HEADER TRANSFERASE/TRANSFERASE INHIBITOR 11-JUL-15 5CI7
TITLE STRUCTURE OF ULK1 BOUND TO A SELECTIVE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE ULK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 1-283);
COMPND 5 SYNONYM: AUTOPHAGY-RELATED PROTEIN 1 HOMOLOG,HATG1,UNC-51-LIKE KINASE
COMPND 6 1;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ULK1, KIAA0722;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS INHIBITOR, KINASE, AUTOPHAGY, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.LAZARUS,K.M.SHOKAT
REVDAT 5 27-SEP-23 5CI7 1 REMARK
REVDAT 4 11-DEC-19 5CI7 1 REMARK
REVDAT 3 27-SEP-17 5CI7 1 JRNL REMARK
REVDAT 2 09-SEP-15 5CI7 1 JRNL
REVDAT 1 26-AUG-15 5CI7 0
JRNL AUTH M.B.LAZARUS,K.M.SHOKAT
JRNL TITL DISCOVERY AND STRUCTURE OF A NEW INHIBITOR SCAFFOLD OF THE
JRNL TITL 2 AUTOPHAGY INITIATING KINASE ULK1.
JRNL REF BIOORG.MED.CHEM. V. 23 5483 2015
JRNL REFN ESSN 1464-3391
JRNL PMID 26275681
JRNL DOI 10.1016/J.BMC.2015.07.034
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 3 NUMBER OF REFLECTIONS : 26552
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1375
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 43.8270 - 3.7480 0.87 2509 114 0.1721 0.1944
REMARK 3 2 3.7480 - 2.9751 0.93 2514 150 0.1607 0.2099
REMARK 3 3 2.9751 - 2.5991 0.96 2551 133 0.1652 0.2089
REMARK 3 4 2.5991 - 2.3615 0.97 2541 147 0.1581 0.1991
REMARK 3 5 2.3615 - 2.1922 0.98 2543 163 0.1503 0.1783
REMARK 3 6 2.1922 - 2.0630 0.98 2554 127 0.1489 0.2066
REMARK 3 7 2.0630 - 1.9597 0.98 2550 134 0.1601 0.2152
REMARK 3 8 1.9597 - 1.8743 0.97 2507 156 0.1850 0.2293
REMARK 3 9 1.8743 - 1.8022 0.97 2516 134 0.2236 0.2519
REMARK 3 10 1.8022 - 1.7400 0.92 2392 117 0.2476 0.2562
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.490
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.007 2361
REMARK 3 ANGLE : 1.094 3184
REMARK 3 CHIRALITY : 0.062 343
REMARK 3 PLANARITY : 0.004 408
REMARK 3 DIHEDRAL : 14.316 904
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 3:24)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9525 -49.4154 -6.8656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1645 T22: 0.1970
REMARK 3 T33: 0.1893 T12: -0.0034
REMARK 3 T13: -0.0202 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 2.4331 L22: 3.5659
REMARK 3 L33: 1.6612 L12: -0.8290
REMARK 3 L13: -1.0272 L23: -0.6347
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: -0.4328 S13: -0.2232
REMARK 3 S21: 0.2814 S22: -0.1072 S23: -0.5505
REMARK 3 S31: 0.0864 S32: 0.4202 S33: 0.0374
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 25:49)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3750 -47.1240 -10.0678
REMARK 3 T TENSOR
REMARK 3 T11: 0.1378 T22: 0.1467
REMARK 3 T33: 0.1146 T12: 0.0451
REMARK 3 T13: 0.0253 T23: 0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 2.2278 L22: 4.2659
REMARK 3 L33: 2.0475 L12: 0.8318
REMARK 3 L13: 0.2685 L23: 0.8196
REMARK 3 S TENSOR
REMARK 3 S11: 0.0480 S12: -0.0168 S13: -0.1181
REMARK 3 S21: 0.0857 S22: 0.0041 S23: -0.3356
REMARK 3 S31: 0.3430 S32: 0.3582 S33: -0.1021
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 50:75)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1333 -39.3531 -6.6477
REMARK 3 T TENSOR
REMARK 3 T11: 0.1151 T22: 0.0722
REMARK 3 T33: 0.1205 T12: 0.0000
REMARK 3 T13: 0.0423 T23: 0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 2.0246 L22: 1.6809
REMARK 3 L33: 5.4662 L12: 0.2118
REMARK 3 L13: 0.6271 L23: 0.6587
REMARK 3 S TENSOR
REMARK 3 S11: -0.0365 S12: -0.2958 S13: -0.0233
REMARK 3 S21: 0.1457 S22: -0.1206 S23: 0.0455
REMARK 3 S31: 0.1560 S32: -0.2412 S33: 0.0656
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 76:103)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3058 -43.2292 -11.7028
REMARK 3 T TENSOR
REMARK 3 T11: 0.0975 T22: 0.0950
REMARK 3 T33: 0.1003 T12: 0.0165
REMARK 3 T13: 0.0184 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 1.3869 L22: 1.4016
REMARK 3 L33: 2.3846 L12: 1.3944
REMARK 3 L13: -1.6915 L23: -1.7032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0692 S12: -0.0688 S13: 0.0033
REMARK 3 S21: 0.0774 S22: -0.0560 S23: -0.0365
REMARK 3 S31: -0.0008 S32: 0.1081 S33: -0.0135
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 104:108)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.4152 -26.4624 -27.1174
REMARK 3 T TENSOR
REMARK 3 T11: 0.0795 T22: 0.2413
REMARK 3 T33: 0.1783 T12: 0.0035
REMARK 3 T13: 0.0021 T23: -0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 4.3888 L22: 2.3248
REMARK 3 L33: 5.9719 L12: -1.7713
REMARK 3 L13: -3.0363 L23: -1.2710
REMARK 3 S TENSOR
REMARK 3 S11: 0.2718 S12: 0.4846 S13: 0.4513
REMARK 3 S21: -0.0366 S22: -0.1872 S23: 0.1313
REMARK 3 S31: -0.1140 S32: 0.7837 S33: -0.0932
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN A AND RESID 109:147)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.9832 -31.2366 -22.2328
REMARK 3 T TENSOR
REMARK 3 T11: 0.1043 T22: 0.0433
REMARK 3 T33: 0.1065 T12: -0.0017
REMARK 3 T13: 0.0213 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.4729 L22: 0.5071
REMARK 3 L33: 2.8882 L12: -0.0521
REMARK 3 L13: -1.2057 L23: 0.2075
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: 0.0552 S13: 0.0177
REMARK 3 S21: -0.0849 S22: -0.0107 S23: -0.0275
REMARK 3 S31: 0.0604 S32: -0.0340 S33: -0.0459
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN A AND RESID 148:157)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2383 -42.6005 -33.4828
REMARK 3 T TENSOR
REMARK 3 T11: 0.3250 T22: 0.5668
REMARK 3 T33: 0.3526 T12: -0.0047
REMARK 3 T13: 0.1013 T23: 0.0556
REMARK 3 L TENSOR
REMARK 3 L11: 1.1036 L22: 4.0625
REMARK 3 L33: 0.5695 L12: 0.8806
REMARK 3 L13: 0.0322 L23: 1.4079
REMARK 3 S TENSOR
REMARK 3 S11: 0.4814 S12: 1.3209 S13: 0.3174
REMARK 3 S21: -0.9991 S22: -0.3330 S23: -1.0930
REMARK 3 S31: -0.5215 S32: 1.0956 S33: 0.0721
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN A AND RESID 158:166)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3607 -37.3479 -21.4085
REMARK 3 T TENSOR
REMARK 3 T11: 0.1169 T22: 0.0455
REMARK 3 T33: 0.0966 T12: 0.0085
REMARK 3 T13: 0.0184 T23: 0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 1.8215 L22: 2.7916
REMARK 3 L33: 7.6512 L12: -0.6355
REMARK 3 L13: -0.9614 L23: 2.5453
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: 0.1018 S13: -0.0419
REMARK 3 S21: -0.0796 S22: -0.0867 S23: 0.0530
REMARK 3 S31: 0.1796 S32: 0.1644 S33: 0.1382
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN A AND RESID 167:217)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0976 -22.6573 -11.8413
REMARK 3 T TENSOR
REMARK 3 T11: 0.0965 T22: 0.0790
REMARK 3 T33: 0.0939 T12: -0.0163
REMARK 3 T13: 0.0026 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.3528 L22: 1.0336
REMARK 3 L33: 1.7811 L12: 0.4688
REMARK 3 L13: -1.1103 L23: -0.7639
REMARK 3 S TENSOR
REMARK 3 S11: 0.1096 S12: -0.0950 S13: 0.0862
REMARK 3 S21: 0.0556 S22: -0.1095 S23: -0.0530
REMARK 3 S31: -0.1776 S32: 0.0672 S33: 0.0046
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN A AND RESID 218:223)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2304 -14.2955 -18.3616
REMARK 3 T TENSOR
REMARK 3 T11: 0.1810 T22: 0.4188
REMARK 3 T33: 0.3999 T12: -0.0477
REMARK 3 T13: 0.0587 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 1.5904 L22: 5.9210
REMARK 3 L33: 2.3600 L12: -2.2447
REMARK 3 L13: 1.7893 L23: -3.5028
REMARK 3 S TENSOR
REMARK 3 S11: 0.3296 S12: -0.5158 S13: 1.0110
REMARK 3 S21: -0.2161 S22: 0.1360 S23: -0.8958
REMARK 3 S31: -0.7390 S32: 1.3409 S33: -0.3740
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN A AND RESID 224:237)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3209 -9.0640 -9.2282
REMARK 3 T TENSOR
REMARK 3 T11: 0.3310 T22: 0.2319
REMARK 3 T33: 0.4550 T12: -0.1071
REMARK 3 T13: 0.0362 T23: -0.1220
REMARK 3 L TENSOR
REMARK 3 L11: 1.7111 L22: 4.4895
REMARK 3 L33: 3.0440 L12: -1.6236
REMARK 3 L13: -0.7714 L23: -2.0878
REMARK 3 S TENSOR
REMARK 3 S11: 0.0274 S12: -0.5069 S13: 0.5869
REMARK 3 S21: 0.8770 S22: -0.3725 S23: 0.0490
REMARK 3 S31: -0.4848 S32: -0.0486 S33: -0.0114
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN A AND RESID 238:279)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7265 -17.8301 -26.5268
REMARK 3 T TENSOR
REMARK 3 T11: 0.0866 T22: 0.0831
REMARK 3 T33: 0.1195 T12: 0.0390
REMARK 3 T13: -0.0020 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 3.1036 L22: 2.4485
REMARK 3 L33: 4.9462 L12: 1.0699
REMARK 3 L13: -1.2543 L23: -1.1211
REMARK 3 S TENSOR
REMARK 3 S11: -0.0220 S12: -0.0622 S13: 0.1319
REMARK 3 S21: -0.0553 S22: -0.0116 S23: 0.0917
REMARK 3 S31: 0.0051 S32: -0.2423 S33: 0.0353
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 5CI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211655.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99997
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26564
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 47.280
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: 4WNO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.55 M SODIUM MALONATE PH 7.0, 0.35 M
REMARK 280 SODIUM MALONATE PH 5.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
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 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 33.43000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.30500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.43000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.43000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.30500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.43000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.43000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.30500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.43000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.43000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 58.30500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
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 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 574 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 651 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 GLY A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 280
REMARK 465 SER A 281
REMARK 465 PRO A 282
REMARK 465 SER A 283
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 HOH A 526 O HOH A 631 2.02
REMARK 500 O HOH A 588 O HOH A 656 2.05
REMARK 500 O HOH A 532 O HOH A 604 2.06
REMARK 500 O HOH A 567 O HOH A 644 2.12
REMARK 500 O HOH A 595 O HOH A 636 2.17
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 O HOH A 543 O HOH A 647 8445 2.01
REMARK 500 O HOH A 622 O HOH A 622 2445 2.13
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 THR A 109 164.68 73.76
REMARK 500 ARG A 137 -11.80 79.26
REMARK 500 ASP A 199 -154.22 -139.03
REMARK 500 LEU A 259 45.86 -95.19
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 51W A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 404
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4WNO RELATED DB: PDB
REMARK 900 SAME CONSTRUCT WITH A DIFFERENT INHIBITOR BOUND
DBREF 5CI7 A 1 283 UNP O75385 ULK1_HUMAN 1 283
SEQADV 5CI7 GLY A -3 UNP O75385 EXPRESSION TAG
SEQADV 5CI7 GLY A -2 UNP O75385 EXPRESSION TAG
SEQADV 5CI7 GLY A -1 UNP O75385 EXPRESSION TAG
SEQADV 5CI7 SER A 0 UNP O75385 EXPRESSION TAG
SEQADV 5CI7 ALA A 37 UNP O75385 GLU 37 ENGINEERED MUTATION
SEQADV 5CI7 ALA A 38 UNP O75385 LYS 38 ENGINEERED MUTATION
SEQRES 1 A 287 GLY GLY GLY SER MET GLU PRO GLY ARG GLY GLY THR GLU
SEQRES 2 A 287 THR VAL GLY LYS PHE GLU PHE SER ARG LYS ASP LEU ILE
SEQRES 3 A 287 GLY HIS GLY ALA PHE ALA VAL VAL PHE LYS GLY ARG HIS
SEQRES 4 A 287 ARG ALA ALA HIS ASP LEU GLU VAL ALA VAL LYS CYS ILE
SEQRES 5 A 287 ASN LYS LYS ASN LEU ALA LYS SER GLN THR LEU LEU GLY
SEQRES 6 A 287 LYS GLU ILE LYS ILE LEU LYS GLU LEU LYS HIS GLU ASN
SEQRES 7 A 287 ILE VAL ALA LEU TYR ASP PHE GLN GLU MET ALA ASN SER
SEQRES 8 A 287 VAL TYR LEU VAL MET GLU TYR CYS ASN GLY GLY ASP LEU
SEQRES 9 A 287 ALA ASP TYR LEU HIS ALA MET ARG THR LEU SER GLU ASP
SEQRES 10 A 287 THR ILE ARG LEU PHE LEU GLN GLN ILE ALA GLY ALA MET
SEQRES 11 A 287 ARG LEU LEU HIS SER LYS GLY ILE ILE HIS ARG ASP LEU
SEQRES 12 A 287 LYS PRO GLN ASN ILE LEU LEU SER ASN PRO ALA GLY ARG
SEQRES 13 A 287 ARG ALA ASN PRO ASN SER ILE ARG VAL LYS ILE ALA ASP
SEQRES 14 A 287 PHE GLY PHE ALA ARG TYR LEU GLN SER ASN MET MET ALA
SEQRES 15 A 287 ALA TPO LEU CYS GLY SER PRO MET TYR MET ALA PRO GLU
SEQRES 16 A 287 VAL ILE MET SER GLN HIS TYR ASP GLY LYS ALA ASP LEU
SEQRES 17 A 287 TRP SER ILE GLY THR ILE VAL TYR GLN CYS LEU THR GLY
SEQRES 18 A 287 LYS ALA PRO PHE GLN ALA SER SER PRO GLN ASP LEU ARG
SEQRES 19 A 287 LEU PHE TYR GLU LYS ASN LYS THR LEU VAL PRO THR ILE
SEQRES 20 A 287 PRO ARG GLU THR SER ALA PRO LEU ARG GLN LEU LEU LEU
SEQRES 21 A 287 ALA LEU LEU GLN ARG ASN HIS LYS ASP ARG MET ASP PHE
SEQRES 22 A 287 ASP GLU PHE PHE HIS HIS PRO PHE LEU ASP ALA SER PRO
SEQRES 23 A 287 SER
MODRES 5CI7 TPO A 180 THR MODIFIED RESIDUE
HET TPO A 180 17
HET 51W A 401 51
HET GOL A 402 14
HET GOL A 403 14
HET GOL A 404 14
HETNAM TPO PHOSPHOTHREONINE
HETNAM 51W N-[3-({4-[(3-AMINOPROPYL)AMINO]-5-IODOPYRIMIDIN-2-
HETNAM 2 51W YL}AMINO)PHENYL]PYRROLIDINE-1-CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 51W C18 H24 I N7 O
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *156(H2 O)
HELIX 1 AA1 ASN A 49 LYS A 51 5 3
HELIX 2 AA2 ASN A 52 LYS A 68 1 17
HELIX 3 AA3 ASP A 99 MET A 107 1 9
HELIX 4 AA4 SER A 111 GLY A 133 1 23
HELIX 5 AA5 LYS A 140 GLN A 142 5 3
HELIX 6 AA6 ASN A 155 ILE A 159 5 5
HELIX 7 AA7 ALA A 189 MET A 194 1 6
HELIX 8 AA8 GLY A 200 GLY A 217 1 18
HELIX 9 AA9 SER A 225 ASN A 236 1 12
HELIX 10 AB1 SER A 248 LEU A 259 1 12
HELIX 11 AB2 ASP A 268 HIS A 274 1 7
HELIX 12 AB3 HIS A 275 ASP A 279 5 5
SHEET 1 AA1 6 GLU A 9 VAL A 11 0
SHEET 2 AA1 6 PHE A 14 GLY A 25 -1 O PHE A 16 N GLU A 9
SHEET 3 AA1 6 ALA A 28 HIS A 35 -1 O VAL A 30 N ILE A 22
SHEET 4 AA1 6 GLU A 42 CYS A 47 -1 O CYS A 47 N VAL A 29
SHEET 5 AA1 6 VAL A 88 GLU A 93 -1 O MET A 92 N ALA A 44
SHEET 6 AA1 6 LEU A 78 GLU A 83 -1 N ASP A 80 O VAL A 91
SHEET 1 AA2 2 ILE A 134 ILE A 135 0
SHEET 2 AA2 2 ARG A 170 TYR A 171 -1 O ARG A 170 N ILE A 135
SHEET 1 AA3 2 ILE A 144 SER A 147 0
SHEET 2 AA3 2 ARG A 160 ILE A 163 -1 O LYS A 162 N LEU A 145
LINK C ALA A 179 N TPO A 180 1555 1555 1.33
LINK C TPO A 180 N LEU A 181 1555 1555 1.33
SITE 1 AC1 12 ILE A 22 ALA A 44 MET A 92 GLU A 93
SITE 2 AC1 12 TYR A 94 CYS A 95 GLY A 98 ASP A 99
SITE 3 AC1 12 HIS A 105 GLN A 142 LEU A 145 HOH A 522
SITE 1 AC2 10 GLU A 73 GLU A 93 PRO A 149 ARG A 160
SITE 2 AC2 10 LYS A 162 ALA A 249 GLN A 253 GOL A 403
SITE 3 AC2 10 HOH A 512 HOH A 530
SITE 1 AC3 9 LEU A 41 GLU A 93 TYR A 94 ALA A 249
SITE 2 AC3 9 GOL A 402 HOH A 508 HOH A 511 HOH A 513
SITE 3 AC3 9 HOH A 569
SITE 1 AC4 3 GLY A 23 ASP A 165 HOH A 523
CRYST1 66.860 66.860 116.610 90.00 90.00 90.00 P 42 21 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 0.014957 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014957 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008576 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
