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HEADER HYDROLASE 07-NOV-19 6TD2
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-(DIETHYLAMINO)
TITLE 2 ETHYL)-1-(4-(TRIFLUOROMETHYL)PHENYL)METHANESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ACHE;
COMPND 5 EC: 3.1.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: ACHE;
SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293F
KEYWDS COMPLEX, INHIBITOR, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.FORSGREN,F.EKSTROM
REVDAT 1 14-OCT-20 6TD2 0
JRNL AUTH C.D.ANDERSSON,B.K.MISHRA,N.FORSGREN,F.EKSTROM,A.LINUSSON
JRNL TITL PHYSICAL MECHANISMS GOVERNING SUBSTITUENT EFFECTS ON
JRNL TITL 2 ARENE-ARENE INTERACTIONS IN A PROTEIN MILIEU.
JRNL REF J.PHYS.CHEM.B V. 124 6529 2020
JRNL REFN ISSN 1089-5647
JRNL PMID 32610016
JRNL DOI 10.1021/ACS.JPCB.0C03778
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.12_2829
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.85
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.338
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 49947
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.964
REMARK 3 FREE R VALUE TEST SET COUNT : 981
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 28.8500 - 5.3465 0.96 7106 143 0.1595 0.1780
REMARK 3 2 5.3465 - 4.2480 0.99 7049 140 0.1310 0.1437
REMARK 3 3 4.2480 - 3.7123 0.99 6994 132 0.1521 0.2220
REMARK 3 4 3.7123 - 3.3735 1.00 7015 144 0.1777 0.2438
REMARK 3 5 3.3735 - 3.1320 1.00 6974 130 0.2271 0.2804
REMARK 3 6 3.1320 - 2.9475 1.00 6906 155 0.2364 0.2781
REMARK 3 7 2.9475 - 2.8000 1.00 6922 137 0.2646 0.3100
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.304
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.826
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.89
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 : 0.008 8823
REMARK 3 ANGLE : 0.994 12038
REMARK 3 CHIRALITY : 0.057 1285
REMARK 3 PLANARITY : 0.007 1572
REMARK 3 DIHEDRAL : 11.318 7094
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 18
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.9887 13.0591 41.4657
REMARK 3 T TENSOR
REMARK 3 T11: 0.4525 T22: 0.2779
REMARK 3 T33: 0.2604 T12: -0.0148
REMARK 3 T13: -0.0386 T23: -0.0165
REMARK 3 L TENSOR
REMARK 3 L11: 3.8626 L22: 1.9726
REMARK 3 L33: 5.6625 L12: -1.0556
REMARK 3 L13: -0.5910 L23: -0.9391
REMARK 3 S TENSOR
REMARK 3 S11: -0.2653 S12: -0.5074 S13: 0.0911
REMARK 3 S21: 0.5785 S22: 0.1653 S23: 0.0197
REMARK 3 S31: -0.1018 S32: -0.0759 S33: 0.0094
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0081 15.9018 27.7083
REMARK 3 T TENSOR
REMARK 3 T11: 0.3075 T22: 0.2997
REMARK 3 T33: 0.1991 T12: 0.0326
REMARK 3 T13: -0.0411 T23: -0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 2.6197 L22: 1.5872
REMARK 3 L33: 2.6267 L12: 0.1742
REMARK 3 L13: -0.4940 L23: -0.0450
REMARK 3 S TENSOR
REMARK 3 S11: -0.0807 S12: -0.2970 S13: 0.0882
REMARK 3 S21: 0.2129 S22: 0.0158 S23: -0.0591
REMARK 3 S31: -0.0386 S32: 0.1057 S33: 0.0520
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.1548 2.9628 21.1334
REMARK 3 T TENSOR
REMARK 3 T11: 0.3407 T22: 0.2611
REMARK 3 T33: 0.2685 T12: 0.0352
REMARK 3 T13: -0.0209 T23: 0.0465
REMARK 3 L TENSOR
REMARK 3 L11: 1.7511 L22: 2.1573
REMARK 3 L33: 4.9431 L12: 0.6327
REMARK 3 L13: -1.2260 L23: -0.7195
REMARK 3 S TENSOR
REMARK 3 S11: -0.1301 S12: -0.1695 S13: -0.2862
REMARK 3 S21: 0.0482 S22: 0.0779 S23: -0.1305
REMARK 3 S31: 0.6966 S32: -0.0308 S33: 0.0525
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 277 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0339 13.8955 12.2105
REMARK 3 T TENSOR
REMARK 3 T11: 0.2957 T22: 0.5673
REMARK 3 T33: 0.4372 T12: 0.0399
REMARK 3 T13: 0.0811 T23: 0.1247
REMARK 3 L TENSOR
REMARK 3 L11: 2.3653 L22: 5.3859
REMARK 3 L33: 8.2190 L12: -0.8944
REMARK 3 L13: 2.7481 L23: 1.5925
REMARK 3 S TENSOR
REMARK 3 S11: 0.1102 S12: 0.2346 S13: -0.0377
REMARK 3 S21: -0.5935 S22: -0.3495 S23: -0.9214
REMARK 3 S31: 0.0070 S32: 1.2704 S33: 0.2154
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 278 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 37.2418 8.0105 9.3267
REMARK 3 T TENSOR
REMARK 3 T11: 0.3674 T22: 0.4053
REMARK 3 T33: 0.2150 T12: 0.0875
REMARK 3 T13: 0.1176 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 3.9545 L22: 4.1097
REMARK 3 L33: 3.6427 L12: 1.5322
REMARK 3 L13: 2.3198 L23: 1.7849
REMARK 3 S TENSOR
REMARK 3 S11: -0.0252 S12: 0.0923 S13: -0.2692
REMARK 3 S21: -0.0090 S22: -0.0265 S23: -0.2318
REMARK 3 S31: 0.3922 S32: 0.1793 S33: 0.0424
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0433 17.0341 6.2351
REMARK 3 T TENSOR
REMARK 3 T11: 0.2089 T22: 0.3218
REMARK 3 T33: 0.2541 T12: -0.0268
REMARK 3 T13: -0.0406 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 1.9393 L22: 1.9581
REMARK 3 L33: 4.1014 L12: -0.3322
REMARK 3 L13: -0.0617 L23: -0.7380
REMARK 3 S TENSOR
REMARK 3 S11: -0.0185 S12: 0.0971 S13: 0.0488
REMARK 3 S21: -0.1274 S22: 0.0834 S23: 0.1957
REMARK 3 S31: 0.0686 S32: -0.3761 S33: -0.0559
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0698 1.4046 13.4500
REMARK 3 T TENSOR
REMARK 3 T11: 0.4529 T22: 0.5552
REMARK 3 T33: 0.5294 T12: -0.2304
REMARK 3 T13: -0.0061 T23: 0.0832
REMARK 3 L TENSOR
REMARK 3 L11: 5.2256 L22: 8.4929
REMARK 3 L33: 4.0099 L12: 0.2285
REMARK 3 L13: 3.9053 L23: -2.0373
REMARK 3 S TENSOR
REMARK 3 S11: 0.0205 S12: -0.1200 S13: -0.6596
REMARK 3 S21: 0.2161 S22: 0.3065 S23: 1.0916
REMARK 3 S31: 0.5415 S32: -1.1830 S33: -0.1740
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6597 6.4548 -1.3024
REMARK 3 T TENSOR
REMARK 3 T11: 0.4572 T22: 0.6728
REMARK 3 T33: 0.3263 T12: -0.0015
REMARK 3 T13: -0.1765 T23: 0.0690
REMARK 3 L TENSOR
REMARK 3 L11: 3.0852 L22: 3.1151
REMARK 3 L33: 8.6278 L12: -1.4433
REMARK 3 L13: -5.0418 L23: 3.2453
REMARK 3 S TENSOR
REMARK 3 S11: 0.0106 S12: 0.1087 S13: -0.1277
REMARK 3 S21: -0.4794 S22: 0.0211 S23: 0.2709
REMARK 3 S31: 0.0446 S32: -0.2153 S33: 0.0031
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5392 6.3729 -62.0030
REMARK 3 T TENSOR
REMARK 3 T11: 0.4891 T22: 0.4954
REMARK 3 T33: 0.3706 T12: 0.0316
REMARK 3 T13: -0.0984 T23: -0.1431
REMARK 3 L TENSOR
REMARK 3 L11: 6.8246 L22: 2.2202
REMARK 3 L33: 5.6757 L12: -1.1690
REMARK 3 L13: -2.9648 L23: 0.6507
REMARK 3 S TENSOR
REMARK 3 S11: 0.0668 S12: 0.7154 S13: 0.0900
REMARK 3 S21: -0.2822 S22: -0.1759 S23: 0.3263
REMARK 3 S31: -0.0077 S32: -1.0163 S33: 0.0908
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 86 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3343 -4.0396 -53.1766
REMARK 3 T TENSOR
REMARK 3 T11: 0.4719 T22: 0.6215
REMARK 3 T33: 0.3024 T12: -0.0429
REMARK 3 T13: -0.0787 T23: -0.0745
REMARK 3 L TENSOR
REMARK 3 L11: 0.7699 L22: 2.2255
REMARK 3 L33: 3.3214 L12: -0.4962
REMARK 3 L13: -0.3078 L23: 0.3980
REMARK 3 S TENSOR
REMARK 3 S11: 0.2109 S12: 0.2151 S13: -0.1306
REMARK 3 S21: -0.1157 S22: -0.2230 S23: 0.1206
REMARK 3 S31: 0.6586 S32: -0.0727 S33: -0.0433
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 87 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2066 6.0204 -53.9496
REMARK 3 T TENSOR
REMARK 3 T11: 0.4490 T22: 0.5957
REMARK 3 T33: 0.3001 T12: 0.0794
REMARK 3 T13: -0.1310 T23: -0.1085
REMARK 3 L TENSOR
REMARK 3 L11: 2.3968 L22: 2.7476
REMARK 3 L33: 2.1240 L12: 0.4718
REMARK 3 L13: -0.7811 L23: 1.0218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0224 S12: 0.5917 S13: 0.0714
REMARK 3 S21: -0.3898 S22: -0.2735 S23: 0.4460
REMARK 3 S31: 0.1665 S32: -0.3089 S33: 0.1976
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 170 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5598 3.0552 -48.9757
REMARK 3 T TENSOR
REMARK 3 T11: 0.3983 T22: 0.4208
REMARK 3 T33: 0.2057 T12: -0.0061
REMARK 3 T13: -0.0212 T23: -0.0463
REMARK 3 L TENSOR
REMARK 3 L11: 4.9557 L22: 1.6805
REMARK 3 L33: 1.7791 L12: -0.9845
REMARK 3 L13: 1.5499 L23: 0.4738
REMARK 3 S TENSOR
REMARK 3 S11: 0.1905 S12: 0.6299 S13: -0.1735
REMARK 3 S21: -0.1145 S22: -0.1753 S23: 0.0545
REMARK 3 S31: 0.1258 S32: 0.0187 S33: -0.0391
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 318 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2785 4.6315 -46.6304
REMARK 3 T TENSOR
REMARK 3 T11: 0.3417 T22: 0.4798
REMARK 3 T33: 0.2401 T12: 0.0213
REMARK 3 T13: -0.0217 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 2.1140 L22: 2.9547
REMARK 3 L33: 3.0502 L12: -1.2144
REMARK 3 L13: 0.0796 L23: 0.7906
REMARK 3 S TENSOR
REMARK 3 S11: 0.1080 S12: 0.1974 S13: -0.0423
REMARK 3 S21: 0.0062 S22: 0.0314 S23: -0.2623
REMARK 3 S31: 0.1714 S32: 0.5280 S33: -0.1328
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 319 THROUGH 348 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5659 4.6141 -31.6541
REMARK 3 T TENSOR
REMARK 3 T11: 0.3194 T22: 0.2838
REMARK 3 T33: 0.2577 T12: -0.0569
REMARK 3 T13: -0.0234 T23: -0.0738
REMARK 3 L TENSOR
REMARK 3 L11: 2.6422 L22: 5.7655
REMARK 3 L33: 5.6005 L12: -2.5978
REMARK 3 L13: 0.7147 L23: -2.2099
REMARK 3 S TENSOR
REMARK 3 S11: 0.0960 S12: -0.0813 S13: -0.1715
REMARK 3 S21: -0.2222 S22: -0.0931 S23: -0.1463
REMARK 3 S31: 0.4093 S32: 0.0093 S33: 0.0115
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 349 THROUGH 440 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.2855 1.3110 -22.3777
REMARK 3 T TENSOR
REMARK 3 T11: 0.5370 T22: 0.4033
REMARK 3 T33: 0.2612 T12: -0.0454
REMARK 3 T13: -0.0361 T23: -0.0608
REMARK 3 L TENSOR
REMARK 3 L11: 2.1696 L22: 1.9578
REMARK 3 L33: 2.5332 L12: -0.4291
REMARK 3 L13: 0.6506 L23: -0.1167
REMARK 3 S TENSOR
REMARK 3 S11: 0.1548 S12: -0.3288 S13: -0.2903
REMARK 3 S21: 0.2974 S22: -0.0054 S23: -0.0127
REMARK 3 S31: 0.5929 S32: 0.0339 S33: -0.1527
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.4938 7.0100 -35.5012
REMARK 3 T TENSOR
REMARK 3 T11: 0.3490 T22: 0.5240
REMARK 3 T33: 0.3548 T12: -0.0372
REMARK 3 T13: -0.0028 T23: -0.1328
REMARK 3 L TENSOR
REMARK 3 L11: 1.8469 L22: 5.9617
REMARK 3 L33: 5.9452 L12: -0.9242
REMARK 3 L13: 1.1148 L23: -2.6045
REMARK 3 S TENSOR
REMARK 3 S11: -0.0774 S12: -0.1710 S13: -0.0613
REMARK 3 S21: 0.2060 S22: 0.1635 S23: 0.4366
REMARK 3 S31: 0.1862 S32: -1.2257 S33: -0.0604
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.5603 22.7729 -28.9379
REMARK 3 T TENSOR
REMARK 3 T11: 0.5162 T22: 0.5210
REMARK 3 T33: 0.4175 T12: 0.0790
REMARK 3 T13: 0.0759 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 4.7904 L22: 4.9988
REMARK 3 L33: 2.2340 L12: -0.8083
REMARK 3 L13: 1.4979 L23: -0.5531
REMARK 3 S TENSOR
REMARK 3 S11: 0.2639 S12: -0.4001 S13: 0.7838
REMARK 3 S21: 0.4964 S22: 0.0197 S23: 0.7367
REMARK 3 S31: -0.7992 S32: -0.5824 S33: -0.2558
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.7391 11.7701 -21.7537
REMARK 3 T TENSOR
REMARK 3 T11: 0.5989 T22: 0.4660
REMARK 3 T33: 0.2093 T12: -0.0543
REMARK 3 T13: 0.0085 T23: -0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 6.3131 L22: 1.8315
REMARK 3 L33: 4.6278 L12: -0.3227
REMARK 3 L13: 5.3707 L23: -0.3320
REMARK 3 S TENSOR
REMARK 3 S11: -0.1007 S12: 0.1704 S13: -0.1603
REMARK 3 S21: 0.3276 S22: -0.0935 S23: -0.1271
REMARK 3 S31: -0.0436 S32: 0.3485 S33: 0.2158
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6TD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-NOV-19.
REMARK 100 THE DEPOSITION ID IS D_1292105261.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX II
REMARK 200 BEAMLINE : I911-5
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.041
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 50138
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 28.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.49400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 1JO6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30 % (W/V) PEG750MME 0.1 M HEPES PH
REMARK 280 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 39.47850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.71450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.97850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.71450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.47850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.97850
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 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 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 PRO A 259
REMARK 465 GLY A 260
REMARK 465 GLY A 261
REMARK 465 ALA A 262
REMARK 465 GLY A 263
REMARK 465 GLY A 264
REMARK 465 THR A 543
REMARK 465 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 PRO B 258
REMARK 465 PRO B 259
REMARK 465 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
REMARK 465 THR B 543
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 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 GLU B 268 CG CD OE1 OE2
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 CYS A 96 4.04 -157.65
REMARK 500 PRO A 104 154.64 -47.95
REMARK 500 ALA A 167 66.50 -163.48
REMARK 500 SER A 203 -126.85 57.23
REMARK 500 ASP A 306 -89.29 -143.54
REMARK 500 ASP A 488 114.62 -169.53
REMARK 500 LEU A 524 92.67 -69.40
REMARK 500 ARG A 525 57.74 29.50
REMARK 500 SER A 541 32.85 -83.83
REMARK 500 PHE B 123 11.39 56.90
REMARK 500 ALA B 167 64.19 -161.99
REMARK 500 SER B 203 -128.33 56.08
REMARK 500 THR B 275 46.87 -89.12
REMARK 500 ASP B 306 -83.06 -139.80
REMARK 500 THR B 318 -14.06 -142.50
REMARK 500 ASP B 323 34.79 -85.21
REMARK 500 TYR B 341 40.87 -106.16
REMARK 500 VAL B 407 -64.75 -124.74
REMARK 500 GLN B 421 46.67 -104.57
REMARK 500 HIS B 447 117.09 -39.35
REMARK 500 PRO B 498 103.11 -55.04
REMARK 500 ASN B 514 -167.65 -167.63
REMARK 500 SER B 541 48.57 -76.30
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PE4 A 610
DBREF 6TD2 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 6TD2 B 1 543 UNP P21836 ACES_MOUSE 32 574
SEQRES 1 A 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 A 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 A 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 A 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 A 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 A 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 A 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 A 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 A 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 A 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 A 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 A 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 A 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 A 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 A 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 A 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 A 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 A 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 A 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 A 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 A 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 A 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 A 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 A 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 A 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 A 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 A 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 A 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 A 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 A 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 A 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 A 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 A 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 A 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 A 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 A 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 A 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 A 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 A 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 A 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 A 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 A 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
SEQRES 1 B 543 GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG
SEQRES 2 B 543 GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY
SEQRES 3 B 543 GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU
SEQRES 4 B 543 PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO
SEQRES 5 B 543 LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE
SEQRES 6 B 543 GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO
SEQRES 7 B 543 GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU
SEQRES 8 B 543 LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO
SEQRES 9 B 543 TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP
SEQRES 10 B 543 ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU
SEQRES 11 B 543 ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY
SEQRES 12 B 543 ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE
SEQRES 13 B 543 GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY
SEQRES 14 B 543 ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP
SEQRES 15 B 543 VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET
SEQRES 16 B 543 SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER
SEQRES 17 B 543 VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU
SEQRES 18 B 543 PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY
SEQRES 19 B 543 PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG
SEQRES 20 B 543 ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY
SEQRES 21 B 543 GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU
SEQRES 22 B 543 ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP
SEQRES 23 B 543 HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE
SEQRES 24 B 543 VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO
SEQRES 25 B 543 GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN
SEQRES 26 B 543 VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE
SEQRES 27 B 543 LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU
SEQRES 28 B 543 SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG
SEQRES 29 B 543 ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA
SEQRES 30 B 543 VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP
SEQRES 31 B 543 PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY
SEQRES 32 B 543 ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY
SEQRES 33 B 543 ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE
SEQRES 34 B 543 PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP
SEQRES 35 B 543 MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE
SEQRES 36 B 543 GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU
SEQRES 37 B 543 GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR
SEQRES 38 B 543 ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP
SEQRES 39 B 543 SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA
SEQRES 40 B 543 GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL
SEQRES 41 B 543 ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN
SEQRES 42 B 543 ARG PHE LEU PRO LYS LEU LEU SER ALA THR
HET NAG A 601 14
HET NAG A 602 14
HET N2K A 603 22
HET EDO A 604 4
HET EDO A 605 4
HET EDO A 606 4
HET PG0 A 607 8
HET PG0 A 608 8
HET PG0 A 609 8
HET PE4 A 610 23
HET N2K B 601 22
HET EDO B 602 4
HET EDO B 603 4
HET EDO B 604 4
HET PG0 B 605 8
HET PG0 B 606 8
HET ETE B 607 14
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM N2K ~{N}-[2-(DIETHYLAMINO)ETHYL]-1-[4-(TRIFLUOROMETHYL)
HETNAM 2 N2K PHENYL]METHANESULFONAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETNAM ETE 2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN EDO ETHYLENE GLYCOL
HETSYN PG0 PEG 6000
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 3 NAG 2(C8 H15 N O6)
FORMUL 5 N2K 2(C14 H21 F3 N2 O2 S)
FORMUL 6 EDO 6(C2 H6 O2)
FORMUL 9 PG0 5(C5 H12 O3)
FORMUL 12 PE4 C16 H34 O8
FORMUL 19 ETE C9 H20 O5
FORMUL 20 HOH *170(H2 O)
HELIX 1 AA1 VAL A 42 ARG A 46 5 5
HELIX 2 AA2 PHE A 80 MET A 85 1 6
HELIX 3 AA3 LEU A 130 ASP A 134 5 5
HELIX 4 AA4 GLY A 135 GLY A 143 1 9
HELIX 5 AA5 VAL A 153 LEU A 159 1 7
HELIX 6 AA6 ASN A 170 ILE A 187 1 18
HELIX 7 AA7 ALA A 188 PHE A 190 5 3
HELIX 8 AA8 SER A 203 SER A 215 1 13
HELIX 9 AA9 LEU A 216 LEU A 221 5 6
HELIX 10 AB1 SER A 240 VAL A 255 1 16
HELIX 11 AB2 ASP A 266 ARG A 274 1 9
HELIX 12 AB3 PRO A 277 GLU A 285 1 9
HELIX 13 AB4 TRP A 286 LEU A 289 5 4
HELIX 14 AB5 THR A 311 GLY A 319 1 9
HELIX 15 AB6 GLY A 335 VAL A 340 1 6
HELIX 16 AB7 SER A 355 VAL A 367 1 13
HELIX 17 AB8 SER A 371 THR A 383 1 13
HELIX 18 AB9 ASP A 390 VAL A 407 1 18
HELIX 19 AC1 VAL A 407 GLN A 421 1 15
HELIX 20 AC2 PRO A 440 GLY A 444 5 5
HELIX 21 AC3 GLU A 450 PHE A 455 1 6
HELIX 22 AC4 GLY A 456 ASN A 464 5 9
HELIX 23 AC5 THR A 466 GLY A 487 1 22
HELIX 24 AC6 ARG A 525 ARG A 534 1 10
HELIX 25 AC7 ARG A 534 SER A 541 1 8
HELIX 26 AC8 ASP B 5 GLN B 7 5 3
HELIX 27 AC9 VAL B 42 ARG B 46 5 5
HELIX 28 AD1 PHE B 80 MET B 85 1 6
HELIX 29 AD2 LEU B 130 ASP B 134 5 5
HELIX 30 AD3 GLY B 135 GLU B 142 1 8
HELIX 31 AD4 VAL B 153 LEU B 159 1 7
HELIX 32 AD5 ASN B 170 ILE B 187 1 18
HELIX 33 AD6 ALA B 188 PHE B 190 5 3
HELIX 34 AD7 SER B 203 SER B 215 1 13
HELIX 35 AD8 SER B 215 SER B 220 1 6
HELIX 36 AD9 ALA B 241 VAL B 255 1 15
HELIX 37 AE1 ASP B 266 THR B 275 1 10
HELIX 38 AE2 PRO B 277 ASP B 283 1 7
HELIX 39 AE3 HIS B 284 LEU B 289 5 6
HELIX 40 AE4 THR B 311 ASN B 317 1 7
HELIX 41 AE5 GLY B 335 VAL B 340 1 6
HELIX 42 AE6 SER B 355 VAL B 367 1 13
HELIX 43 AE7 SER B 371 THR B 383 1 13
HELIX 44 AE8 ASP B 390 VAL B 407 1 18
HELIX 45 AE9 VAL B 407 GLN B 421 1 15
HELIX 46 AF1 PRO B 440 GLY B 444 5 5
HELIX 47 AF2 GLU B 450 PHE B 455 1 6
HELIX 48 AF3 GLY B 456 ASN B 464 5 9
HELIX 49 AF4 THR B 466 GLY B 487 1 22
HELIX 50 AF5 ARG B 525 ARG B 534 1 10
HELIX 51 AF6 ARG B 534 SER B 541 1 8
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 AA1 3 VAL A 59 ASP A 61 1 O LEU A 60 N GLN A 16
SHEET 1 AA211 ILE A 20 ALA A 24 0
SHEET 2 AA211 GLY A 27 PRO A 36 -1 O ALA A 31 N ILE A 20
SHEET 3 AA211 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 AA211 VAL A 145 MET A 149 -1 O SER A 148 N ASN A 100
SHEET 5 AA211 THR A 112 ILE A 118 1 N LEU A 115 O VAL A 145
SHEET 6 AA211 GLY A 192 GLU A 202 1 O ASP A 193 N THR A 112
SHEET 7 AA211 ARG A 224 GLN A 228 1 O GLN A 228 N GLY A 201
SHEET 8 AA211 GLN A 325 VAL A 331 1 O LEU A 327 N LEU A 227
SHEET 9 AA211 ARG A 424 PHE A 430 1 O PHE A 430 N VAL A 330
SHEET 10 AA211 GLN A 509 LEU A 513 1 O LEU A 513 N ILE A 429
SHEET 11 AA211 GLU A 519 ARG A 522 -1 O ARG A 521 N TYR A 510
SHEET 1 AA3 2 VAL A 68 CYS A 69 0
SHEET 2 AA3 2 LEU A 92 SER A 93 1 O SER A 93 N VAL A 68
SHEET 1 AA4 3 LEU B 9 VAL B 12 0
SHEET 2 AA4 3 GLY B 15 ARG B 18 -1 O LEU B 17 N VAL B 10
SHEET 3 AA4 3 VAL B 59 ASP B 61 1 O LEU B 60 N GLN B 16
SHEET 1 AA511 ILE B 20 ALA B 24 0
SHEET 2 AA511 GLY B 27 PRO B 36 -1 O GLY B 27 N ALA B 24
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 AA511 VAL B 145 MET B 149 -1 O SER B 148 N ASN B 100
SHEET 5 AA511 THR B 112 ILE B 118 1 N TRP B 117 O VAL B 147
SHEET 6 AA511 GLY B 192 GLU B 202 1 O SER B 196 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O GLN B 228 N GLY B 201
SHEET 8 AA511 GLN B 325 VAL B 331 1 O LEU B 327 N LEU B 227
SHEET 9 AA511 ARG B 424 PHE B 430 1 O PHE B 430 N VAL B 330
SHEET 10 AA511 GLN B 509 LEU B 513 1 O LEU B 513 N ILE B 429
SHEET 11 AA511 GLU B 519 ARG B 522 -1 O ARG B 521 N TYR B 510
SHEET 1 AA6 2 VAL B 68 CYS B 69 0
SHEET 2 AA6 2 LEU B 92 SER B 93 1 O SER B 93 N VAL B 68
SHEET 1 AA7 2 VAL B 239 SER B 240 0
SHEET 2 AA7 2 VAL B 302 VAL B 303 1 O VAL B 303 N VAL B 239
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.05
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.07
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.05
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.10
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.05
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 464 C1 NAG A 602 1555 1555 1.46
CISPEP 1 TYR A 105 PRO A 106 0 -2.41
CISPEP 2 TYR B 105 PRO B 106 0 3.55
CRYST1 78.957 111.957 227.429 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 0.012665 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008932 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004397 0.00000
TER 4220 ALA A 542
TER 8398 ALA B 542
MASTER 552 0 17 51 34 0 0 6 8670 2 187 84
END |