HEADER TRANSFERASE 19-OCT-16 5PA7
TITLE HUMANIZED RAT COMT IN COMPLEX WITH 6-BROMO-3-CHLOROQUINOLIN-8-OL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATECHOL O-METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: SOLUBLE FORM, RESIDUES 44-264;
COMPND 5 SYNONYM: HUMANIZED RAT COMT;
COMPND 6 EC: 2.1.1.6;
COMPND 7 ENGINEERED: YES;
COMPND 8 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 3 17-NOV-21 5PA7 1 LINK
REVDAT 2 21-FEB-18 5PA7 1 REMARK
REVDAT 1 22-NOV-17 5PA7 0
JRNL AUTH C.LERNER,R.JAKOB-ROETNE,K.GROEBKE-ZBINDEN,B.BUETTELMANN,
JRNL AUTH 2 M.G.RUDOLPH
JRNL TITL CRYSTAL STRUCTURE OF A COMT COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.12 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_764
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) : 2.12
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.20
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 29565
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1502
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 45.2147 - 4.7134 1.00 2731 155 0.1548 0.1910
REMARK 3 2 4.7134 - 3.7417 1.00 2591 154 0.1405 0.2025
REMARK 3 3 3.7417 - 3.2689 1.00 2585 121 0.1755 0.2356
REMARK 3 4 3.2689 - 2.9701 1.00 2569 101 0.2121 0.2870
REMARK 3 5 2.9701 - 2.7572 1.00 2565 115 0.2176 0.2884
REMARK 3 6 2.7572 - 2.5947 1.00 2493 161 0.2203 0.2809
REMARK 3 7 2.5947 - 2.4648 1.00 2554 134 0.2575 0.3055
REMARK 3 8 2.4648 - 2.3575 1.00 2522 128 0.2711 0.3429
REMARK 3 9 2.3575 - 2.2667 0.99 2503 125 0.2904 0.3357
REMARK 3 10 2.2667 - 2.1885 0.99 2465 159 0.3035 0.3591
REMARK 3 11 2.1885 - 2.1201 1.00 2485 149 0.3314 0.3387
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.95
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 43.93
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.630
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.150
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 21.62930
REMARK 3 B22 (A**2) : -11.28300
REMARK 3 B33 (A**2) : -10.34630
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3446
REMARK 3 ANGLE : 1.067 4674
REMARK 3 CHIRALITY : 0.069 531
REMARK 3 PLANARITY : 0.004 593
REMARK 3 DIHEDRAL : 15.813 1302
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 3:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0800 -11.2625 21.8405
REMARK 3 T TENSOR
REMARK 3 T11: 0.2843 T22: 0.4613
REMARK 3 T33: 0.3423 T12: 0.0442
REMARK 3 T13: 0.0228 T23: -0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.9965 L22: 3.9319
REMARK 3 L33: 3.6031 L12: -0.1910
REMARK 3 L13: -0.2576 L23: 2.2136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0839 S12: -0.2401 S13: -0.3489
REMARK 3 S21: 0.2776 S22: 0.5247 S23: -0.0861
REMARK 3 S31: 0.5423 S32: 0.8510 S33: -0.3892
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 17:35)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7136 -0.7362 18.7742
REMARK 3 T TENSOR
REMARK 3 T11: 0.4248 T22: 0.3786
REMARK 3 T33: 0.4352 T12: -0.0531
REMARK 3 T13: -0.0019 T23: 0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 5.7305 L22: 4.9749
REMARK 3 L33: 5.1609 L12: -1.6246
REMARK 3 L13: -1.6292 L23: 0.9148
REMARK 3 S TENSOR
REMARK 3 S11: 0.0925 S12: 0.3275 S13: 0.9566
REMARK 3 S21: -0.2017 S22: 0.1983 S23: -0.8248
REMARK 3 S31: -0.9884 S32: 0.4174 S33: -0.2420
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 36:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.5826 -0.2904 7.4578
REMARK 3 T TENSOR
REMARK 3 T11: 0.5086 T22: 0.4632
REMARK 3 T33: 0.3903 T12: -0.0315
REMARK 3 T13: 0.0173 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 2.8844 L22: 4.1259
REMARK 3 L33: 2.1689 L12: -1.2970
REMARK 3 L13: -0.3460 L23: -0.2249
REMARK 3 S TENSOR
REMARK 3 S11: -0.0131 S12: -0.0772 S13: -0.1067
REMARK 3 S21: -0.4996 S22: 0.0418 S23: 0.2047
REMARK 3 S31: -0.4243 S32: 0.5394 S33: -0.0326
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 58:70)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1472 -5.3832 10.9645
REMARK 3 T TENSOR
REMARK 3 T11: 0.3542 T22: 0.4116
REMARK 3 T33: 0.3530 T12: 0.0701
REMARK 3 T13: -0.0155 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.0087 L22: 1.3190
REMARK 3 L33: 0.9755 L12: 0.0656
REMARK 3 L13: 0.8072 L23: -0.4294
REMARK 3 S TENSOR
REMARK 3 S11: 0.1673 S12: 0.3224 S13: 0.5010
REMARK 3 S21: -0.0966 S22: -0.2960 S23: -0.0868
REMARK 3 S31: -0.3706 S32: 0.1999 S33: 0.0966
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 71:118)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5112 -6.1539 17.5702
REMARK 3 T TENSOR
REMARK 3 T11: 0.3440 T22: 0.3368
REMARK 3 T33: 0.3388 T12: 0.0325
REMARK 3 T13: 0.0012 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.9588 L22: 0.8040
REMARK 3 L33: 1.3318 L12: 0.7192
REMARK 3 L13: 0.1725 L23: -0.4445
REMARK 3 S TENSOR
REMARK 3 S11: -0.0005 S12: -0.1364 S13: 0.1192
REMARK 3 S21: -0.0516 S22: 0.0351 S23: -0.0186
REMARK 3 S31: -0.2005 S32: -0.0461 S33: -0.0213
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 119:136)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.3570 -11.2626 10.0358
REMARK 3 T TENSOR
REMARK 3 T11: 0.2990 T22: 0.4844
REMARK 3 T33: 0.4283 T12: 0.0471
REMARK 3 T13: -0.0491 T23: -0.0070
REMARK 3 L TENSOR
REMARK 3 L11: 1.0817 L22: 2.7447
REMARK 3 L33: 0.8902 L12: -0.3624
REMARK 3 L13: 0.1756 L23: -0.4088
REMARK 3 S TENSOR
REMARK 3 S11: -0.0177 S12: -0.1957 S13: -0.0062
REMARK 3 S21: 0.2482 S22: -0.0181 S23: 0.3475
REMARK 3 S31: -0.1434 S32: -0.3261 S33: 0.0265
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 137:156)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.2557 -12.0728 0.9101
REMARK 3 T TENSOR
REMARK 3 T11: 0.4511 T22: 0.3272
REMARK 3 T33: 0.2715 T12: 0.0364
REMARK 3 T13: -0.0632 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 2.6647 L22: 2.2466
REMARK 3 L33: 1.7173 L12: 0.0509
REMARK 3 L13: 0.1913 L23: 0.5885
REMARK 3 S TENSOR
REMARK 3 S11: 0.0297 S12: 0.1565 S13: -0.1831
REMARK 3 S21: -0.5479 S22: 0.1008 S23: -0.0795
REMARK 3 S31: 0.4138 S32: -0.1275 S33: -0.1367
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 157:188)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7924 -6.3117 -4.2401
REMARK 3 T TENSOR
REMARK 3 T11: 0.5114 T22: 0.3481
REMARK 3 T33: 0.3419 T12: 0.0152
REMARK 3 T13: -0.0880 T23: 0.0640
REMARK 3 L TENSOR
REMARK 3 L11: 1.5527 L22: 0.8313
REMARK 3 L33: 1.2800 L12: 0.4046
REMARK 3 L13: -0.1307 L23: 0.4505
REMARK 3 S TENSOR
REMARK 3 S11: -0.1497 S12: 0.1763 S13: 0.0461
REMARK 3 S21: -0.5584 S22: 0.1567 S23: 0.2599
REMARK 3 S31: -0.0166 S32: -0.1548 S33: 0.0027
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 189:215)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.7477 -2.2715 -3.3855
REMARK 3 T TENSOR
REMARK 3 T11: 0.6038 T22: 0.3651
REMARK 3 T33: 0.3478 T12: -0.0036
REMARK 3 T13: -0.0202 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 2.5481 L22: 1.8864
REMARK 3 L33: 1.0019 L12: -0.8402
REMARK 3 L13: -0.4455 L23: -0.0849
REMARK 3 S TENSOR
REMARK 3 S11: -0.2475 S12: 0.2332 S13: 0.4815
REMARK 3 S21: -0.6161 S22: 0.2009 S23: 0.0425
REMARK 3 S31: -0.1469 S32: -0.2168 S33: -0.0283
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 300:300)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.9257 -13.7917 8.9488
REMARK 3 T TENSOR
REMARK 3 T11: 0.5386 T22: 0.3779
REMARK 3 T33: 0.3061 T12: 0.0763
REMARK 3 T13: 0.1328 T23: 0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 0.0738 L22: 0.0998
REMARK 3 L33: 0.0165 L12: 0.0673
REMARK 3 L13: -0.0114 L23: 0.0158
REMARK 3 S TENSOR
REMARK 3 S11: -0.0926 S12: -0.1772 S13: 0.0594
REMARK 3 S21: 0.1038 S22: -0.0577 S23: -0.1010
REMARK 3 S31: -0.0955 S32: 0.3277 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 301:302)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7554 -11.8315 3.4989
REMARK 3 T TENSOR
REMARK 3 T11: 0.4109 T22: 1.0326
REMARK 3 T33: 0.5625 T12: 0.0215
REMARK 3 T13: 0.1269 T23: -0.1873
REMARK 3 L TENSOR
REMARK 3 L11: 0.5548 L22: 0.2907
REMARK 3 L33: 0.0611 L12: -0.1150
REMARK 3 L13: 0.0722 L23: -0.1321
REMARK 3 S TENSOR
REMARK 3 S11: -0.1755 S12: 0.0444 S13: -0.0907
REMARK 3 S21: -0.0288 S22: -0.2264 S23: -0.1984
REMARK 3 S31: 0.0921 S32: 0.0729 S33: -0.0091
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 3:35)
REMARK 3 ORIGIN FOR THE GROUP (A): -23.0059 -20.5750 29.2990
REMARK 3 T TENSOR
REMARK 3 T11: 0.3690 T22: 0.7066
REMARK 3 T33: 0.7242 T12: 0.3326
REMARK 3 T13: -0.0185 T23: 0.1366
REMARK 3 L TENSOR
REMARK 3 L11: 2.0571 L22: 1.0780
REMARK 3 L33: 4.0335 L12: 1.2727
REMARK 3 L13: -0.2703 L23: -0.4973
REMARK 3 S TENSOR
REMARK 3 S11: 0.0307 S12: 0.4509 S13: 1.1863
REMARK 3 S21: 0.0396 S22: 0.5880 S23: 0.7927
REMARK 3 S31: -0.8690 S32: -0.5398 S33: -0.2138
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 36:57)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.1258 -25.1654 20.8891
REMARK 3 T TENSOR
REMARK 3 T11: 0.4605 T22: 0.4692
REMARK 3 T33: 0.3761 T12: 0.0555
REMARK 3 T13: 0.0561 T23: 0.0305
REMARK 3 L TENSOR
REMARK 3 L11: 3.6076 L22: 1.5666
REMARK 3 L33: 1.1767 L12: 0.6251
REMARK 3 L13: 0.6343 L23: -1.1335
REMARK 3 S TENSOR
REMARK 3 S11: 0.1713 S12: -0.2295 S13: 0.1909
REMARK 3 S21: -0.0929 S22: -0.2810 S23: 0.5160
REMARK 3 S31: -0.1189 S32: -0.3432 S33: -0.0070
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 58:143)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1408 -37.7280 29.1447
REMARK 3 T TENSOR
REMARK 3 T11: 0.3330 T22: 0.3628
REMARK 3 T33: 0.4166 T12: -0.0818
REMARK 3 T13: -0.0753 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 1.4546 L22: 1.4540
REMARK 3 L33: 2.8722 L12: -1.0414
REMARK 3 L13: -0.0362 L23: -1.0817
REMARK 3 S TENSOR
REMARK 3 S11: -0.0739 S12: 0.0532 S13: 0.0059
REMARK 3 S21: -0.3753 S22: 0.1351 S23: 0.4599
REMARK 3 S31: 0.4137 S32: -0.5802 S33: -0.0775
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 144:216)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6139 -33.0800 28.5592
REMARK 3 T TENSOR
REMARK 3 T11: 0.2930 T22: 0.2779
REMARK 3 T33: 0.3005 T12: 0.0619
REMARK 3 T13: 0.0144 T23: -0.0045
REMARK 3 L TENSOR
REMARK 3 L11: 0.8778 L22: 1.4144
REMARK 3 L33: 1.7971 L12: 0.9981
REMARK 3 L13: -0.1658 L23: -0.5351
REMARK 3 S TENSOR
REMARK 3 S11: -0.0584 S12: 0.0299 S13: -0.1221
REMARK 3 S21: -0.0715 S22: -0.0919 S23: -0.1596
REMARK 3 S31: 0.1204 S32: 0.1179 S33: 0.1495
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 300:300)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.2707 -31.3110 36.5609
REMARK 3 T TENSOR
REMARK 3 T11: 0.4695 T22: 0.4437
REMARK 3 T33: 0.4815 T12: 0.0342
REMARK 3 T13: 0.0954 T23: 0.0612
REMARK 3 L TENSOR
REMARK 3 L11: 0.0264 L22: 0.0372
REMARK 3 L33: 0.0340 L12: 0.0089
REMARK 3 L13: -0.0232 L23: -0.0242
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: 0.2040 S13: 0.2594
REMARK 3 S21: -0.0285 S22: -0.0073 S23: 0.1975
REMARK 3 S31: 0.0232 S32: -0.1469 S33: -0.0001
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PARTIAL RADIOLYSIS OF BROMINE. NO SIGMA
REMARK 3 -HOLE EFFECT OF CHLORINE AND AMIDE CARBONYL. LYSINE BINDS TO
REMARK 3 SAID CARBONYL.
REMARK 4
REMARK 4 5PA7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1001400412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100.0
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) : 1.0000
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29641
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.120
REMARK 200 RESOLUTION RANGE LOW (A) : 46.610
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.610
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : 0.12400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.83400
REMARK 200 R SYM FOR SHELL (I) : 0.83400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.230
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: INHOUSE MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
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: 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 28.59250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 73.80700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.05250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 73.80700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.59250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.05250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 MET A 1
REMARK 465 GLY A 2
REMARK 465 SER A 216
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 TRP B 38
REMARK 465 ALA B 39
REMARK 465 MET B 40
REMARK 465 ASN B 41
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 430 O HOH B 433 1.87
REMARK 500 O HOH A 433 O HOH A 436 1.98
REMARK 500 O HOH B 427 O HOH B 443 2.14
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 MET A 40 35.82 -78.63
REMARK 500 TYR A 68 -115.01 60.39
REMARK 500 ASP A 133 -75.28 -90.10
REMARK 500 ASP A 141 27.31 -158.24
REMARK 500 HIS A 142 -153.76 -97.68
REMARK 500 ASP A 205 -164.61 -122.51
REMARK 500 GLN B 15 -62.94 -93.02
REMARK 500 TYR B 68 -115.20 56.61
REMARK 500 ASP B 133 -77.31 -98.64
REMARK 500 ASP B 141 25.46 -141.87
REMARK 500 HIS B 142 -146.27 -107.14
REMARK 500 ASP B 205 -157.15 -93.66
REMARK 500
REMARK 500 REMARK: NULL
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 MG A 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 141 OD1
REMARK 620 2 ASP A 169 OD2 94.6
REMARK 620 3 ASN A 170 OD1 84.3 88.3
REMARK 620 4 7JX A 302 O12 160.7 104.7 97.8
REMARK 620 5 HOH A 412 O 87.1 97.2 170.1 88.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL A 183 O
REMARK 620 2 ARG A 184 O 78.1
REMARK 620 3 SER A 186 O 72.1 98.6
REMARK 620 4 PHE A 189 O 90.0 158.9 60.8
REMARK 620 5 HOH A 437 O 133.2 102.0 61.6 73.5
REMARK 620 6 HOH A 441 O 115.8 88.2 170.7 112.7 110.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 VAL B 183 O
REMARK 620 2 ARG B 184 O 81.1
REMARK 620 3 SER B 186 O 82.9 115.0
REMARK 620 4 PHE B 189 O 93.4 166.5 76.2
REMARK 620 5 HOH B 440 O 105.3 78.4 165.6 91.3
REMARK 620 6 HOH B 442 O 159.1 78.6 101.3 107.5 75.2
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 SAH A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 7JX A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 302
DBREF 5PA7 A 1 221 UNP P22734 COMT_RAT 44 264
DBREF 5PA7 B 1 221 UNP P22734 COMT_RAT 44 264
SEQADV 5PA7 ILE A 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5PA7 CYS A 95 UNP P22734 TYR 138 ENGINEERED MUTATION
SEQADV 5PA7 ILE B 91 UNP P22734 MET 134 ENGINEERED MUTATION
SEQADV 5PA7 CYS B 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
HET SAH A 300 26
HET MG A 301 1
HET 7JX A 302 13
HET NA A 303 1
HET SAH B 301 26
HET NA B 302 1
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
HETNAM MG MAGNESIUM ION
HETNAM 7JX 6-BROMANYL-3-CHLORANYL-QUINOLIN-8-OL
HETNAM NA SODIUM ION
FORMUL 3 SAH 2(C14 H20 N6 O5 S)
FORMUL 4 MG MG 2+
FORMUL 5 7JX C9 H5 BR CL N O
FORMUL 6 NA 2(NA 1+)
FORMUL 9 HOH *91(H2 O)
HELIX 1 AA1 THR A 4 ALA A 17 1 14
HELIX 2 AA2 ASP A 21 LYS A 36 1 16
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 ALA A 118 ILE A 123 1 6
HELIX 7 AA7 GLN A 125 TYR A 130 1 6
HELIX 8 AA8 TRP A 143 ASP A 145 5 3
HELIX 9 AA9 ARG A 146 CYS A 157 1 12
HELIX 10 AB1 THR A 176 SER A 186 1 11
HELIX 11 AB2 THR B 4 ALA B 17 1 14
HELIX 12 AB3 ASP B 21 LYS B 36 1 16
HELIX 13 AB4 GLY B 43 SER B 58 1 16
HELIX 14 AB5 GLY B 70 ARG B 78 1 9
HELIX 15 AB6 ASN B 92 GLY B 107 1 16
HELIX 16 AB7 ALA B 118 ILE B 123 1 6
HELIX 17 AB8 GLN B 125 TYR B 130 1 6
HELIX 18 AB9 TRP B 143 ASP B 145 5 3
HELIX 19 AC1 ARG B 146 CYS B 157 1 12
HELIX 20 AC2 THR B 176 SER B 186 1 11
SHEET 1 AA1 7 VAL A 112 ASN A 116 0
SHEET 2 AA1 7 ARG A 85 GLU A 90 1 N THR A 88 O LEU A 115
SHEET 3 AA1 7 LEU A 61 LEU A 65 1 N VAL A 62 O LEU A 87
SHEET 4 AA1 7 MET A 137 LEU A 140 1 O PHE A 139 N LEU A 65
SHEET 5 AA1 7 VAL A 165 ALA A 168 1 O LEU A 167 N VAL A 138
SHEET 6 AA1 7 VAL A 203 TYR A 212 -1 O ALA A 210 N LEU A 166
SHEET 7 AA1 7 PHE A 189 LEU A 198 -1 N SER A 196 O ASP A 205
SHEET 1 AA2 7 VAL B 112 ASN B 116 0
SHEET 2 AA2 7 ARG B 85 GLU B 90 1 N THR B 88 O LEU B 115
SHEET 3 AA2 7 LEU B 61 LEU B 65 1 N GLU B 64 O LEU B 87
SHEET 4 AA2 7 LEU B 135 LEU B 140 1 O PHE B 139 N LEU B 63
SHEET 5 AA2 7 LEU B 160 ALA B 168 1 O LEU B 167 N VAL B 138
SHEET 6 AA2 7 VAL B 203 TYR B 212 -1 O TYR B 212 N GLY B 163
SHEET 7 AA2 7 PHE B 189 LEU B 198 -1 N LEU B 198 O VAL B 203
LINK OD1 ASP A 141 MG MG A 301 1555 1555 2.27
LINK OD2 ASP A 169 MG MG A 301 1555 1555 2.23
LINK OD1 ASN A 170 MG MG A 301 1555 1555 2.17
LINK O VAL A 183 NA NA A 303 1555 1555 2.80
LINK O ARG A 184 NA NA A 303 1555 1555 2.86
LINK O SER A 186 NA NA A 303 1555 1555 3.00
LINK O PHE A 189 NA NA A 303 1555 1555 2.75
LINK MG MG A 301 O12 7JX A 302 1555 1555 2.19
LINK MG MG A 301 O HOH A 412 1555 1555 2.27
LINK NA NA A 303 O HOH A 437 1555 1555 2.98
LINK NA NA A 303 O HOH A 441 1555 1555 2.88
LINK O VAL B 183 NA NA B 302 1555 1555 2.76
LINK O ARG B 184 NA NA B 302 1555 1555 2.73
LINK O SER B 186 NA NA B 302 1555 1555 2.71
LINK O PHE B 189 NA NA B 302 1555 1555 2.59
LINK NA NA B 302 O HOH B 440 1555 1555 2.90
LINK NA NA B 302 O HOH B 442 1555 1555 2.91
CISPEP 1 VAL A 173 PRO A 174 0 -2.26
CISPEP 2 VAL B 173 PRO B 174 0 6.85
SITE 1 AC1 19 MET A 40 VAL A 42 GLY A 66 ALA A 67
SITE 2 AC1 19 TYR A 68 TYR A 71 SER A 72 MET A 89
SITE 3 AC1 19 GLU A 90 ILE A 91 CYS A 95 GLY A 117
SITE 4 AC1 19 ALA A 118 SER A 119 ASP A 141 HIS A 142
SITE 5 AC1 19 TRP A 143 7JX A 302 HOH A 408
SITE 1 AC2 5 ASP A 141 ASP A 169 ASN A 170 7JX A 302
SITE 2 AC2 5 HOH A 412
SITE 1 AC3 8 ASP A 141 HIS A 142 LYS A 144 ASP A 169
SITE 2 AC3 8 ASN A 170 SAH A 300 MG A 301 HOH A 402
SITE 1 AC4 6 VAL A 183 ARG A 184 SER A 186 PHE A 189
SITE 2 AC4 6 HOH A 437 HOH A 441
SITE 1 AC5 17 LYS B 46 GLY B 66 ALA B 67 TYR B 68
SITE 2 AC5 17 TYR B 71 SER B 72 GLU B 90 ILE B 91
SITE 3 AC5 17 GLY B 117 ALA B 118 SER B 119 GLN B 120
SITE 4 AC5 17 ASP B 141 TRP B 143 ARG B 146 HOH B 401
SITE 5 AC5 17 HOH B 414
SITE 1 AC6 6 VAL B 183 ARG B 184 SER B 186 PHE B 189
SITE 2 AC6 6 HOH B 440 HOH B 442
CRYST1 57.185 60.105 147.614 90.00 90.00 90.00 P 21 21 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 0.017487 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016638 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006774 0.00000
(ATOM LINES ARE NOT SHOWN.)
END