HEADER TRANSFERASE 22-MAR-12 4EAI
TITLE CO-CRYSTAL STRUCTURE OF AN AMPK CORE WITH AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AMPK SUBUNIT ALPHA-1,ACETYL-COA CARBOXYLASE KINASE,ACACA
COMPND 5 KINASE,HYDROXYMETHYLGLUTARYL-COA REDUCTASE KINASE,HMGCR KINASE,TAU-
COMPND 6 PROTEIN KINASE PRKAA1;
COMPND 7 EC: 2.7.11.1,2.7.11.27,2.7.11.31,2.7.11.26;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: CHIMERA PROTEIN OF RESIDUES 405-479 AND RESIDUES 540-
COMPND 10 559 FROM 5'-AMP-ACTIVATED PROTEIN KINASE CATALYTIC SUBUNIT ALPHA-1
COMPND 11 (UNIPROT P54645), LINKED BY LINKER GGGGGG;
COMPND 12 MOL_ID: 2;
COMPND 13 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2;
COMPND 14 CHAIN: B;
COMPND 15 FRAGMENT: UNP RESIDUES 189-272;
COMPND 16 SYNONYM: AMPK SUBUNIT BETA-2;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 3;
COMPND 19 MOLECULE: 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT GAMMA-1;
COMPND 20 CHAIN: C;
COMPND 21 SYNONYM: AMPKG;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: PRKAA1, AMPK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: PRKAB2;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 19 ORGANISM_COMMON: RAT;
SOURCE 20 ORGANISM_TAXID: 10116;
SOURCE 21 GENE: PRKAG1;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS AMPK, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.CHEN,J.WANG,Y.-Y.ZHANG,S.F.YAN,D.NEUMANN,U.SCHLATTNER,Z.-X.WANG,J.-
AUTHOR 2 W.WU
REVDAT 4 08-NOV-23 4EAI 1 REMARK
REVDAT 3 21-JUN-17 4EAI 1 COMPND SOURCE
REVDAT 2 12-MAR-14 4EAI 1 JRNL
REVDAT 1 06-JUN-12 4EAI 0
JRNL AUTH L.CHEN,J.WANG,Y.-Y.ZHANG,S.F.YAN,D.NEUMANN,U.SCHLATTNER,
JRNL AUTH 2 Z.-X.WANG,J.-W.WU
JRNL TITL AMP-ACTIVATED PROTEIN KINASE UNDERGOES NUCLEOTIDE-DEPENDENT
JRNL TITL 2 CONFORMATIONAL CHANGES
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 716 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 22659875
JRNL DOI 10.1038/NSMB.2319
REMARK 2
REMARK 2 RESOLUTION. 2.29 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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) : 2.29
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.060
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 23163
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1172
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 29.5498 - 4.5649 0.94 3020 154 0.1946 0.2498
REMARK 3 2 4.5649 - 3.6254 0.96 2952 152 0.1609 0.1952
REMARK 3 3 3.6254 - 3.1677 0.96 2925 148 0.1870 0.2722
REMARK 3 4 3.1677 - 2.8784 0.94 2813 156 0.1967 0.2597
REMARK 3 5 2.8784 - 2.6722 0.92 2783 157 0.2047 0.2812
REMARK 3 6 2.6722 - 2.5148 0.90 2658 146 0.2106 0.2718
REMARK 3 7 2.5148 - 2.3889 0.85 2567 125 0.2260 0.2763
REMARK 3 8 2.3889 - 2.2849 0.77 2273 134 0.2485 0.3038
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 43.80
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.29
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.35330
REMARK 3 B22 (A**2) : -2.07530
REMARK 3 B33 (A**2) : -7.27800
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 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 : 0.004 3694
REMARK 3 ANGLE : 0.908 5017
REMARK 3 CHIRALITY : 0.055 591
REMARK 3 PLANARITY : 0.004 604
REMARK 3 DIHEDRAL : 17.181 1341
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 394:425)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8809 39.2871 -13.5484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0844 T22: -0.0295
REMARK 3 T33: 0.1458 T12: -0.1653
REMARK 3 T13: -0.1837 T23: -0.1208
REMARK 3 L TENSOR
REMARK 3 L11: 1.7152 L22: 1.1019
REMARK 3 L33: 1.0385 L12: 0.1211
REMARK 3 L13: 0.8511 L23: -0.0870
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0976 S13: 0.1917
REMARK 3 S21: 0.2197 S22: 0.0675 S23: 0.3190
REMARK 3 S31: -0.5542 S32: -0.2712 S33: 0.1366
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 426:445)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6419 28.7851 -18.6338
REMARK 3 T TENSOR
REMARK 3 T11: 0.0260 T22: 0.1197
REMARK 3 T33: 0.4210 T12: -0.0066
REMARK 3 T13: 0.0028 T23: 0.0579
REMARK 3 L TENSOR
REMARK 3 L11: 0.0348 L22: 3.0236
REMARK 3 L33: 1.8196 L12: 0.3104
REMARK 3 L13: -0.1526 L23: -1.9025
REMARK 3 S TENSOR
REMARK 3 S11: 0.3440 S12: -0.0350 S13: 0.4778
REMARK 3 S21: 0.0073 S22: -0.3405 S23: -0.1823
REMARK 3 S31: -0.0201 S32: 0.4830 S33: 0.0404
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 446:472)
REMARK 3 ORIGIN FOR THE GROUP (A): 0.3875 36.4146 -20.9768
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.1304
REMARK 3 T33: 0.2397 T12: -0.0190
REMARK 3 T13: -0.0545 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.9826 L22: 5.4990
REMARK 3 L33: 0.7847 L12: -2.5241
REMARK 3 L13: 0.4143 L23: -0.6139
REMARK 3 S TENSOR
REMARK 3 S11: -0.2084 S12: 0.2776 S13: -0.0620
REMARK 3 S21: 0.4091 S22: -0.0124 S23: 0.1292
REMARK 3 S31: -0.1227 S32: 0.0425 S33: 0.2255
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 473:493)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0457 26.6322 -11.7315
REMARK 3 T TENSOR
REMARK 3 T11: 0.0987 T22: 0.0983
REMARK 3 T33: 0.1607 T12: 0.0199
REMARK 3 T13: -0.0426 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 2.1442 L22: 2.0881
REMARK 3 L33: 0.7819 L12: 2.0985
REMARK 3 L13: 0.3377 L23: 0.1196
REMARK 3 S TENSOR
REMARK 3 S11: -0.0969 S12: 0.0112 S13: -0.3217
REMARK 3 S21: 0.0903 S22: -0.0414 S23: -0.5582
REMARK 3 S31: 0.0501 S32: -0.0243 S33: 0.0578
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 204:210)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5889 44.0105 -27.2138
REMARK 3 T TENSOR
REMARK 3 T11: 0.3328 T22: 0.3539
REMARK 3 T33: 0.5176 T12: -0.0772
REMARK 3 T13: -0.1251 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 4.6463 L22: 3.7223
REMARK 3 L33: 0.5961 L12: 3.6353
REMARK 3 L13: 0.9506 L23: 0.6725
REMARK 3 S TENSOR
REMARK 3 S11: 0.0434 S12: -0.0952 S13: 0.6105
REMARK 3 S21: -0.4926 S22: -0.3426 S23: 0.3659
REMARK 3 S31: 0.0473 S32: 0.0408 S33: 0.3308
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 211:236)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3313 34.7628 -22.6496
REMARK 3 T TENSOR
REMARK 3 T11: 0.2691 T22: 0.1350
REMARK 3 T33: 0.3359 T12: 0.0519
REMARK 3 T13: -0.0729 T23: 0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 2.3307 L22: 2.4631
REMARK 3 L33: 2.5288 L12: 1.2608
REMARK 3 L13: 1.0739 L23: -1.3238
REMARK 3 S TENSOR
REMARK 3 S11: 0.2023 S12: -0.0225 S13: 0.5985
REMARK 3 S21: 0.0785 S22: -0.0582 S23: 0.5171
REMARK 3 S31: 0.4394 S32: 0.2028 S33: -0.1267
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 237:245)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4364 30.5676 -19.0715
REMARK 3 T TENSOR
REMARK 3 T11: 0.0755 T22: 0.1137
REMARK 3 T33: 0.1392 T12: -0.0392
REMARK 3 T13: 0.0202 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.2959 L22: 2.2870
REMARK 3 L33: 3.8055 L12: 0.3945
REMARK 3 L13: 1.0024 L23: 0.5558
REMARK 3 S TENSOR
REMARK 3 S11: -0.1222 S12: 0.0336 S13: -0.0032
REMARK 3 S21: -0.0193 S22: -0.0800 S23: -0.3933
REMARK 3 S31: -0.1551 S32: 0.3898 S33: 0.1550
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 246:251)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8470 30.4925 -2.3433
REMARK 3 T TENSOR
REMARK 3 T11: 0.4897 T22: 0.3192
REMARK 3 T33: 0.3307 T12: 0.0104
REMARK 3 T13: -0.0024 T23: -0.1492
REMARK 3 L TENSOR
REMARK 3 L11: 0.1551 L22: 0.0149
REMARK 3 L33: 0.4975 L12: -0.0478
REMARK 3 L13: 0.2790 L23: -0.0833
REMARK 3 S TENSOR
REMARK 3 S11: 0.2534 S12: -0.0965 S13: 0.2133
REMARK 3 S21: -0.2561 S22: -0.1803 S23: 0.0945
REMARK 3 S31: 0.0537 S32: 0.0199 S33: -0.0815
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 252:271)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1204 21.0839 -19.4253
REMARK 3 T TENSOR
REMARK 3 T11: 0.1300 T22: 0.1507
REMARK 3 T33: 0.0796 T12: -0.0087
REMARK 3 T13: 0.0226 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 0.3653 L22: 0.4518
REMARK 3 L33: 0.2611 L12: 0.0937
REMARK 3 L13: 0.1138 L23: -0.2751
REMARK 3 S TENSOR
REMARK 3 S11: -0.1300 S12: 0.0410 S13: 0.0335
REMARK 3 S21: -0.1216 S22: -0.1427 S23: -0.0216
REMARK 3 S31: -0.0556 S32: 0.1104 S33: 0.1914
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 26:106)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.7825 10.8941 -8.1631
REMARK 3 T TENSOR
REMARK 3 T11: 0.0916 T22: 0.1021
REMARK 3 T33: 0.0769 T12: 0.0360
REMARK 3 T13: -0.0169 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 0.2352 L22: 0.2804
REMARK 3 L33: 0.3507 L12: 0.0676
REMARK 3 L13: 0.1405 L23: -0.2483
REMARK 3 S TENSOR
REMARK 3 S11: -0.0406 S12: -0.0555 S13: -0.0063
REMARK 3 S21: 0.0645 S22: -0.0502 S23: -0.0075
REMARK 3 S31: -0.0515 S32: -0.0614 S33: 0.0488
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 107:126)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8511 11.9455 5.2964
REMARK 3 T TENSOR
REMARK 3 T11: 0.3580 T22: 0.3302
REMARK 3 T33: 0.0575 T12: -0.1126
REMARK 3 T13: -0.0223 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.5643 L22: 1.3998
REMARK 3 L33: 0.3561 L12: -0.5907
REMARK 3 L13: -0.3665 L23: 0.6853
REMARK 3 S TENSOR
REMARK 3 S11: 0.4063 S12: -0.1031 S13: -0.0123
REMARK 3 S21: -0.3879 S22: -0.4247 S23: 0.1210
REMARK 3 S31: -0.0908 S32: -0.5442 S33: 0.0063
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 127:222)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.5743 -1.3887 -16.4731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1876 T22: 0.0751
REMARK 3 T33: 0.0737 T12: 0.0068
REMARK 3 T13: -0.0250 T23: -0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.1896 L22: 0.4455
REMARK 3 L33: 0.5771 L12: 0.6777
REMARK 3 L13: 0.1474 L23: 0.4542
REMARK 3 S TENSOR
REMARK 3 S11: -0.0083 S12: -0.0416 S13: -0.0504
REMARK 3 S21: -0.0093 S22: 0.0365 S23: -0.0920
REMARK 3 S31: 0.3139 S32: -0.0974 S33: -0.0213
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 223:265)
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8492 5.3928 -2.7993
REMARK 3 T TENSOR
REMARK 3 T11: 0.1222 T22: 0.3068
REMARK 3 T33: 0.1336 T12: 0.0595
REMARK 3 T13: -0.0757 T23: -0.1601
REMARK 3 L TENSOR
REMARK 3 L11: 0.4821 L22: 0.6479
REMARK 3 L33: 1.8423 L12: 0.3842
REMARK 3 L13: 0.6517 L23: 0.9234
REMARK 3 S TENSOR
REMARK 3 S11: -0.1876 S12: -0.4113 S13: 0.0215
REMARK 3 S21: -0.0390 S22: -0.2632 S23: 0.0330
REMARK 3 S31: -0.0220 S32: -0.5955 S33: 0.3708
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 266:273)
REMARK 3 ORIGIN FOR THE GROUP (A): -36.7860 12.5655 -12.0587
REMARK 3 T TENSOR
REMARK 3 T11: 1.0736 T22: 0.7381
REMARK 3 T33: 0.5313 T12: -0.0590
REMARK 3 T13: -0.2319 T23: -0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 0.7641 L22: 0.6913
REMARK 3 L33: 1.2161 L12: 0.0173
REMARK 3 L13: 0.0554 L23: 0.1404
REMARK 3 S TENSOR
REMARK 3 S11: 0.2956 S12: 0.2696 S13: -0.0791
REMARK 3 S21: 0.5141 S22: 0.4116 S23: -0.0906
REMARK 3 S31: -0.2051 S32: -0.0691 S33: -0.6328
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 274:324)
REMARK 3 ORIGIN FOR THE GROUP (A): -30.6575 -5.8549 -17.9458
REMARK 3 T TENSOR
REMARK 3 T11: 0.1794 T22: 0.1802
REMARK 3 T33: 0.1154 T12: -0.0707
REMARK 3 T13: -0.0275 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.9858 L22: 1.0253
REMARK 3 L33: 0.3962 L12: 0.5873
REMARK 3 L13: -0.1575 L23: 0.3382
REMARK 3 S TENSOR
REMARK 3 S11: 0.1352 S12: 0.1023 S13: -0.0076
REMARK 3 S21: -0.1245 S22: -0.2102 S23: -0.0126
REMARK 3 S31: 0.1540 S32: -0.1924 S33: 0.0540
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 4EAI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071374.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.26
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99583
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24647
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.285
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.230
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: PDB ENTRY 2V8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.47
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, 16% IPP, 1% 1,4-BUTANEDIOL, PH
REMARK 280 6.26, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298 K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 48.79700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.66700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.79700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.66700
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 389
REMARK 465 PRO A 390
REMARK 465 HIS A 391
REMARK 465 MET A 392
REMARK 465 GLY A 393
REMARK 465 GLN A 494
REMARK 465 MET B 188
REMARK 465 TYR B 189
REMARK 465 GLY B 190
REMARK 465 GLN B 191
REMARK 465 GLU B 192
REMARK 465 MET B 193
REMARK 465 TYR B 194
REMARK 465 ALA B 195
REMARK 465 PHE B 196
REMARK 465 ARG B 197
REMARK 465 SER B 198
REMARK 465 GLU B 199
REMARK 465 GLU B 200
REMARK 465 ARG B 201
REMARK 465 PHE B 202
REMARK 465 LYS B 203
REMARK 465 LYS B 219
REMARK 465 ASP B 220
REMARK 465 THR B 221
REMARK 465 ASN B 222
REMARK 465 ILE B 223
REMARK 465 SER B 224
REMARK 465 CYS B 225
REMARK 465 ASP B 226
REMARK 465 PRO B 227
REMARK 465 ALA B 228
REMARK 465 LEU B 229
REMARK 465 LEU B 230
REMARK 465 PRO B 231
REMARK 465 GLU B 232
REMARK 465 PRO B 233
REMARK 465 ASN B 234
REMARK 465 HIS B 235
REMARK 465 ILE B 272
REMARK 465 MET C 1
REMARK 465 GLU C 2
REMARK 465 SER C 3
REMARK 465 VAL C 4
REMARK 465 ALA C 5
REMARK 465 ALA C 6
REMARK 465 GLU C 7
REMARK 465 SER C 8
REMARK 465 ALA C 9
REMARK 465 PRO C 10
REMARK 465 ALA C 11
REMARK 465 PRO C 12
REMARK 465 GLU C 13
REMARK 465 ASN C 14
REMARK 465 GLU C 15
REMARK 465 HIS C 16
REMARK 465 SER C 17
REMARK 465 GLN C 18
REMARK 465 GLU C 19
REMARK 465 THR C 20
REMARK 465 PRO C 21
REMARK 465 GLU C 22
REMARK 465 SER C 23
REMARK 465 ASN C 24
REMARK 465 SER C 25
REMARK 465 LEU C 121
REMARK 465 GLN C 122
REMARK 465 ASP C 123
REMARK 465 SER C 124
REMARK 465 PHE C 125
REMARK 465 GLU C 251
REMARK 465 LYS C 252
REMARK 465 THR C 253
REMARK 465 TYR C 254
REMARK 465 ASN C 255
REMARK 465 GLY C 325
REMARK 465 GLY C 326
REMARK 465 GLU C 327
REMARK 465 LYS C 328
REMARK 465 LYS C 329
REMARK 465 PRO C 330
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 LEU A 492 -136.57 -66.26
REMARK 500 ASN B 239 -0.98 73.77
REMARK 500 LYS B 260 -130.04 52.29
REMARK 500 GLU C 109 -72.14 -53.86
REMARK 500 ASP C 231 -159.51 -112.57
REMARK 500 LEU C 265 40.43 -90.07
REMARK 500 HIS C 267 25.74 -77.75
REMARK 500 ARG C 268 99.56 -54.40
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 AMP C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AMP C 403
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EAG RELATED DB: PDB
REMARK 900 RELATED ID: 4EAJ RELATED DB: PDB
REMARK 900 RELATED ID: 4EAK RELATED DB: PDB
REMARK 900 RELATED ID: 4EAL RELATED DB: PDB
DBREF 4EAI A 394 468 UNP P54645 AAPK1_RAT 405 479
DBREF 4EAI A 475 494 UNP P54645 AAPK1_RAT 540 559
DBREF 4EAI B 189 272 UNP O43741 AAKB2_HUMAN 189 272
DBREF 4EAI C 1 330 UNP P80385 AAKG1_RAT 1 330
SEQADV 4EAI GLY A 389 UNP P54645 EXPRESSION TAG
SEQADV 4EAI PRO A 390 UNP P54645 EXPRESSION TAG
SEQADV 4EAI HIS A 391 UNP P54645 EXPRESSION TAG
SEQADV 4EAI MET A 392 UNP P54645 EXPRESSION TAG
SEQADV 4EAI GLY A 393 UNP P54645 EXPRESSION TAG
SEQADV 4EAI GLY A 469 UNP P54645 LINKER
SEQADV 4EAI GLY A 470 UNP P54645 LINKER
SEQADV 4EAI GLY A 471 UNP P54645 LINKER
SEQADV 4EAI GLY A 472 UNP P54645 LINKER
SEQADV 4EAI GLY A 473 UNP P54645 LINKER
SEQADV 4EAI GLY A 474 UNP P54645 LINKER
SEQADV 4EAI MET B 188 UNP O43741 EXPRESSION TAG
SEQRES 1 A 106 GLY PRO HIS MET GLY ALA LYS TRP HIS LEU GLY ILE ARG
SEQRES 2 A 106 SER GLN SER ARG PRO ASN ASP ILE MET ALA GLU VAL CYS
SEQRES 3 A 106 ARG ALA ILE LYS GLN LEU ASP TYR GLU TRP LYS VAL VAL
SEQRES 4 A 106 ASN PRO TYR TYR LEU ARG VAL ARG ARG LYS ASN PRO VAL
SEQRES 5 A 106 THR SER THR PHE SER LYS MET SER LEU GLN LEU TYR GLN
SEQRES 6 A 106 VAL ASP SER ARG THR TYR LEU LEU ASP PHE ARG SER ILE
SEQRES 7 A 106 ASP ASP GLY GLY GLY GLY GLY GLY GLY SER HIS THR ILE
SEQRES 8 A 106 GLU PHE PHE GLU MET CYS ALA ASN LEU ILE LYS ILE LEU
SEQRES 9 A 106 ALA GLN
SEQRES 1 B 85 MET TYR GLY GLN GLU MET TYR ALA PHE ARG SER GLU GLU
SEQRES 2 B 85 ARG PHE LYS SER PRO PRO ILE LEU PRO PRO HIS LEU LEU
SEQRES 3 B 85 GLN VAL ILE LEU ASN LYS ASP THR ASN ILE SER CYS ASP
SEQRES 4 B 85 PRO ALA LEU LEU PRO GLU PRO ASN HIS VAL MET LEU ASN
SEQRES 5 B 85 HIS LEU TYR ALA LEU SER ILE LYS ASP SER VAL MET VAL
SEQRES 6 B 85 LEU SER ALA THR HIS ARG TYR LYS LYS LYS TYR VAL THR
SEQRES 7 B 85 THR LEU LEU TYR LYS PRO ILE
SEQRES 1 C 330 MET GLU SER VAL ALA ALA GLU SER ALA PRO ALA PRO GLU
SEQRES 2 C 330 ASN GLU HIS SER GLN GLU THR PRO GLU SER ASN SER SER
SEQRES 3 C 330 VAL TYR THR THR PHE MET LYS SER HIS ARG CYS TYR ASP
SEQRES 4 C 330 LEU ILE PRO THR SER SER LYS LEU VAL VAL PHE ASP THR
SEQRES 5 C 330 SER LEU GLN VAL LYS LYS ALA PHE PHE ALA LEU VAL THR
SEQRES 6 C 330 ASN GLY VAL ARG ALA ALA PRO LEU TRP ASP SER LYS LYS
SEQRES 7 C 330 GLN SER PHE VAL GLY MET LEU THR ILE THR ASP PHE ILE
SEQRES 8 C 330 ASN ILE LEU HIS ARG TYR TYR LYS SER ALA LEU VAL GLN
SEQRES 9 C 330 ILE TYR GLU LEU GLU GLU HIS LYS ILE GLU THR TRP ARG
SEQRES 10 C 330 GLU VAL TYR LEU GLN ASP SER PHE LYS PRO LEU VAL CYS
SEQRES 11 C 330 ILE SER PRO ASN ALA SER LEU PHE ASP ALA VAL SER SER
SEQRES 12 C 330 LEU ILE ARG ASN LYS ILE HIS ARG LEU PRO VAL ILE ASP
SEQRES 13 C 330 PRO GLU SER GLY ASN THR LEU TYR ILE LEU THR HIS LYS
SEQRES 14 C 330 ARG ILE LEU LYS PHE LEU LYS LEU PHE ILE THR GLU PHE
SEQRES 15 C 330 PRO LYS PRO GLU PHE MET SER LYS SER LEU GLU GLU LEU
SEQRES 16 C 330 GLN ILE GLY THR TYR ALA ASN ILE ALA MET VAL ARG THR
SEQRES 17 C 330 THR THR PRO VAL TYR VAL ALA LEU GLY ILE PHE VAL GLN
SEQRES 18 C 330 HIS ARG VAL SER ALA LEU PRO VAL VAL ASP GLU LYS GLY
SEQRES 19 C 330 ARG VAL VAL ASP ILE TYR SER LYS PHE ASP VAL ILE ASN
SEQRES 20 C 330 LEU ALA ALA GLU LYS THR TYR ASN ASN LEU ASP VAL SER
SEQRES 21 C 330 VAL THR LYS ALA LEU GLN HIS ARG SER HIS TYR PHE GLU
SEQRES 22 C 330 GLY VAL LEU LYS CYS TYR LEU HIS GLU THR LEU GLU ALA
SEQRES 23 C 330 ILE ILE ASN ARG LEU VAL GLU ALA GLU VAL HIS ARG LEU
SEQRES 24 C 330 VAL VAL VAL ASP GLU HIS ASP VAL VAL LYS GLY ILE VAL
SEQRES 25 C 330 SER LEU SER ASP ILE LEU GLN ALA LEU VAL LEU THR GLY
SEQRES 26 C 330 GLY GLU LYS LYS PRO
HET AMP C 401 23
HET AMP C 402 23
HET AMP C 403 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 4 AMP 3(C10 H14 N5 O7 P)
FORMUL 7 HOH *102(H2 O)
HELIX 1 1 ARG A 405 ASP A 421 1 17
HELIX 2 2 SER A 476 LEU A 492 1 17
HELIX 3 3 VAL C 27 SER C 34 1 8
HELIX 4 4 ARG C 36 ILE C 41 5 6
HELIX 5 5 GLN C 55 GLY C 67 1 13
HELIX 6 6 ILE C 87 VAL C 103 1 17
HELIX 7 7 LYS C 112 TYR C 120 1 9
HELIX 8 8 SER C 136 LYS C 148 1 13
HELIX 9 9 THR C 167 ILE C 179 1 13
HELIX 10 10 PRO C 185 LYS C 190 5 6
HELIX 11 11 SER C 191 GLN C 196 1 6
HELIX 12 12 PRO C 211 ARG C 223 1 13
HELIX 13 13 PHE C 243 ALA C 250 5 8
HELIX 14 14 SER C 260 LEU C 265 1 6
HELIX 15 15 THR C 283 GLU C 295 1 13
HELIX 16 16 LEU C 314 LEU C 323 1 10
SHEET 1 A 8 VAL B 215 LEU B 217 0
SHEET 2 A 8 LYS A 395 LEU A 398 -1 N TRP A 396 O ILE B 216
SHEET 3 A 8 TYR B 242 LEU B 244 -1 O ALA B 243 N HIS A 397
SHEET 4 A 8 MET B 251 TYR B 259 -1 O SER B 254 N TYR B 242
SHEET 5 A 8 LYS B 262 LYS B 270 -1 O LYS B 270 N MET B 251
SHEET 6 A 8 SER C 44 ASP C 51 1 O VAL C 49 N LEU B 267
SHEET 7 A 8 ALA C 70 TRP C 74 1 O TRP C 74 N PHE C 50
SHEET 8 A 8 PHE C 81 THR C 86 -1 O GLY C 83 N LEU C 73
SHEET 1 B 5 ILE A 400 SER A 402 0
SHEET 2 B 5 TYR A 459 SER A 465 -1 O LEU A 461 N ILE A 400
SHEET 3 B 5 PHE A 444 GLN A 453 -1 N GLN A 450 O ASP A 462
SHEET 4 B 5 TYR A 431 LYS A 437 -1 N LEU A 432 O LEU A 449
SHEET 5 B 5 GLU A 423 ASN A 428 -1 N LYS A 425 O ARG A 433
SHEET 1 C 2 LEU C 152 ILE C 155 0
SHEET 2 C 2 THR C 162 LEU C 166 -1 O LEU C 163 N VAL C 154
SHEET 1 D 3 VAL C 206 ARG C 207 0
SHEET 2 D 3 ALA C 226 VAL C 230 1 O VAL C 230 N VAL C 206
SHEET 3 D 3 VAL C 236 SER C 241 -1 O ASP C 238 N VAL C 229
SHEET 1 E 3 LYS C 277 CYS C 278 0
SHEET 2 E 3 ARG C 298 VAL C 302 1 O VAL C 302 N CYS C 278
SHEET 3 E 3 VAL C 308 SER C 313 -1 O VAL C 312 N LEU C 299
CISPEP 1 PHE C 182 PRO C 183 0 6.19
SITE 1 AC1 15 ARG C 69 LYS C 169 ILE C 239 SER C 241
SITE 2 AC1 15 PHE C 243 ASP C 244 ARG C 268 PHE C 272
SITE 3 AC1 15 GLY C 274 VAL C 275 LEU C 276 VAL C 296
SITE 4 AC1 15 HIS C 297 ARG C 298 HOH C 558
SITE 1 AC2 15 MET C 84 THR C 86 THR C 88 ASP C 89
SITE 2 AC2 15 LYS C 126 PRO C 127 LEU C 128 VAL C 129
SITE 3 AC2 15 ILE C 149 HIS C 150 ARG C 151 PRO C 153
SITE 4 AC2 15 HOH C 508 HOH C 528 HOH C 536
SITE 1 AC3 13 HIS C 150 THR C 199 ILE C 203 ALA C 204
SITE 2 AC3 13 VAL C 224 SER C 225 ALA C 226 HIS C 297
SITE 3 AC3 13 SER C 313 SER C 315 ASP C 316 HOH C 516
SITE 4 AC3 13 HOH C 518
CRYST1 97.594 115.334 48.522 90.00 90.00 90.00 P 21 21 2 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 0.010247 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020609 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
