNER,
JRNL AUTH 4 B.D.HAMMOCK,E.PROSCHAK
JRNL TITL COMPUTER-AIDED SELECTIVE OPTIMIZATION OF SIDE ACTIVITIES OF
JRNL TITL 2 TALINOLOL.
JRNL REF ACS MED.CHEM.LETT. V. 10 899 2019
JRNL REFN ISSN 1948-5875
JRNL PMID 31223445
JRNL DOI 10.1021/ACSMEDCHEMLETT.9B00075
REMARK 2
REMARK 2 RESOLUTION. 2.16 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) : 2.16
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 52.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 21197
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.640
REMARK 3 FREE R VALUE TEST SET COUNT : 2043
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 52.8658 - 5.3254 1.00 1372 146 0.1835 0.2197
REMARK 3 2 5.3254 - 4.2275 1.00 1309 140 0.1409 0.2014
REMARK 3 3 4.2275 - 3.6933 1.00 1292 137 0.1503 0.1814
REMARK 3 4 3.6933 - 3.3556 1.00 1288 137 0.1730 0.2351
REMARK 3 5 3.3556 - 3.1152 1.00 1280 136 0.1959 0.2402
REMARK 3 6 3.1152 - 2.9315 1.00 1281 137 0.2457 0.3461
REMARK 3 7 2.9315 - 2.7847 1.00 1250 134 0.2552 0.2796
REMARK 3 8 2.7847 - 2.6635 1.00 1284 136 0.2924 0.3637
REMARK 3 9 2.6635 - 2.5610 1.00 1269 137 0.2872 0.3495
REMARK 3 10 2.5610 - 2.4726 1.00 1259 134 0.2769 0.2969
REMARK 3 11 2.4726 - 2.3953 1.00 1258 134 0.2740 0.3475
REMARK 3 12 2.3953 - 2.3268 1.00 1273 135 0.2682 0.3251
REMARK 3 13 2.3268 - 2.2656 0.99 1254 133 0.2588 0.3020
REMARK 3 14 2.2656 - 2.2103 1.00 1242 134 0.2793 0.3486
REMARK 3 15 2.2103 - 2.1600 1.00 1243 133 0.2997 0.3201
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.43
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 : 0.008 2683
REMARK 3 ANGLE : 1.006 3647
REMARK 3 CHIRALITY : 0.054 378
REMARK 3 PLANARITY : 0.006 470
REMARK 3 DIHEDRAL : 24.131 1002
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 229 THROUGH 370 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0704 -13.7721 -32.8440
REMARK 3 T TENSOR
REMARK 3 T11: 0.1972 T22: 0.2281
REMARK 3 T33: 0.2800 T12: 0.0038
REMARK 3 T13: 0.0410 T23: 0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 3.1190 L22: 3.5538
REMARK 3 L33: 2.7071 L12: 1.0245
REMARK 3 L13: -0.1535 L23: 0.0270
REMARK 3 S TENSOR
REMARK 3 S11: -0.0629 S12: -0.0614 S13: -0.1676
REMARK 3 S21: -0.1444 S22: -0.0068 S23: -0.1623
REMARK 3 S31: 0.0973 S32: 0.1045 S33: 0.0330
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 399 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3155 -31.2642 -44.8033
REMARK 3 T TENSOR
REMARK 3 T11: 0.8525 T22: 0.5614
REMARK 3 T33: 0.7426 T12: -0.1327
REMARK 3 T13: 0.1040 T23: 0.0545
REMARK 3 L TENSOR
REMARK 3 L11: 3.2975 L22: 3.2234
REMARK 3 L33: 4.4811 L12: -3.1367
REMARK 3 L13: 0.6741 L23: 0.1009
REMARK 3 S TENSOR
REMARK 3 S11: -0.4563 S12: -0.3036 S13: -1.4579
REMARK 3 S21: -0.1793 S22: 0.5075 S23: 0.6477
REMARK 3 S31: 1.2944 S32: -0.7960 S33: 0.0448
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 400 THROUGH 421 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6448 -20.8989 -43.3282
REMARK 3 T TENSOR
REMARK 3 T11: 0.4434 T22: 0.4647
REMARK 3 T33: 0.5156 T12: -0.0246
REMARK 3 T13: -0.0879 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 4.1845 L22: 4.3593
REMARK 3 L33: 4.5688 L12: 3.0785
REMARK 3 L13: -3.9970 L23: -1.6803
REMARK 3 S TENSOR
REMARK 3 S11: -0.3691 S12: -0.2598 S13: -0.6804
REMARK 3 S21: -0.3281 S22: 0.2148 S23: -0.1537
REMARK 3 S31: 0.8655 S32: 0.3222 S33: 0.2054
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 422 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1692 -20.6689 -32.1476
REMARK 3 T TENSOR
REMARK 3 T11: 0.3187 T22: 0.2527
REMARK 3 T33: 0.3145 T12: -0.0535
REMARK 3 T13: 0.0280 T23: 0.0276
REMARK 3 L TENSOR
REMARK 3 L11: 2.9719 L22: 2.9229
REMARK 3 L33: 2.2203 L12: -0.1512
REMARK 3 L13: 0.0138 L23: -0.1670
REMARK 3 S TENSOR
REMARK 3 S11: -0.0899 S12: -0.0144 S13: -0.2692
REMARK 3 S21: -0.1751 S22: 0.0851 S23: 0.0734
REMARK 3 S31: 0.2147 S32: -0.1057 S33: -0.0214
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 6HGX 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_1200011561.
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 : 21319
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 52.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 6.362
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.2800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.41
REMARK 200 R MERGE FOR SHELL (I) : 1.01600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.390
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 (%): 49.69
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
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 39.90000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 46.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 52.85000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 39.90000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 46.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 52.85000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 39.90000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 46.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 52.85000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 39.90000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 46.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 52.85000
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: 100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 744 LIES ON A SPECIAL POSITION.
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 -161.28 -100.02
REMARK 500 GLU A 269 -140.63 -127.03
REMARK 500 ASP A 335 -129.30 61.95
REMARK 500 ASN A 359 -48.62 81.89
REMARK 500 PRO A 367 1.15 -69.30
REMARK 500 GLU A 435 76.27 -112.67
REMARK 500 MET A 503 -9.90 -56.14
REMARK 500 HIS A 513 30.12 -97.53
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 A 812 DISTANCE = 6.14 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 509 OD1
REMARK 620 2 ASP A 509 OD2 55.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue G3T A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6HGV RELATED DB: PDB
REMARK 900 6HGV CONTAINS THE SAME PROTEIN IN COMPLEX WITH TALINOLOL
DBREF 6HGX 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 MG A 601 1
HET G3T A 602 28
HETNAM MG MAGNESIUM ION
HETNAM G3T 1-[4-[[(2~{S})-4-~{TERT}-BUTYLMORPHOLIN-2-
HETNAM 2 G3T YL]METHOXY]PHENYL]-3-CYCLOHEXYL-UREA
FORMUL 2 MG MG 2+
FORMUL 3 G3T C22 H35 N3 O3
FORMUL 4 HOH *112(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 ALA A 377 1 8
HELIX 8 AA8 ASN A 378 VAL A 380 5 3
HELIX 9 AA9 PHE A 381 PHE A 387 1 7
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 LYS A 421 GLY A 426 1 6
HELIX 14 AB5 THR A 443 GLY A 458 1 16
HELIX 15 AB6 PHE A 459 ASN A 464 1 6
HELIX 16 AB7 TRP A 465 ARG A 467 5 3
HELIX 17 AB8 ASN A 468 LYS A 478 1 11
HELIX 18 AB9 VAL A 500 GLN A 505 5 6
HELIX 19 AC1 HIS A 506 TRP A 510 5 5
HELIX 20 AC2 TRP A 525 LYS A 530 1 6
HELIX 21 AC3 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 VAL A 288 N LEU A 255
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 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 LEU A 514 ILE A 519 1 O ILE A 519 N THR A 492
LINK OD1 ASP A 509 MG MG A 601 1555 1555 2.57
LINK OD2 ASP A 509 MG MG A 601 1555 1555 1.98
CISPEP 1 PHE A 267 PRO A 268 0 -8.39
SITE 1 AC1 2 HIS A 506 ASP A 509
SITE 1 AC2 11 PHE A 267 ASP A 335 TRP A 336 MET A 339
SITE 2 AC2 11 ILE A 375 TYR A 383 GLN A 384 MET A 419
SITE 3 AC2 11 TYR A 466 MET A 469 HIS A 524
CRYST1 79.800 92.000 105.700 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 0.012531 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010870 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009461 0.00000
TER 2575 ARG A 547
MASTER 402 0 2 21 8 0 4 6 2689 1 31 27
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