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HEADER HYDROLASE 18-NOV-21 7QB4
TITLE MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 7-[(1-
TITLE 2 BENZYLPIPERIDIN-3-YL)METHOXY]-3,4-DIMETHYL-2H-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
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 INHIBITOR, COMPLEX, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.J.EKSTROM,N.FORSGREN
REVDAT 1 06-APR-22 7QB4 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 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.V.AFONINE
REMARK 1 TITL TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH
REMARK 1 TITL 2 PHENIX.REFINE.
REMARK 1 REF ACTA CRYSTALLOGR., SECT. D: V. 68 352 2012
REMARK 1 REF 2 BIOL. CRYSTALLOGR.
REMARK 1 REFN ISSN 0907-4449
REMARK 2
REMARK 2 RESOLUTION. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.336
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 69765
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.001
REMARK 3 FREE R VALUE TEST SET COUNT : 1396
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 46.1910 - 5.3835 1.00 7227 142 0.1722 0.1955
REMARK 3 2 5.3835 - 4.2741 1.00 6970 136 0.1462 0.1481
REMARK 3 3 4.2741 - 3.7341 1.00 6928 134 0.1623 0.1912
REMARK 3 4 3.7341 - 3.3928 1.00 6847 147 0.1916 0.2367
REMARK 3 5 3.3928 - 3.1496 1.00 6846 123 0.2120 0.2732
REMARK 3 6 3.1496 - 2.9640 0.99 6751 149 0.2193 0.2360
REMARK 3 7 2.9640 - 2.8156 0.99 6765 139 0.2285 0.3159
REMARK 3 8 2.8156 - 2.6930 0.98 6701 134 0.2383 0.3015
REMARK 3 9 2.6930 - 2.5894 0.98 6685 147 0.2421 0.2908
REMARK 3 10 2.5894 - 2.5000 0.98 6649 145 0.2626 0.2886
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) : 0.255
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.774
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 68.91
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 : 0.005 8877
REMARK 3 ANGLE : 0.730 12081
REMARK 3 CHIRALITY : 0.046 1289
REMARK 3 PLANARITY : 0.005 1574
REMARK 3 DIHEDRAL : 16.118 5227
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 14
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 214 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1919 12.1471 29.7719
REMARK 3 T TENSOR
REMARK 3 T11: 0.5127 T22: 0.4467
REMARK 3 T33: 0.3871 T12: 0.0161
REMARK 3 T13: -0.0157 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.1562 L22: 1.6076
REMARK 3 L33: 3.1433 L12: -0.0799
REMARK 3 L13: 0.2004 L23: -0.2010
REMARK 3 S TENSOR
REMARK 3 S11: -0.0599 S12: -0.2138 S13: 0.0310
REMARK 3 S21: 0.2400 S22: 0.0126 S23: -0.0140
REMARK 3 S31: 0.0922 S32: -0.0210 S33: 0.0520
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 215 THROUGH 324 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9261 8.3741 11.8402
REMARK 3 T TENSOR
REMARK 3 T11: 0.4921 T22: 0.4053
REMARK 3 T33: 0.3751 T12: 0.1011
REMARK 3 T13: 0.0370 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 4.3300 L22: 2.0048
REMARK 3 L33: 2.8302 L12: 1.2738
REMARK 3 L13: 0.2167 L23: -0.0289
REMARK 3 S TENSOR
REMARK 3 S11: -0.0886 S12: 0.2637 S13: -0.3604
REMARK 3 S21: -0.0903 S22: 0.0498 S23: -0.2086
REMARK 3 S31: 0.4140 S32: 0.2143 S33: 0.0325
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 366 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8070 22.2375 1.2919
REMARK 3 T TENSOR
REMARK 3 T11: 0.4045 T22: 0.5230
REMARK 3 T33: 0.4377 T12: -0.0377
REMARK 3 T13: -0.0210 T23: 0.0314
REMARK 3 L TENSOR
REMARK 3 L11: 1.3114 L22: 7.7758
REMARK 3 L33: 4.4810 L12: 1.7934
REMARK 3 L13: -0.7859 L23: -2.9521
REMARK 3 S TENSOR
REMARK 3 S11: 0.0564 S12: -0.0232 S13: 0.1680
REMARK 3 S21: 0.4047 S22: -0.0169 S23: -0.0205
REMARK 3 S31: -0.5729 S32: 0.0524 S33: -0.0141
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 367 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.7918 15.1399 8.5566
REMARK 3 T TENSOR
REMARK 3 T11: 0.3311 T22: 0.4562
REMARK 3 T33: 0.4287 T12: -0.0489
REMARK 3 T13: -0.0312 T23: 0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 1.4698 L22: 2.0564
REMARK 3 L33: 5.3439 L12: -0.3313
REMARK 3 L13: 0.1809 L23: 0.1592
REMARK 3 S TENSOR
REMARK 3 S11: -0.0426 S12: 0.0693 S13: -0.0360
REMARK 3 S21: -0.1561 S22: 0.0174 S23: 0.3175
REMARK 3 S31: -0.0039 S32: -0.5942 S33: 0.0232
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7795 1.3432 13.9327
REMARK 3 T TENSOR
REMARK 3 T11: 0.6896 T22: 0.9000
REMARK 3 T33: 0.6871 T12: -0.3336
REMARK 3 T13: 0.0495 T23: 0.0804
REMARK 3 L TENSOR
REMARK 3 L11: 2.6476 L22: 4.6513
REMARK 3 L33: 7.9100 L12: -0.7081
REMARK 3 L13: 2.6872 L23: -0.8772
REMARK 3 S TENSOR
REMARK 3 S11: -0.1259 S12: -0.0008 S13: -0.7357
REMARK 3 S21: 0.2946 S22: 0.1277 S23: 0.8549
REMARK 3 S31: 0.9771 S32: -1.8198 S33: 0.0777
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 514 THROUGH 542 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.4216 6.3489 -0.8599
REMARK 3 T TENSOR
REMARK 3 T11: 0.6306 T22: 0.7356
REMARK 3 T33: 0.4613 T12: -0.0214
REMARK 3 T13: -0.1373 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 3.5130 L22: 2.6379
REMARK 3 L33: 4.8360 L12: -1.1960
REMARK 3 L13: -3.2557 L23: 1.8878
REMARK 3 S TENSOR
REMARK 3 S11: 0.1655 S12: -0.0010 S13: 0.0122
REMARK 3 S21: -0.3599 S22: -0.0542 S23: 0.1343
REMARK 3 S31: 0.1797 S32: 0.1266 S33: -0.0595
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6783 5.9026 -61.6107
REMARK 3 T TENSOR
REMARK 3 T11: 0.6244 T22: 0.6209
REMARK 3 T33: 0.4739 T12: -0.0178
REMARK 3 T13: -0.0957 T23: -0.1213
REMARK 3 L TENSOR
REMARK 3 L11: 6.9886 L22: 2.9493
REMARK 3 L33: 6.5555 L12: -1.7753
REMARK 3 L13: -4.6996 L23: 1.8491
REMARK 3 S TENSOR
REMARK 3 S11: 0.0645 S12: 0.6886 S13: 0.1586
REMARK 3 S21: -0.4101 S22: -0.1661 S23: 0.2744
REMARK 3 S31: -0.0466 S32: -0.9472 S33: 0.0762
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 141 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8313 0.5324 -51.6306
REMARK 3 T TENSOR
REMARK 3 T11: 0.5422 T22: 0.5790
REMARK 3 T33: 0.4071 T12: -0.0785
REMARK 3 T13: -0.0661 T23: -0.0820
REMARK 3 L TENSOR
REMARK 3 L11: 0.6291 L22: 2.4215
REMARK 3 L33: 3.1928 L12: -0.0400
REMARK 3 L13: 0.0346 L23: 0.1802
REMARK 3 S TENSOR
REMARK 3 S11: 0.1906 S12: 0.2663 S13: -0.2853
REMARK 3 S21: -0.1219 S22: -0.2146 S23: 0.3106
REMARK 3 S31: 0.5495 S32: -0.3052 S33: 0.0034
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 142 THROUGH 255 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5182 7.8890 -48.4166
REMARK 3 T TENSOR
REMARK 3 T11: 0.4553 T22: 0.5059
REMARK 3 T33: 0.3532 T12: -0.0383
REMARK 3 T13: 0.0036 T23: -0.0540
REMARK 3 L TENSOR
REMARK 3 L11: 2.8484 L22: 3.2771
REMARK 3 L33: 2.8372 L12: -1.7430
REMARK 3 L13: 0.0894 L23: 0.2424
REMARK 3 S TENSOR
REMARK 3 S11: 0.2218 S12: 0.2833 S13: 0.0625
REMARK 3 S21: -0.2477 S22: -0.1368 S23: -0.1934
REMARK 3 S31: -0.1120 S32: 0.2731 S33: -0.0694
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 256 THROUGH 331 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9745 0.9555 -43.8712
REMARK 3 T TENSOR
REMARK 3 T11: 0.5485 T22: 0.5595
REMARK 3 T33: 0.3579 T12: 0.0416
REMARK 3 T13: -0.1185 T23: -0.0471
REMARK 3 L TENSOR
REMARK 3 L11: 2.7009 L22: 3.2631
REMARK 3 L33: 3.3118 L12: -0.7890
REMARK 3 L13: -1.0470 L23: 1.5534
REMARK 3 S TENSOR
REMARK 3 S11: 0.0840 S12: 0.1329 S13: -0.1530
REMARK 3 S21: -0.0947 S22: 0.0917 S23: -0.3428
REMARK 3 S31: 0.3054 S32: 0.6023 S33: -0.1595
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 332 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9032 -6.4197 -21.6874
REMARK 3 T TENSOR
REMARK 3 T11: 0.8999 T22: 0.4422
REMARK 3 T33: 0.4255 T12: 0.0017
REMARK 3 T13: -0.0549 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 4.3889 L22: 4.4985
REMARK 3 L33: 2.4591 L12: 0.6288
REMARK 3 L13: 0.1735 L23: 0.1007
REMARK 3 S TENSOR
REMARK 3 S11: 0.3147 S12: -0.2351 S13: -0.6106
REMARK 3 S21: 0.6493 S22: -0.1163 S23: -0.0256
REMARK 3 S31: 0.8476 S32: 0.0907 S33: -0.2241
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 486 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.5278 5.5739 -28.9795
REMARK 3 T TENSOR
REMARK 3 T11: 0.5644 T22: 0.4872
REMARK 3 T33: 0.4661 T12: -0.0766
REMARK 3 T13: 0.0277 T23: -0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 2.3964 L22: 1.5484
REMARK 3 L33: 2.9908 L12: 0.1951
REMARK 3 L13: 0.4766 L23: -0.2092
REMARK 3 S TENSOR
REMARK 3 S11: 0.2004 S12: -0.2606 S13: -0.1377
REMARK 3 S21: 0.2357 S22: -0.1038 S23: 0.2380
REMARK 3 S31: 0.2652 S32: -0.3520 S33: -0.1055
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 487 THROUGH 513 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3307 22.1727 -28.6145
REMARK 3 T TENSOR
REMARK 3 T11: 0.7457 T22: 0.4529
REMARK 3 T33: 0.5224 T12: 0.0637
REMARK 3 T13: 0.0252 T23: -0.1023
REMARK 3 L TENSOR
REMARK 3 L11: 9.9582 L22: 4.0855
REMARK 3 L33: 6.3776 L12: 1.5488
REMARK 3 L13: 1.7615 L23: -1.7910
REMARK 3 S TENSOR
REMARK 3 S11: -0.1317 S12: -0.5486 S13: 1.0562
REMARK 3 S21: 0.2058 S22: 0.0247 S23: 0.4099
REMARK 3 S31: -0.6823 S32: -0.4687 S33: 0.1526
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 514 THROUGH 543 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9926 11.1593 -21.4551
REMARK 3 T TENSOR
REMARK 3 T11: 0.7827 T22: 0.6419
REMARK 3 T33: 0.3970 T12: -0.0406
REMARK 3 T13: -0.0230 T23: -0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 5.2223 L22: 1.4286
REMARK 3 L33: 2.6963 L12: -0.5231
REMARK 3 L13: 2.7200 L23: 0.2153
REMARK 3 S TENSOR
REMARK 3 S11: 0.1482 S12: 0.2444 S13: -0.2366
REMARK 3 S21: 0.0653 S22: -0.0980 S23: 0.0245
REMARK 3 S31: 0.2589 S32: 0.2789 S33: -0.0340
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 7QB4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1292119236.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.1
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 : 70307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 46.191
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.27440
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.0500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.63000
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 (%): 70.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.22
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 39.70300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 113.54600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.52400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 113.54600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.70300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.52400
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 GLY B 260
REMARK 465 GLY B 261
REMARK 465 ALA B 262
REMARK 465 GLY B 263
REMARK 465 GLY B 264
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 81 CG CD OE1 OE2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 496 CG CD CE NZ
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 SER A 44 2.49 -69.78
REMARK 500 PHE A 47 -5.88 77.03
REMARK 500 THR A 75 14.27 -140.72
REMARK 500 CYS A 96 8.01 -150.97
REMARK 500 PHE A 158 -5.99 -144.71
REMARK 500 ALA A 167 64.74 -154.87
REMARK 500 SER A 203 -125.35 52.04
REMARK 500 ASP A 306 -85.39 -126.74
REMARK 500 VAL A 367 61.99 -119.56
REMARK 500 HIS A 387 58.79 -144.96
REMARK 500 VAL A 407 -60.32 -128.97
REMARK 500 ASP A 494 98.46 -61.37
REMARK 500 ARG A 525 58.18 38.41
REMARK 500 ALA A 542 -77.49 -89.36
REMARK 500 ALA B 62 51.91 -115.50
REMARK 500 SER B 93 140.24 -173.03
REMARK 500 PHE B 158 -2.37 -140.35
REMARK 500 ALA B 167 83.03 -150.10
REMARK 500 SER B 203 -121.15 47.65
REMARK 500 ASP B 306 -85.52 -118.54
REMARK 500 ASP B 323 33.24 -93.46
REMARK 500 VAL B 367 65.50 -118.76
REMARK 500 VAL B 407 -62.25 -132.37
REMARK 500 SER B 497 39.85 -95.52
REMARK 500 ALA B 506 -70.62 -61.37
REMARK 500 ASN B 514 -167.51 -167.04
REMARK 500 ALA B 542 49.48 -71.87
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 AJ9 A 603
REMARK 610 PG0 A 606
REMARK 610 AJ9 B 602
DBREF 7QB4 A 1 543 UNP P21836 ACES_MOUSE 32 574
DBREF 7QB4 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 AJ9 A 603 14
HET PG0 A 604 8
HET PG0 A 605 8
HET PG0 A 606 5
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 PG0 A 613 20
HET PG0 A 614 20
HET NAG B 601 14
HET AJ9 B 602 14
HET EDO B 603 4
HET EDO B 604 4
HET EDO B 605 4
HET PG0 B 606 8
HET PG0 B 607 8
HET PG0 B 608 20
HET PG0 B 609 20
HET TOE B 610 11
HET 9YU B 611 23
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM AJ9 3,4-DIMETHYL-7-[[1-(PHENYLMETHYL)PIPERIDIN-4-
HETNAM 2 AJ9 YL]METHOXY]CHROMEN-2-ONE
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM TOE 2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXYL
HETNAM 9YU 2-[2-[2-[2-[2-[2-(2-METHOXYETHOXY)
HETNAM 2 9YU ETHOXY]ETHOXY]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 AJ9 7-[(1-BENZYLPIPERIDIN-3-YL)METHOXY]-3,4-DIMETHYL-2H-
HETSYN 2 AJ9 CHROMEN-2-ONE
HETSYN PG0 PEG 6000
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NAG 3(C8 H15 N O6)
FORMUL 5 AJ9 2(C24 H27 N O3)
FORMUL 6 PG0 15(C5 H12 O3)
FORMUL 19 EDO 3(C2 H6 O2)
FORMUL 26 TOE C7 H16 O4
FORMUL 27 9YU C15 H32 O8
FORMUL 28 HOH *123(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 GLU A 285 1 9
HELIX 14 AB5 TRP A 286 LEU A 289 5 4
HELIX 15 AB6 THR A 311 THR A 318 1 8
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 LEU B 214 1 12
HELIX 36 AD9 SER B 215 SER B 220 1 6
HELIX 37 AE1 ALA B 241 VAL B 255 1 15
HELIX 38 AE2 ASP B 266 THR B 275 1 10
HELIX 39 AE3 PRO B 277 ASP B 283 1 7
HELIX 40 AE4 HIS B 284 LEU B 289 5 6
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 PHE B 535 ALA B 542 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 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 VAL A 29 N LEU A 22
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 SER A 196 N VAL A 114
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 ALA B 31 N ILE B 20
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 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 2.06
SSBOND 3 CYS A 409 CYS A 529 1555 1555 2.04
SSBOND 4 CYS B 69 CYS B 96 1555 1555 2.05
SSBOND 5 CYS B 257 CYS B 272 1555 1555 2.06
SSBOND 6 CYS B 409 CYS B 529 1555 1555 2.04
LINK ND2 ASN A 350 C1 NAG A 601 1555 1555 1.45
LINK ND2 ASN A 464 C1 NAG A 602 1555 1555 1.45
LINK ND2 ASN B 350 C1 NAG B 601 1555 1555 1.45
CISPEP 1 TYR A 105 PRO A 106 0 -2.44
CISPEP 2 CYS A 257 PRO A 258 0 -1.05
CISPEP 3 TYR B 105 PRO B 106 0 8.82
CISPEP 4 CYS B 257 PRO B 258 0 -5.91
CRYST1 79.406 111.048 227.092 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 0.012594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009005 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004404 0.00000
TER 4197 THR A 543
TER 8400 THR B 543
MASTER 500 0 25 52 34 0 0 6 8705 2 296 84
END |