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HEADER HYDROLASE 17-NOV-21 7QAK
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 7-[(4-
TITLE 2 {[BENZYL(METHYL)AMINO]METHYL}BENZYL)OXY]-4-(HYDROXYMETHYL)-2H-
TITLE 3 CHROMEN-2-ONE
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;
COMPND 7 OTHER_DETAILS: FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 32-574
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: HEK293
KEYWDS INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.EKSTROM,N.FORSGREN
REVDAT 1 06-APR-22 7QAK 0
JRNL AUTH F.EKSTROM,A.GOTTINGER,N.FORSGREN,M.CATTO,L.G.IACOVINO,
JRNL AUTH 2 L.PISANI,C.BINDA
JRNL TITL DUAL REVERSIBLE COUMARIN INHIBITORS MUTUALLY BOUND TO
JRNL TITL 2 MONOAMINE OXIDASE B AND ACETYLCHOLINESTERASE CRYSTAL
JRNL TITL 3 STRUCTURES.
JRNL REF ACS MED.CHEM.LETT. V. 13 499 2022
JRNL REFN ISSN 1948-5875
JRNL PMID 35300078
JRNL DOI 10.1021/ACSMEDCHEMLETT.2C00001
REMARK 2
REMARK 2 RESOLUTION. 2.60 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.02
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.338
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 62454
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.995
REMARK 3 FREE R VALUE TEST SET COUNT : 1246
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 49.0197 - 5.4061 1.00 7155 140 0.1784 0.1889
REMARK 3 2 5.4061 - 4.2918 1.00 6889 134 0.1516 0.1675
REMARK 3 3 4.2918 - 3.7495 1.00 6839 141 0.1643 0.1975
REMARK 3 4 3.7495 - 3.4068 1.00 6784 138 0.1946 0.2462
REMARK 3 5 3.4068 - 3.1626 1.00 6789 128 0.2278 0.2669
REMARK 3 6 3.1626 - 2.9762 1.00 6705 147 0.2372 0.2777
REMARK 3 7 2.9762 - 2.8272 0.99 6712 135 0.2523 0.3273
REMARK 3 8 2.8272 - 2.7041 0.99 6649 133 0.2603 0.3266
REMARK 3 9 2.7041 - 2.6000 0.99 6686 150 0.2555 0.3115
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) : 0.309
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 58.52
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.62
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 : 0.003 8891
REMARK 3 ANGLE : 0.695 12109
REMARK 3 CHIRALITY : 0.049 1292
REMARK 3 PLANARITY : 0.006 1576
REMARK 3 DIHEDRAL : 10.471 7094
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 240 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9705 11.5492 28.3959
REMARK 3 T TENSOR
REMARK 3 T11: 0.4652 T22: 0.3531
REMARK 3 T33: 0.3964 T12: 0.0097
REMARK 3 T13: 0.0221 T23: 0.0308
REMARK 3 L TENSOR
REMARK 3 L11: 1.3279 L22: 1.2304
REMARK 3 L33: 3.7311 L12: 0.0245
REMARK 3 L13: -0.1551 L23: -0.4533
REMARK 3 S TENSOR
REMARK 3 S11: -0.1077 S12: -0.1337 S13: -0.0080
REMARK 3 S21: 0.1698 S22: 0.0126 S23: -0.0892
REMARK 3 S31: 0.1639 S32: 0.0545 S33: 0.1023
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6980 10.5720 11.0946
REMARK 3 T TENSOR
REMARK 3 T11: 0.5375 T22: 0.4332
REMARK 3 T33: 0.3938 T12: 0.1012
REMARK 3 T13: 0.0617 T23: 0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 5.5385 L22: 1.3634
REMARK 3 L33: 2.7125 L12: 1.8305
REMARK 3 L13: 0.0567 L23: -0.1165
REMARK 3 S TENSOR
REMARK 3 S11: -0.1347 S12: 0.3477 S13: -0.2666
REMARK 3 S21: -0.0823 S22: 0.0097 S23: -0.2895
REMARK 3 S31: 0.2413 S32: 0.3841 S33: 0.1306
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 332 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6037 17.5868 6.5445
REMARK 3 T TENSOR
REMARK 3 T11: 0.3740 T22: 0.4635
REMARK 3 T33: 0.4485 T12: -0.0609
REMARK 3 T13: -0.0005 T23: 0.0025
REMARK 3 L TENSOR
REMARK 3 L11: 1.3837 L22: 1.6011
REMARK 3 L33: 3.9996 L12: -0.1894
REMARK 3 L13: -0.0759 L23: -0.4619
REMARK 3 S TENSOR
REMARK 3 S11: -0.0851 S12: 0.1374 S13: -0.0453
REMARK 3 S21: -0.0965 S22: 0.0090 S23: 0.1825
REMARK 3 S31: 0.0746 S32: -0.3516 S33: 0.0687
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9542 1.5191 14.0716
REMARK 3 T TENSOR
REMARK 3 T11: 0.5936 T22: 0.7057
REMARK 3 T33: 0.6299 T12: -0.2777
REMARK 3 T13: 0.0702 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 7.2706 L22: 9.3973
REMARK 3 L33: 6.8895 L12: 0.4480
REMARK 3 L13: 4.6093 L23: -1.8099
REMARK 3 S TENSOR
REMARK 3 S11: -0.1364 S12: 0.0570 S13: -0.5301
REMARK 3 S21: 0.3784 S22: 0.2040 S23: 0.6971
REMARK 3 S31: 0.6444 S32: -1.7945 S33: -0.0006
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4293 6.5595 -0.7611
REMARK 3 T TENSOR
REMARK 3 T11: 0.5708 T22: 0.8135
REMARK 3 T33: 0.4446 T12: -0.0484
REMARK 3 T13: -0.0958 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 2.2280 L22: 3.4502
REMARK 3 L33: 3.3591 L12: -2.1592
REMARK 3 L13: -2.3804 L23: 3.1043
REMARK 3 S TENSOR
REMARK 3 S11: 0.0552 S12: -0.3386 S13: -0.0190
REMARK 3 S21: -0.2953 S22: -0.0402 S23: 0.1060
REMARK 3 S31: 0.0329 S32: 0.1930 S33: 0.0890
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3625 5.6308 -61.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.6508 T22: 0.5628
REMARK 3 T33: 0.5567 T12: 0.0267
REMARK 3 T13: -0.1315 T23: -0.1322
REMARK 3 L TENSOR
REMARK 3 L11: 6.8460 L22: 1.6495
REMARK 3 L33: 4.2629 L12: -0.9079
REMARK 3 L13: -1.6788 L23: 0.5136
REMARK 3 S TENSOR
REMARK 3 S11: 0.1050 S12: 0.4803 S13: 0.2359
REMARK 3 S21: -0.3047 S22: -0.1445 S23: 0.3893
REMARK 3 S31: -0.1063 S32: -0.6564 S33: 0.1220
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 158 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1558 0.9620 -51.1385
REMARK 3 T TENSOR
REMARK 3 T11: 0.4554 T22: 0.4859
REMARK 3 T33: 0.5144 T12: -0.0298
REMARK 3 T13: -0.0737 T23: -0.1151
REMARK 3 L TENSOR
REMARK 3 L11: 1.2829 L22: 2.3553
REMARK 3 L33: 3.8779 L12: -0.1139
REMARK 3 L13: 0.2671 L23: 0.4572
REMARK 3 S TENSOR
REMARK 3 S11: 0.0992 S12: 0.1955 S13: -0.1610
REMARK 3 S21: -0.1802 S22: -0.2525 S23: 0.4676
REMARK 3 S31: 0.3511 S32: -0.4100 S33: 0.1367
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 159 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3814 7.2308 -54.7412
REMARK 3 T TENSOR
REMARK 3 T11: 0.5434 T22: 0.5096
REMARK 3 T33: 0.5323 T12: -0.0243
REMARK 3 T13: -0.0273 T23: -0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 9.7149 L22: 6.0404
REMARK 3 L33: 5.5610 L12: -6.7108
REMARK 3 L13: 4.9491 L23: -4.2254
REMARK 3 S TENSOR
REMARK 3 S11: 0.3603 S12: 0.5398 S13: 0.2786
REMARK 3 S21: -0.5121 S22: -0.4647 S23: 0.0189
REMARK 3 S31: -0.2248 S32: 0.2492 S33: 0.0564
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 187 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8224 8.5002 -44.7045
REMARK 3 T TENSOR
REMARK 3 T11: 0.3821 T22: 0.3466
REMARK 3 T33: 0.3311 T12: -0.0458
REMARK 3 T13: -0.0188 T23: -0.0669
REMARK 3 L TENSOR
REMARK 3 L11: 2.9183 L22: 2.7131
REMARK 3 L33: 3.4996 L12: -1.0360
REMARK 3 L13: 0.1931 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: 0.1386 S12: 0.1771 S13: 0.0739
REMARK 3 S21: 0.0040 S22: -0.2013 S23: -0.0277
REMARK 3 S31: -0.1831 S32: 0.3068 S33: 0.0392
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 298 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6003 -9.8059 -46.8753
REMARK 3 T TENSOR
REMARK 3 T11: 0.7303 T22: 0.5933
REMARK 3 T33: 0.5652 T12: 0.1074
REMARK 3 T13: -0.1089 T23: -0.0543
REMARK 3 L TENSOR
REMARK 3 L11: 2.8795 L22: 3.4024
REMARK 3 L33: 4.5422 L12: -1.0877
REMARK 3 L13: -1.5780 L23: 2.2757
REMARK 3 S TENSOR
REMARK 3 S11: 0.0389 S12: 0.2336 S13: -0.1560
REMARK 3 S21: 0.0094 S22: 0.0438 S23: -0.2044
REMARK 3 S31: 0.3599 S32: 0.5367 S33: -0.0399
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 299 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9879 14.4262 -39.9577
REMARK 3 T TENSOR
REMARK 3 T11: 0.4924 T22: 0.4838
REMARK 3 T33: 0.4756 T12: -0.0515
REMARK 3 T13: -0.0632 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 5.0079 L22: 2.2600
REMARK 3 L33: 3.7113 L12: -2.5801
REMARK 3 L13: -1.6723 L23: 1.4374
REMARK 3 S TENSOR
REMARK 3 S11: 0.2509 S12: 0.3038 S13: 0.6331
REMARK 3 S21: -0.1277 S22: -0.1866 S23: -0.2173
REMARK 3 S31: -0.3493 S32: 0.4924 S33: -0.0609
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8264 -6.2008 -21.4696
REMARK 3 T TENSOR
REMARK 3 T11: 0.9263 T22: 0.5247
REMARK 3 T33: 0.4649 T12: -0.0312
REMARK 3 T13: 0.0266 T23: -0.0263
REMARK 3 L TENSOR
REMARK 3 L11: 5.0443 L22: 3.1853
REMARK 3 L33: 3.2798 L12: 0.2882
REMARK 3 L13: 0.8485 L23: -0.2863
REMARK 3 S TENSOR
REMARK 3 S11: 0.1897 S12: -0.1687 S13: -0.2908
REMARK 3 S21: 0.5269 S22: -0.0205 S23: -0.0185
REMARK 3 S31: 0.6912 S32: 0.0352 S33: -0.1653
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.4833 5.8007 -28.7948
REMARK 3 T TENSOR
REMARK 3 T11: 0.4972 T22: 0.5340
REMARK 3 T33: 0.4882 T12: -0.0706
REMARK 3 T13: 0.0776 T23: -0.1695
REMARK 3 L TENSOR
REMARK 3 L11: 1.7493 L22: 1.8708
REMARK 3 L33: 2.9815 L12: 0.0870
REMARK 3 L13: 0.3989 L23: -0.6141
REMARK 3 S TENSOR
REMARK 3 S11: 0.1594 S12: -0.2107 S13: 0.0068
REMARK 3 S21: 0.2820 S22: -0.1867 S23: 0.3646
REMARK 3 S31: 0.1277 S32: -0.3750 S33: 0.0244
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3845 22.4299 -28.5810
REMARK 3 T TENSOR
REMARK 3 T11: 0.7390 T22: 0.5452
REMARK 3 T33: 0.6778 T12: 0.0636
REMARK 3 T13: 0.0507 T23: -0.1586
REMARK 3 L TENSOR
REMARK 3 L11: 6.6192 L22: 8.7633
REMARK 3 L33: 5.6682 L12: 3.1576
REMARK 3 L13: -0.4761 L23: -1.1270
REMARK 3 S TENSOR
REMARK 3 S11: 0.0966 S12: -0.2837 S13: 0.9931
REMARK 3 S21: -0.2676 S22: 0.0689 S23: 0.8894
REMARK 3 S31: -0.5670 S32: -0.4305 S33: -0.2100
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9831 11.4479 -21.3818
REMARK 3 T TENSOR
REMARK 3 T11: 0.6992 T22: 0.6285
REMARK 3 T33: 0.4166 T12: -0.0682
REMARK 3 T13: 0.0456 T23: -0.0553
REMARK 3 L TENSOR
REMARK 3 L11: 4.4556 L22: 1.6915
REMARK 3 L33: 2.7783 L12: 0.4133
REMARK 3 L13: 3.1213 L23: 0.5461
REMARK 3 S TENSOR
REMARK 3 S11: 0.1636 S12: -0.2819 S13: -0.1208
REMARK 3 S21: 0.1563 S22: -0.1363 S23: 0.0770
REMARK 3 S31: 0.0891 S32: 0.1998 S33: -0.0061
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 7QAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1292119210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MAX IV
REMARK 200 BEAMLINE : BIOMAX
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 62618
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.07385
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.1300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.58530
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: PHENIX
REMARK 200 STARTING MODEL: 1J06
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) POLYETHYLENE GLYCOL 750
REMARK 280 MONOMETHYLETHER, 100 MM HEPES, PH 7.1, VAPOR DIFFUSION, HANGING
REMARK 280 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 39.22650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.35200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.35500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.35200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.22650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.35500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 GLU B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
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 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 GLU B 268 CG CD OE1 OE2
REMARK 470 ASP B 323 CG OD1 OD2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
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 PHE A 47 -1.68 72.46
REMARK 500 ASP A 95 93.55 -68.99
REMARK 500 CYS A 96 3.71 -150.03
REMARK 500 PHE A 158 -6.32 -143.36
REMARK 500 SER A 203 -123.07 58.81
REMARK 500 ASP A 306 -87.61 -134.18
REMARK 500 VAL A 407 -69.12 -126.22
REMARK 500 SER A 495 -56.31 -174.01
REMARK 500 ARG B 13 -9.51 -59.83
REMARK 500 ALA B 62 52.18 -105.88
REMARK 500 SER B 93 138.48 -170.05
REMARK 500 SER B 203 -123.49 57.87
REMARK 500 GLU B 285 -54.59 -27.61
REMARK 500 ASP B 306 -82.22 -122.72
REMARK 500 ASP B 323 30.66 -84.02
REMARK 500 TYR B 341 41.24 -109.91
REMARK 500 VAL B 367 72.53 -113.39
REMARK 500 VAL B 407 -61.75 -125.24
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 PG0 B 606
DBREF 7QAK A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7QAK 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 5IK A 603 31
HET EDO A 604 4
HET PG0 A 605 8
HET PG0 A 606 8
HET PG0 A 607 8
HET PG0 A 608 8
HET PG0 A 609 8
HET PG0 A 610 8
HET PG0 A 611 8
HET PG0 A 612 8
HET NAG B 601 14
HET NAG B 602 14
HET 5IK B 603 31
HET PG0 B 604 8
HET PG0 B 605 8
HET PG0 B 606 6
HET PG0 B 607 8
HET TOE B 608 11
HET P15 B 609 20
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM 5IK 4-(HYDROXYMETHYL)-7-[[4-[[METHYL-(PHENYLMETHYL)
HETNAM 2 5IK AMINO]METHYL]PHENYL]METHOXY]CHROMEN-2-ONE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM P15 2,5,8,11,14,17-HEXAOXANONADECAN-19-OL
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
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 5IK 2(C26 H25 N O4)
FORMUL 6 EDO C2 H6 O2
FORMUL 7 PG0 12(C5 H12 O3)
FORMUL 22 TOE C7 H16 O4
FORMUL 23 P15 C13 H28 O7
FORMUL 24 HOH *129(H2 O)
HELIX 1 AA1 ASP A 5 GLN A 7 5 3
HELIX 2 AA2 VAL A 42 ARG A 46 5 5
HELIX 3 AA3 PHE A 80 MET A 85 1 6
HELIX 4 AA4 LEU A 130 ASP A 134 5 5
HELIX 5 AA5 GLY A 135 GLY A 143 1 9
HELIX 6 AA6 VAL A 153 LEU A 159 1 7
HELIX 7 AA7 ASN A 170 ILE A 187 1 18
HELIX 8 AA8 ALA A 188 PHE A 190 5 3
HELIX 9 AA9 SER A 203 SER A 215 1 13
HELIX 10 AB1 SER A 215 SER A 220 1 6
HELIX 11 AB2 SER A 240 VAL A 255 1 16
HELIX 12 AB3 ASP A 266 ARG A 274 1 9
HELIX 13 AB4 PRO A 277 TRP A 286 1 10
HELIX 14 AB5 HIS A 287 LEU A 289 5 3
HELIX 15 AB6 THR A 311 GLY A 319 1 9
HELIX 16 AB7 GLY A 335 VAL A 340 1 6
HELIX 17 AB8 SER A 355 VAL A 367 1 13
HELIX 18 AB9 SER A 371 THR A 383 1 13
HELIX 19 AC1 ASP A 390 VAL A 407 1 18
HELIX 20 AC2 VAL A 407 GLN A 421 1 15
HELIX 21 AC3 PRO A 440 GLY A 444 5 5
HELIX 22 AC4 GLU A 450 PHE A 455 1 6
HELIX 23 AC5 GLY A 456 ASN A 464 5 9
HELIX 24 AC6 THR A 466 GLY A 487 1 22
HELIX 25 AC7 ARG A 525 ARG A 534 1 10
HELIX 26 AC8 ARG A 534 THR A 543 1 10
HELIX 27 AC9 ASP B 5 GLN B 7 5 3
HELIX 28 AD1 VAL B 42 ARG B 46 5 5
HELIX 29 AD2 PHE B 80 MET B 85 1 6
HELIX 30 AD3 LEU B 130 ASP B 134 5 5
HELIX 31 AD4 GLY B 135 GLU B 142 1 8
HELIX 32 AD5 VAL B 153 LEU B 159 1 7
HELIX 33 AD6 ASN B 170 ILE B 187 1 18
HELIX 34 AD7 ALA B 188 PHE B 190 5 3
HELIX 35 AD8 SER B 203 SER B 215 1 13
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 SER B 240 VAL B 255 1 16
HELIX 38 AE2 ASN B 265 ARG B 274 1 10
HELIX 39 AE3 PRO B 277 GLU B 285 1 9
HELIX 40 AE4 TRP B 286 LEU B 289 5 4
HELIX 41 AE5 THR B 311 GLY B 319 1 9
HELIX 42 AE6 GLY B 335 VAL B 340 1 6
HELIX 43 AE7 SER B 355 VAL B 367 1 13
HELIX 44 AE8 SER B 371 THR B 383 1 13
HELIX 45 AE9 ASP B 390 VAL B 407 1 18
HELIX 46 AF1 VAL B 407 GLN B 421 1 15
HELIX 47 AF2 PRO B 440 GLY B 444 5 5
HELIX 48 AF3 GLU B 450 PHE B 455 1 6
HELIX 49 AF4 GLY B 456 ASN B 464 5 9
HELIX 50 AF5 THR B 466 GLY B 487 1 22
HELIX 51 AF6 ARG B 525 ARG B 534 1 10
HELIX 52 AF7 ARG B 534 ALA B 542 1 9
SHEET 1 AA1 3 LEU A 9 VAL A 12 0
SHEET 2 AA1 3 GLY A 15 ARG A 18 -1 O LEU A 17 N VAL A 10
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 VAL A 101 N PHE A 32
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 TRP A 117 O VAL A 147
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 ARG A 224 N LEU A 199
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 ARG A 424 N VAL A 326
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 GLY B 15 N VAL B 12
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 VAL B 29 N LEU B 22
SHEET 3 AA511 TYR B 98 PRO B 104 -1 O VAL B 101 N PHE B 32
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 THR B 198 N VAL B 114
SHEET 7 AA511 ARG B 224 GLN B 228 1 O ARG B 224 N LEU B 199
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 ARG B 424 N VAL B 326
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
SSBOND 1 CYS A 69 CYS A 96 1555 1555 2.04
SSBOND 2 CYS A 257 CYS A 272 1555 1555 2.03
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.03
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.04
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.44
LINK ND2 ASN A 464 C1 NAG A 602 1555 1555 1.42
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.40
LINK ND2 ASN B 464 C1 NAG B 602 1555 1555 1.44
CISPEP 1 TYR A 105 PRO A 106 0 -1.47
CISPEP 2 TYR B 105 PRO B 106 0 4.16
CISPEP 3 SER B 497 PRO B 498 0 8.69
CRYST1 78.453 112.710 226.704 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 0.012746 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004411 0.00000
TER 4197 THR A 543
TER 8392 THR B 543
MASTER 495 0 21 52 32 0 0 6 8723 2 263 84
END |