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HEADER HYDROLASE/INHIBITOR 27-OCT-22 8HAY
TITLE D4-BOUND BTDPP4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BTDPP4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: NCBI ACCESSION CODE: WP_022302284.1
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 818;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333
KEYWDS PEPTIDASE, GUT MICROBIOTA, ISOZYME, SECRETED, INHIBITOR, HYDROLASE,
KEYWDS 2 HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HANG,C.JIANG,K.WANG,Z.ZHANG,F.GUO,J.LIU,G.WANG,X.LEI,F.GONZALEZ,
AUTHOR 2 J.QIAO
REVDAT 1 26-JUL-23 8HAY 0
JRNL AUTH K.WANG,Z.ZHANG,J.HANG,J.LIU,F.GUO,Y.DING,M.LI,Q.NIE,J.LIN,
JRNL AUTH 2 Y.ZHUO,L.SUN,X.LUO,Q.ZHONG,C.YE,C.YUN,Y.ZHANG,J.WANG,R.BAO,
JRNL AUTH 3 Y.PANG,G.WANG,F.GONZALEZ,X.LEI,J.QIAO,C.JIANG
JRNL TITL MICROBIAL-HOST-ISOZYME ANALYSES REVEAL MICROBIAL DPP4
JRNL TITL 2 INHIBITION AS A POTENTIAL ANTIDIABETIC TARGET
JRNL REF SCIENCE
JRNL REFN ESSN 1095-9203
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.1
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) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 3 NUMBER OF REFLECTIONS : 95306
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 9491
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 37.5500 - 6.5900 1.00 7031 151 0.1404 0.1504
REMARK 3 2 6.5900 - 5.2400 1.00 6980 150 0.1492 0.1405
REMARK 3 3 5.2400 - 4.5800 1.00 6898 147 0.1226 0.1089
REMARK 3 4 4.5800 - 4.1600 1.00 6959 149 0.1311 0.1506
REMARK 3 5 4.1600 - 3.8600 1.00 6897 148 0.1635 0.1730
REMARK 3 6 3.8600 - 3.6500 0.75 4778 102 0.2964 0.3101
REMARK 3 7 3.6100 - 3.4500 0.95 5924 127 0.2127 0.2250
REMARK 3 8 3.4500 - 3.3000 1.00 6903 147 0.2061 0.2062
REMARK 3 9 3.3000 - 3.1800 1.00 6890 147 0.2362 0.2352
REMARK 3 10 3.1800 - 3.0700 1.00 6893 148 0.2525 0.2987
REMARK 3 11 3.0700 - 2.9700 0.99 6874 147 0.2391 0.2388
REMARK 3 12 2.9700 - 2.8800 0.99 6872 148 0.2458 0.2704
REMARK 3 13 2.8800 - 2.8100 0.99 6843 146 0.2581 0.2928
REMARK 3 14 2.8100 - 2.7400 0.95 6562 140 0.2795 0.3374
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.009 23828
REMARK 3 ANGLE : 1.066 32254
REMARK 3 CHIRALITY : 0.059 3372
REMARK 3 PLANARITY : 0.009 4164
REMARK 3 DIHEDRAL : 16.940 8831
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 23 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.3923 13.3858 28.1406
REMARK 3 T TENSOR
REMARK 3 T11: 0.4855 T22: 0.3886
REMARK 3 T33: 0.3914 T12: 0.0387
REMARK 3 T13: -0.0135 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 0.0861 L22: 0.0741
REMARK 3 L33: 0.4607 L12: -0.0724
REMARK 3 L13: 0.1163 L23: -0.1902
REMARK 3 S TENSOR
REMARK 3 S11: -0.0762 S12: -0.1788 S13: 0.1188
REMARK 3 S21: 0.0879 S22: -0.0124 S23: 0.0539
REMARK 3 S31: -0.3210 S32: 0.0205 S33: 0.0359
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 208 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.7576 -3.6882 35.7047
REMARK 3 T TENSOR
REMARK 3 T11: 0.3009 T22: 0.4413
REMARK 3 T33: 0.3746 T12: 0.0218
REMARK 3 T13: 0.0202 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 0.3836 L22: 0.4665
REMARK 3 L33: 0.8731 L12: 0.1576
REMARK 3 L13: 0.0454 L23: 0.0337
REMARK 3 S TENSOR
REMARK 3 S11: 0.0525 S12: -0.1886 S13: 0.0367
REMARK 3 S21: -0.0125 S22: -0.0693 S23: -0.0769
REMARK 3 S31: -0.0876 S32: -0.1351 S33: 0.0030
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 209 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1454 -13.2533 20.7822
REMARK 3 T TENSOR
REMARK 3 T11: 0.2630 T22: 0.3499
REMARK 3 T33: 0.2799 T12: -0.0212
REMARK 3 T13: 0.0153 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4563 L22: 0.3503
REMARK 3 L33: 0.1635 L12: -0.0153
REMARK 3 L13: -0.0224 L23: -0.0334
REMARK 3 S TENSOR
REMARK 3 S11: 0.0576 S12: -0.0440 S13: -0.0792
REMARK 3 S21: 0.0241 S22: -0.0333 S23: 0.0757
REMARK 3 S31: -0.0126 S32: -0.1305 S33: -0.0150
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 380 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8622 4.5343 0.0617
REMARK 3 T TENSOR
REMARK 3 T11: 0.2595 T22: 0.2701
REMARK 3 T33: 0.2690 T12: 0.0010
REMARK 3 T13: -0.0125 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.2122 L22: 0.3852
REMARK 3 L33: 0.4792 L12: -0.1573
REMARK 3 L13: -0.2510 L23: -0.0547
REMARK 3 S TENSOR
REMARK 3 S11: -0.0298 S12: 0.0919 S13: 0.1486
REMARK 3 S21: -0.0097 S22: 0.0320 S23: -0.0012
REMARK 3 S31: -0.0761 S32: -0.1191 S33: -0.0174
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 23 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -60.9947 15.0599 39.0660
REMARK 3 T TENSOR
REMARK 3 T11: 0.5216 T22: 0.3660
REMARK 3 T33: 0.4147 T12: -0.0473
REMARK 3 T13: 0.0024 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 0.2123 L22: 0.1390
REMARK 3 L33: 0.3265 L12: 0.1622
REMARK 3 L13: 0.0612 L23: 0.0897
REMARK 3 S TENSOR
REMARK 3 S11: -0.0829 S12: -0.0240 S13: 0.0083
REMARK 3 S21: -0.1281 S22: -0.0395 S23: -0.0009
REMARK 3 S31: -0.3325 S32: 0.0453 S33: 0.0825
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 119 THROUGH 314 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.0875 -7.1396 45.7996
REMARK 3 T TENSOR
REMARK 3 T11: 0.2825 T22: 0.3436
REMARK 3 T33: 0.3058 T12: -0.0211
REMARK 3 T13: 0.0079 T23: -0.0217
REMARK 3 L TENSOR
REMARK 3 L11: 0.4399 L22: 0.1876
REMARK 3 L33: 0.7105 L12: 0.0783
REMARK 3 L13: -0.1311 L23: 0.1514
REMARK 3 S TENSOR
REMARK 3 S11: -0.0028 S12: -0.0650 S13: -0.0164
REMARK 3 S21: -0.0153 S22: 0.0192 S23: -0.0700
REMARK 3 S31: 0.0099 S32: 0.1105 S33: -0.0257
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 315 THROUGH 481 )
REMARK 3 ORIGIN FOR THE GROUP (A): -41.9848 10.5261 53.9494
REMARK 3 T TENSOR
REMARK 3 T11: 0.3949 T22: 0.5273
REMARK 3 T33: 0.4096 T12: -0.0940
REMARK 3 T13: -0.0031 T23: -0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.6135 L22: 0.7461
REMARK 3 L33: 0.6611 L12: 0.0461
REMARK 3 L13: -0.2765 L23: -0.1518
REMARK 3 S TENSOR
REMARK 3 S11: 0.0621 S12: 0.0258 S13: 0.0775
REMARK 3 S21: -0.0075 S22: -0.0712 S23: -0.0317
REMARK 3 S31: -0.1795 S32: 0.2785 S33: 0.0002
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 482 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A): -65.0959 13.9022 74.9720
REMARK 3 T TENSOR
REMARK 3 T11: 0.3526 T22: 0.4062
REMARK 3 T33: 0.3538 T12: -0.0404
REMARK 3 T13: -0.0112 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.7323 L22: 0.3241
REMARK 3 L33: 0.5550 L12: -0.0205
REMARK 3 L13: -0.2015 L23: 0.1106
REMARK 3 S TENSOR
REMARK 3 S11: -0.0036 S12: -0.2460 S13: 0.1634
REMARK 3 S21: 0.0240 S22: 0.0513 S23: -0.0043
REMARK 3 S31: -0.1754 S32: 0.1149 S33: -0.0371
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 23 THROUGH 91 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4267 -35.2404 -20.1980
REMARK 3 T TENSOR
REMARK 3 T11: 0.4284 T22: 0.3747
REMARK 3 T33: 0.4301 T12: -0.0155
REMARK 3 T13: 0.0026 T23: -0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 0.0395 L22: 0.7514
REMARK 3 L33: 0.1000 L12: -0.1677
REMARK 3 L13: 0.0670 L23: -0.2950
REMARK 3 S TENSOR
REMARK 3 S11: -0.0013 S12: 0.0907 S13: -0.0832
REMARK 3 S21: -0.1687 S22: 0.0926 S23: 0.1751
REMARK 3 S31: 0.1495 S32: -0.1405 S33: -0.0558
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 92 THROUGH 265 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.3167 -35.6815 3.2426
REMARK 3 T TENSOR
REMARK 3 T11: 0.3016 T22: 0.2203
REMARK 3 T33: 0.3570 T12: 0.0168
REMARK 3 T13: 0.0062 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.4727 L22: 0.4079
REMARK 3 L33: 0.2824 L12: -0.4366
REMARK 3 L13: -0.2309 L23: 0.1353
REMARK 3 S TENSOR
REMARK 3 S11: -0.0150 S12: 0.0156 S13: -0.1457
REMARK 3 S21: 0.0672 S22: -0.0473 S23: 0.0845
REMARK 3 S31: 0.0521 S32: 0.0140 S33: 0.0573
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 266 THROUGH 442 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.8059 -25.3118 2.1171
REMARK 3 T TENSOR
REMARK 3 T11: 0.2364 T22: 0.2868
REMARK 3 T33: 0.3469 T12: 0.0268
REMARK 3 T13: -0.0047 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 0.3656 L22: 0.8620
REMARK 3 L33: 0.5746 L12: 0.0939
REMARK 3 L13: -0.0044 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0232 S12: -0.0689 S13: -0.0683
REMARK 3 S21: -0.0150 S22: 0.0514 S23: -0.1235
REMARK 3 S31: 0.0632 S32: 0.1373 S33: -0.0333
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 443 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8891 -3.9199 -9.0494
REMARK 3 T TENSOR
REMARK 3 T11: 0.2566 T22: 0.2286
REMARK 3 T33: 0.2786 T12: -0.0180
REMARK 3 T13: 0.0066 T23: -0.0146
REMARK 3 L TENSOR
REMARK 3 L11: 0.6638 L22: 0.1414
REMARK 3 L33: 0.4864 L12: -0.0546
REMARK 3 L13: 0.0064 L23: -0.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.0130 S12: 0.0862 S13: 0.0023
REMARK 3 S21: -0.0586 S22: 0.0157 S23: -0.0395
REMARK 3 S31: -0.0456 S32: -0.0460 S33: -0.0151
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 23 THROUGH 379 )
REMARK 3 ORIGIN FOR THE GROUP (A):-109.0091 -20.7866 78.9345
REMARK 3 T TENSOR
REMARK 3 T11: 0.3946 T22: 0.4407
REMARK 3 T33: 0.3927 T12: -0.0730
REMARK 3 T13: -0.0107 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 0.8214 L22: 0.2026
REMARK 3 L33: 0.4864 L12: 0.1177
REMARK 3 L13: -0.2426 L23: 0.1323
REMARK 3 S TENSOR
REMARK 3 S11: -0.0203 S12: 0.0030 S13: -0.2482
REMARK 3 S21: 0.0623 S22: -0.0481 S23: -0.0101
REMARK 3 S31: 0.1746 S32: -0.1613 S33: 0.0524
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 380 THROUGH 736 )
REMARK 3 ORIGIN FOR THE GROUP (A):-107.7365 7.5146 81.3979
REMARK 3 T TENSOR
REMARK 3 T11: 0.2980 T22: 0.4162
REMARK 3 T33: 0.3054 T12: 0.0106
REMARK 3 T13: -0.0182 T23: 0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 0.6414 L22: 0.2947
REMARK 3 L33: 0.7579 L12: 0.1657
REMARK 3 L13: 0.0085 L23: 0.0570
REMARK 3 S TENSOR
REMARK 3 S11: 0.0128 S12: -0.0819 S13: 0.0783
REMARK 3 S21: 0.0471 S22: -0.0223 S23: 0.0541
REMARK 3 S31: -0.0366 S32: -0.1891 S33: 0.0156
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 8HAY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-APR-23.
REMARK 100 THE DEPOSITION ID IS D_1300033125.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-OCT-22
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 : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95310
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 36.940
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.5500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.79
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1R9N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 8.35, 12% PEG 3,350,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 74.70550
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3890 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 54430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS B 412 O HOH B 901 1.80
REMARK 500 O VAL A 554 O HOH A 901 1.81
REMARK 500 O HOH D 845 O HOH D 854 1.83
REMARK 500 CA ASP A 555 O HOH A 901 1.84
REMARK 500 ND1 HIS A 114 O HOH A 902 1.86
REMARK 500 NZ LYS A 23 O HOH A 903 1.87
REMARK 500 OG1 THR B 279 O HOH B 902 1.88
REMARK 500 O GLU C 584 O HOH C 901 1.89
REMARK 500 O LEU C 172 O HOH C 902 1.93
REMARK 500 ND2 ASN C 730 O HOH C 903 1.93
REMARK 500 NZ LYS C 442 O HOH C 904 1.93
REMARK 500 NH1 ARG D 721 O HOH D 801 1.95
REMARK 500 N ASP A 287 O HOH A 904 1.96
REMARK 500 O HOH A 979 O HOH C 991 1.97
REMARK 500 O ASP C 394 O HOH C 905 1.98
REMARK 500 O HOH A 951 O HOH A 973 1.99
REMARK 500 OH TYR D 116 O HOH D 802 2.00
REMARK 500 O HOH C 972 O HOH C 985 2.00
REMARK 500 CE LYS A 23 O HOH A 903 2.01
REMARK 500 O HOH C 988 O HOH C 990 2.03
REMARK 500 O HOH D 827 O HOH D 847 2.05
REMARK 500 N GLY C 398 O HOH C 905 2.05
REMARK 500 OE1 GLU D 74 O HOH D 803 2.06
REMARK 500 OG SER B 427 O HOH B 903 2.06
REMARK 500 NZ LYS C 299 O HOH C 906 2.07
REMARK 500 OH TYR C 402 O HOH C 907 2.09
REMARK 500 OD1 ASN A 472 O HOH A 905 2.09
REMARK 500 NZ LYS A 378 O HOH A 906 2.10
REMARK 500 O HOH A 980 O HOH C 991 2.10
REMARK 500 O GLY A 537 O HOH A 907 2.11
REMARK 500 OG1 THR A 492 O HOH A 908 2.11
REMARK 500 N SER D 265 O HOH D 804 2.11
REMARK 500 CE2 PHE C 493 O HOH C 901 2.11
REMARK 500 N ASP A 555 O HOH A 901 2.12
REMARK 500 O MET D 46 O HOH D 805 2.12
REMARK 500 C VAL A 554 O HOH A 901 2.13
REMARK 500 N LEU C 25 O HOH C 908 2.13
REMARK 500 OE2 GLU B 406 O HOH B 904 2.14
REMARK 500 O HOH D 857 O HOH D 858 2.15
REMARK 500 O GLY D 42 O HOH D 806 2.15
REMARK 500 NE ARG B 324 O HOH B 905 2.15
REMARK 500 OD1 ASP A 555 O HOH A 901 2.15
REMARK 500 O HOH D 828 O HOH D 846 2.15
REMARK 500 N THR B 500 O HOH B 906 2.16
REMARK 500 N ASP C 143 O HOH C 909 2.16
REMARK 500 O GLU D 200 O HOH D 807 2.17
REMARK 500 N GLN D 487 O HOH D 808 2.18
REMARK 500 ND2 ASN C 472 OD1 ASP C 474 2.18
REMARK 500 ND2 ASN D 128 O HOH D 809 2.18
REMARK 500 O PHE A 364 O HOH A 909 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU A 191 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 ALA B 396 CB - CA - C ANGL. DEV. = -10.1 DEGREES
REMARK 500 GLY C 204 N - CA - C ANGL. DEV. = 15.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 111 -80.82 -114.97
REMARK 500 TYR A 112 -155.06 -102.84
REMARK 500 VAL A 149 57.29 35.64
REMARK 500 SER A 189 -67.79 -135.37
REMARK 500 LEU A 209 119.55 -162.38
REMARK 500 TYR A 257 103.61 -163.28
REMARK 500 TYR A 338 -83.75 -117.33
REMARK 500 MET A 372 0.00 -64.56
REMARK 500 LYS A 378 149.31 -171.24
REMARK 500 MET A 455 123.00 -174.56
REMARK 500 ALA A 509 -6.95 -57.46
REMARK 500 ASN A 510 58.02 -118.24
REMARK 500 LEU A 572 -1.13 77.71
REMARK 500 LYS A 573 69.22 -157.50
REMARK 500 ARG A 599 54.99 -151.60
REMARK 500 SER A 606 -129.46 63.38
REMARK 500 ARG A 648 -168.79 55.76
REMARK 500 ASN A 653 50.58 -117.59
REMARK 500 ASN A 683 -69.72 -109.74
REMARK 500 ASN A 712 -155.07 -106.00
REMARK 500 TYR B 112 -157.25 -129.24
REMARK 500 VAL B 149 59.90 33.81
REMARK 500 ASN B 176 48.50 38.08
REMARK 500 SER B 189 -66.84 -138.40
REMARK 500 TYR B 338 -88.91 -120.57
REMARK 500 LYS B 384 69.17 -100.32
REMARK 500 TYR B 524 -58.93 -124.33
REMARK 500 LYS B 573 55.56 -155.18
REMARK 500 SER B 606 -122.52 61.87
REMARK 500 ARG B 648 -167.26 68.46
REMARK 500 ASN B 683 -64.24 -108.65
REMARK 500 ILE C 111 -70.03 -113.12
REMARK 500 TYR C 112 -156.07 -114.06
REMARK 500 VAL C 149 50.38 34.99
REMARK 500 SER C 189 -69.95 -140.51
REMARK 500 ALA C 240 72.73 40.91
REMARK 500 PRO C 285 44.64 -79.68
REMARK 500 ASP C 289 38.37 -91.10
REMARK 500 TYR C 338 -84.29 -119.91
REMARK 500 MET C 455 119.74 -168.56
REMARK 500 ASN C 510 56.63 -108.22
REMARK 500 SER C 512 114.86 -162.19
REMARK 500 THR C 513 0.87 -65.47
REMARK 500 LEU C 572 -9.54 75.13
REMARK 500 SER C 606 -131.58 68.50
REMARK 500 ARG C 648 -166.23 69.50
REMARK 500 ALA C 680 33.62 -95.16
REMARK 500 ASN C 683 -82.07 -113.40
REMARK 500 ILE D 111 -69.17 -125.48
REMARK 500 TYR D 112 -168.57 -117.25
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 294 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8HAY A 23 736 PDB 8HAY 8HAY 23 736
DBREF 8HAY B 23 736 PDB 8HAY 8HAY 23 736
DBREF 8HAY C 23 736 PDB 8HAY 8HAY 23 736
DBREF 8HAY D 23 736 PDB 8HAY 8HAY 23 736
SEQRES 1 A 714 LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG PHE
SEQRES 2 A 714 ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO ASP
SEQRES 3 A 714 GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR GLN
SEQRES 4 A 714 ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL GLU
SEQRES 5 A 714 VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP PHE
SEQRES 6 A 714 LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY ASP
SEQRES 7 A 714 LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR ARG
SEQRES 8 A 714 HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU LYS
SEQRES 9 A 714 ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE GLU
SEQRES 10 A 714 ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL PHE
SEQRES 11 A 714 SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP ASN
SEQRES 12 A 714 ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER GLU
SEQRES 13 A 714 SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL LEU
SEQRES 14 A 714 ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE GLY
SEQRES 15 A 714 PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR MET
SEQRES 16 A 714 ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO SER
SEQRES 17 A 714 TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN ILE
SEQRES 18 A 714 THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR LYS
SEQRES 19 A 714 TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU VAL
SEQRES 20 A 714 ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR MET
SEQRES 21 A 714 LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG ILE
SEQRES 22 A 714 ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET THR
SEQRES 23 A 714 LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE ALA
SEQRES 24 A 714 ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG ASP
SEQRES 25 A 714 GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP ASN
SEQRES 26 A 714 ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER GLU
SEQRES 27 A 714 ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET GLY
SEQRES 28 A 714 GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR GLU
SEQRES 29 A 714 VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY SER
SEQRES 30 A 714 PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG LYS
SEQRES 31 A 714 ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU LYS
SEQRES 32 A 714 LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE SER
SEQRES 33 A 714 GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN LEU
SEQRES 34 A 714 ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR GLY
SEQRES 35 A 714 LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU LYS
SEQRES 36 A 714 GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU PHE
SEQRES 37 A 714 PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN GLY
SEQRES 38 A 714 TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS LYS
SEQRES 39 A 714 TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY SER
SEQRES 40 A 714 GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU THR
SEQRES 41 A 714 TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL ASP
SEQRES 42 A 714 GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU LYS
SEQRES 43 A 714 CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS ASP
SEQRES 44 A 714 GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO TYR
SEQRES 45 A 714 VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER TYR
SEQRES 46 A 714 GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY THR
SEQRES 47 A 714 PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO THR
SEQRES 48 A 714 ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG PHE
SEQRES 49 A 714 MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS GLU
SEQRES 50 A 714 SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY ASN
SEQRES 51 A 714 LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL HIS
SEQRES 52 A 714 PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL GLN
SEQRES 53 A 714 LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN ARG
SEQRES 54 A 714 ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS LEU
SEQRES 55 A 714 TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 B 714 LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG PHE
SEQRES 2 B 714 ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO ASP
SEQRES 3 B 714 GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR GLN
SEQRES 4 B 714 ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL GLU
SEQRES 5 B 714 VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP PHE
SEQRES 6 B 714 LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY ASP
SEQRES 7 B 714 LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR ARG
SEQRES 8 B 714 HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU LYS
SEQRES 9 B 714 ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE GLU
SEQRES 10 B 714 ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL PHE
SEQRES 11 B 714 SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP ASN
SEQRES 12 B 714 ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER GLU
SEQRES 13 B 714 SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL LEU
SEQRES 14 B 714 ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE GLY
SEQRES 15 B 714 PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR MET
SEQRES 16 B 714 ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO SER
SEQRES 17 B 714 TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN ILE
SEQRES 18 B 714 THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR LYS
SEQRES 19 B 714 TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU VAL
SEQRES 20 B 714 ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR MET
SEQRES 21 B 714 LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG ILE
SEQRES 22 B 714 ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET THR
SEQRES 23 B 714 LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE ALA
SEQRES 24 B 714 ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG ASP
SEQRES 25 B 714 GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP ASN
SEQRES 26 B 714 ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER GLU
SEQRES 27 B 714 ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET GLY
SEQRES 28 B 714 GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR GLU
SEQRES 29 B 714 VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY SER
SEQRES 30 B 714 PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG LYS
SEQRES 31 B 714 ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU LYS
SEQRES 32 B 714 LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE SER
SEQRES 33 B 714 GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN LEU
SEQRES 34 B 714 ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR GLY
SEQRES 35 B 714 LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU LYS
SEQRES 36 B 714 GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU PHE
SEQRES 37 B 714 PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN GLY
SEQRES 38 B 714 TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS LYS
SEQRES 39 B 714 TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY SER
SEQRES 40 B 714 GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU THR
SEQRES 41 B 714 TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL ASP
SEQRES 42 B 714 GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU LYS
SEQRES 43 B 714 CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS ASP
SEQRES 44 B 714 GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO TYR
SEQRES 45 B 714 VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER TYR
SEQRES 46 B 714 GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY THR
SEQRES 47 B 714 PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO THR
SEQRES 48 B 714 ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG PHE
SEQRES 49 B 714 MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS GLU
SEQRES 50 B 714 SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY ASN
SEQRES 51 B 714 LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL HIS
SEQRES 52 B 714 PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL GLN
SEQRES 53 B 714 LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN ARG
SEQRES 54 B 714 ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS LEU
SEQRES 55 B 714 TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 C 714 LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG PHE
SEQRES 2 C 714 ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO ASP
SEQRES 3 C 714 GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR GLN
SEQRES 4 C 714 ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL GLU
SEQRES 5 C 714 VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP PHE
SEQRES 6 C 714 LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY ASP
SEQRES 7 C 714 LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR ARG
SEQRES 8 C 714 HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU LYS
SEQRES 9 C 714 ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE GLU
SEQRES 10 C 714 ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL PHE
SEQRES 11 C 714 SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP ASN
SEQRES 12 C 714 ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER GLU
SEQRES 13 C 714 SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL LEU
SEQRES 14 C 714 ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE GLY
SEQRES 15 C 714 PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR MET
SEQRES 16 C 714 ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO SER
SEQRES 17 C 714 TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN ILE
SEQRES 18 C 714 THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR LYS
SEQRES 19 C 714 TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU VAL
SEQRES 20 C 714 ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR MET
SEQRES 21 C 714 LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG ILE
SEQRES 22 C 714 ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET THR
SEQRES 23 C 714 LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE ALA
SEQRES 24 C 714 ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG ASP
SEQRES 25 C 714 GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP ASN
SEQRES 26 C 714 ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER GLU
SEQRES 27 C 714 ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET GLY
SEQRES 28 C 714 GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR GLU
SEQRES 29 C 714 VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY SER
SEQRES 30 C 714 PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG LYS
SEQRES 31 C 714 ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU LYS
SEQRES 32 C 714 LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE SER
SEQRES 33 C 714 GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN LEU
SEQRES 34 C 714 ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR GLY
SEQRES 35 C 714 LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU LYS
SEQRES 36 C 714 GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU PHE
SEQRES 37 C 714 PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN GLY
SEQRES 38 C 714 TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS LYS
SEQRES 39 C 714 TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY SER
SEQRES 40 C 714 GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU THR
SEQRES 41 C 714 TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL ASP
SEQRES 42 C 714 GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU LYS
SEQRES 43 C 714 CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS ASP
SEQRES 44 C 714 GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO TYR
SEQRES 45 C 714 VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER TYR
SEQRES 46 C 714 GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY THR
SEQRES 47 C 714 PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO THR
SEQRES 48 C 714 ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG PHE
SEQRES 49 C 714 MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS GLU
SEQRES 50 C 714 SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY ASN
SEQRES 51 C 714 LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL HIS
SEQRES 52 C 714 PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL GLN
SEQRES 53 C 714 LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN ARG
SEQRES 54 C 714 ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS LEU
SEQRES 55 C 714 TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
SEQRES 1 D 714 LYS ALA LEU ASP LEU LYS ASP ILE THR SER GLY ARG PHE
SEQRES 2 D 714 ARG PRO GLU ASN ILE GLN GLY VAL ILE PRO MET PRO ASP
SEQRES 3 D 714 GLY GLU HIS TYR THR GLN MET SER ALA ASP GLY THR GLN
SEQRES 4 D 714 ILE ILE LYS TYR SER PHE ARG THR GLY GLU LYS VAL GLU
SEQRES 5 D 714 VAL ILE PHE ASP VAL ASN GLN ALA ARG GLU CYS ASP PHE
SEQRES 6 D 714 LYS ASN PHE ASP SER TYR GLN PHE SER PRO ASP GLY ASP
SEQRES 7 D 714 LYS LEU LEU ILE ALA THR ARG THR THR PRO ILE TYR ARG
SEQRES 8 D 714 HIS SER TYR THR ALA VAL HIS TYR ILE TYR PRO LEU LYS
SEQRES 9 D 714 ARG ASN ASP LYS GLY VAL THR THR ASN ASN ILE ILE GLU
SEQRES 10 D 714 ARG LEU SER ASP GLY GLY PRO GLN GLN VAL PRO VAL PHE
SEQRES 11 D 714 SER PRO ASP GLY THR MET ILE ALA PHE VAL ARG ASP ASN
SEQRES 12 D 714 ASN ILE PHE LEU VAL LYS LEU LEU TYR GLY ASN SER GLU
SEQRES 13 D 714 SER GLN VAL THR GLU ASP GLY LYS GLN ASN SER VAL LEU
SEQRES 14 D 714 ASN GLY ILE PRO ASP TRP VAL TYR GLU GLU GLU PHE GLY
SEQRES 15 D 714 PHE ASN ARG ALA LEU GLU PHE SER ALA ASP ASN THR MET
SEQRES 16 D 714 ILE ALA PHE ILE ARG PHE ASP GLU SER GLU VAL PRO SER
SEQRES 17 D 714 TYR SER PHE PRO MET PHE ALA GLY GLU ALA PRO GLN ILE
SEQRES 18 D 714 THR PRO LEU LYS ASP TYR PRO GLY GLU TYR THR TYR LYS
SEQRES 19 D 714 TYR PRO LYS ALA GLY TYR PRO ASN SER LYS VAL GLU VAL
SEQRES 20 D 714 ARG THR TYR ASP ILE LYS SER HIS VAL THR ARG THR MET
SEQRES 21 D 714 LYS LEU PRO ILE ASP ALA ASP GLY TYR ILE PRO ARG ILE
SEQRES 22 D 714 ARG PHE THR LYS ASP ALA SER LYS LEU ALA VAL MET THR
SEQRES 23 D 714 LEU ASN ARG HIS GLN ASP ARG PHE ASP LEU TYR PHE ALA
SEQRES 24 D 714 ASP PRO ARG SER THR LEU CYS LYS LEU VAL LEU ARG ASP
SEQRES 25 D 714 GLU SER PRO TYR TYR ILE LYS GLU ASN VAL PHE ASP ASN
SEQRES 26 D 714 ILE LYS PHE TYR PRO GLU THR PHE SER LEU LEU SER GLU
SEQRES 27 D 714 ARG ASP GLY PHE SER HIS LEU TYR TRP TYR SER MET GLY
SEQRES 28 D 714 GLY ASN LEU ILE LYS LYS VAL THR ASN GLY LYS TYR GLU
SEQRES 29 D 714 VAL LYS ASP PHE LEU GLY TYR ASP GLU ALA ASP GLY SER
SEQRES 30 D 714 PHE TYR TYR THR SER ASN GLU GLU SER PRO LEU ARG LYS
SEQRES 31 D 714 ALA VAL TYR LYS ILE ASP LYS LYS GLY LYS LYS LEU LYS
SEQRES 32 D 714 LEU SER GLN ARG GLU GLY THR ASN THR PRO LEU PHE SER
SEQRES 33 D 714 GLN SER MET LYS TYR TYR MET ASN LYS PHE SER ASN LEU
SEQRES 34 D 714 ASP THR PRO MET LEU VAL THR LEU ASN ASP ASN THR GLY
SEQRES 35 D 714 LYS THR LEU LYS THR LEU ILE ASN ASN ASP GLN LEU LYS
SEQRES 36 D 714 GLN THR LEU SER GLY TYR ALA ILE PRO GLN LYS GLU PHE
SEQRES 37 D 714 PHE THR PHE GLN THR THR ASP GLY VAL THR LEU ASN GLY
SEQRES 38 D 714 TRP MET MET LYS PRO ALA ASN PHE SER THR SER LYS LYS
SEQRES 39 D 714 TYR PRO VAL LEU MET TYR GLN TYR SER GLY PRO GLY SER
SEQRES 40 D 714 GLN GLN VAL LEU ASP THR TRP GLY ILE SER TRP GLU THR
SEQRES 41 D 714 TYR MET ALA SER LEU GLY TYR ILE VAL VAL CYS VAL ASP
SEQRES 42 D 714 GLY ARG GLY THR GLY GLY ARG GLY GLU ALA PHE GLU LYS
SEQRES 43 D 714 CYS THR TYR LEU LYS ILE GLY VAL LYS GLU ALA LYS ASP
SEQRES 44 D 714 GLN VAL GLU THR ALA LEU TYR LEU GLY LYS GLN PRO TYR
SEQRES 45 D 714 VAL ASP LYS ASP ARG ILE GLY ILE TRP GLY TRP SER TYR
SEQRES 46 D 714 GLY GLY TYR MET THR LEU MET SER MET SER GLU GLY THR
SEQRES 47 D 714 PRO VAL PHE LYS ALA GLY VAL ALA VAL ALA ALA PRO THR
SEQRES 48 D 714 ASP TRP ARG PHE TYR ASP THR ILE TYR THR GLU ARG PHE
SEQRES 49 D 714 MET ARG THR PRO LYS GLU ASN ALA GLU GLY TYR LYS GLU
SEQRES 50 D 714 SER SER ALA PHE THR ARG ALA ASP LYS LEU HIS GLY ASN
SEQRES 51 D 714 LEU LEU LEU VAL HIS GLY MET ALA ASP ASP ASN VAL HIS
SEQRES 52 D 714 PHE GLN ASN CYS ALA GLU TYR ALA GLU HIS LEU VAL GLN
SEQRES 53 D 714 LEU GLY LYS GLN PHE ASP MET GLN VAL TYR THR ASN ARG
SEQRES 54 D 714 ASN HIS GLY ILE TYR GLY GLY ASN THR ARG GLN HIS LEU
SEQRES 55 D 714 TYR THR ARG LEU THR ASN PHE PHE LEU ASN ASN LEU
HET KYL A 801 47
HET KYL B 801 47
HET KYL C 801 47
HETNAM KYL (1~{R})-1-[[4-[5-[[(1~{R})-6,7-DIMETHOXY-2-METHYL-3,4-
HETNAM 2 KYL DIHYDRO-1~{H}-ISOQUINOLIN-1-YL]METHYL]-2-METHOXY-
HETNAM 3 KYL PHENOXY]PHENYL]METHYL]-6,7-DIMETHOXY-2-METHYL-3,4-
HETNAM 4 KYL DIHYDRO-1~{H}-ISOQUINOLINE
FORMUL 5 KYL 3(C39 H46 N2 O6)
FORMUL 8 HOH *304(H2 O)
HELIX 1 AA1 ASP A 26 SER A 32 1 7
HELIX 2 AA2 ASP A 196 PHE A 203 1 8
HELIX 3 AA3 ILE A 243 LYS A 247 5 5
HELIX 4 AA4 LYS A 341 ILE A 348 5 8
HELIX 5 AA5 ASN A 473 GLY A 482 1 10
HELIX 6 AA6 SER A 539 LEU A 547 1 9
HELIX 7 AA7 ARG A 562 LYS A 568 1 7
HELIX 8 AA8 CYS A 569 TYR A 571 5 3
HELIX 9 AA9 GLY A 575 GLN A 592 1 18
HELIX 10 AB1 SER A 606 SER A 617 1 12
HELIX 11 AB2 ASP A 634 TYR A 638 5 5
HELIX 12 AB3 ASP A 639 ARG A 648 1 10
HELIX 13 AB4 ASN A 653 SER A 661 1 9
HELIX 14 AB5 ARG A 665 LEU A 669 5 5
HELIX 15 AB6 HIS A 685 GLY A 700 1 16
HELIX 16 AB7 ASN A 719 LEU A 736 1 18
HELIX 17 AB8 ASP B 26 GLY B 33 1 8
HELIX 18 AB9 LEU B 173 GLY B 175 5 3
HELIX 19 AC1 ASP B 196 PHE B 203 1 8
HELIX 20 AC2 ILE B 243 LYS B 247 5 5
HELIX 21 AC3 LYS B 341 ILE B 348 5 8
HELIX 22 AC4 ASN B 473 GLY B 482 1 10
HELIX 23 AC5 SER B 539 LEU B 547 1 9
HELIX 24 AC6 GLY B 563 CYS B 569 1 7
HELIX 25 AC7 GLY B 575 LYS B 591 1 17
HELIX 26 AC8 SER B 606 SER B 617 1 12
HELIX 27 AC9 ASP B 634 TYR B 638 5 5
HELIX 28 AD1 ASP B 639 ARG B 648 1 10
HELIX 29 AD2 ASN B 653 SER B 661 1 9
HELIX 30 AD3 ARG B 665 LEU B 669 5 5
HELIX 31 AD4 HIS B 685 LEU B 699 1 15
HELIX 32 AD5 ASN B 719 LEU B 736 1 18
HELIX 33 AD6 ASP C 26 SER C 32 1 7
HELIX 34 AD7 LEU C 173 GLY C 175 5 3
HELIX 35 AD8 ASP C 196 PHE C 203 1 8
HELIX 36 AD9 ILE C 243 LYS C 247 5 5
HELIX 37 AE1 LYS C 341 ILE C 348 5 8
HELIX 38 AE2 ASN C 473 SER C 481 1 9
HELIX 39 AE3 SER C 539 LEU C 547 1 9
HELIX 40 AE4 GLY C 563 LYS C 568 1 6
HELIX 41 AE5 CYS C 569 TYR C 571 5 3
HELIX 42 AE6 GLY C 575 GLN C 592 1 18
HELIX 43 AE7 SER C 606 SER C 617 1 12
HELIX 44 AE8 ASP C 634 TYR C 638 5 5
HELIX 45 AE9 ASP C 639 ARG C 648 1 10
HELIX 46 AF1 ASN C 653 SER C 661 1 9
HELIX 47 AF2 ARG C 665 LEU C 669 5 5
HELIX 48 AF3 HIS C 685 GLY C 700 1 16
HELIX 49 AF4 ASN C 719 LEU C 736 1 18
HELIX 50 AF5 ASP D 26 SER D 32 1 7
HELIX 51 AF6 ASP D 196 PHE D 203 1 8
HELIX 52 AF7 ILE D 243 LYS D 247 5 5
HELIX 53 AF8 LYS D 341 ILE D 348 5 8
HELIX 54 AF9 ASN D 473 GLY D 482 1 10
HELIX 55 AG1 SER D 539 LEU D 547 1 9
HELIX 56 AG2 ARG D 562 CYS D 569 1 8
HELIX 57 AG3 GLY D 575 LYS D 591 1 17
HELIX 58 AG4 SER D 606 SER D 617 1 12
HELIX 59 AG5 ASP D 639 ARG D 648 1 10
HELIX 60 AG6 ASN D 653 SER D 660 1 8
HELIX 61 AG7 ARG D 665 LEU D 669 5 5
HELIX 62 AG8 HIS D 685 LEU D 699 1 15
HELIX 63 AG9 ASN D 719 LEU D 736 1 18
SHEET 1 AA1 4 ILE A 44 PRO A 45 0
SHEET 2 AA1 4 HIS A 51 MET A 55 -1 O THR A 53 N ILE A 44
SHEET 3 AA1 4 GLN A 61 SER A 66 -1 O TYR A 65 N TYR A 52
SHEET 4 AA1 4 LYS A 72 ASP A 78 -1 O GLU A 74 N LYS A 64
SHEET 1 AA2 4 SER A 92 PHE A 95 0
SHEET 2 AA2 4 LYS A 101 PRO A 110 -1 O ALA A 105 N SER A 92
SHEET 3 AA2 4 TYR A 116 PRO A 124 -1 O THR A 117 N THR A 109
SHEET 4 AA2 4 GLU A 139 ARG A 140 -1 O GLU A 139 N ILE A 122
SHEET 1 AA3 4 GLN A 148 PHE A 152 0
SHEET 2 AA3 4 MET A 158 ARG A 163 -1 O ALA A 160 N VAL A 151
SHEET 3 AA3 4 ASN A 166 LYS A 171 -1 O PHE A 168 N PHE A 161
SHEET 4 AA3 4 SER A 177 GLN A 180 -1 O SER A 179 N LEU A 169
SHEET 1 AA4 3 VAL A 190 ASN A 192 0
SHEET 2 AA4 3 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA4 3 LEU A 209 PHE A 211 -1 N GLU A 210 O ALA A 219
SHEET 1 AA5 4 VAL A 190 ASN A 192 0
SHEET 2 AA5 4 MET A 217 ASP A 224 -1 O PHE A 223 N LEU A 191
SHEET 3 AA5 4 LYS A 266 ASP A 273 -1 O TYR A 272 N ILE A 218
SHEET 4 AA5 4 THR A 279 THR A 281 -1 O ARG A 280 N THR A 271
SHEET 1 AA6 2 SER A 230 MET A 235 0
SHEET 2 AA6 2 GLY A 251 LYS A 256 -1 O TYR A 255 N TYR A 231
SHEET 1 AA7 4 TYR A 291 PHE A 297 0
SHEET 2 AA7 4 LEU A 304 LEU A 309 -1 O MET A 307 N ARG A 294
SHEET 3 AA7 4 ARG A 315 ALA A 321 -1 O ALA A 321 N LEU A 304
SHEET 4 AA7 4 CYS A 328 GLU A 335 -1 O LYS A 329 N PHE A 320
SHEET 1 AA8 3 THR A 354 SER A 359 0
SHEET 2 AA8 3 HIS A 366 SER A 371 -1 O TYR A 368 N LEU A 357
SHEET 3 AA8 3 LEU A 376 LYS A 379 -1 O ILE A 377 N TRP A 369
SHEET 1 AA9 4 VAL A 387 ASP A 394 0
SHEET 2 AA9 4 SER A 399 SER A 404 -1 O SER A 399 N ASP A 394
SHEET 3 AA9 4 ALA A 413 ILE A 417 -1 O ILE A 417 N PHE A 400
SHEET 4 AA9 4 LYS A 423 LYS A 425 -1 O LEU A 424 N LYS A 416
SHEET 1 AB1 4 THR A 432 PHE A 437 0
SHEET 2 AB1 4 TYR A 443 ASN A 450 -1 O LYS A 447 N THR A 434
SHEET 3 AB1 4 THR A 453 ASP A 461 -1 O ASN A 460 N TYR A 444
SHEET 4 AB1 4 THR A 466 ILE A 471 -1 O LYS A 468 N LEU A 459
SHEET 1 AB2 8 GLN A 487 GLN A 494 0
SHEET 2 AB2 8 THR A 500 LYS A 507 -1 O LEU A 501 N PHE A 493
SHEET 3 AB2 8 ILE A 550 ASP A 555 -1 O VAL A 551 N MET A 506
SHEET 4 AB2 8 TYR A 517 TYR A 522 1 N LEU A 520 O ILE A 550
SHEET 5 AB2 8 VAL A 595 TRP A 605 1 O GLY A 601 N MET A 521
SHEET 6 AB2 8 ALA A 625 VAL A 629 1 O VAL A 629 N GLY A 604
SHEET 7 AB2 8 ASN A 672 GLY A 678 1 O LEU A 674 N ALA A 628
SHEET 8 AB2 8 ASP A 704 TYR A 708 1 O ASP A 704 N LEU A 675
SHEET 1 AB3 4 ILE B 44 PRO B 45 0
SHEET 2 AB3 4 HIS B 51 MET B 55 -1 O THR B 53 N ILE B 44
SHEET 3 AB3 4 GLN B 61 SER B 66 -1 O TYR B 65 N TYR B 52
SHEET 4 AB3 4 LYS B 72 ASP B 78 -1 O GLU B 74 N LYS B 64
SHEET 1 AB4 4 SER B 92 PHE B 95 0
SHEET 2 AB4 4 LYS B 101 PRO B 110 -1 O ALA B 105 N SER B 92
SHEET 3 AB4 4 TYR B 116 PRO B 124 -1 O VAL B 119 N THR B 106
SHEET 4 AB4 4 GLU B 139 ARG B 140 -1 O GLU B 139 N ILE B 122
SHEET 1 AB5 4 GLN B 148 PHE B 152 0
SHEET 2 AB5 4 MET B 158 ARG B 163 -1 O VAL B 162 N GLN B 148
SHEET 3 AB5 4 ASN B 166 LYS B 171 -1 O PHE B 168 N PHE B 161
SHEET 4 AB5 4 SER B 177 GLN B 180 -1 O SER B 177 N LYS B 171
SHEET 1 AB6 3 VAL B 190 ASN B 192 0
SHEET 2 AB6 3 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB6 3 LEU B 209 PHE B 211 -1 N GLU B 210 O ALA B 219
SHEET 1 AB7 4 VAL B 190 ASN B 192 0
SHEET 2 AB7 4 MET B 217 ASP B 224 -1 O PHE B 223 N LEU B 191
SHEET 3 AB7 4 LYS B 266 ASP B 273 -1 O LYS B 266 N ASP B 224
SHEET 4 AB7 4 THR B 279 THR B 281 -1 O ARG B 280 N THR B 271
SHEET 1 AB8 2 SER B 230 MET B 235 0
SHEET 2 AB8 2 GLY B 251 LYS B 256 -1 O TYR B 255 N TYR B 231
SHEET 1 AB9 4 TYR B 291 PHE B 297 0
SHEET 2 AB9 4 LEU B 304 LEU B 309 -1 O ALA B 305 N ARG B 296
SHEET 3 AB9 4 ARG B 315 ALA B 321 -1 O ASP B 317 N THR B 308
SHEET 4 AB9 4 CYS B 328 GLU B 335 -1 O ASP B 334 N PHE B 316
SHEET 1 AC1 3 THR B 354 SER B 359 0
SHEET 2 AC1 3 HIS B 366 SER B 371 -1 O TYR B 368 N LEU B 357
SHEET 3 AC1 3 LEU B 376 LYS B 379 -1 O ILE B 377 N TRP B 369
SHEET 1 AC2 4 VAL B 387 ASP B 394 0
SHEET 2 AC2 4 SER B 399 SER B 404 -1 O TYR B 401 N GLY B 392
SHEET 3 AC2 4 ALA B 413 ILE B 417 -1 O TYR B 415 N TYR B 402
SHEET 4 AC2 4 LYS B 423 LYS B 425 -1 O LEU B 424 N LYS B 416
SHEET 1 AC3 4 THR B 432 PHE B 437 0
SHEET 2 AC3 4 TYR B 443 ASN B 450 -1 O SER B 449 N THR B 432
SHEET 3 AC3 4 THR B 453 ASP B 461 -1 O THR B 458 N ASN B 446
SHEET 4 AC3 4 THR B 466 ILE B 471 -1 O LEU B 467 N LEU B 459
SHEET 1 AC4 8 GLN B 487 GLN B 494 0
SHEET 2 AC4 8 THR B 500 LYS B 507 -1 O LEU B 501 N PHE B 493
SHEET 3 AC4 8 ILE B 550 ASP B 555 -1 O VAL B 551 N MET B 506
SHEET 4 AC4 8 TYR B 517 TYR B 522 1 N PRO B 518 O ILE B 550
SHEET 5 AC4 8 VAL B 595 TRP B 605 1 O GLY B 601 N MET B 521
SHEET 6 AC4 8 ALA B 625 VAL B 629 1 O VAL B 627 N GLY B 604
SHEET 7 AC4 8 ASN B 672 GLY B 678 1 O ASN B 672 N GLY B 626
SHEET 8 AC4 8 ASP B 704 TYR B 708 1 O TYR B 708 N HIS B 677
SHEET 1 AC5 4 VAL C 43 PRO C 45 0
SHEET 2 AC5 4 HIS C 51 MET C 55 -1 O THR C 53 N ILE C 44
SHEET 3 AC5 4 GLN C 61 SER C 66 -1 O ILE C 63 N GLN C 54
SHEET 4 AC5 4 LYS C 72 ASP C 78 -1 O GLU C 74 N LYS C 64
SHEET 1 AC6 4 SER C 92 PHE C 95 0
SHEET 2 AC6 4 LYS C 101 PRO C 110 -1 O ALA C 105 N SER C 92
SHEET 3 AC6 4 TYR C 116 PRO C 124 -1 O VAL C 119 N THR C 106
SHEET 4 AC6 4 GLU C 139 ARG C 140 -1 O GLU C 139 N ILE C 122
SHEET 1 AC7 4 GLN C 148 PHE C 152 0
SHEET 2 AC7 4 MET C 158 ARG C 163 -1 O ALA C 160 N VAL C 151
SHEET 3 AC7 4 ASN C 166 LYS C 171 -1 O VAL C 170 N ILE C 159
SHEET 4 AC7 4 SER C 177 GLN C 180 -1 O SER C 177 N LYS C 171
SHEET 1 AC8 3 VAL C 190 ASN C 192 0
SHEET 2 AC8 3 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC8 3 LEU C 209 PHE C 211 -1 N GLU C 210 O ALA C 219
SHEET 1 AC9 4 VAL C 190 ASN C 192 0
SHEET 2 AC9 4 MET C 217 ASP C 224 -1 O PHE C 223 N LEU C 191
SHEET 3 AC9 4 LYS C 266 ASP C 273 -1 O TYR C 272 N ILE C 218
SHEET 4 AC9 4 VAL C 278 THR C 281 -1 O VAL C 278 N ASP C 273
SHEET 1 AD1 2 SER C 230 MET C 235 0
SHEET 2 AD1 2 GLY C 251 LYS C 256 -1 O TYR C 255 N TYR C 231
SHEET 1 AD2 4 TYR C 291 PHE C 297 0
SHEET 2 AD2 4 LEU C 304 LEU C 309 -1 O LEU C 309 N TYR C 291
SHEET 3 AD2 4 ARG C 315 ALA C 321 -1 O ASP C 317 N THR C 308
SHEET 4 AD2 4 CYS C 328 GLU C 335 -1 O LYS C 329 N PHE C 320
SHEET 1 AD3 3 THR C 354 SER C 359 0
SHEET 2 AD3 3 HIS C 366 SER C 371 -1 O TYR C 368 N LEU C 357
SHEET 3 AD3 3 LEU C 376 LYS C 379 -1 O LYS C 378 N TRP C 369
SHEET 1 AD4 4 VAL C 387 ASP C 394 0
SHEET 2 AD4 4 SER C 399 SER C 404 -1 O TYR C 401 N GLY C 392
SHEET 3 AD4 4 ALA C 413 ILE C 417 -1 O TYR C 415 N TYR C 402
SHEET 4 AD4 4 LYS C 423 LYS C 425 -1 O LEU C 424 N LYS C 416
SHEET 1 AD5 4 THR C 432 PHE C 437 0
SHEET 2 AD5 4 TYR C 443 SER C 449 -1 O SER C 449 N THR C 432
SHEET 3 AD5 4 LEU C 456 ASP C 461 -1 O LEU C 456 N PHE C 448
SHEET 4 AD5 4 THR C 466 ILE C 471 -1 O LEU C 467 N LEU C 459
SHEET 1 AD6 8 LYS C 488 GLN C 494 0
SHEET 2 AD6 8 THR C 500 MET C 506 -1 O LEU C 501 N PHE C 493
SHEET 3 AD6 8 ILE C 550 ASP C 555 -1 O VAL C 551 N MET C 506
SHEET 4 AD6 8 TYR C 517 TYR C 522 1 N TYR C 522 O VAL C 552
SHEET 5 AD6 8 VAL C 595 TRP C 605 1 O GLY C 601 N MET C 521
SHEET 6 AD6 8 ALA C 625 VAL C 629 1 O VAL C 629 N GLY C 604
SHEET 7 AD6 8 ASN C 672 GLY C 678 1 O VAL C 676 N ALA C 628
SHEET 8 AD6 8 PHE C 703 TYR C 708 1 O ASP C 704 N LEU C 675
SHEET 1 AD7 4 ILE D 44 PRO D 45 0
SHEET 2 AD7 4 HIS D 51 MET D 55 -1 O THR D 53 N ILE D 44
SHEET 3 AD7 4 GLN D 61 SER D 66 -1 O ILE D 63 N GLN D 54
SHEET 4 AD7 4 LYS D 72 ASP D 78 -1 O VAL D 73 N LYS D 64
SHEET 1 AD8 4 SER D 92 PHE D 95 0
SHEET 2 AD8 4 LYS D 101 PRO D 110 -1 O LEU D 103 N GLN D 94
SHEET 3 AD8 4 TYR D 116 PRO D 124 -1 O VAL D 119 N THR D 106
SHEET 4 AD8 4 GLU D 139 ARG D 140 -1 O GLU D 139 N ILE D 122
SHEET 1 AD9 4 GLN D 148 PHE D 152 0
SHEET 2 AD9 4 MET D 158 ARG D 163 -1 O ALA D 160 N VAL D 151
SHEET 3 AD9 4 ASN D 166 LYS D 171 -1 O VAL D 170 N ILE D 159
SHEET 4 AD9 4 SER D 177 GLN D 180 -1 O SER D 177 N LYS D 171
SHEET 1 AE1 3 VAL D 190 ASN D 192 0
SHEET 2 AE1 3 MET D 217 ASP D 224 -1 O PHE D 223 N LEU D 191
SHEET 3 AE1 3 LEU D 209 PHE D 211 -1 N GLU D 210 O ALA D 219
SHEET 1 AE2 4 VAL D 190 ASN D 192 0
SHEET 2 AE2 4 MET D 217 ASP D 224 -1 O PHE D 223 N LEU D 191
SHEET 3 AE2 4 LYS D 266 ASP D 273 -1 O ARG D 270 N PHE D 220
SHEET 4 AE2 4 THR D 279 THR D 281 -1 O ARG D 280 N THR D 271
SHEET 1 AE3 2 SER D 230 MET D 235 0
SHEET 2 AE3 2 GLY D 251 LYS D 256 -1 O GLY D 251 N MET D 235
SHEET 1 AE4 4 TYR D 291 PHE D 297 0
SHEET 2 AE4 4 LEU D 304 LEU D 309 -1 O LEU D 309 N TYR D 291
SHEET 3 AE4 4 ARG D 315 ALA D 321 -1 O TYR D 319 N VAL D 306
SHEET 4 AE4 4 CYS D 328 GLU D 335 -1 O ASP D 334 N PHE D 316
SHEET 1 AE5 3 THR D 354 SER D 359 0
SHEET 2 AE5 3 HIS D 366 SER D 371 -1 O TYR D 370 N PHE D 355
SHEET 3 AE5 3 LYS D 378 LYS D 379 -1 O LYS D 378 N TRP D 369
SHEET 1 AE6 4 VAL D 387 ASP D 394 0
SHEET 2 AE6 4 SER D 399 SER D 404 -1 O THR D 403 N ASP D 389
SHEET 3 AE6 4 ALA D 413 ILE D 417 -1 O ILE D 417 N PHE D 400
SHEET 4 AE6 4 LYS D 423 LYS D 425 -1 O LEU D 424 N LYS D 416
SHEET 1 AE7 4 THR D 432 PHE D 437 0
SHEET 2 AE7 4 TYR D 443 SER D 449 -1 O SER D 449 N THR D 432
SHEET 3 AE7 4 LEU D 456 ASP D 461 -1 O ASN D 460 N TYR D 444
SHEET 4 AE7 4 THR D 466 ILE D 471 -1 O LYS D 468 N LEU D 459
SHEET 1 AE8 8 LYS D 488 GLN D 494 0
SHEET 2 AE8 8 THR D 500 MET D 506 -1 O LEU D 501 N PHE D 493
SHEET 3 AE8 8 ILE D 550 ASP D 555 -1 O VAL D 551 N MET D 506
SHEET 4 AE8 8 TYR D 517 TYR D 522 1 N LEU D 520 O ILE D 550
SHEET 5 AE8 8 VAL D 595 TRP D 605 1 O GLY D 601 N VAL D 519
SHEET 6 AE8 8 ALA D 625 VAL D 629 1 O VAL D 629 N GLY D 604
SHEET 7 AE8 8 ASN D 672 GLY D 678 1 O LEU D 674 N ALA D 628
SHEET 8 AE8 8 ASP D 704 TYR D 708 1 O ASP D 704 N LEU D 675
CISPEP 1 ALA A 240 PRO A 241 0 -2.06
CISPEP 2 ALA B 240 PRO B 241 0 -0.65
CISPEP 3 ALA C 240 PRO C 241 0 -2.95
CISPEP 4 ALA D 240 PRO D 241 0 -6.36
CRYST1 96.106 149.411 137.898 90.00 103.74 90.00 P 1 21 1 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 0.010405 0.000000 0.002544 0.00000
SCALE2 0.000000 0.006693 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007465 0.00000
TER 5771 LEU A 736
TER 11542 LEU B 736
TER 17313 LEU C 736
TER 23084 LEU D 736
MASTER 584 0 3 63 176 0 0 623525 4 141 220
END |