HEADER TRANSFERASE/TRANSFERASE INHIBITOR 17-MAY-16 5K00
TITLE MELK IN COMPLEX WITH NVS-MELK5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HMELK,PROTEIN KINASE EG3,PEG3 KINASE,PROTEIN KINASE PK38,
COMPND 5 HPK38,TYROSINE-PROTEIN KINASE MELK;
COMPND 6 EC: 2.7.11.1,2.7.10.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MELK, KIAA0175;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)
KEYWDS KINASE UBA TYPEII INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR E.R.SPRAGUE
REVDAT 5 06-MAR-24 5K00 1 REMARK
REVDAT 4 22-MAR-17 5K00 1 JRNL
REVDAT 3 15-MAR-17 5K00 1 JRNL
REVDAT 2 08-MAR-17 5K00 1 JRNL
REVDAT 1 01-MAR-17 5K00 0
JRNL AUTH X.CHEN,J.GIRALDES,E.R.SPRAGUE,S.SHAKYA,Z.CHEN,Y.WANG,C.JOUD,
JRNL AUTH 2 S.MATHIEU,C.H.CHEN,C.STRAUB,J.DUCA,K.HUROV,Y.YUAN,W.SHAO,
JRNL AUTH 3 B.B.TOURE
JRNL TITL "ADDITION" AND "SUBTRACTION": SELECTIVITY DESIGN FOR TYPE II
JRNL TITL 2 MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 2155 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28186750
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00033
REMARK 2
REMARK 2 RESOLUTION. 1.77 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 40242
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.196
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2015
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.82
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2913
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2108
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2752
REMARK 3 BIN R VALUE (WORKING SET) : 0.2086
REMARK 3 BIN FREE R VALUE : 0.2499
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.53
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 161
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2537
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.35510
REMARK 3 B22 (A**2) : 7.54480
REMARK 3 B33 (A**2) : 2.81030
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.214
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.101
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.094
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.096
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.092
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2672 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3619 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 946 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 64 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 377 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2672 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 332 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3296 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.16
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.50
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3551 -3.1028 10.6063
REMARK 3 T TENSOR
REMARK 3 T11: -0.0402 T22: -0.1133
REMARK 3 T33: -0.0810 T12: -0.0164
REMARK 3 T13: 0.0075 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.9474 L22: 0.9336
REMARK 3 L33: 1.4369 L12: -0.1699
REMARK 3 L13: 0.4580 L23: -0.3361
REMARK 3 S TENSOR
REMARK 3 S11: -0.0125 S12: 0.0369 S13: 0.0238
REMARK 3 S21: -0.0257 S22: -0.0108 S23: 0.0416
REMARK 3 S31: -0.0337 S32: -0.0363 S33: 0.0232
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5K00 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1000221521.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40469
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.768
REMARK 200 RESOLUTION RANGE LOW (A) : 67.403
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.50400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.6, 0.2M NACL, 13.3%
REMARK 280 PEG 3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 28.73550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 52.31250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.70150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 52.31250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.73550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 33.70150
REMARK 290 SMTRY3 4 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: 14890 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 GLY A 21
REMARK 465 PHE A 22
REMARK 465 LYS A 158
REMARK 465 GLY A 159
REMARK 465 ASN A 160
REMARK 465 LYS A 161
REMARK 465 ASP A 162
REMARK 465 TYR A 163
REMARK 465 HIS A 164
REMARK 465 LEU A 165
REMARK 465 GLN A 166
REMARK 465 THR A 167
REMARK 465 CYS A 168
REMARK 465 CYS A 169
REMARK 465 GLY A 170
REMARK 465 LYS A 328
REMARK 465 PRO A 329
REMARK 465 VAL A 330
REMARK 465 HIS A 331
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 HIS A 334
REMARK 465 HIS A 335
REMARK 465 HIS A 336
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 HIS A 14 -159.51 -112.53
REMARK 500 ASP A 102 -59.53 76.67
REMARK 500 ARG A 131 -2.16 74.31
REMARK 500 TRP A 308 57.49 39.93
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 6PV A 401
DBREF 5K00 A 3 330 UNP Q14680 MELK_HUMAN 3 330
SEQADV 5K00 MET A 2 UNP Q14680 INITIATING METHIONINE
SEQADV 5K00 HIS A 331 UNP Q14680 EXPRESSION TAG
SEQADV 5K00 HIS A 332 UNP Q14680 EXPRESSION TAG
SEQADV 5K00 HIS A 333 UNP Q14680 EXPRESSION TAG
SEQADV 5K00 HIS A 334 UNP Q14680 EXPRESSION TAG
SEQADV 5K00 HIS A 335 UNP Q14680 EXPRESSION TAG
SEQADV 5K00 HIS A 336 UNP Q14680 EXPRESSION TAG
SEQRES 1 A 335 MET ASP TYR ASP GLU LEU LEU LYS TYR TYR GLU LEU HIS
SEQRES 2 A 335 GLU THR ILE GLY THR GLY GLY PHE ALA LYS VAL LYS LEU
SEQRES 3 A 335 ALA CYS HIS ILE LEU THR GLY GLU MET VAL ALA ILE LYS
SEQRES 4 A 335 ILE MET ASP LYS ASN THR LEU GLY SER ASP LEU PRO ARG
SEQRES 5 A 335 ILE LYS THR GLU ILE GLU ALA LEU LYS ASN LEU ARG HIS
SEQRES 6 A 335 GLN HIS ILE CYS GLN LEU TYR HIS VAL LEU GLU THR ALA
SEQRES 7 A 335 ASN LYS ILE PHE MET VAL LEU GLU TYR CYS PRO GLY GLY
SEQRES 8 A 335 GLU LEU PHE ASP TYR ILE ILE SER GLN ASP ARG LEU SER
SEQRES 9 A 335 GLU GLU GLU THR ARG VAL VAL PHE ARG GLN ILE VAL SER
SEQRES 10 A 335 ALA VAL ALA TYR VAL HIS SER GLN GLY TYR ALA HIS ARG
SEQRES 11 A 335 ASP LEU LYS PRO GLU ASN LEU LEU PHE ASP GLU TYR HIS
SEQRES 12 A 335 LYS LEU LYS LEU ILE ASP PHE GLY LEU CYS ALA LYS PRO
SEQRES 13 A 335 LYS GLY ASN LYS ASP TYR HIS LEU GLN THR CYS CYS GLY
SEQRES 14 A 335 SER LEU ALA TYR ALA ALA PRO GLU LEU ILE GLN GLY LYS
SEQRES 15 A 335 SER TYR LEU GLY SER GLU ALA ASP VAL TRP SER MET GLY
SEQRES 16 A 335 ILE LEU LEU TYR VAL LEU MET CYS GLY PHE LEU PRO PHE
SEQRES 17 A 335 ASP ASP ASP ASN VAL MET ALA LEU TYR LYS LYS ILE MET
SEQRES 18 A 335 ARG GLY LYS TYR ASP VAL PRO LYS TRP LEU SER PRO SER
SEQRES 19 A 335 SER ILE LEU LEU LEU GLN GLN MET LEU GLN VAL ASP PRO
SEQRES 20 A 335 LYS LYS ARG ILE SER MET LYS ASN LEU LEU ASN HIS PRO
SEQRES 21 A 335 TRP ILE MET GLN ASP TYR ASN TYR PRO VAL GLU TRP GLN
SEQRES 22 A 335 SER LYS ASN PRO PHE ILE HIS LEU ASP ASP ASP CYS VAL
SEQRES 23 A 335 THR GLU LEU SER VAL HIS HIS ARG ASN ASN ARG GLN THR
SEQRES 24 A 335 MET GLU ASP LEU ILE SER LEU TRP GLN TYR ASP HIS LEU
SEQRES 25 A 335 THR ALA THR TYR LEU LEU LEU LEU ALA LYS LYS ALA ARG
SEQRES 26 A 335 GLY LYS PRO VAL HIS HIS HIS HIS HIS HIS
HET 6PV A 401 42
HETNAM 6PV 4-{2-[(3-METHOXYPHENYL)AMINO]-4-[(PIPERIDIN-4-YL)
HETNAM 2 6PV METHOXY]PYRIMIDIN-5-YL}-N-[2-OXO-2-(PHENYLAMINO)
HETNAM 3 6PV ETHYL]BENZAMIDE
FORMUL 2 6PV C32 H34 N6 O4
FORMUL 3 HOH *235(H2 O)
HELIX 1 AA1 GLU A 6 LYS A 9 5 4
HELIX 2 AA2 LYS A 44 GLY A 48 1 5
HELIX 3 AA3 ASP A 50 ASN A 63 1 14
HELIX 4 AA4 LEU A 94 ASP A 102 1 9
HELIX 5 AA5 SER A 105 GLN A 126 1 22
HELIX 6 AA6 LYS A 134 GLU A 136 5 3
HELIX 7 AA7 SER A 171 ALA A 175 5 5
HELIX 8 AA8 ALA A 176 GLY A 182 1 7
HELIX 9 AA9 LEU A 186 GLY A 205 1 20
HELIX 10 AB1 ASN A 213 GLY A 224 1 12
HELIX 11 AB2 SER A 233 LEU A 244 1 12
HELIX 12 AB3 ASP A 247 ARG A 251 5 5
HELIX 13 AB4 SER A 253 ASN A 259 1 7
HELIX 14 AB5 HIS A 260 GLN A 265 1 6
HELIX 15 AB6 ASP A 283 VAL A 292 1 10
HELIX 16 AB7 ASN A 297 LEU A 307 1 11
HELIX 17 AB8 ASP A 311 GLY A 327 1 17
SHEET 1 AA1 5 TYR A 11 GLY A 18 0
SHEET 2 AA1 5 LYS A 24 HIS A 30 -1 O VAL A 25 N ILE A 17
SHEET 3 AA1 5 MET A 36 ASP A 43 -1 O ILE A 41 N LYS A 24
SHEET 4 AA1 5 LYS A 81 GLU A 87 -1 O LEU A 86 N ALA A 38
SHEET 5 AA1 5 LEU A 72 GLU A 77 -1 N TYR A 73 O VAL A 85
SHEET 1 AA2 3 GLY A 92 GLU A 93 0
SHEET 2 AA2 3 LEU A 138 PHE A 140 -1 O PHE A 140 N GLY A 92
SHEET 3 AA2 3 LEU A 146 LEU A 148 -1 O LYS A 147 N LEU A 139
SITE 1 AC1 21 ALA A 38 LYS A 40 LEU A 61 LEU A 64
SITE 2 AC1 21 CYS A 70 ASN A 80 LEU A 86 GLU A 87
SITE 3 AC1 21 TYR A 88 CYS A 89 PRO A 90 GLY A 92
SITE 4 AC1 21 GLU A 93 GLU A 136 LEU A 139 ILE A 149
SITE 5 AC1 21 ASP A 150 PHE A 151 ALA A 155 HOH A 502
SITE 6 AC1 21 HOH A 574
CRYST1 57.471 67.403 104.625 90.00 90.00 90.00 P 21 21 21 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 0.017400 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014836 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009558 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
