HEADER TRANSFERASE 17-MAR-17 5NGB
TITLE X-RAY DIFFRACTION CRYSTAL STRUCTURE OF THE MURINE PI3K P110DELTA IN
TITLE 2 COMPLEX WITH A PAN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE 3-KINASE CATALYTIC
COMPND 3 SUBUNIT DELTA ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: PUTATIVE UNCHARACTERIZED PROTEIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: RESIDUES 106-1044
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PIK3CD;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: SF21;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC HTA
KEYWDS PI3K P110, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.BERNDT,R.L.WILLIAMS
REVDAT 4 17-JAN-24 5NGB 1 REMARK
REVDAT 3 20-FEB-19 5NGB 1 REMARK LINK
REVDAT 2 27-SEP-17 5NGB 1 JRNL
REVDAT 1 13-SEP-17 5NGB 0
JRNL AUTH T.PIRALI,E.CIRAOLO,S.APRILE,A.MASSAROTTI,A.BERNDT,A.GRIGLIO,
JRNL AUTH 2 M.SERAFINI,V.MERCALLI,C.LANDONI,C.C.CAMPA,J.P.MARGARIA,
JRNL AUTH 3 R.L.SILVA,G.GROSA,G.SORBA,R.WILLIAMS,E.HIRSCH,G.C.TRON
JRNL TITL IDENTIFICATION OF A POTENT PHOSPHOINOSITIDE 3-KINASE PAN
JRNL TITL 2 INHIBITOR DISPLAYING A STRATEGIC CARBOXYLIC ACID GROUP AND
JRNL TITL 3 DEVELOPMENT OF ITS PRODRUGS.
JRNL REF CHEMMEDCHEM V. 12 1542 2017
JRNL REFN ESSN 1860-7187
JRNL PMID 28857471
JRNL DOI 10.1002/CMDC.201700340
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 21718
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.242
REMARK 3 FREE R VALUE : 0.290
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1170
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) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1524
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.4460
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6593
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.67000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -2.69000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.472
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.402
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.734
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.888
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.831
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6770 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6323 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9135 ; 1.492 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14660 ; 1.093 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 804 ; 5.662 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 315 ;35.677 ;23.905
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1224 ;18.737 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;19.727 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1005 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7362 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1398 ; 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): 3252 ; 3.273 ; 5.021
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3251 ; 3.273 ; 5.020
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4044 ; 5.427 ; 7.509
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4045 ; 5.427 ; 7.511
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3517 ; 2.872 ; 5.293
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3518 ; 2.871 ; 5.292
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5092 ; 4.918 ; 7.838
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 28219 ;10.834 ;93.464
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 28220 ;10.834 ;93.462
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 5NGB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200002568.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-SEP-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SILICON CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS MARCH 15 2012
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22926
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 45.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 10.00
REMARK 200 R MERGE (I) : 0.25100
REMARK 200 R SYM (I) : 0.25200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : 1.10400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: 2WXH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% (V/V) GLYCEROL, 13% (W/V) PEG 4K,
REMARK 280 3 MM NANO3, 3 MM NA2HPO4, 3 MM (NH4)2SO4, 100 MM IMIDAZOLE PH
REMARK 280 6.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 110.09650
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 110.09650
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 31.71850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.79300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 31.71850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.79300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 110.09650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 31.71850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.79300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 110.09650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 31.71850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.79300
REMARK 290 SMTRY3 8 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: 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: 36430 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 -34
REMARK 465 SER A -33
REMARK 465 TYR A -32
REMARK 465 TYR 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 HIS A -25
REMARK 465 ASP A -24
REMARK 465 TYR A -23
REMARK 465 ASP A -22
REMARK 465 ILE A -21
REMARK 465 PRO A -20
REMARK 465 THR A -19
REMARK 465 THR A -18
REMARK 465 GLU A -17
REMARK 465 ASN A -16
REMARK 465 LEU A -15
REMARK 465 TYR A -14
REMARK 465 PHE A -13
REMARK 465 GLN A -12
REMARK 465 GLY A -11
REMARK 465 ALA A -10
REMARK 465 MET A -9
REMARK 465 ASP A -8
REMARK 465 LEU A -7
REMARK 465 MET A -6
REMARK 465 PRO A -5
REMARK 465 PRO A -4
REMARK 465 GLY A -3
REMARK 465 VAL A -2
REMARK 465 ASP A -1
REMARK 465 CYS A 0
REMARK 465 PRO A 1
REMARK 465 MET A 2
REMARK 465 GLU A 3
REMARK 465 PHE A 4
REMARK 465 TRP A 5
REMARK 465 THR A 6
REMARK 465 LYS A 7
REMARK 465 GLU A 8
REMARK 465 GLU A 9
REMARK 465 SER A 10
REMARK 465 GLN A 11
REMARK 465 SER A 12
REMARK 465 VAL A 13
REMARK 465 VAL A 14
REMARK 465 VAL A 15
REMARK 465 ASP A 16
REMARK 465 PHE A 17
REMARK 465 LEU A 18
REMARK 465 LEU A 19
REMARK 465 PRO A 20
REMARK 465 THR A 21
REMARK 465 GLY A 22
REMARK 465 VAL A 23
REMARK 465 TYR A 24
REMARK 465 LEU A 25
REMARK 465 ASN A 26
REMARK 465 PHE A 27
REMARK 465 PRO A 28
REMARK 465 VAL A 29
REMARK 465 SER A 30
REMARK 465 ARG A 31
REMARK 465 ASN A 32
REMARK 465 ALA A 33
REMARK 465 ASN A 34
REMARK 465 LEU A 35
REMARK 465 SER A 36
REMARK 465 THR A 37
REMARK 465 ILE A 38
REMARK 465 LYS A 39
REMARK 465 GLN A 40
REMARK 465 VAL A 41
REMARK 465 LEU A 42
REMARK 465 TRP A 43
REMARK 465 HIS A 44
REMARK 465 ARG A 45
REMARK 465 ALA A 46
REMARK 465 GLN A 47
REMARK 465 TYR A 48
REMARK 465 GLU A 49
REMARK 465 PRO A 50
REMARK 465 LEU A 51
REMARK 465 PHE A 52
REMARK 465 HIS A 53
REMARK 465 MET A 54
REMARK 465 LEU A 55
REMARK 465 SER A 56
REMARK 465 ASP A 57
REMARK 465 PRO A 58
REMARK 465 GLU A 59
REMARK 465 ALA A 60
REMARK 465 TYR A 61
REMARK 465 VAL A 62
REMARK 465 PHE A 63
REMARK 465 THR A 64
REMARK 465 CYS A 65
REMARK 465 VAL A 66
REMARK 465 ASN A 67
REMARK 465 GLN A 68
REMARK 465 THR A 69
REMARK 465 ALA A 70
REMARK 465 GLU A 71
REMARK 465 GLN A 72
REMARK 465 GLN A 73
REMARK 465 GLU A 74
REMARK 465 LEU A 75
REMARK 465 GLU A 76
REMARK 465 ASP A 77
REMARK 465 GLU A 78
REMARK 465 GLN A 79
REMARK 465 ARG A 80
REMARK 465 ARG A 81
REMARK 465 LEU A 82
REMARK 465 CYS A 83
REMARK 465 ASP A 84
REMARK 465 ILE A 85
REMARK 465 GLN A 86
REMARK 465 PRO A 87
REMARK 465 PHE A 88
REMARK 465 LEU A 89
REMARK 465 PRO A 90
REMARK 465 VAL A 91
REMARK 465 LEU A 92
REMARK 465 ARG A 93
REMARK 465 LEU A 94
REMARK 465 VAL A 95
REMARK 465 ALA A 96
REMARK 465 ARG A 97
REMARK 465 GLU A 98
REMARK 465 GLU A 99
REMARK 465 ASN A 100
REMARK 465 LEU A 101
REMARK 465 TYR A 102
REMARK 465 PHE A 103
REMARK 465 GLN A 104
REMARK 465 GLY A 105
REMARK 465 GLY A 106
REMARK 465 ASP A 107
REMARK 465 ARG A 108
REMARK 465 SER A 174
REMARK 465 ALA A 175
REMARK 465 ARG A 176
REMARK 465 GLY A 177
REMARK 465 TRP A 178
REMARK 465 ARG A 179
REMARK 465 ALA A 180
REMARK 465 GLY A 181
REMARK 465 LEU A 182
REMARK 465 LEU A 183
REMARK 465 ARG A 184
REMARK 465 VAL A 185
REMARK 465 SER A 186
REMARK 465 PRO A 231
REMARK 465 LEU A 232
REMARK 465 VAL A 233
REMARK 465 GLU A 234
REMARK 465 PRO A 292
REMARK 465 ALA A 293
REMARK 465 PRO A 294
REMARK 465 GLN A 295
REMARK 465 VAL A 296
REMARK 465 GLN A 297
REMARK 465 LYS A 298
REMARK 465 PRO A 299
REMARK 465 ARG A 300
REMARK 465 ALA A 301
REMARK 465 LYS A 302
REMARK 465 PRO A 303
REMARK 465 PRO A 304
REMARK 465 PRO A 305
REMARK 465 ILE A 306
REMARK 465 PRO A 307
REMARK 465 ALA A 308
REMARK 465 LYS A 309
REMARK 465 LYS A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 SER A 313
REMARK 465 VAL A 314
REMARK 465 SER A 315
REMARK 465 ASP A 336
REMARK 465 GLU A 337
REMARK 465 ARG A 338
REMARK 465 GLU A 399
REMARK 465 LYS A 400
REMARK 465 ALA A 401
REMARK 465 LYS A 402
REMARK 465 LYS A 403
REMARK 465 ALA A 404
REMARK 465 ARG A 405
REMARK 465 SER A 406
REMARK 465 THR A 407
REMARK 465 LYS A 408
REMARK 465 LYS A 409
REMARK 465 LYS A 410
REMARK 465 SER A 411
REMARK 465 LYS A 412
REMARK 465 LYS A 413
REMARK 465 ALA A 414
REMARK 465 PRO A 446
REMARK 465 ASP A 447
REMARK 465 GLU A 448
REMARK 465 LYS A 449
REMARK 465 GLY A 450
REMARK 465 GLU A 451
REMARK 465 PRO A 480
REMARK 465 HIS A 481
REMARK 465 GLY A 495
REMARK 465 ARG A 496
REMARK 465 HIS A 497
REMARK 465 GLY A 498
REMARK 465 GLU A 499
REMARK 465 ARG A 500
REMARK 465 GLY A 501
REMARK 465 ARG A 502
REMARK 465 ILE A 503
REMARK 465 THR A 504
REMARK 465 GLU A 505
REMARK 465 GLU A 506
REMARK 465 GLU A 507
REMARK 465 GLN A 508
REMARK 465 LEU A 509
REMARK 465 GLN A 510
REMARK 465 ARG A 518
REMARK 465 GLY A 519
REMARK 465 SER A 520
REMARK 465 GLY A 521
REMARK 465 ASN A 840
REMARK 465 LYS A 841
REMARK 465 SER A 842
REMARK 465 ASN A 843
REMARK 465 MET A 844
REMARK 465 ALA A 845
REMARK 465 ALA A 846
REMARK 465 PHE A 919
REMARK 465 LYS A 920
REMARK 465 THR A 921
REMARK 465 LYS A 922
REMARK 465 PHE A 923
REMARK 465 GLY A 924
REMARK 465 ILE A 925
REMARK 465 ASN A 926
REMARK 465 LYS A 1028
REMARK 465 THR A 1029
REMARK 465 LYS A 1030
REMARK 465 VAL A 1031
REMARK 465 ASN A 1032
REMARK 465 TRP A 1033
REMARK 465 LEU A 1034
REMARK 465 ALA A 1035
REMARK 465 HIS A 1036
REMARK 465 ASN A 1037
REMARK 465 VAL A 1038
REMARK 465 SER A 1039
REMARK 465 LYS A 1040
REMARK 465 ASP A 1041
REMARK 465 ASN A 1042
REMARK 465 ARG A 1043
REMARK 465 GLN A 1044
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 LEU A 452 CG CD1 CD2
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 LEU A 157 NH1 ARG A 286 1.44
REMARK 500 O VAL A 746 N GLN A 748 1.83
REMARK 500 NZ LYS A 708 OBC 8WH A 1101 1.94
REMARK 500 O PRO A 369 CE3 TRP A 371 2.06
REMARK 500 O LEU A 916 N ASN A 918 2.09
REMARK 500 NH2 ARG A 374 OE1 GLU A 376 2.10
REMARK 500 OG1 THR A 706 OE1 GLN A 710 2.11
REMARK 500 O GLY A 435 N LEU A 475 2.13
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 ND2 ASN A 948 ND2 ASN A 948 3655 2.02
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 957 NE - CZ - NH2 ANGL. DEV. = 3.1 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 ARG A 229 11.36 46.04
REMARK 500 ILE A 328 -72.82 -83.55
REMARK 500 ARG A 331 84.08 -168.88
REMARK 500 CYS A 355 -175.09 -179.88
REMARK 500 ASN A 364 156.90 -40.51
REMARK 500 VAL A 365 71.04 -100.14
REMARK 500 SER A 367 -129.05 49.77
REMARK 500 TRP A 371 -55.87 -133.66
REMARK 500 ILE A 379 137.11 -171.47
REMARK 500 ILE A 418 -55.63 -120.01
REMARK 500 SER A 675 86.73 -152.64
REMARK 500 HIS A 730 64.34 67.09
REMARK 500 ASP A 736 105.21 -163.83
REMARK 500 GLU A 742 -98.05 -89.16
REMARK 500 VAL A 746 -84.00 -50.03
REMARK 500 GLU A 747 -24.90 -20.42
REMARK 500 LYS A 755 -71.31 67.46
REMARK 500 LYS A 757 58.77 35.39
REMARK 500 LEU A 916 72.11 32.05
REMARK 500 GLU A 928 -159.63 -97.27
REMARK 500 ASN A 949 72.74 -161.72
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 8WH A 1101
DBREF 5NGB A -6 1044 UNP Q3UDT3 Q3UDT3_MOUSE 1 1044
SEQADV 5NGB MET A -34 UNP Q3UDT3 INITIATING METHIONINE
SEQADV 5NGB SER A -33 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB TYR A -32 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB TYR A -31 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -30 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -29 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -28 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -27 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -26 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB HIS A -25 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ASP A -24 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB TYR A -23 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ASP A -22 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ILE A -21 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB PRO A -20 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB THR A -19 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB THR A -18 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB GLU A -17 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ASN A -16 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB LEU A -15 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB TYR A -14 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB PHE A -13 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB GLN A -12 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB GLY A -11 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ALA A -10 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB MET A -9 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB ASP A -8 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB LEU A -7 UNP Q3UDT3 EXPRESSION TAG
SEQADV 5NGB GLU A 99 UNP Q3UDT3 INSERTION
SEQADV 5NGB ASN A 100 UNP Q3UDT3 INSERTION
SEQADV 5NGB LEU A 101 UNP Q3UDT3 INSERTION
SEQADV 5NGB TYR A 102 UNP Q3UDT3 INSERTION
SEQADV 5NGB PHE A 103 UNP Q3UDT3 INSERTION
SEQADV 5NGB GLN A 104 UNP Q3UDT3 INSERTION
SEQADV 5NGB GLY A 105 UNP Q3UDT3 INSERTION
SEQRES 1 A 1079 MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ASP
SEQRES 2 A 1079 ILE PRO THR THR GLU ASN LEU TYR PHE GLN GLY ALA MET
SEQRES 3 A 1079 ASP LEU MET PRO PRO GLY VAL ASP CYS PRO MET GLU PHE
SEQRES 4 A 1079 TRP THR LYS GLU GLU SER GLN SER VAL VAL VAL ASP PHE
SEQRES 5 A 1079 LEU LEU PRO THR GLY VAL TYR LEU ASN PHE PRO VAL SER
SEQRES 6 A 1079 ARG ASN ALA ASN LEU SER THR ILE LYS GLN VAL LEU TRP
SEQRES 7 A 1079 HIS ARG ALA GLN TYR GLU PRO LEU PHE HIS MET LEU SER
SEQRES 8 A 1079 ASP PRO GLU ALA TYR VAL PHE THR CYS VAL ASN GLN THR
SEQRES 9 A 1079 ALA GLU GLN GLN GLU LEU GLU ASP GLU GLN ARG ARG LEU
SEQRES 10 A 1079 CYS ASP ILE GLN PRO PHE LEU PRO VAL LEU ARG LEU VAL
SEQRES 11 A 1079 ALA ARG GLU GLU ASN LEU TYR PHE GLN GLY GLY ASP ARG
SEQRES 12 A 1079 VAL LYS LYS LEU ILE ASN SER GLN ILE SER LEU LEU ILE
SEQRES 13 A 1079 GLY LYS GLY LEU HIS GLU PHE ASP SER LEU ARG ASP PRO
SEQRES 14 A 1079 GLU VAL ASN ASP PHE ARG THR LYS MET ARG GLN PHE CYS
SEQRES 15 A 1079 GLU GLU ALA ALA ALA HIS ARG GLN GLN LEU GLY TRP VAL
SEQRES 16 A 1079 GLU TRP LEU GLN TYR SER PHE PRO LEU GLN LEU GLU PRO
SEQRES 17 A 1079 SER ALA ARG GLY TRP ARG ALA GLY LEU LEU ARG VAL SER
SEQRES 18 A 1079 ASN ARG ALA LEU LEU VAL ASN VAL LYS PHE GLU GLY SER
SEQRES 19 A 1079 GLU GLU SER PHE THR PHE GLN VAL SER THR LYS ASP MET
SEQRES 20 A 1079 PRO LEU ALA LEU MET ALA CYS ALA LEU ARG LYS LYS ALA
SEQRES 21 A 1079 THR VAL PHE ARG GLN PRO LEU VAL GLU GLN PRO GLU GLU
SEQRES 22 A 1079 TYR ALA LEU GLN VAL ASN GLY ARG HIS GLU TYR LEU TYR
SEQRES 23 A 1079 GLY ASN TYR PRO LEU CYS HIS PHE GLN TYR ILE CYS SER
SEQRES 24 A 1079 CYS LEU HIS SER GLY LEU THR PRO HIS LEU THR MET VAL
SEQRES 25 A 1079 HIS SER SER SER ILE LEU ALA MET ARG ASP GLU GLN SER
SEQRES 26 A 1079 ASN PRO ALA PRO GLN VAL GLN LYS PRO ARG ALA LYS PRO
SEQRES 27 A 1079 PRO PRO ILE PRO ALA LYS LYS PRO SER SER VAL SER LEU
SEQRES 28 A 1079 TRP SER LEU GLU GLN PRO PHE SER ILE GLU LEU ILE GLU
SEQRES 29 A 1079 GLY ARG LYS VAL ASN ALA ASP GLU ARG MET LYS LEU VAL
SEQRES 30 A 1079 VAL GLN ALA GLY LEU PHE HIS GLY ASN GLU MET LEU CYS
SEQRES 31 A 1079 LYS THR VAL SER SER SER GLU VAL ASN VAL CYS SER GLU
SEQRES 32 A 1079 PRO VAL TRP LYS GLN ARG LEU GLU PHE ASP ILE SER VAL
SEQRES 33 A 1079 CYS ASP LEU PRO ARG MET ALA ARG LEU CYS PHE ALA LEU
SEQRES 34 A 1079 TYR ALA VAL VAL GLU LYS ALA LYS LYS ALA ARG SER THR
SEQRES 35 A 1079 LYS LYS LYS SER LYS LYS ALA ASP CYS PRO ILE ALA TRP
SEQRES 36 A 1079 ALA ASN LEU MET LEU PHE ASP TYR LYS ASP GLN LEU LYS
SEQRES 37 A 1079 THR GLY GLU ARG CYS LEU TYR MET TRP PRO SER VAL PRO
SEQRES 38 A 1079 ASP GLU LYS GLY GLU LEU LEU ASN PRO ALA GLY THR VAL
SEQRES 39 A 1079 ARG GLY ASN PRO ASN THR GLU SER ALA ALA ALA LEU VAL
SEQRES 40 A 1079 ILE TYR LEU PRO GLU VAL ALA PRO HIS PRO VAL TYR PHE
SEQRES 41 A 1079 PRO ALA LEU GLU LYS ILE LEU GLU LEU GLY ARG HIS GLY
SEQRES 42 A 1079 GLU ARG GLY ARG ILE THR GLU GLU GLU GLN LEU GLN LEU
SEQRES 43 A 1079 ARG GLU ILE LEU GLU ARG ARG GLY SER GLY GLU LEU TYR
SEQRES 44 A 1079 GLU HIS GLU LYS ASP LEU VAL TRP LYS MET ARG HIS GLU
SEQRES 45 A 1079 VAL GLN GLU HIS PHE PRO GLU ALA LEU ALA ARG LEU LEU
SEQRES 46 A 1079 LEU VAL THR LYS TRP ASN LYS HIS GLU ASP VAL ALA GLN
SEQRES 47 A 1079 MET LEU TYR LEU LEU CYS SER TRP PRO GLU LEU PRO VAL
SEQRES 48 A 1079 LEU SER ALA LEU GLU LEU LEU ASP PHE SER PHE PRO ASP
SEQRES 49 A 1079 CYS TYR VAL GLY SER PHE ALA ILE LYS SER LEU ARG LYS
SEQRES 50 A 1079 LEU THR ASP ASP GLU LEU PHE GLN TYR LEU LEU GLN LEU
SEQRES 51 A 1079 VAL GLN VAL LEU LYS TYR GLU SER TYR LEU ASP CYS GLU
SEQRES 52 A 1079 LEU THR LYS PHE LEU LEU GLY ARG ALA LEU ALA ASN ARG
SEQRES 53 A 1079 LYS ILE GLY HIS PHE LEU PHE TRP HIS LEU ARG SER GLU
SEQRES 54 A 1079 MET HIS VAL PRO SER VAL ALA LEU ARG PHE GLY LEU ILE
SEQRES 55 A 1079 MET GLU ALA TYR CYS ARG GLY SER THR HIS HIS MET LYS
SEQRES 56 A 1079 VAL LEU MET LYS GLN GLY GLU ALA LEU SER LYS LEU LYS
SEQRES 57 A 1079 ALA LEU ASN ASP PHE VAL LYS VAL SER SER GLN LYS THR
SEQRES 58 A 1079 THR LYS PRO GLN THR LYS GLU MET MET HIS MET CYS MET
SEQRES 59 A 1079 ARG GLN GLU THR TYR MET GLU ALA LEU SER HIS LEU GLN
SEQRES 60 A 1079 SER PRO LEU ASP PRO SER THR LEU LEU GLU GLU VAL CYS
SEQRES 61 A 1079 VAL GLU GLN CYS THR PHE MET ASP SER LYS MET LYS PRO
SEQRES 62 A 1079 LEU TRP ILE MET TYR SER SER GLU GLU ALA GLY SER ALA
SEQRES 63 A 1079 GLY ASN VAL GLY ILE ILE PHE LYS ASN GLY ASP ASP LEU
SEQRES 64 A 1079 ARG GLN ASP MET LEU THR LEU GLN MET ILE GLN LEU MET
SEQRES 65 A 1079 ASP VAL LEU TRP LYS GLN GLU GLY LEU ASP LEU ARG MET
SEQRES 66 A 1079 THR PRO TYR GLY CYS LEU PRO THR GLY ASP ARG THR GLY
SEQRES 67 A 1079 LEU ILE GLU VAL VAL LEU HIS SER ASP THR ILE ALA ASN
SEQRES 68 A 1079 ILE GLN LEU ASN LYS SER ASN MET ALA ALA THR ALA ALA
SEQRES 69 A 1079 PHE ASN LYS ASP ALA LEU LEU ASN TRP LEU LYS SER LYS
SEQRES 70 A 1079 ASN PRO GLY GLU ALA LEU ASP ARG ALA ILE GLU GLU PHE
SEQRES 71 A 1079 THR LEU SER CYS ALA GLY TYR CYS VAL ALA THR TYR VAL
SEQRES 72 A 1079 LEU GLY ILE GLY ASP ARG HIS SER ASP ASN ILE MET ILE
SEQRES 73 A 1079 ARG GLU SER GLY GLN LEU PHE HIS ILE ASP PHE GLY HIS
SEQRES 74 A 1079 PHE LEU GLY ASN PHE LYS THR LYS PHE GLY ILE ASN ARG
SEQRES 75 A 1079 GLU ARG VAL PRO PHE ILE LEU THR TYR ASP PHE VAL HIS
SEQRES 76 A 1079 VAL ILE GLN GLN GLY LYS THR ASN ASN SER GLU LYS PHE
SEQRES 77 A 1079 GLU ARG PHE ARG GLY TYR CYS GLU ARG ALA TYR THR ILE
SEQRES 78 A 1079 LEU ARG ARG HIS GLY LEU LEU PHE LEU HIS LEU PHE ALA
SEQRES 79 A 1079 LEU MET ARG ALA ALA GLY LEU PRO GLU LEU SER CYS SER
SEQRES 80 A 1079 LYS ASP ILE GLN TYR LEU LYS ASP SER LEU ALA LEU GLY
SEQRES 81 A 1079 LYS THR GLU GLU GLU ALA LEU LYS HIS PHE ARG VAL LYS
SEQRES 82 A 1079 PHE ASN GLU ALA LEU ARG GLU SER TRP LYS THR LYS VAL
SEQRES 83 A 1079 ASN TRP LEU ALA HIS ASN VAL SER LYS ASP ASN ARG GLN
HET 8WH A1101 32
HETNAM 8WH 3-[[4-(2-MORPHOLIN-4-YL-4-OXIDANYLIDENE-3~{H}-QUINOLIN-
HETNAM 2 8WH 8-YL)-1,2,3-TRIAZOL-1-YL]METHYL]BENZOIC ACID
FORMUL 2 8WH C23 H21 N5 O4
HELIX 1 AA1 VAL A 109 GLY A 122 1 14
HELIX 2 AA2 GLY A 124 SER A 130 1 7
HELIX 3 AA3 ASP A 133 GLN A 156 1 24
HELIX 4 AA4 GLY A 158 PHE A 167 1 10
HELIX 5 AA5 MET A 212 PHE A 228 1 17
HELIX 6 AA6 GLN A 235 GLU A 237 5 3
HELIX 7 AA7 PHE A 259 GLY A 269 1 11
HELIX 8 AA8 SER A 279 GLU A 288 1 10
HELIX 9 AA9 CYS A 382 LEU A 384 5 3
HELIX 10 AB1 ALA A 487 LEU A 494 1 8
HELIX 11 AB2 ARG A 512 GLU A 516 1 5
HELIX 12 AB3 TYR A 524 MET A 534 1 11
HELIX 13 AB4 MET A 534 PHE A 542 1 9
HELIX 14 AB5 ALA A 545 THR A 553 1 9
HELIX 15 AB6 LYS A 557 CYS A 569 1 13
HELIX 16 AB7 PRO A 575 LEU A 583 1 9
HELIX 17 AB8 ASP A 589 ARG A 601 1 13
HELIX 18 AB9 THR A 604 LEU A 619 1 16
HELIX 19 AC1 LYS A 620 GLU A 622 5 3
HELIX 20 AC2 CYS A 627 ASN A 640 1 14
HELIX 21 AC3 ASN A 640 SER A 653 1 14
HELIX 22 AC4 VAL A 657 SER A 675 1 19
HELIX 23 AC5 SER A 675 SER A 703 1 29
HELIX 24 AC6 THR A 707 GLN A 721 1 15
HELIX 25 AC7 GLN A 721 SER A 729 1 9
HELIX 26 AC8 VAL A 746 CYS A 749 5 4
HELIX 27 AC9 ALA A 768 ASN A 773 5 6
HELIX 28 AD1 LEU A 784 GLN A 803 1 20
HELIX 29 AD2 ILE A 834 GLN A 838 1 5
HELIX 30 AD3 PHE A 850 LYS A 852 5 3
HELIX 31 AD4 ASP A 853 ASN A 863 1 11
HELIX 32 AD5 GLU A 866 GLY A 890 1 25
HELIX 33 AD6 THR A 935 GLN A 943 1 9
HELIX 34 AD7 ASN A 949 HIS A 970 1 22
HELIX 35 AD8 HIS A 970 ARG A 982 1 13
HELIX 36 AD9 ALA A 983 GLY A 985 5 3
HELIX 37 AE1 CYS A 991 LEU A 1002 1 12
HELIX 38 AE2 THR A 1007 SER A 1026 1 20
SHEET 1 AA1 5 SER A 202 SER A 208 0
SHEET 2 AA1 5 ALA A 189 PHE A 196 -1 N LEU A 190 O VAL A 207
SHEET 3 AA1 5 HIS A 273 HIS A 278 1 O MET A 276 N LYS A 195
SHEET 4 AA1 5 TYR A 239 VAL A 243 -1 N GLN A 242 O THR A 275
SHEET 5 AA1 5 TYR A 249 LEU A 250 -1 O LEU A 250 N LEU A 241
SHEET 1 AA2 4 GLN A 373 SER A 380 0
SHEET 2 AA2 4 PRO A 322 GLY A 330 -1 N PHE A 323 O PHE A 377
SHEET 3 AA2 4 ALA A 470 LEU A 475 -1 O VAL A 472 N GLU A 329
SHEET 4 AA2 4 GLY A 435 TYR A 440 -1 N GLY A 435 O LEU A 475
SHEET 1 AA3 3 GLU A 352 MET A 353 0
SHEET 2 AA3 3 LYS A 340 HIS A 349 -1 N HIS A 349 O GLU A 352
SHEET 3 AA3 3 VAL A 363 ASN A 364 -1 O VAL A 363 N LEU A 341
SHEET 1 AA4 5 GLU A 352 MET A 353 0
SHEET 2 AA4 5 LYS A 340 HIS A 349 -1 N HIS A 349 O GLU A 352
SHEET 3 AA4 5 ARG A 389 VAL A 397 -1 O ARG A 389 N PHE A 348
SHEET 4 AA4 5 CYS A 416 MET A 424 -1 O LEU A 423 N LEU A 390
SHEET 5 AA4 5 TRP A 442 PRO A 443 -1 O TRP A 442 N TRP A 420
SHEET 1 AA5 2 LEU A 731 SER A 733 0
SHEET 2 AA5 2 ASP A 736 LEU A 741 -1 O LEU A 741 N LEU A 731
SHEET 1 AA6 3 GLU A 743 VAL A 744 0
SHEET 2 AA6 3 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 3 AA6 3 THR A 750 PHE A 751 -1 N THR A 750 O TRP A 760
SHEET 1 AA7 5 GLU A 743 VAL A 744 0
SHEET 2 AA7 5 LEU A 759 SER A 764 -1 O SER A 764 N GLU A 743
SHEET 3 AA7 5 VAL A 774 ASN A 780 -1 O ILE A 776 N ILE A 761
SHEET 4 AA7 5 THR A 822 GLU A 826 -1 O ILE A 825 N ILE A 777
SHEET 5 AA7 5 CYS A 815 GLY A 819 -1 N LEU A 816 O LEU A 824
SHEET 1 AA8 3 SER A 831 THR A 833 0
SHEET 2 AA8 3 ILE A 899 ARG A 902 -1 O ILE A 901 N ASP A 832
SHEET 3 AA8 3 LEU A 907 HIS A 909 -1 O PHE A 908 N MET A 900
CISPEP 1 THR A 434 GLY A 435 0 -1.59
SITE 1 AC1 11 LYS A 708 MET A 752 ASP A 753 TRP A 760
SITE 2 AC1 11 ILE A 777 GLU A 826 VAL A 827 VAL A 828
SITE 3 AC1 11 MET A 900 ILE A 910 ASP A 911
CRYST1 63.437 143.586 220.193 90.00 90.00 90.00 C 2 2 21 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 0.015764 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006964 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004541 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
