HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-NOV-16 5TWY
TITLE STRUCTURE OF MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE;
COMPND 3 CHAIN: A, B;
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, INHIBITOR, BREAST CANCER, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.-S.SEO,S.DHE-PAGANON
REVDAT 3 06-MAR-24 5TWY 1 REMARK
REVDAT 2 05-JUN-19 5TWY 1 JRNL
REVDAT 1 22-NOV-17 5TWY 0
JRNL AUTH H.T.HUANG,H.S.SEO,T.ZHANG,Y.WANG,B.JIANG,Q.LI,D.L.BUCKLEY,
JRNL AUTH 2 B.NABET,J.M.ROBERTS,J.PAULK,S.DASTJERDI,G.E.WINTER,
JRNL AUTH 3 H.MCLAUCHLAN,J.MORAN,J.E.BRADNER,M.J.ECK,S.DHE-PAGANON,
JRNL AUTH 4 J.J.ZHAO,N.S.GRAY
JRNL TITL MELK IS NOT NECESSARY FOR THE PROLIFERATION OF BASAL-LIKE
JRNL TITL 2 BREAST CANCER CELLS.
JRNL REF ELIFE V. 6 2017
JRNL REFN ESSN 2050-084X
JRNL PMID 28926338
JRNL DOI 10.7554/ELIFE.26693
REMARK 2
REMARK 2 RESOLUTION. 2.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 15765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.289
REMARK 3 R VALUE (WORKING SET) : 0.286
REMARK 3 FREE R VALUE : 0.330
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.830
REMARK 3 FREE R VALUE TEST SET COUNT : 762
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 58.1594 - 4.9754 0.97 3055 172 0.2467 0.2782
REMARK 3 2 4.9754 - 3.9494 0.98 3006 175 0.2604 0.3436
REMARK 3 3 3.9494 - 3.4502 0.97 2992 142 0.3304 0.3810
REMARK 3 4 3.4502 - 3.1348 0.97 2970 141 0.3638 0.3634
REMARK 3 5 3.1348 - 2.9101 0.97 2980 132 0.4211 0.4912
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) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 41.790
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 88.38
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 107.7
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 4845
REMARK 3 ANGLE : 0.873 6593
REMARK 3 CHIRALITY : 0.046 749
REMARK 3 PLANARITY : 0.006 892
REMARK 3 DIHEDRAL : 3.548 2907
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 25.4080 -20.8473 17.8991
REMARK 3 T TENSOR
REMARK 3 T11: 0.3113 T22: 0.3409
REMARK 3 T33: 0.2147 T12: 0.0204
REMARK 3 T13: 0.0529 T23: 0.1209
REMARK 3 L TENSOR
REMARK 3 L11: 1.0375 L22: 1.9526
REMARK 3 L33: 0.2886 L12: -0.8856
REMARK 3 L13: 0.1333 L23: 0.3632
REMARK 3 S TENSOR
REMARK 3 S11: -0.0300 S12: 0.1328 S13: -0.0665
REMARK 3 S21: 0.2398 S22: 0.0334 S23: -0.1513
REMARK 3 S31: 0.0383 S32: 0.2029 S33: 0.0754
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 5TWY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1000224945.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-14
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 : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.11
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15793
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.910
REMARK 200 RESOLUTION RANGE LOW (A) : 58.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.61400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
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 40.01000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 LEU A 47
REMARK 465 GLY A 48
REMARK 465 SER A 49
REMARK 465 ALA A 155
REMARK 465 LYS A 156
REMARK 465 PRO A 157
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 SER A 184
REMARK 465 TYR A 185
REMARK 465 LEU A 186
REMARK 465 LEU A 334
REMARK 465 SER A 335
REMARK 465 SER A 336
REMARK 465 PHE A 337
REMARK 465 SER A 338
REMARK 465 CYS A 339
REMARK 465 GLY A 340
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 PHE B 22
REMARK 465 THR B 46
REMARK 465 LEU B 47
REMARK 465 GLY B 48
REMARK 465 SER B 49
REMARK 465 ALA B 155
REMARK 465 LYS B 156
REMARK 465 PRO B 157
REMARK 465 LYS B 158
REMARK 465 GLY B 159
REMARK 465 ASN B 160
REMARK 465 LYS B 161
REMARK 465 ASP B 162
REMARK 465 TYR B 163
REMARK 465 HIS B 164
REMARK 465 LEU B 165
REMARK 465 GLN B 166
REMARK 465 THR B 167
REMARK 465 CYS B 168
REMARK 465 CYS B 169
REMARK 465 GLY B 170
REMARK 465 SER B 171
REMARK 465 SER B 184
REMARK 465 TYR B 185
REMARK 465 LEU B 186
REMARK 465 ARG B 333
REMARK 465 LEU B 334
REMARK 465 SER B 335
REMARK 465 SER B 336
REMARK 465 PHE B 337
REMARK 465 SER B 338
REMARK 465 CYS B 339
REMARK 465 GLY B 340
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 2 CG CD CE NZ
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 ASP A 5 CG OD1 OD2
REMARK 470 LYS A 9 CG CD CE NZ
REMARK 470 PHE A 22 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 26 CG CD CE NZ
REMARK 470 LEU A 76 CG CD1 CD2
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 THR A 78 OG1 CG2
REMARK 470 ASN A 80 CG OD1 ND2
REMARK 470 LYS A 81 CG CD CE NZ
REMARK 470 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 106 CG CD OE1 OE2
REMARK 470 GLU A 107 CG CD OE1 OE2
REMARK 470 GLU A 108 CG CD OE1 OE2
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 134 CG CD CE NZ
REMARK 470 GLU A 136 CG CD OE1 OE2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 ASP A 150 CG OD1 OD2
REMARK 470 LEU A 153 CG CD1 CD2
REMARK 470 SER A 171 OG
REMARK 470 LEU A 179 CG CD1 CD2
REMARK 470 ILE A 180 CG1 CG2 CD1
REMARK 470 GLN A 181 CG CD OE1 NE2
REMARK 470 LYS A 183 CG CD CE NZ
REMARK 470 ASP A 211 CG OD1 OD2
REMARK 470 ASN A 213 CG OD1 ND2
REMARK 470 VAL A 214 CG1 CG2
REMARK 470 MET A 215 CG SD CE
REMARK 470 TYR A 218 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 ARG A 223 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 225 CG CD CE NZ
REMARK 470 ASP A 247 CG OD1 OD2
REMARK 470 LYS A 250 CG CD CE NZ
REMARK 470 GLN A 265 CG CD OE1 NE2
REMARK 470 ASN A 297 CG OD1 ND2
REMARK 470 GLN A 299 CG CD OE1 NE2
REMARK 470 LYS B 2 CG CD CE NZ
REMARK 470 ASP B 3 CG OD1 OD2
REMARK 470 TYR B 4 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 7 CG CD1 CD2
REMARK 470 LEU B 8 CG CD1 CD2
REMARK 470 LYS B 9 CG CD CE NZ
REMARK 470 TYR B 11 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 12 CG CD OE1 OE2
REMARK 470 LYS B 26 CG CD CE NZ
REMARK 470 LEU B 27 CG CD1 CD2
REMARK 470 ILE B 31 CG1 CG2 CD1
REMARK 470 LEU B 32 CG CD1 CD2
REMARK 470 GLU B 35 CG CD OE1 OE2
REMARK 470 MET B 36 CG SD CE
REMARK 470 ILE B 39 CG1 CG2 CD1
REMARK 470 LYS B 40 CG CD CE NZ
REMARK 470 ILE B 41 CG1 CG2 CD1
REMARK 470 MET B 42 CG SD CE
REMARK 470 LYS B 44 CG CD CE NZ
REMARK 470 ASN B 45 CG OD1 ND2
REMARK 470 ASP B 50 CG OD1 OD2
REMARK 470 LEU B 51 CG CD1 CD2
REMARK 470 ARG B 53 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 54 CG1 CG2 CD1
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 GLU B 57 CG CD OE1 OE2
REMARK 470 ILE B 58 CG1 CG2 CD1
REMARK 470 GLU B 59 CG CD OE1 OE2
REMARK 470 LEU B 61 CG CD1 CD2
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 ASN B 63 CG OD1 ND2
REMARK 470 LEU B 64 CG CD1 CD2
REMARK 470 HIS B 74 CG ND1 CD2 CE1 NE2
REMARK 470 VAL B 75 CG1 CG2
REMARK 470 LEU B 76 CG CD1 CD2
REMARK 470 GLU B 77 CG CD OE1 OE2
REMARK 470 THR B 78 OG1 CG2
REMARK 470 ASN B 80 CG OD1 ND2
REMARK 470 LYS B 81 CG CD CE NZ
REMARK 470 ILE B 82 CG1 CG2 CD1
REMARK 470 PHE B 83 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET B 84 CG SD CE
REMARK 470 TYR B 88 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 94 CG CD1 CD2
REMARK 470 ASP B 96 CG OD1 OD2
REMARK 470 SER B 100 OG
REMARK 470 ASP B 102 CG OD1 OD2
REMARK 470 GLU B 106 CG CD OE1 OE2
REMARK 470 GLU B 107 CG CD OE1 OE2
REMARK 470 GLU B 108 CG CD OE1 OE2
REMARK 470 ARG B 131 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 136 CG CD OE1 OE2
REMARK 470 LEU B 139 CG CD1 CD2
REMARK 470 GLU B 142 CG CD OE1 OE2
REMARK 470 TYR B 143 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS B 144 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 PHE B 151 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL B 214 CG1 CG2
REMARK 470 TYR B 218 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 219 CG CD CE NZ
REMARK 470 LYS B 225 CG CD CE NZ
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 LYS B 276 CG CD CE NZ
REMARK 470 ASN B 277 CG OD1 ND2
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 178 NH2 ARG A 251 2.17
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 TYR A 4 36.84 -80.04
REMARK 500 HIS A 14 -146.71 -136.39
REMARK 500 ALA A 60 -72.77 -52.86
REMARK 500 GLN A 67 16.05 -66.63
REMARK 500 TYR A 73 -122.52 -102.73
REMARK 500 ASP A 102 -113.12 54.28
REMARK 500 ARG A 131 -22.88 67.57
REMARK 500 CYS A 204 -143.95 -90.88
REMARK 500 PRO A 229 -171.44 -62.55
REMARK 500 LEU A 244 43.47 -93.43
REMARK 500 GLN A 265 -71.33 -57.85
REMARK 500 ASP A 266 -67.55 -99.70
REMARK 500 TYR A 267 79.58 -47.74
REMARK 500 ASN A 268 76.99 -109.65
REMARK 500 TYR A 269 146.60 -179.50
REMARK 500 ASP A 311 -159.18 -97.34
REMARK 500 LEU A 332 -133.60 -98.77
REMARK 500 SER B 1 99.86 -67.18
REMARK 500 HIS B 14 -140.38 -131.94
REMARK 500 ILE B 31 -76.90 -55.71
REMARK 500 ASP B 43 124.53 85.35
REMARK 500 CYS B 70 109.43 -51.77
REMARK 500 PHE B 95 -72.82 -44.89
REMARK 500 ASP B 102 -57.26 61.87
REMARK 500 ARG B 131 -22.08 63.75
REMARK 500 ASP B 150 61.97 60.77
REMARK 500 PHE B 151 58.70 -105.80
REMARK 500 LEU B 202 -70.05 -54.60
REMARK 500 LEU B 244 56.26 -94.76
REMARK 500 ASN B 268 45.63 -160.70
REMARK 500 TYR B 310 39.66 73.12
REMARK 500 ASP B 311 -140.02 -80.89
REMARK 500 VAL B 330 34.01 -80.42
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 7LY A 4000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7LY B 4000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5TVT RELATED DB: PDB
REMARK 900 RELATED ID: 5TWL RELATED DB: PDB
REMARK 900 RELATED ID: 5TWU RELATED DB: PDB
REMARK 900 RELATED ID: 5TWZ RELATED DB: PDB
DBREF 5TWY A 2 340 UNP Q14680 MELK_HUMAN 2 340
DBREF 5TWY B 2 340 UNP Q14680 MELK_HUMAN 2 340
SEQADV 5TWY GLY A 0 UNP Q14680 EXPRESSION TAG
SEQADV 5TWY SER A 1 UNP Q14680 EXPRESSION TAG
SEQADV 5TWY GLY B 0 UNP Q14680 EXPRESSION TAG
SEQADV 5TWY SER B 1 UNP Q14680 EXPRESSION TAG
SEQRES 1 A 341 GLY SER LYS ASP TYR ASP GLU LEU LEU LYS TYR TYR GLU
SEQRES 2 A 341 LEU HIS GLU THR ILE GLY THR GLY GLY PHE ALA LYS VAL
SEQRES 3 A 341 LYS LEU ALA CYS HIS ILE LEU THR GLY GLU MET VAL ALA
SEQRES 4 A 341 ILE LYS ILE MET ASP LYS ASN THR LEU GLY SER ASP LEU
SEQRES 5 A 341 PRO ARG ILE LYS THR GLU ILE GLU ALA LEU LYS ASN LEU
SEQRES 6 A 341 ARG HIS GLN HIS ILE CYS GLN LEU TYR HIS VAL LEU GLU
SEQRES 7 A 341 THR ALA ASN LYS ILE PHE MET VAL LEU GLU TYR CYS PRO
SEQRES 8 A 341 GLY GLY GLU LEU PHE ASP TYR ILE ILE SER GLN ASP ARG
SEQRES 9 A 341 LEU SER GLU GLU GLU THR ARG VAL VAL PHE ARG GLN ILE
SEQRES 10 A 341 VAL SER ALA VAL ALA TYR VAL HIS SER GLN GLY TYR ALA
SEQRES 11 A 341 HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU PHE ASP GLU
SEQRES 12 A 341 TYR HIS LYS LEU LYS LEU ILE ASP PHE GLY LEU CYS ALA
SEQRES 13 A 341 LYS PRO LYS GLY ASN LYS ASP TYR HIS LEU GLN THR CYS
SEQRES 14 A 341 CYS GLY SER LEU ALA TYR ALA ALA PRO GLU LEU ILE GLN
SEQRES 15 A 341 GLY LYS SER TYR LEU GLY SER GLU ALA ASP VAL TRP SER
SEQRES 16 A 341 MET GLY ILE LEU LEU TYR VAL LEU MET CYS GLY PHE LEU
SEQRES 17 A 341 PRO PHE ASP ASP ASP ASN VAL MET ALA LEU TYR LYS LYS
SEQRES 18 A 341 ILE MET ARG GLY LYS TYR ASP VAL PRO LYS TRP LEU SER
SEQRES 19 A 341 PRO SER SER ILE LEU LEU LEU GLN GLN MET LEU GLN VAL
SEQRES 20 A 341 ASP PRO LYS LYS ARG ILE SER MET LYS ASN LEU LEU ASN
SEQRES 21 A 341 HIS PRO TRP ILE MET GLN ASP TYR ASN TYR PRO VAL GLU
SEQRES 22 A 341 TRP GLN SER LYS ASN PRO PHE ILE HIS LEU ASP ASP ASP
SEQRES 23 A 341 CYS VAL THR GLU LEU SER VAL HIS HIS ARG ASN ASN ARG
SEQRES 24 A 341 GLN THR MET GLU ASP LEU ILE SER LEU TRP GLN TYR ASP
SEQRES 25 A 341 HIS LEU THR ALA THR TYR LEU LEU LEU LEU ALA LYS LYS
SEQRES 26 A 341 ALA ARG GLY LYS PRO VAL ARG LEU ARG LEU SER SER PHE
SEQRES 27 A 341 SER CYS GLY
SEQRES 1 B 341 GLY SER LYS ASP TYR ASP GLU LEU LEU LYS TYR TYR GLU
SEQRES 2 B 341 LEU HIS GLU THR ILE GLY THR GLY GLY PHE ALA LYS VAL
SEQRES 3 B 341 LYS LEU ALA CYS HIS ILE LEU THR GLY GLU MET VAL ALA
SEQRES 4 B 341 ILE LYS ILE MET ASP LYS ASN THR LEU GLY SER ASP LEU
SEQRES 5 B 341 PRO ARG ILE LYS THR GLU ILE GLU ALA LEU LYS ASN LEU
SEQRES 6 B 341 ARG HIS GLN HIS ILE CYS GLN LEU TYR HIS VAL LEU GLU
SEQRES 7 B 341 THR ALA ASN LYS ILE PHE MET VAL LEU GLU TYR CYS PRO
SEQRES 8 B 341 GLY GLY GLU LEU PHE ASP TYR ILE ILE SER GLN ASP ARG
SEQRES 9 B 341 LEU SER GLU GLU GLU THR ARG VAL VAL PHE ARG GLN ILE
SEQRES 10 B 341 VAL SER ALA VAL ALA TYR VAL HIS SER GLN GLY TYR ALA
SEQRES 11 B 341 HIS ARG ASP LEU LYS PRO GLU ASN LEU LEU PHE ASP GLU
SEQRES 12 B 341 TYR HIS LYS LEU LYS LEU ILE ASP PHE GLY LEU CYS ALA
SEQRES 13 B 341 LYS PRO LYS GLY ASN LYS ASP TYR HIS LEU GLN THR CYS
SEQRES 14 B 341 CYS GLY SER LEU ALA TYR ALA ALA PRO GLU LEU ILE GLN
SEQRES 15 B 341 GLY LYS SER TYR LEU GLY SER GLU ALA ASP VAL TRP SER
SEQRES 16 B 341 MET GLY ILE LEU LEU TYR VAL LEU MET CYS GLY PHE LEU
SEQRES 17 B 341 PRO PHE ASP ASP ASP ASN VAL MET ALA LEU TYR LYS LYS
SEQRES 18 B 341 ILE MET ARG GLY LYS TYR ASP VAL PRO LYS TRP LEU SER
SEQRES 19 B 341 PRO SER SER ILE LEU LEU LEU GLN GLN MET LEU GLN VAL
SEQRES 20 B 341 ASP PRO LYS LYS ARG ILE SER MET LYS ASN LEU LEU ASN
SEQRES 21 B 341 HIS PRO TRP ILE MET GLN ASP TYR ASN TYR PRO VAL GLU
SEQRES 22 B 341 TRP GLN SER LYS ASN PRO PHE ILE HIS LEU ASP ASP ASP
SEQRES 23 B 341 CYS VAL THR GLU LEU SER VAL HIS HIS ARG ASN ASN ARG
SEQRES 24 B 341 GLN THR MET GLU ASP LEU ILE SER LEU TRP GLN TYR ASP
SEQRES 25 B 341 HIS LEU THR ALA THR TYR LEU LEU LEU LEU ALA LYS LYS
SEQRES 26 B 341 ALA ARG GLY LYS PRO VAL ARG LEU ARG LEU SER SER PHE
SEQRES 27 B 341 SER CYS GLY
HET 7LY A4000 33
HET 7LY B4000 33
HETNAM 7LY 2-(BENZYLOXY)-4-(1H-PYRAZOL-4-YL)-N-(2,3,4,5-
HETNAM 2 7LY TETRAHYDRO-1H-3-BENZAZEPIN-7-YL)BENZAMIDE
FORMUL 3 7LY 2(C27 H26 N4 O2)
HELIX 1 AA1 TYR A 4 TYR A 10 1 7
HELIX 2 AA2 LEU A 51 LEU A 64 1 14
HELIX 3 AA3 LEU A 94 GLN A 101 1 8
HELIX 4 AA4 SER A 105 GLN A 126 1 22
HELIX 5 AA5 ALA A 176 GLN A 181 1 6
HELIX 6 AA6 SER A 188 CYS A 204 1 17
HELIX 7 AA7 ASN A 213 GLY A 224 1 12
HELIX 8 AA8 SER A 233 LEU A 244 1 12
HELIX 9 AA9 SER A 253 ASN A 259 1 7
HELIX 10 AB1 ASP A 283 ARG A 295 1 13
HELIX 11 AB2 ASN A 297 SER A 306 1 10
HELIX 12 AB3 ASP A 311 ARG A 326 1 16
HELIX 13 AB4 GLU B 6 TYR B 10 1 5
HELIX 14 AB5 PRO B 52 LEU B 64 1 13
HELIX 15 AB6 LEU B 94 ASP B 102 1 9
HELIX 16 AB7 SER B 105 GLY B 127 1 23
HELIX 17 AB8 SER B 188 GLY B 205 1 18
HELIX 18 AB9 ASN B 213 GLY B 224 1 12
HELIX 19 AC1 SER B 233 LEU B 244 1 12
HELIX 20 AC2 SER B 253 ASN B 259 1 7
HELIX 21 AC3 ASP B 283 ARG B 295 1 13
HELIX 22 AC4 ASN B 297 SER B 306 1 10
HELIX 23 AC5 ASP B 311 ARG B 326 1 16
SHEET 1 AA1 5 TYR A 11 ILE A 17 0
SHEET 2 AA1 5 LYS A 24 HIS A 30 -1 O VAL A 25 N ILE A 17
SHEET 3 AA1 5 GLU A 35 ASP A 43 -1 O VAL A 37 N ALA A 28
SHEET 4 AA1 5 LYS A 81 LEU A 86 -1 O LEU A 86 N ALA A 38
SHEET 5 AA1 5 LEU A 72 GLU A 77 -1 N LEU A 76 O PHE A 83
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
SHEET 1 AA3 5 TYR B 11 ILE B 17 0
SHEET 2 AA3 5 LYS B 24 HIS B 30 -1 O VAL B 25 N ILE B 17
SHEET 3 AA3 5 MET B 36 ILE B 41 -1 O VAL B 37 N ALA B 28
SHEET 4 AA3 5 ILE B 82 LEU B 86 -1 O MET B 84 N LYS B 40
SHEET 5 AA3 5 LEU B 72 GLU B 77 -1 N TYR B 73 O VAL B 85
SHEET 1 AA4 3 GLY B 92 GLU B 93 0
SHEET 2 AA4 3 LEU B 138 PHE B 140 -1 O PHE B 140 N GLY B 92
SHEET 3 AA4 3 LEU B 146 LEU B 148 -1 O LYS B 147 N LEU B 139
SITE 1 AC1 8 VAL A 25 LEU A 27 ALA A 38 LEU A 86
SITE 2 AC1 8 GLU A 87 CYS A 89 PRO A 90 ILE A 149
SITE 1 AC2 5 ALA B 38 GLU B 87 CYS B 89 PRO B 90
SITE 2 AC2 5 ILE B 149
CRYST1 61.860 80.020 79.800 90.00 109.95 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 0.016166 0.000000 0.005868 0.00000
SCALE2 0.000000 0.012497 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013331 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
