HEADER TRANSFERASE 25-AUG-16 5P8W
TITLE CRYSTAL STRUCTURE OF COMT IN COMPLEX WITH [5-(2,4-DIMETHYL-1,3-
TITLE 2 THIAZOL-5-YL)-1H-PYRAZOL-3-YL]METHANAMINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: SOLUBLE FORM, RESIDUES 44-264;
COMPND 5 EC: 2.1.1.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: COMT;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS METHYLTRANSFERASE, NEUROTRANSMITTER DEGRADATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.EHLER,C.LERNER,M.G.RUDOLPH
REVDAT 4 03-APR-24 5P8W 1 REMARK
REVDAT 3 17-NOV-21 5P8W 1 LINK
REVDAT 2 21-FEB-18 5P8W 1 REMARK
REVDAT 1 07-SEP-16 5P8W 0
JRNL AUTH C.LERNER,M.G.RUDOLPH
JRNL TITL CRYSTAL STRUCTURE OF COMT COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_2481
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) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 64942
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 3291
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 48.6501 - 5.8523 1.00 2726 163 0.1514 0.1734
REMARK 3 2 5.8523 - 4.6463 1.00 2636 140 0.1366 0.1696
REMARK 3 3 4.6463 - 4.0593 1.00 2617 142 0.1121 0.1191
REMARK 3 4 4.0593 - 3.6883 1.00 2600 130 0.1278 0.1639
REMARK 3 5 3.6883 - 3.4240 1.00 2589 129 0.1463 0.1869
REMARK 3 6 3.4240 - 3.2222 1.00 2577 138 0.1646 0.2170
REMARK 3 7 3.2222 - 3.0608 1.00 2552 156 0.1875 0.2153
REMARK 3 8 3.0608 - 2.9276 1.00 2576 141 0.2023 0.2603
REMARK 3 9 2.9276 - 2.8149 1.00 2576 130 0.2020 0.2736
REMARK 3 10 2.8149 - 2.7178 1.00 2525 147 0.1972 0.2293
REMARK 3 11 2.7178 - 2.6328 1.00 2560 129 0.1815 0.2170
REMARK 3 12 2.6328 - 2.5576 1.00 2576 129 0.1811 0.2158
REMARK 3 13 2.5576 - 2.4903 1.00 2575 127 0.1846 0.2435
REMARK 3 14 2.4903 - 2.4295 1.00 2522 143 0.1960 0.2468
REMARK 3 15 2.4295 - 2.3743 1.00 2561 141 0.1916 0.2478
REMARK 3 16 2.3743 - 2.3237 1.00 2551 122 0.1914 0.2357
REMARK 3 17 2.3237 - 2.2773 1.00 2547 136 0.2054 0.2504
REMARK 3 18 2.2773 - 2.2343 1.00 2549 133 0.2107 0.2629
REMARK 3 19 2.2343 - 2.1944 1.00 2539 144 0.2254 0.2594
REMARK 3 20 2.1944 - 2.1572 1.00 2563 131 0.2332 0.3040
REMARK 3 21 2.1572 - 2.1224 1.00 2543 111 0.2556 0.3098
REMARK 3 22 2.1224 - 2.0897 1.00 2515 149 0.2642 0.3347
REMARK 3 23 2.0897 - 2.0590 1.00 2552 120 0.2990 0.3232
REMARK 3 24 2.0590 - 2.0300 1.00 2524 160 0.3088 0.3731
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.800
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.62
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.17
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 : 0.016 5253
REMARK 3 ANGLE : 0.812 7075
REMARK 3 CHIRALITY : 0.048 799
REMARK 3 PLANARITY : 0.005 907
REMARK 3 DIHEDRAL : 14.864 3210
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1684 43.9038 -4.2462
REMARK 3 T TENSOR
REMARK 3 T11: 0.3856 T22: 0.3490
REMARK 3 T33: 0.3971 T12: 0.0358
REMARK 3 T13: 0.1312 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 2.5820 L22: 7.9563
REMARK 3 L33: 2.5920 L12: 1.1891
REMARK 3 L13: 1.2579 L23: 2.0232
REMARK 3 S TENSOR
REMARK 3 S11: 0.0057 S12: -0.3711 S13: -0.3060
REMARK 3 S21: 0.8529 S22: -0.1223 S23: 0.7817
REMARK 3 S31: 0.3225 S32: -0.2032 S33: 0.1166
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 17 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3355 48.7893 -12.5574
REMARK 3 T TENSOR
REMARK 3 T11: 0.3835 T22: 0.3248
REMARK 3 T33: 0.2977 T12: 0.0080
REMARK 3 T13: 0.0741 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 0.9322 L22: 0.3257
REMARK 3 L33: 1.4611 L12: -0.1878
REMARK 3 L13: -0.5244 L23: -0.2562
REMARK 3 S TENSOR
REMARK 3 S11: 0.0912 S12: -0.1698 S13: 0.1335
REMARK 3 S21: 0.1117 S22: 0.1202 S23: -0.0196
REMARK 3 S31: 0.0759 S32: 0.1293 S33: -0.1835
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.7747 48.3173 -24.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.3253 T22: 0.4056
REMARK 3 T33: 0.3404 T12: 0.1199
REMARK 3 T13: 0.0632 T23: 0.0345
REMARK 3 L TENSOR
REMARK 3 L11: 1.5853 L22: 1.7280
REMARK 3 L33: 2.5083 L12: -0.5958
REMARK 3 L13: -0.7587 L23: 1.1406
REMARK 3 S TENSOR
REMARK 3 S11: 0.1225 S12: 0.1963 S13: 0.0229
REMARK 3 S21: 0.0018 S22: -0.1127 S23: 0.3280
REMARK 3 S31: -0.3696 S32: -0.5426 S33: -0.0145
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 144 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3461 39.5620 -34.0256
REMARK 3 T TENSOR
REMARK 3 T11: 0.3228 T22: 0.3634
REMARK 3 T33: 0.2656 T12: 0.0474
REMARK 3 T13: 0.0285 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 1.9590 L22: 1.2476
REMARK 3 L33: 1.8427 L12: -0.3860
REMARK 3 L13: -0.7188 L23: 0.7886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0542 S12: 0.3313 S13: -0.0595
REMARK 3 S21: -0.1280 S22: -0.0282 S23: 0.0751
REMARK 3 S31: -0.1491 S32: -0.2254 S33: -0.0447
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7611 20.7268 -13.6397
REMARK 3 T TENSOR
REMARK 3 T11: 0.3692 T22: 0.3222
REMARK 3 T33: 0.2942 T12: -0.0547
REMARK 3 T13: 0.0327 T23: -0.0046
REMARK 3 L TENSOR
REMARK 3 L11: 1.4232 L22: 2.4846
REMARK 3 L33: 0.9552 L12: 0.3602
REMARK 3 L13: 0.0830 L23: -0.2760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0615 S12: 0.2094 S13: -0.0558
REMARK 3 S21: -0.0406 S22: 0.2378 S23: -0.0897
REMARK 3 S31: 0.1001 S32: -0.0974 S33: -0.2154
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 216 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5215 0.6686 -27.4201
REMARK 3 T TENSOR
REMARK 3 T11: 1.7701 T22: 2.2231
REMARK 3 T33: 1.8091 T12: 0.1357
REMARK 3 T13: -0.6285 T23: 0.2074
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0000
REMARK 3 L33: 2.0000 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: -3.1490 S12: -19.2180 S13: -11.2784
REMARK 3 S21: 16.0589 S22: 6.1701 S23: -8.8918
REMARK 3 S31: 13.5936 S32: 27.1441 S33: -3.0644
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7948 25.9903 -0.2089
REMARK 3 T TENSOR
REMARK 3 T11: 0.3513 T22: 0.3838
REMARK 3 T33: 0.4178 T12: -0.0191
REMARK 3 T13: -0.0866 T23: 0.0279
REMARK 3 L TENSOR
REMARK 3 L11: 1.6295 L22: 1.9118
REMARK 3 L33: 1.6296 L12: 1.6689
REMARK 3 L13: 0.3177 L23: 0.8898
REMARK 3 S TENSOR
REMARK 3 S11: 0.0272 S12: -0.1561 S13: 0.2512
REMARK 3 S21: 0.2666 S22: -0.1045 S23: 0.3184
REMARK 3 S31: -0.1008 S32: -0.1157 S33: 0.0243
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 71 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7234 20.0488 -10.1511
REMARK 3 T TENSOR
REMARK 3 T11: 0.2505 T22: 0.3257
REMARK 3 T33: 0.3778 T12: -0.0009
REMARK 3 T13: -0.0374 T23: 0.0040
REMARK 3 L TENSOR
REMARK 3 L11: 1.0589 L22: 1.5927
REMARK 3 L33: 3.0909 L12: 0.8071
REMARK 3 L13: 0.6233 L23: 0.0163
REMARK 3 S TENSOR
REMARK 3 S11: 0.0066 S12: 0.0048 S13: -0.1625
REMARK 3 S21: 0.0723 S22: -0.0808 S23: -0.4437
REMARK 3 S31: -0.0118 S32: 0.4089 S33: 0.0623
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 144 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2823 20.0535 -19.8334
REMARK 3 T TENSOR
REMARK 3 T11: 0.2767 T22: 0.3032
REMARK 3 T33: 0.2797 T12: -0.0491
REMARK 3 T13: -0.0251 T23: -0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 0.5425 L22: 1.3406
REMARK 3 L33: 1.4518 L12: -0.1623
REMARK 3 L13: -0.1113 L23: -0.4384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0234 S12: 0.0565 S13: -0.1584
REMARK 3 S21: 0.0534 S22: 0.1119 S23: 0.0419
REMARK 3 S31: 0.1418 S32: -0.1018 S33: -0.0852
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 21 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.0594 22.9899 -20.0810
REMARK 3 T TENSOR
REMARK 3 T11: 0.5957 T22: 0.6776
REMARK 3 T33: 0.6581 T12: -0.0035
REMARK 3 T13: -0.1429 T23: 0.0837
REMARK 3 L TENSOR
REMARK 3 L11: 7.9518 L22: 5.0300
REMARK 3 L33: 5.1585 L12: 1.4959
REMARK 3 L13: -1.1118 L23: -0.5139
REMARK 3 S TENSOR
REMARK 3 S11: 0.4188 S12: 0.6266 S13: 0.9932
REMARK 3 S21: -0.7071 S22: 0.0468 S23: 0.6239
REMARK 3 S31: 0.4534 S32: 0.6368 S33: -0.4939
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 22 THROUGH 41 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.7126 13.2015 -18.4524
REMARK 3 T TENSOR
REMARK 3 T11: 0.7196 T22: 0.5985
REMARK 3 T33: 0.6116 T12: -0.1087
REMARK 3 T13: -0.1232 T23: 0.0068
REMARK 3 L TENSOR
REMARK 3 L11: 3.1959 L22: 5.9429
REMARK 3 L33: 5.2040 L12: -1.3523
REMARK 3 L13: 0.0467 L23: -0.6643
REMARK 3 S TENSOR
REMARK 3 S11: -0.2376 S12: 0.3594 S13: -0.2660
REMARK 3 S21: -1.2326 S22: 0.2800 S23: 0.5524
REMARK 3 S31: 0.6075 S32: 0.3528 S33: 0.0395
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 42 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.4972 6.4046 -3.6046
REMARK 3 T TENSOR
REMARK 3 T11: 0.5892 T22: 0.3692
REMARK 3 T33: 0.6989 T12: -0.0282
REMARK 3 T13: 0.0016 T23: 0.0995
REMARK 3 L TENSOR
REMARK 3 L11: 4.4701 L22: 2.1107
REMARK 3 L33: 6.2636 L12: 0.1028
REMARK 3 L13: -1.7905 L23: -0.5218
REMARK 3 S TENSOR
REMARK 3 S11: 0.1640 S12: 0.2019 S13: -0.3981
REMARK 3 S21: -0.1092 S22: 0.0060 S23: 0.6968
REMARK 3 S31: 0.8299 S32: -0.1286 S33: -0.1667
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 58 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5259 22.2589 -1.8231
REMARK 3 T TENSOR
REMARK 3 T11: 0.3389 T22: 0.3703
REMARK 3 T33: 0.6092 T12: 0.0403
REMARK 3 T13: 0.0975 T23: 0.0497
REMARK 3 L TENSOR
REMARK 3 L11: 1.3170 L22: 2.7568
REMARK 3 L33: 2.4025 L12: -0.0007
REMARK 3 L13: 0.6450 L23: -0.4658
REMARK 3 S TENSOR
REMARK 3 S11: 0.0610 S12: 0.0162 S13: 0.0272
REMARK 3 S21: 0.1060 S22: 0.0829 S23: 0.8023
REMARK 3 S31: -0.1983 S32: -0.3684 S33: -0.1170
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 130 THROUGH 143 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6959 19.3614 6.1539
REMARK 3 T TENSOR
REMARK 3 T11: 0.5315 T22: 0.4273
REMARK 3 T33: 0.5439 T12: 0.0255
REMARK 3 T13: 0.1217 T23: 0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 2.0725 L22: 2.9660
REMARK 3 L33: 2.2379 L12: 1.5880
REMARK 3 L13: -0.2918 L23: -0.7070
REMARK 3 S TENSOR
REMARK 3 S11: -0.2589 S12: -0.1226 S13: -0.0581
REMARK 3 S21: 0.2867 S22: 0.1490 S23: 0.6828
REMARK 3 S31: -0.1124 S32: -0.2254 S33: 0.1143
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 144 THROUGH 196 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5054 12.5044 8.1649
REMARK 3 T TENSOR
REMARK 3 T11: 0.5060 T22: 0.3878
REMARK 3 T33: 0.3793 T12: 0.0017
REMARK 3 T13: 0.0609 T23: 0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 0.8901 L22: 2.5059
REMARK 3 L33: 0.4416 L12: -0.2801
REMARK 3 L13: 0.5756 L23: 0.0565
REMARK 3 S TENSOR
REMARK 3 S11: -0.0025 S12: -0.1836 S13: 0.0725
REMARK 3 S21: 0.6355 S22: 0.0829 S23: 0.1774
REMARK 3 S31: 0.0361 S32: -0.0695 S33: -0.0675
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 197 THROUGH 215 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9335 4.7423 -1.0458
REMARK 3 T TENSOR
REMARK 3 T11: 0.4305 T22: 0.3339
REMARK 3 T33: 0.3918 T12: -0.0202
REMARK 3 T13: 0.0154 T23: 0.0923
REMARK 3 L TENSOR
REMARK 3 L11: 1.7826 L22: 3.2570
REMARK 3 L33: 6.2408 L12: -0.3552
REMARK 3 L13: -0.5226 L23: 1.0318
REMARK 3 S TENSOR
REMARK 3 S11: 0.1911 S12: 0.0462 S13: 0.2221
REMARK 3 S21: 0.1126 S22: 0.2814 S23: 0.0941
REMARK 3 S31: -0.1152 S32: 0.2376 S33: -0.2949
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 216 THROUGH 216 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3866 10.7102 23.5374
REMARK 3 T TENSOR
REMARK 3 T11: 1.2081 T22: 1.7668
REMARK 3 T33: 2.0537 T12: 0.2020
REMARK 3 T13: -0.1499 T23: -0.3112
REMARK 3 L TENSOR
REMARK 3 L11: 2.0000 L22: 2.0000
REMARK 3 L33: 2.0000 L12: 2.0000
REMARK 3 L13: 2.0000 L23: 2.0000
REMARK 3 S TENSOR
REMARK 3 S11: -2.1049 S12: -10.8227 S13: -3.0959
REMARK 3 S21: 15.6190 S22: -4.7904 S23: 19.4969
REMARK 3 S31: 0.9666 S32: -8.3492 S33: 6.8910
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DTT CROSSLINKS CYS 33 AND 69
REMARK 4
REMARK 4 5P8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1001400365.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64984
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 88.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.760
REMARK 200 R MERGE (I) : 0.08900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.46200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.270
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: INHOUSE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CHES, PH 9, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 59.80000
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 59.80000
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 47.46550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 88.18950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.46550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 88.18950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.80000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.46550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 88.18950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.80000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.46550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 88.18950
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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 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 B 521 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 461 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 MET A 1
REMARK 465 SER A 217
REMARK 465 PRO A 218
REMARK 465 ASP A 219
REMARK 465 LYS A 220
REMARK 465 SER A 221
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 SER B 216
REMARK 465 SER B 217
REMARK 465 PRO B 218
REMARK 465 ASP B 219
REMARK 465 LYS B 220
REMARK 465 SER B 221
REMARK 465 MET C 1
REMARK 465 GLY C 2
REMARK 465 GLU C 37
REMARK 465 TRP C 38
REMARK 465 SER C 217
REMARK 465 PRO C 218
REMARK 465 ASP C 219
REMARK 465 LYS C 220
REMARK 465 SER C 221
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 OH TYR A 197 O HOH A 401 1.91
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 432 O HOH A 432 3554 1.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 68 -131.62 62.16
REMARK 500 ASP A 133 -82.21 -90.06
REMARK 500 ASP A 141 38.52 -150.84
REMARK 500 HIS A 142 -143.37 -109.19
REMARK 500 SER A 196 -149.10 -156.42
REMARK 500 LYS A 202 64.92 63.87
REMARK 500 ASP A 205 -163.29 -127.86
REMARK 500 TYR B 68 -112.88 61.23
REMARK 500 ASP B 133 -78.82 -88.99
REMARK 500 ASP B 141 30.81 -146.56
REMARK 500 HIS B 142 -144.10 -106.34
REMARK 500 ASN C 16 -28.49 -146.02
REMARK 500 SER C 58 58.29 35.54
REMARK 500 TYR C 68 -123.33 53.69
REMARK 500 ASP C 133 -80.19 -85.58
REMARK 500 ASP C 141 29.84 -147.60
REMARK 500 HIS C 142 -115.57 -109.47
REMARK 500 ILE C 172 -53.44 -125.09
REMARK 500 LEU C 198 -135.84 43.74
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 521 DISTANCE = 6.01 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 41 OD1
REMARK 620 2 ASP A 141 OD1 112.2
REMARK 620 3 ASP A 141 OD2 86.9 50.0
REMARK 620 4 ASP A 169 OD2 121.9 88.1 65.2
REMARK 620 5 ASN A 170 OD1 153.4 80.7 117.7 80.1
REMARK 620 6 HOH A 472 O 82.0 163.5 143.0 91.2 82.9
REMARK 620 7 HOH A 489 O 80.8 79.3 117.5 157.1 79.1 95.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 183 O
REMARK 620 2 ARG A 184 O 84.1
REMARK 620 3 SER A 186 O 90.6 110.4
REMARK 620 4 PHE A 189 O 94.8 161.4 88.2
REMARK 620 5 TYR A 197 OH 71.6 72.3 161.8 89.7
REMARK 620 6 HOH A 401 O 175.9 97.5 85.3 84.8 112.5
REMARK 620 7 HOH A 531 O 105.1 79.3 162.6 83.0 33.7 78.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 305 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 33 O
REMARK 620 2 LYS B 36 O 73.7
REMARK 620 3 ALA B 39 O 102.7 93.2
REMARK 620 4 ASN B 41 OD1 75.4 146.7 81.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 183 O
REMARK 620 2 ARG B 184 O 87.9
REMARK 620 3 SER B 186 O 92.2 105.4
REMARK 620 4 PHE B 189 O 93.5 166.5 88.0
REMARK 620 5 HOH B 489 O 102.3 84.3 162.9 82.2
REMARK 620 6 HOH B 496 O 175.4 87.9 90.6 90.1 75.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL C 183 O
REMARK 620 2 ARG C 184 O 89.6
REMARK 620 3 SER C 186 O 90.2 106.1
REMARK 620 4 PHE C 189 O 96.4 167.8 84.5
REMARK 620 5 GLU C 199 O 75.3 82.9 163.1 88.4
REMARK 620 6 HOH C 411 O 104.2 80.7 164.3 87.6 29.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue O01 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue O01 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DTT C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue O01 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 304
DBREF 5P8W A 1 221 UNP P22734 COMT_RAT 44 264
DBREF 5P8W B 1 221 UNP P22734 COMT_RAT 44 264
DBREF 5P8W C 1 221 UNP P22734 COMT_RAT 44 264
SEQADV 5P8W ILE A 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5P8W CYS A 95 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQADV 5P8W ILE B 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5P8W CYS B 95 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQADV 5P8W ILE C 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5P8W CYS C 95 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQRES 1 A 221 MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES 2 A 221 GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES 3 A 221 GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES 4 A 221 MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES 5 A 221 VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES 6 A 221 GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES 7 A 221 LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES 8 A 221 ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES 9 A 221 PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES 10 A 221 ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES 11 A 221 ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES 12 A 221 LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES 13 A 221 CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES 14 A 221 ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES 15 A 221 VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES 16 A 221 SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES 17 A 221 LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
SEQRES 1 B 221 MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES 2 B 221 GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES 3 B 221 GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES 4 B 221 MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES 5 B 221 VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES 6 B 221 GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES 7 B 221 LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES 8 B 221 ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES 9 B 221 PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES 10 B 221 ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES 11 B 221 ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES 12 B 221 LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES 13 B 221 CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES 14 B 221 ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES 15 B 221 VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES 16 B 221 SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES 17 B 221 LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
SEQRES 1 C 221 MET GLY ASP THR LYS GLU GLN ARG ILE LEU ARG TYR VAL
SEQRES 2 C 221 GLN GLN ASN ALA LYS PRO GLY ASP PRO GLN SER VAL LEU
SEQRES 3 C 221 GLU ALA ILE ASP THR TYR CYS THR GLN LYS GLU TRP ALA
SEQRES 4 C 221 MET ASN VAL GLY ASP ALA LYS GLY GLN ILE MET ASP ALA
SEQRES 5 C 221 VAL ILE ARG GLU TYR SER PRO SER LEU VAL LEU GLU LEU
SEQRES 6 C 221 GLY ALA TYR CYS GLY TYR SER ALA VAL ARG MET ALA ARG
SEQRES 7 C 221 LEU LEU GLN PRO GLY ALA ARG LEU LEU THR MET GLU ILE
SEQRES 8 C 221 ASN PRO ASP CYS ALA ALA ILE THR GLN GLN MET LEU ASN
SEQRES 9 C 221 PHE ALA GLY LEU GLN ASP LYS VAL THR ILE LEU ASN GLY
SEQRES 10 C 221 ALA SER GLN ASP LEU ILE PRO GLN LEU LYS LYS LYS TYR
SEQRES 11 C 221 ASP VAL ASP THR LEU ASP MET VAL PHE LEU ASP HIS TRP
SEQRES 12 C 221 LYS ASP ARG TYR LEU PRO ASP THR LEU LEU LEU GLU LYS
SEQRES 13 C 221 CYS GLY LEU LEU ARG LYS GLY THR VAL LEU LEU ALA ASP
SEQRES 14 C 221 ASN VAL ILE VAL PRO GLY THR PRO ASP PHE LEU ALA TYR
SEQRES 15 C 221 VAL ARG GLY SER SER SER PHE GLU CYS THR HIS TYR SER
SEQRES 16 C 221 SER TYR LEU GLU TYR MET LYS VAL VAL ASP GLY LEU GLU
SEQRES 17 C 221 LYS ALA ILE TYR GLN GLY PRO SER SER PRO ASP LYS SER
HET DTT A 301 8
HET O01 A 302 14
HET FMT A 303 3
HET NA A 304 1
HET NA A 305 1
HET DTT B 301 8
HET O01 B 302 14
HET FMT B 303 3
HET NA B 304 1
HET NA B 305 1
HET DTT C 301 8
HET O01 C 302 14
HET FMT C 303 3
HET NA C 304 1
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM O01 [5-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-3-
HETNAM 2 O01 YL]METHANAMINE
HETNAM FMT FORMIC ACID
HETNAM NA SODIUM ION
HETSYN DTT 1,4-DITHIOTHREITOL
HETSYN O01 1-[3-(2,4-DIMETHYL-1,3-THIAZOL-5-YL)-1H-PYRAZOL-5-
HETSYN 2 O01 YL]METHANAMINE
FORMUL 4 DTT 3(C4 H10 O2 S2)
FORMUL 5 O01 3(C9 H12 N4 S)
FORMUL 6 FMT 3(C H2 O2)
FORMUL 7 NA 5(NA 1+)
FORMUL 18 HOH *364(H2 O)
HELIX 1 AA1 THR A 4 ALA A 17 1 14
HELIX 2 AA2 ASP A 21 GLU A 37 1 17
HELIX 3 AA3 GLY A 43 SER A 58 1 16
HELIX 4 AA4 GLY A 70 ARG A 78 1 9
HELIX 5 AA5 ASN A 92 GLY A 107 1 16
HELIX 6 AA6 LEU A 108 ASP A 110 5 3
HELIX 7 AA7 ALA A 118 ILE A 123 1 6
HELIX 8 AA8 GLN A 125 ASP A 131 1 7
HELIX 9 AA9 TRP A 143 ASP A 145 5 3
HELIX 10 AB1 ARG A 146 CYS A 157 1 12
HELIX 11 AB2 THR A 176 SER A 186 1 11
HELIX 12 AB3 THR B 4 ALA B 17 1 14
HELIX 13 AB4 ASP B 21 LYS B 36 1 16
HELIX 14 AB5 GLY B 43 SER B 58 1 16
HELIX 15 AB6 GLY B 70 ARG B 78 1 9
HELIX 16 AB7 ASN B 92 GLY B 107 1 16
HELIX 17 AB8 LEU B 108 ASP B 110 5 3
HELIX 18 AB9 ALA B 118 ILE B 123 1 6
HELIX 19 AC1 GLN B 125 ASP B 131 1 7
HELIX 20 AC2 TRP B 143 ASP B 145 5 3
HELIX 21 AC3 ARG B 146 CYS B 157 1 12
HELIX 22 AC4 THR B 176 SER B 186 1 11
HELIX 23 AC5 THR C 4 GLN C 15 1 12
HELIX 24 AC6 ASP C 21 LYS C 36 1 16
HELIX 25 AC7 ASN C 41 SER C 58 1 18
HELIX 26 AC8 GLY C 70 ARG C 78 1 9
HELIX 27 AC9 ASN C 92 GLY C 107 1 16
HELIX 28 AD1 LEU C 108 ASP C 110 5 3
HELIX 29 AD2 ALA C 118 ILE C 123 1 6
HELIX 30 AD3 GLN C 125 ASP C 131 1 7
HELIX 31 AD4 TRP C 143 ASP C 145 5 3
HELIX 32 AD5 ARG C 146 CYS C 157 1 12
HELIX 33 AD6 THR C 176 SER C 186 1 11
SHEET 1 AA112 VAL A 112 ASN A 116 0
SHEET 2 AA112 ARG A 85 GLU A 90 1 N THR A 88 O LEU A 115
SHEET 3 AA112 LEU A 61 LEU A 65 1 N GLU A 64 O LEU A 87
SHEET 4 AA112 LEU A 135 LEU A 140 1 O PHE A 139 N LEU A 63
SHEET 5 AA112 LEU A 160 ALA A 168 1 O LEU A 167 N VAL A 138
SHEET 6 AA112 PHE B 189 TYR B 212 -1 O TYR B 212 N GLY A 163
SHEET 7 AA112 PHE A 189 TYR A 212 -1 N THR A 192 O LYS B 209
SHEET 8 AA112 LEU B 160 ALA B 168 -1 O LEU B 166 N ALA A 210
SHEET 9 AA112 LEU B 135 LEU B 140 1 N VAL B 138 O VAL B 165
SHEET 10 AA112 LEU B 61 LEU B 65 1 N LEU B 63 O PHE B 139
SHEET 11 AA112 ARG B 85 GLU B 90 1 O LEU B 87 N GLU B 64
SHEET 12 AA112 VAL B 112 ASN B 116 1 O LEU B 115 N THR B 88
SHEET 1 AA2 7 VAL C 112 ASN C 116 0
SHEET 2 AA2 7 ARG C 85 GLU C 90 1 N THR C 88 O LEU C 115
SHEET 3 AA2 7 LEU C 61 LEU C 65 1 N GLU C 64 O LEU C 87
SHEET 4 AA2 7 LEU C 135 LEU C 140 1 O PHE C 139 N LEU C 65
SHEET 5 AA2 7 LEU C 160 ASP C 169 1 O ASP C 169 N LEU C 140
SHEET 6 AA2 7 ASP C 205 TYR C 212 -1 O TYR C 212 N GLY C 163
SHEET 7 AA2 7 PHE C 189 SER C 196 -1 N THR C 192 O LYS C 209
SSBOND 1 CYS A 33 DTT A 301 1555 1555 2.01
SSBOND 2 CYS A 69 DTT A 301 1555 1555 2.01
SSBOND 3 CYS B 33 DTT B 301 1555 1555 2.01
SSBOND 4 CYS B 69 DTT B 301 1555 1555 2.01
SSBOND 5 CYS C 33 DTT C 301 1555 1555 2.01
SSBOND 6 CYS C 69 DTT C 301 1555 1555 2.01
LINK OD1 ASN A 41 NA NA A 304 1555 1555 2.41
LINK OD1 ASP A 141 NA NA A 304 1555 1555 2.39
LINK OD2 ASP A 141 NA NA A 304 1555 1555 2.69
LINK OD2 ASP A 169 NA NA A 304 1555 1555 2.61
LINK OD1 ASN A 170 NA NA A 304 1555 1555 2.26
LINK O VAL A 183 NA NA A 305 1555 1555 2.50
LINK O ARG A 184 NA NA A 305 1555 1555 2.56
LINK O SER A 186 NA NA A 305 1555 1555 2.32
LINK O PHE A 189 NA NA A 305 1555 1555 2.37
LINK OH TYR A 197 NA NA A 305 1555 3554 3.06
LINK NA NA A 304 O HOH A 472 1555 1555 2.69
LINK NA NA A 304 O HOH A 489 1555 1555 2.49
LINK NA NA A 305 O HOH A 401 1555 3554 2.46
LINK NA NA A 305 O HOH A 531 1555 1555 2.39
LINK O CYS B 33 NA NA B 305 1555 1555 2.63
LINK O LYS B 36 NA NA B 305 1555 1555 2.51
LINK O ALA B 39 NA NA B 305 1555 1555 2.78
LINK OD1 ASN B 41 NA NA B 305 1555 1555 2.47
LINK O VAL B 183 NA NA B 304 1555 1555 2.40
LINK O ARG B 184 NA NA B 304 1555 1555 2.51
LINK O SER B 186 NA NA B 304 1555 1555 2.34
LINK O PHE B 189 NA NA B 304 1555 1555 2.34
LINK NA NA B 304 O HOH B 489 1555 1555 2.53
LINK NA NA B 304 O HOH B 496 1555 1555 2.41
LINK O VAL C 183 NA NA C 304 1555 1555 2.44
LINK O ARG C 184 NA NA C 304 1555 1555 2.59
LINK O SER C 186 NA NA C 304 1555 1555 2.43
LINK O PHE C 189 NA NA C 304 1555 1555 2.39
LINK O GLU C 199 NA NA C 304 1555 4555 2.68
LINK NA NA C 304 O HOH C 411 1555 4555 2.36
CISPEP 1 VAL A 173 PRO A 174 0 2.39
CISPEP 2 VAL B 173 PRO B 174 0 1.59
CISPEP 3 VAL C 173 PRO C 174 0 2.59
SITE 1 AC1 9 LYS A 5 ILE A 9 CYS A 33 TRP A 38
SITE 2 AC1 9 ALA A 39 MET A 40 ASN A 41 CYS A 69
SITE 3 AC1 9 HOH A 415
SITE 1 AC2 13 GLY A 66 TYR A 68 MET A 89 GLU A 90
SITE 2 AC2 13 ILE A 91 GLY A 117 ALA A 118 SER A 119
SITE 3 AC2 13 GLN A 120 HIS A 142 TRP A 143 ARG A 146
SITE 4 AC2 13 HOH C 403
SITE 1 AC3 6 THR A 176 PRO A 177 ASP A 178 PHE A 179
SITE 2 AC3 6 HOH A 439 HOH A 466
SITE 1 AC4 6 ASN A 41 ASP A 141 ASP A 169 ASN A 170
SITE 2 AC4 6 HOH A 472 HOH A 489
SITE 1 AC5 7 VAL A 183 ARG A 184 SER A 186 PHE A 189
SITE 2 AC5 7 TYR A 197 HOH A 401 HOH A 531
SITE 1 AC6 5 ILE B 9 CYS B 33 ALA B 39 MET B 40
SITE 2 AC6 5 CYS B 69
SITE 1 AC7 14 GLY B 66 TYR B 68 MET B 89 GLU B 90
SITE 2 AC7 14 ILE B 91 GLY B 117 ALA B 118 SER B 119
SITE 3 AC7 14 GLN B 120 HIS B 142 TRP B 143 ARG B 146
SITE 4 AC7 14 HOH B 409 HOH B 437
SITE 1 AC8 6 THR B 176 PRO B 177 ASP B 178 PHE B 179
SITE 2 AC8 6 HOH B 423 HOH B 424
SITE 1 AC9 6 VAL B 183 ARG B 184 SER B 186 PHE B 189
SITE 2 AC9 6 HOH B 489 HOH B 496
SITE 1 AD1 4 CYS B 33 LYS B 36 ALA B 39 ASN B 41
SITE 1 AD2 4 ILE C 9 CYS C 33 TYR C 68 CYS C 69
SITE 1 AD3 12 VAL A 204 TYR B 197 GLY C 66 GLU C 90
SITE 2 AD3 12 ILE C 91 GLY C 117 ALA C 118 SER C 119
SITE 3 AD3 12 GLN C 120 HIS C 142 HOH C 414 HOH C 415
SITE 1 AD4 7 LYS C 144 ASN C 170 ILE C 172 VAL C 173
SITE 2 AD4 7 PRO C 174 GLY C 175 HOH C 436
SITE 1 AD5 6 VAL C 183 ARG C 184 SER C 186 PHE C 189
SITE 2 AD5 6 GLU C 199 HOH C 411
CRYST1 94.931 176.379 119.600 90.00 90.00 90.00 C 2 2 21 24
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 0.010534 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005670 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008361 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
