HEADER TRANSFERASE 12-SEP-17 6EGW
TITLE CRYSTAL STRUCTURE OF THE PROTEIN-KINASE A CATALYTIC SUBUNIT FROM
TITLE 2 CRITECULUS GRISEUS IN COMPLEX WITH COMPOUNDS RKP017 AND RKP117
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES;
COMPND 9 OTHER_DETAILS: PKI 5-22 WITH S9RBS MUTATION.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 3 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 4 ORGANISM_TAXID: 10029;
SOURCE 5 ORGAN: OVARY;
SOURCE 6 TISSUE: OVARY;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: CRICETULUS GRISEUS;
SOURCE 12 ORGANISM_COMMON: CHINESE HAMSTER;
SOURCE 13 ORGANISM_TAXID: 10029
KEYWDS COMPLEX, PEPTIDIC LIGAND, RIBOSE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.M.MUELLER,A.HEINE,G.KLEBE
REVDAT 3 29-JUL-20 6EGW 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 15-MAY-19 6EGW 1 COMPND JRNL
REVDAT 1 10-OCT-18 6EGW 0
JRNL AUTH J.M.MUELLER,R.KIRSCHNER,A.GEYER,G.KLEBE
JRNL TITL CONCEPTIONAL DESIGN OF SELF-ASSEMBLING BISUBSTRATE-LIKE
JRNL TITL 2 INHIBITORS OF PROTEIN KINASE A RESULTING IN A BORONIC ACID
JRNL TITL 3 GLUTAMATE LINKAGE
JRNL REF ACS OMEGA 2019
JRNL REFN ESSN 2470-1343
JRNL DOI 10.1021/ACSOMEGA.8B02364
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 38853
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.172
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1942
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 41.6290 - 4.1833 0.97 2797 148 0.1696 0.1677
REMARK 3 2 4.1833 - 3.3208 1.00 2737 144 0.1564 0.1856
REMARK 3 3 3.3208 - 2.9012 0.96 2617 137 0.1774 0.2038
REMARK 3 4 2.9012 - 2.6360 1.00 2689 142 0.1842 0.1865
REMARK 3 5 2.6360 - 2.4471 0.99 2670 140 0.1676 0.2178
REMARK 3 6 2.4471 - 2.3028 0.99 2666 141 0.1622 0.2000
REMARK 3 7 2.3028 - 2.1875 1.00 2651 139 0.1629 0.2468
REMARK 3 8 2.1875 - 2.0923 0.94 2513 133 0.1675 0.2047
REMARK 3 9 2.0923 - 2.0117 0.99 2617 137 0.1781 0.2047
REMARK 3 10 2.0117 - 1.9423 0.99 2640 139 0.1749 0.2230
REMARK 3 11 1.9423 - 1.8816 0.99 2642 139 0.1739 0.2757
REMARK 3 12 1.8816 - 1.8278 0.98 2622 138 0.1837 0.2271
REMARK 3 13 1.8278 - 1.7797 0.99 2590 136 0.1982 0.2548
REMARK 3 14 1.7797 - 1.7363 0.93 2460 129 0.2393 0.3078
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) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.850
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 : 0.010 2968
REMARK 3 ANGLE : 1.013 4035
REMARK 3 CHIRALITY : 0.056 429
REMARK 3 PLANARITY : 0.007 538
REMARK 3 DIHEDRAL : 17.697 1761
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 13 THROUGH 31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.4889 31.3732 14.6521
REMARK 3 T TENSOR
REMARK 3 T11: 0.1635 T22: 0.1861
REMARK 3 T33: 0.2182 T12: -0.0259
REMARK 3 T13: -0.0360 T23: 0.0265
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0830
REMARK 3 L33: 0.0493 L12: -0.0361
REMARK 3 L13: -0.0248 L23: 0.0673
REMARK 3 S TENSOR
REMARK 3 S11: -0.1194 S12: 0.0865 S13: 0.1113
REMARK 3 S21: -0.0372 S22: -0.0030 S23: -0.2803
REMARK 3 S31: -0.0745 S32: 0.0769 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 32 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.6201 15.3633 -3.8543
REMARK 3 T TENSOR
REMARK 3 T11: 0.1917 T22: 0.2051
REMARK 3 T33: 0.1607 T12: 0.0080
REMARK 3 T13: 0.0214 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.1783 L22: 0.0964
REMARK 3 L33: 0.0601 L12: -0.1310
REMARK 3 L13: -0.0084 L23: 0.0006
REMARK 3 S TENSOR
REMARK 3 S11: -0.0121 S12: 0.1027 S13: 0.0092
REMARK 3 S21: 0.0036 S22: 0.0637 S23: 0.1089
REMARK 3 S31: 0.0032 S32: -0.0254 S33: 0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8425 13.8288 -2.4791
REMARK 3 T TENSOR
REMARK 3 T11: 0.1444 T22: 0.1854
REMARK 3 T33: 0.1800 T12: 0.0168
REMARK 3 T13: -0.0142 T23: -0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 0.0608 L22: 0.1491
REMARK 3 L33: 0.0795 L12: 0.0436
REMARK 3 L13: 0.0722 L23: 0.0714
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0444 S13: 0.0162
REMARK 3 S21: -0.1101 S22: 0.0033 S23: -0.0409
REMARK 3 S31: 0.0792 S32: 0.0263 S33: -0.0053
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 140 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3287 15.8454 9.0226
REMARK 3 T TENSOR
REMARK 3 T11: 0.1186 T22: 0.1353
REMARK 3 T33: 0.1311 T12: 0.0115
REMARK 3 T13: -0.0089 T23: -0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.0999 L22: 0.0082
REMARK 3 L33: 0.3826 L12: 0.0128
REMARK 3 L13: 0.0150 L23: -0.0625
REMARK 3 S TENSOR
REMARK 3 S11: 0.0072 S12: 0.0673 S13: -0.0444
REMARK 3 S21: -0.0110 S22: -0.0243 S23: 0.0131
REMARK 3 S31: 0.0372 S32: 0.0909 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 141 THROUGH 179 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1549 16.2931 20.6061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1224 T22: 0.1140
REMARK 3 T33: 0.1157 T12: 0.0065
REMARK 3 T13: -0.0012 T23: 0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 0.2522 L22: 0.0881
REMARK 3 L33: 0.1041 L12: 0.1422
REMARK 3 L13: -0.0369 L23: -0.0432
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: 0.0325 S13: -0.0754
REMARK 3 S21: 0.0222 S22: -0.0707 S23: -0.0062
REMARK 3 S31: 0.0506 S32: 0.0247 S33: -0.0100
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 180 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2068 26.3839 20.5733
REMARK 3 T TENSOR
REMARK 3 T11: 0.1453 T22: 0.1001
REMARK 3 T33: 0.1393 T12: 0.0159
REMARK 3 T13: 0.0079 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.1765 L22: 0.2208
REMARK 3 L33: 0.1548 L12: 0.1398
REMARK 3 L13: 0.0851 L23: -0.0599
REMARK 3 S TENSOR
REMARK 3 S11: -0.0030 S12: 0.0055 S13: 0.0523
REMARK 3 S21: 0.0675 S22: -0.0064 S23: -0.0115
REMARK 3 S31: -0.0755 S32: 0.0395 S33: -0.0302
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 217 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0701 15.6049 27.6022
REMARK 3 T TENSOR
REMARK 3 T11: 0.1092 T22: 0.0896
REMARK 3 T33: 0.2015 T12: -0.0022
REMARK 3 T13: 0.0364 T23: -0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 0.3573 L22: 0.0908
REMARK 3 L33: 0.2913 L12: 0.1088
REMARK 3 L13: -0.1891 L23: -0.1593
REMARK 3 S TENSOR
REMARK 3 S11: 0.1405 S12: -0.1633 S13: 0.0311
REMARK 3 S21: 0.2568 S22: -0.1208 S23: 0.3861
REMARK 3 S31: -0.0626 S32: -0.0080 S33: 0.0060
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 272 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6181 12.1808 38.2932
REMARK 3 T TENSOR
REMARK 3 T11: 0.2393 T22: 0.1698
REMARK 3 T33: 0.1015 T12: 0.0006
REMARK 3 T13: 0.0421 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.1246 L22: 0.9239
REMARK 3 L33: 0.0956 L12: 0.0716
REMARK 3 L13: -0.0006 L23: 0.2850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0658 S12: -0.2199 S13: 0.0086
REMARK 3 S21: 0.4100 S22: -0.0399 S23: -0.0317
REMARK 3 S31: -0.0238 S32: -0.0724 S33: 0.0449
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 273 THROUGH 316 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4675 17.3437 30.6366
REMARK 3 T TENSOR
REMARK 3 T11: 0.1227 T22: 0.1553
REMARK 3 T33: 0.1444 T12: -0.0279
REMARK 3 T13: -0.0130 T23: 0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.3251 L22: 0.3046
REMARK 3 L33: 0.6200 L12: 0.0548
REMARK 3 L13: 0.2358 L23: -0.2456
REMARK 3 S TENSOR
REMARK 3 S11: -0.0423 S12: -0.2147 S13: 0.0124
REMARK 3 S21: 0.2287 S22: -0.0508 S23: -0.0447
REMARK 3 S31: 0.0065 S32: 0.1700 S33: -0.0548
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 317 THROUGH 350 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.9740 13.7508 -2.5222
REMARK 3 T TENSOR
REMARK 3 T11: 0.2024 T22: 0.1677
REMARK 3 T33: 0.1445 T12: -0.0037
REMARK 3 T13: -0.0360 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 0.1469 L22: 0.2102
REMARK 3 L33: 0.3139 L12: 0.1058
REMARK 3 L13: -0.0867 L23: 0.1406
REMARK 3 S TENSOR
REMARK 3 S11: -0.0116 S12: 0.0752 S13: -0.0529
REMARK 3 S21: 0.0698 S22: 0.0609 S23: 0.2166
REMARK 3 S31: 0.0897 S32: -0.1244 S33: 0.0219
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1476 2.9708 28.6672
REMARK 3 T TENSOR
REMARK 3 T11: 0.1459 T22: 0.1629
REMARK 3 T33: 0.1787 T12: -0.0112
REMARK 3 T13: 0.0422 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.0173 L22: 0.0115
REMARK 3 L33: 0.0107 L12: 0.0134
REMARK 3 L13: -0.0057 L23: -0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.1800 S12: -0.0325 S13: 0.0920
REMARK 3 S21: 0.0628 S22: -0.0002 S23: 0.1359
REMARK 3 S31: -0.1241 S32: 0.0459 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 17 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6113 11.5277 17.3231
REMARK 3 T TENSOR
REMARK 3 T11: 0.1418 T22: 0.1214
REMARK 3 T33: 0.2150 T12: -0.0095
REMARK 3 T13: -0.0222 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 0.0031 L22: 0.0153
REMARK 3 L33: 0.0027 L12: 0.0005
REMARK 3 L13: -0.0024 L23: 0.0055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0284 S13: -0.0270
REMARK 3 S21: -0.0249 S22: 0.0483 S23: 0.1196
REMARK 3 S31: 0.1647 S32: -0.0061 S33: 0.0001
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 6EGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006609.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9184
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38857
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 41.617
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 5.570
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.66
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.760
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 (%): 47.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES-BIS-TRIS, 75 MM LITHIUM
REMARK 280 CHLORIDE, 1 MM DTT, 0.1 MM SODIUM EDTA, 0.25 MM MEGA 8, 0.7 MM
REMARK 280 PEPTIDIC LIGAND, 5 MM RKP117, 18% V/V METHANOL/WATER IN
REMARK 280 RESERVOIR, PH 6.9, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277.15K
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 34.26950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.09000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.06700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.09000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.26950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.06700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15630 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLY A -2
REMARK 465 HIS A -1
REMARK 465 MET A 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 GLY A 9
REMARK 465 SEP A 10
REMARK 465 GLU A 11
REMARK 465 GLN A 12
REMARK 465 SER A 252
REMARK 465 PRO A 321
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 GLU A 13 CG CD OE1 OE2
REMARK 470 SER A 14 OG
REMARK 470 VAL A 15 CG1 CG2
REMARK 470 LYS A 16 CG CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 PHE A 18 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 LYS A 23 CE NZ
REMARK 470 GLU A 24 CD OE1 OE2
REMARK 470 LYS A 28 CG CD CE NZ
REMARK 470 LYS A 61 NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 78 CE NZ
REMARK 470 LYS A 81 CD CE NZ
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 ILE A 135 CD1
REMARK 470 GLN A 176 CG CD OE1 NE2
REMARK 470 GLN A 177 CG CD OE1 NE2
REMARK 470 LYS A 192 CE NZ
REMARK 470 SER A 212 OG
REMARK 470 LYS A 217 CD CE NZ
REMARK 470 ASP A 241 CG OD1 OD2
REMARK 470 ILE A 244 CG1 CG2 CD1
REMARK 470 GLN A 245 CG CD OE1 NE2
REMARK 470 LYS A 249 NZ
REMARK 470 VAL A 251 CG1 CG2
REMARK 470 VAL A 255 CG1 CG2
REMARK 470 ARG A 256 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 279 CE NZ
REMARK 470 LYS A 285 CE NZ
REMARK 470 LYS A 295 CE NZ
REMARK 470 ILE A 303 CD1
REMARK 470 LYS A 309 CE NZ
REMARK 470 GLU A 311 CG CD OE1 OE2
REMARK 470 LYS A 317 CG CD CE NZ
REMARK 470 LYS A 319 CG CD CE NZ
REMARK 470 GLU A 331 CG CD OE1 OE2
REMARK 470 GLU A 333 CD OE1 OE2
REMARK 470 GLU A 334 CG CD OE1 OE2
REMARK 470 ILE A 339 CG1 CG2 CD1
REMARK 470 LYS A 345 CG CD CE NZ
REMARK 470 ILE B 25 CG1 CG2 CD1
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 OG SER B 16 O4 RIB B 101 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 199 CB CYS A 199 SG -0.117
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 144 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 144 NE - CZ - NH2 ANGL. DEV. = 3.3 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 LEU A 273 46.70 -86.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 RIB B 101
DBREF 6EGW A 0 350 UNP P25321 KAPCA_CRIGR 1 351
DBREF 6EGW B 8 25 PDB 6EGW 6EGW 8 25
SEQADV 6EGW GLY A -2 UNP P25321 EXPRESSION TAG
SEQADV 6EGW HIS A -1 UNP P25321 EXPRESSION TAG
SEQRES 1 A 353 GLY HIS MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SEP
SEQRES 2 A 353 GLU GLN GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS
SEQRES 3 A 353 GLU GLU PHE LEU LYS LYS TRP GLU SER PRO SER GLN ASN
SEQRES 4 A 353 THR ALA GLN LEU ASP HIS PHE ASP ARG ILE LYS THR LEU
SEQRES 5 A 353 GLY THR GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS
SEQRES 6 A 353 LYS GLU THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP
SEQRES 7 A 353 LYS GLN LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR
SEQRES 8 A 353 LEU ASN GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO
SEQRES 9 A 353 PHE LEU VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER
SEQRES 10 A 353 ASN LEU TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU
SEQRES 11 A 353 MET PHE SER HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU
SEQRES 12 A 353 PRO HIS ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR
SEQRES 13 A 353 PHE GLU TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP
SEQRES 14 A 353 LEU LYS PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR
SEQRES 15 A 353 ILE GLN VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS
SEQRES 16 A 353 GLY ARG THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU
SEQRES 17 A 353 ALA PRO GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA
SEQRES 18 A 353 VAL ASP TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET
SEQRES 19 A 353 ALA ALA GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE
SEQRES 20 A 353 GLN ILE TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE
SEQRES 21 A 353 PRO SER HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG
SEQRES 22 A 353 ASN LEU LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN
SEQRES 23 A 353 LEU LYS ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP
SEQRES 24 A 353 PHE ALA THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS
SEQRES 25 A 353 VAL GLU ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY
SEQRES 26 A 353 ASP THR SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE
SEQRES 27 A 353 ARG VAL SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE THR
SEQRES 28 A 353 GLU PHE
SEQRES 1 B 18 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 B 18 ARG ARG ASN ALA ILE
MODRES 6EGW SEP A 139 SER MODIFIED RESIDUE
MODRES 6EGW TPO A 197 THR MODIFIED RESIDUE
MODRES 6EGW SEP A 338 SER MODIFIED RESIDUE
HET SEP A 139 14
HET TPO A 197 17
HET SEP A 338 14
HET 9LQ A 401 54
HET RIB B 101 3
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM 9LQ [2-[(4-ISOQUINOLIN-5-YLSULFONYL-1,4-DIAZEPAN-1-YL)
HETNAM 2 9LQ METHYL]PHENYL]BORONIC ACID
HETNAM RIB ALPHA-D-RIBOFURANOSE
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 9LQ C21 H24 B N3 O4 S
FORMUL 4 RIB C5 H10 O5
FORMUL 5 HOH *202(H2 O)
HELIX 1 AA1 GLU A 13 SER A 32 1 20
HELIX 2 AA2 GLN A 39 ASP A 41 5 3
HELIX 3 AA3 LYS A 76 LEU A 82 1 7
HELIX 4 AA4 GLN A 84 VAL A 98 1 15
HELIX 5 AA5 GLU A 127 GLY A 136 1 10
HELIX 6 AA6 SEP A 139 LEU A 160 1 22
HELIX 7 AA7 LYS A 168 GLU A 170 5 3
HELIX 8 AA8 THR A 201 LEU A 205 5 5
HELIX 9 AA9 ALA A 206 LEU A 211 1 6
HELIX 10 AB1 LYS A 217 GLY A 234 1 18
HELIX 11 AB2 GLN A 242 VAL A 251 1 10
HELIX 12 AB3 SER A 262 LEU A 273 1 12
HELIX 13 AB4 VAL A 288 ASN A 293 1 6
HELIX 14 AB5 HIS A 294 ALA A 298 5 5
HELIX 15 AB6 ASP A 301 GLN A 307 1 7
HELIX 16 AB7 GLY A 344 THR A 348 5 5
HELIX 17 AB8 THR B 9 GLY B 17 1 9
SHEET 1 AA1 5 PHE A 43 THR A 51 0
SHEET 2 AA1 5 GLY A 55 HIS A 62 -1 O LEU A 59 N LYS A 47
SHEET 3 AA1 5 HIS A 68 ASP A 75 -1 O ILE A 73 N ARG A 56
SHEET 4 AA1 5 ASN A 115 GLU A 121 -1 O MET A 120 N ALA A 70
SHEET 5 AA1 5 LEU A 106 LYS A 111 -1 N PHE A 108 O VAL A 119
SHEET 1 AA2 2 LEU A 162 ILE A 163 0
SHEET 2 AA2 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AA3 2 LEU A 172 ILE A 174 0
SHEET 2 AA3 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
LINK C PHE A 138 N SEP A 139 1555 1555 1.33
LINK C SEP A 139 N GLU A 140 1555 1555 1.33
LINK C TRP A 196 N TPO A 197 1555 1555 1.33
LINK C TPO A 197 N LEU A 198 1555 1555 1.34
LINK C VAL A 337 N SEP A 338 1555 1555 1.33
LINK C SEP A 338 N ILE A 339 1555 1555 1.33
LINK OG SER B 16 C1 RIB B 101 1555 1555 1.38
CRYST1 68.539 72.134 76.180 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 0.014590 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013863 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013127 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
