HEADER TRANSFERASE 30-NOV-09 3KVX
TITLE JNK3 BOUND TO AMINOPYRIMIDINE INHIBITOR, SR-3562
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 10;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 39-402;
COMPND 5 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE JNK3, C-JUN N-TERMINAL
COMPND 6 KINASE 3, MAP KINASE P49 3F12;
COMPND 7 EC: 2.7.11.24;
COMPND 8 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: MAPK10, JNK3, JNK3A, PRKM10;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST14
KEYWDS JNK3, MAPK10, INHIBITOR, ATP-BINDING, EPILEPSY, KINASE, NUCLEOTIDE-
KEYWDS 2 BINDING, PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE,
KEYWDS 3 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.HABEL,J.D.LAUGHLIN,P.LOGRASSO
REVDAT 4 06-SEP-23 3KVX 1 REMARK LINK
REVDAT 3 13-JUL-11 3KVX 1 VERSN
REVDAT 2 19-JAN-10 3KVX 1 JRNL
REVDAT 1 22-DEC-09 3KVX 0
JRNL AUTH T.KAMENECKA,R.JIANG,X.SONG,D.DUCKETT,W.CHEN,Y.Y.LING,
JRNL AUTH 2 J.HABEL,J.D.LAUGHLIN,J.CHAMBERS,M.FIGUERA-LOSADA,
JRNL AUTH 3 M.D.CAMERON,L.LIN,C.H.RUIZ,P.V.LOGRASSO
JRNL TITL SYNTHESIS, BIOLOGICAL EVALUATION, X-RAY STRUCTURE, AND
JRNL TITL 2 PHARMACOKINETICS OF AMINOPYRIMIDINE C-JUN-N-TERMINAL KINASE
JRNL TITL 3 (JNK) INHIBITORS
JRNL REF J.MED.CHEM. V. 53 419 2010
JRNL REFN ISSN 0022-2623
JRNL PMID 19947601
JRNL DOI 10.1021/JM901351F
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 13142
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 708
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 858
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.3220
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.3440
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2531
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.81000
REMARK 3 B22 (A**2) : 1.02000
REMARK 3 B33 (A**2) : 1.79000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.507
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.228
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.828
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2636 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3587 ; 2.107 ; 1.984
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 329 ; 6.884 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;37.783 ;23.925
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 407 ;17.682 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;23.342 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 406 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1982 ; 0.022 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1652 ; 1.210 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2638 ; 2.134 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 984 ; 3.347 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 948 ; 4.788 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 45 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): -28.4080 52.1780 15.8550
REMARK 3 T TENSOR
REMARK 3 T11: 0.2490 T22: 0.1986
REMARK 3 T33: 0.2986 T12: -0.0020
REMARK 3 T13: 0.0970 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 9.4226 L22: 3.9417
REMARK 3 L33: 9.7266 L12: -3.2793
REMARK 3 L13: 4.6491 L23: -0.1523
REMARK 3 S TENSOR
REMARK 3 S11: 0.1042 S12: -0.2554 S13: 1.0510
REMARK 3 S21: -0.0032 S22: -0.2907 S23: -0.1663
REMARK 3 S31: -0.4255 S32: -0.1057 S33: 0.1865
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): -35.0840 44.0020 13.1590
REMARK 3 T TENSOR
REMARK 3 T11: 0.2820 T22: 0.2883
REMARK 3 T33: 0.4151 T12: -0.0810
REMARK 3 T13: 0.0896 T23: -0.1035
REMARK 3 L TENSOR
REMARK 3 L11: 3.5005 L22: 13.4066
REMARK 3 L33: 7.2524 L12: -2.4876
REMARK 3 L13: -1.4403 L23: 3.8498
REMARK 3 S TENSOR
REMARK 3 S11: 0.0642 S12: -0.0630 S13: 0.1681
REMARK 3 S21: 0.1250 S22: -0.6230 S23: 1.0853
REMARK 3 S31: 0.7641 S32: -0.6900 S33: 0.5588
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 90 A 105
REMARK 3 ORIGIN FOR THE GROUP (A): -15.6750 43.2750 10.6310
REMARK 3 T TENSOR
REMARK 3 T11: 0.3498 T22: 0.3823
REMARK 3 T33: 0.3904 T12: 0.0501
REMARK 3 T13: 0.0231 T23: -0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 11.2934 L22: 1.7494
REMARK 3 L33: 2.9999 L12: -1.6297
REMARK 3 L13: -4.2912 L23: 0.1862
REMARK 3 S TENSOR
REMARK 3 S11: -0.5464 S12: -0.6957 S13: -0.2557
REMARK 3 S21: 0.0624 S22: 0.1949 S23: -0.4065
REMARK 3 S31: 0.5923 S32: 0.5596 S33: 0.3515
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 106 A 118
REMARK 3 ORIGIN FOR THE GROUP (A): -17.9990 39.1940 -0.4810
REMARK 3 T TENSOR
REMARK 3 T11: 0.4764 T22: 0.3031
REMARK 3 T33: 0.4753 T12: 0.0173
REMARK 3 T13: 0.0326 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 11.1047 L22: 5.3071
REMARK 3 L33: 18.1695 L12: 7.0595
REMARK 3 L13: 7.4070 L23: 4.8521
REMARK 3 S TENSOR
REMARK 3 S11: 0.3043 S12: 0.3674 S13: -0.1835
REMARK 3 S21: -0.1351 S22: 0.0029 S23: 0.1352
REMARK 3 S31: 1.0122 S32: -0.4106 S33: -0.3072
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 119 A 127
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8310 34.6480 -1.4380
REMARK 3 T TENSOR
REMARK 3 T11: 0.8513 T22: 0.3335
REMARK 3 T33: 0.3403 T12: 0.0637
REMARK 3 T13: -0.1957 T23: -0.0830
REMARK 3 L TENSOR
REMARK 3 L11: 5.8427 L22: 12.7626
REMARK 3 L33: 1.8186 L12: -8.4874
REMARK 3 L13: 3.2339 L23: -4.6150
REMARK 3 S TENSOR
REMARK 3 S11: 0.5198 S12: 0.2693 S13: -0.2185
REMARK 3 S21: -1.2971 S22: -0.4622 S23: 0.5815
REMARK 3 S31: 0.2272 S32: 0.1352 S33: -0.0576
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 128 A 148
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0870 50.4910 8.2310
REMARK 3 T TENSOR
REMARK 3 T11: 0.2517 T22: 0.1989
REMARK 3 T33: 0.2753 T12: 0.0325
REMARK 3 T13: 0.0314 T23: -0.0410
REMARK 3 L TENSOR
REMARK 3 L11: 12.2958 L22: 8.2845
REMARK 3 L33: 3.8230 L12: 5.4424
REMARK 3 L13: -0.0474 L23: 1.1124
REMARK 3 S TENSOR
REMARK 3 S11: 0.1607 S12: -0.0581 S13: 0.5624
REMARK 3 S21: -0.0646 S22: 0.0947 S23: -0.1652
REMARK 3 S31: -0.2317 S32: 0.1126 S33: -0.2553
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 149 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): -34.9710 19.9290 11.4580
REMARK 3 T TENSOR
REMARK 3 T11: 0.3102 T22: 0.3015
REMARK 3 T33: 0.2479 T12: 0.0103
REMARK 3 T13: 0.1158 T23: -0.0138
REMARK 3 L TENSOR
REMARK 3 L11: 3.4418 L22: 11.3271
REMARK 3 L33: 3.5285 L12: 0.5691
REMARK 3 L13: 1.7144 L23: 0.6405
REMARK 3 S TENSOR
REMARK 3 S11: -0.1092 S12: -0.2417 S13: 0.0993
REMARK 3 S21: 1.3173 S22: 0.1846 S23: 0.5567
REMARK 3 S31: 0.1741 S32: -0.0259 S33: -0.0754
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 167 A 200
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4020 25.0340 1.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.2811 T22: 0.2257
REMARK 3 T33: 0.2885 T12: -0.0334
REMARK 3 T13: -0.0339 T23: -0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 6.4447 L22: 4.5579
REMARK 3 L33: 3.2109 L12: -0.5201
REMARK 3 L13: -1.1936 L23: 1.3656
REMARK 3 S TENSOR
REMARK 3 S11: -0.0094 S12: 0.0444 S13: 0.4497
REMARK 3 S21: -0.0173 S22: 0.1919 S23: 0.0052
REMARK 3 S31: -0.2350 S32: 0.1947 S33: -0.1825
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 201 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9480 20.5370 6.7430
REMARK 3 T TENSOR
REMARK 3 T11: 0.3244 T22: 0.4269
REMARK 3 T33: 0.2314 T12: 0.0210
REMARK 3 T13: -0.0914 T23: -0.1038
REMARK 3 L TENSOR
REMARK 3 L11: 2.2478 L22: 4.6837
REMARK 3 L33: 3.4382 L12: -3.0356
REMARK 3 L13: -0.9683 L23: 1.4518
REMARK 3 S TENSOR
REMARK 3 S11: -0.1966 S12: -0.4080 S13: 0.3373
REMARK 3 S21: 0.4257 S22: 0.5262 S23: -0.4636
REMARK 3 S31: 0.1247 S32: 0.7030 S33: -0.3296
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 262 A 291
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9540 10.9270 11.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.4429 T22: 0.7181
REMARK 3 T33: 0.3982 T12: 0.2589
REMARK 3 T13: -0.3228 T23: -0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 12.5471 L22: 6.6129
REMARK 3 L33: 1.4982 L12: -0.3859
REMARK 3 L13: -2.8455 L23: 0.5025
REMARK 3 S TENSOR
REMARK 3 S11: -0.6612 S12: -0.8902 S13: -0.3305
REMARK 3 S21: 0.8477 S22: 0.6089 S23: -0.9603
REMARK 3 S31: 0.4114 S32: 0.6321 S33: 0.0523
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 292 A 309
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5970 6.3560 10.8780
REMARK 3 T TENSOR
REMARK 3 T11: 1.0238 T22: 1.4464
REMARK 3 T33: 0.9560 T12: 0.4759
REMARK 3 T13: -0.3894 T23: 0.2265
REMARK 3 L TENSOR
REMARK 3 L11: 2.8144 L22: 8.4790
REMARK 3 L33: 13.2513 L12: 4.7545
REMARK 3 L13: 1.4819 L23: 0.4442
REMARK 3 S TENSOR
REMARK 3 S11: 0.9469 S12: 0.0655 S13: -1.0987
REMARK 3 S21: 1.8148 S22: -0.3458 S23: -1.7097
REMARK 3 S31: 0.7657 S32: 3.2643 S33: -0.6011
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 310 A 343
REMARK 3 ORIGIN FOR THE GROUP (A): -30.0420 4.5550 6.1330
REMARK 3 T TENSOR
REMARK 3 T11: 1.2618 T22: 0.6137
REMARK 3 T33: 0.7241 T12: 0.6247
REMARK 3 T13: 0.5181 T23: 0.3885
REMARK 3 L TENSOR
REMARK 3 L11: 5.8526 L22: 7.6778
REMARK 3 L33: 3.5858 L12: 1.1023
REMARK 3 L13: 3.2547 L23: 2.5917
REMARK 3 S TENSOR
REMARK 3 S11: -0.2808 S12: -0.6762 S13: -0.8499
REMARK 3 S21: 1.5175 S22: 0.2370 S23: 1.3631
REMARK 3 S31: 1.2909 S32: 0.3244 S33: 0.0438
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 344 A 363
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1660 13.2060 -4.7730
REMARK 3 T TENSOR
REMARK 3 T11: 0.2883 T22: 0.2038
REMARK 3 T33: 0.1887 T12: -0.0045
REMARK 3 T13: -0.0610 T23: -0.0464
REMARK 3 L TENSOR
REMARK 3 L11: 7.6923 L22: 4.2102
REMARK 3 L33: 2.5757 L12: -1.4973
REMARK 3 L13: -0.5581 L23: -0.2043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1868 S12: 0.3547 S13: -0.2562
REMARK 3 S21: -0.2076 S22: 0.1244 S23: 0.1773
REMARK 3 S31: 0.1845 S32: 0.3695 S33: 0.0624
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 383 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2260 48.9140 0.8350
REMARK 3 T TENSOR
REMARK 3 T11: 0.3060 T22: 0.3105
REMARK 3 T33: 0.3615 T12: -0.0561
REMARK 3 T13: 0.0784 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 17.0178 L22: 5.1278
REMARK 3 L33: 4.2507 L12: -1.9992
REMARK 3 L13: -4.0917 L23: -0.3716
REMARK 3 S TENSOR
REMARK 3 S11: -0.4382 S12: 1.0452 S13: 0.0730
REMARK 3 S21: -0.2313 S22: 0.2949 S23: -0.1966
REMARK 3 S31: -0.3622 S32: -0.0553 S33: 0.1433
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3KVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-DEC-09.
REMARK 100 THE DEPOSITION ID IS D_1000056513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 68.290
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.06200
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) : 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: PDB ENTRY 3FI3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10MG/ML JNK3 MIXED WITH 1MM AMP-PCP,
REMARK 280 2MM MGCL2, 0.4MM ZWITTERGENT 3-14, AND 10% ETHYLENE GLYCOL.
REMARK 280 CRYSTALS GROWN IN 0.2M NACL, 0.1M BIS-TRIS, 28-31% PEG 3350, PH
REMARK 280 5.5. LIGAND SOAKED IN TO CRYSTALS., MICROBATCH, TEMPERATURE
REMARK 280 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 34.37200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 34.37200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 40.68100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 62.82100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 40.68100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 62.82100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 34.37200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 40.68100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 62.82100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 34.37200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 40.68100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 62.82100
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 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 MET A 39
REMARK 465 SER A 40
REMARK 465 LYS A 41
REMARK 465 SER A 42
REMARK 465 LYS A 43
REMARK 465 VAL A 44
REMARK 465 ASP A 45
REMARK 465 THR A 213
REMARK 465 ALA A 214
REMARK 465 GLY A 215
REMARK 465 THR A 216
REMARK 465 SER A 217
REMARK 465 PHE A 218
REMARK 465 MET A 219
REMARK 465 MET A 220
REMARK 465 THR A 221
REMARK 465 PRO A 222
REMARK 465 TYR A 223
REMARK 465 VAL A 224
REMARK 465 VAL A 368
REMARK 465 GLU A 369
REMARK 465 ALA A 370
REMARK 465 PRO A 371
REMARK 465 PRO A 372
REMARK 465 PRO A 373
REMARK 465 GLN A 374
REMARK 465 ILE A 375
REMARK 465 TYR A 376
REMARK 465 ASP A 377
REMARK 465 LYS A 378
REMARK 465 GLN A 379
REMARK 465 LEU A 380
REMARK 465 ASP A 381
REMARK 465 GLU A 402
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 52 CG CD OE1 OE2
REMARK 470 ASN A 66 CG OD1 ND2
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 470 LYS A 106 CG CD CE NZ
REMARK 470 ASN A 119 CG OD1 ND2
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 GLN A 158 CG CD OE1 NE2
REMARK 470 GLU A 160 CG CD OE1 OE2
REMARK 470 ARG A 165 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 VAL A 225 CG1 CG2
REMARK 470 THR A 226 OG1 CG2
REMARK 470 ARG A 227 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 241 CG CD CE NZ
REMARK 470 LYS A 260 CG CD CE NZ
REMARK 470 ARG A 266 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 267 CG OD1 OD2
REMARK 470 TYR A 268 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ILE A 269 CG1 CG2 CD1
REMARK 470 LYS A 274 CG CD CE NZ
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 GLU A 285 CG CD OE1 OE2
REMARK 470 LYS A 288 CG CD CE NZ
REMARK 470 LYS A 289 CG CD CE NZ
REMARK 470 GLN A 291 CG CD OE1 NE2
REMARK 470 VAL A 294 CG1 CG2
REMARK 470 ARG A 295 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 296 CG OD1 ND2
REMARK 470 TYR A 297 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 298 CG1 CG2
REMARK 470 ASN A 300 CG OD1 ND2
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 LYS A 311 CG CD CE NZ
REMARK 470 ASP A 321 CG OD1 OD2
REMARK 470 LYS A 326 CG CD CE NZ
REMARK 470 LYS A 346 CG CD CE NZ
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 GLU A 382 CG CD OE1 OE2
REMARK 470 GLU A 388 CG CD OE1 OE2
REMARK 470 LYS A 396 CG CD CE NZ
REMARK 470 ASN A 400 CG OD1 ND2
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 417 O HOH A 418 3555 2.04
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 79 CB CYS A 79 SG -0.110
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 ARG A 97 68.25 37.04
REMARK 500 GLN A 140 -53.74 -138.54
REMARK 500 ARG A 188 -8.98 79.94
REMARK 500 LYS A 288 2.72 -53.97
REMARK 500 PRO A 319 -176.63 -46.38
REMARK 500 ALA A 320 -154.13 -178.21
REMARK 500 PRO A 365 85.13 -37.44
REMARK 500 ALA A 366 -28.72 162.16
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 FMY A 403
DBREF 3KVX A 39 402 UNP P53779 MK10_HUMAN 39 402
SEQRES 1 A 364 MET SER LYS SER LYS VAL ASP ASN GLN PHE TYR SER VAL
SEQRES 2 A 364 GLU VAL GLY ASP SER THR PHE THR VAL LEU LYS ARG TYR
SEQRES 3 A 364 GLN ASN LEU LYS PRO ILE GLY SER GLY ALA GLN GLY ILE
SEQRES 4 A 364 VAL CYS ALA ALA TYR ASP ALA VAL LEU ASP ARG ASN VAL
SEQRES 5 A 364 ALA ILE LYS LYS LEU SER ARG PRO PHE GLN ASN GLN THR
SEQRES 6 A 364 HIS ALA LYS ARG ALA TYR ARG GLU LEU VAL LEU MET LYS
SEQRES 7 A 364 CYS VAL ASN HIS LYS ASN ILE ILE SER LEU LEU ASN VAL
SEQRES 8 A 364 PHE THR PRO GLN LYS THR LEU GLU GLU PHE GLN ASP VAL
SEQRES 9 A 364 TYR LEU VAL MET GLU LEU MET ASP ALA ASN LEU OCY GLN
SEQRES 10 A 364 VAL ILE GLN MET GLU LEU ASP HIS GLU ARG MET SER TYR
SEQRES 11 A 364 LEU LEU TYR GLN MET LEU OCY GLY ILE LYS HIS LEU HIS
SEQRES 12 A 364 SER ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO SER ASN
SEQRES 13 A 364 ILE VAL VAL LYS SER ASP OCY THR LEU LYS ILE LEU ASP
SEQRES 14 A 364 PHE GLY LEU ALA ARG THR ALA GLY THR SER PHE MET MET
SEQRES 15 A 364 THR PRO TYR VAL VAL THR ARG TYR TYR ARG ALA PRO GLU
SEQRES 16 A 364 VAL ILE LEU GLY MET GLY TYR LYS GLU ASN VAL ASP ILE
SEQRES 17 A 364 TRP SER VAL GLY CYS ILE MET GLY GLU MET VAL ARG HIS
SEQRES 18 A 364 LYS ILE LEU PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP
SEQRES 19 A 364 ASN LYS VAL ILE GLU GLN LEU GLY THR PRO CYS PRO GLU
SEQRES 20 A 364 PHE MET LYS LYS LEU GLN PRO THR VAL ARG ASN TYR VAL
SEQRES 21 A 364 GLU ASN ARG PRO LYS TYR ALA GLY LEU THR PHE PRO LYS
SEQRES 22 A 364 LEU PHE PRO ASP SER LEU PHE PRO ALA ASP SER GLU HIS
SEQRES 23 A 364 ASN LYS LEU LYS ALA SER GLN ALA ARG ASP LEU LEU SER
SEQRES 24 A 364 LYS MET LEU VAL ILE ASP PRO ALA LYS ARG ILE SER VAL
SEQRES 25 A 364 ASP ASP ALA LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR
SEQRES 26 A 364 ASP PRO ALA GLU VAL GLU ALA PRO PRO PRO GLN ILE TYR
SEQRES 27 A 364 ASP LYS GLN LEU ASP GLU ARG GLU HIS THR ILE GLU GLU
SEQRES 28 A 364 TRP LYS GLU LEU ILE TYR LYS GLU VAL MET ASN SER GLU
MODRES 3KVX OCY A 154 CYS HYDROXYETHYLCYSTEINE
MODRES 3KVX OCY A 175 CYS HYDROXYETHYLCYSTEINE
MODRES 3KVX OCY A 201 CYS HYDROXYETHYLCYSTEINE
HET OCY A 154 9
HET OCY A 175 9
HET OCY A 201 9
HET FMY A 403 37
HETNAM OCY HYDROXYETHYLCYSTEINE
HETNAM FMY N-[(2Z)-4-(3-FLUORO-5-MORPHOLIN-4-YLPHENYL)PYRIMIDIN-
HETNAM 2 FMY 2(1H)-YLIDENE]-4-(3-MORPHOLIN-4-YL-1H-1,2,4-TRIAZOL-1-
HETNAM 3 FMY YL)ANILINE
FORMUL 1 OCY 3(C5 H11 N O3 S)
FORMUL 2 FMY C26 H27 F N8 O2
FORMUL 3 HOH *27(H2 O)
HELIX 1 1 PRO A 98 GLN A 100 5 3
HELIX 2 2 ASN A 101 MET A 115 1 15
HELIX 3 3 LEU A 153 MET A 159 1 7
HELIX 4 4 ASP A 162 ALA A 183 1 22
HELIX 5 5 LYS A 191 SER A 193 5 3
HELIX 6 6 ALA A 231 LEU A 236 1 6
HELIX 7 7 ASN A 243 HIS A 259 1 17
HELIX 8 8 ASP A 267 GLY A 280 1 14
HELIX 9 9 CYS A 283 LYS A 288 1 6
HELIX 10 10 GLN A 291 ASN A 300 1 10
HELIX 11 11 THR A 308 PHE A 313 1 6
HELIX 12 12 PRO A 314 PHE A 318 5 5
HELIX 13 13 SER A 322 LEU A 340 1 19
HELIX 14 14 ASP A 343 ARG A 347 5 5
HELIX 15 15 SER A 349 HIS A 356 1 8
HELIX 16 16 ILE A 359 TYR A 363 5 5
HELIX 17 17 THR A 386 ASN A 400 1 15
SHEET 1 A 2 PHE A 48 VAL A 53 0
SHEET 2 A 2 SER A 56 LEU A 61 -1 O PHE A 58 N VAL A 51
SHEET 1 B 5 TYR A 64 GLY A 71 0
SHEET 2 B 5 VAL A 78 ASP A 83 -1 O VAL A 78 N ILE A 70
SHEET 3 B 5 ARG A 88 SER A 96 -1 O ARG A 88 N ASP A 83
SHEET 4 B 5 ASP A 141 GLU A 147 -1 O VAL A 142 N LEU A 95
SHEET 5 B 5 LEU A 126 PHE A 130 -1 N ASN A 128 O VAL A 145
SHEET 1 C 3 ALA A 151 ASN A 152 0
SHEET 2 C 3 ILE A 195 VAL A 197 -1 O VAL A 197 N ALA A 151
SHEET 3 C 3 LEU A 203 ILE A 205 -1 O LYS A 204 N VAL A 196
LINK C LEU A 153 N OCY A 154 1555 1555 1.35
LINK C OCY A 154 N GLN A 155 1555 1555 1.32
LINK C LEU A 174 N OCY A 175 1555 1555 1.32
LINK C OCY A 175 N GLY A 176 1555 1555 1.33
LINK C ASP A 200 N OCY A 201 1555 1555 1.36
LINK C OCY A 201 N THR A 202 1555 1555 1.34
SITE 1 AC1 14 ILE A 70 SER A 72 GLY A 73 ALA A 74
SITE 2 AC1 14 GLN A 75 VAL A 78 ALA A 91 LYS A 93
SITE 3 AC1 14 GLU A 147 MET A 149 ALA A 151 GLN A 155
SITE 4 AC1 14 SER A 193 LEU A 206
CRYST1 81.362 125.642 68.744 90.00 90.00 90.00 C 2 2 21 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 0.012291 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014547 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
