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HEADER HYDROLASE 20-SEP-22 8EKG
TITLE MHETASE VARIANT THR159VAL, MET192TYR, TYR252PHE, TYR503TRP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONO(2-HYDROXYETHYL) TEREPHTHALATE HYDROLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MHET HYDROLASE,MHETASE;
COMPND 5 EC: 3.1.1.102;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: NBRC 110686 / TISTR 2288 / 201-F6;
SOURCE 5 GENE: ISF6_0224;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMG96;
SOURCE 9 EXPRESSION_SYSTEM_VARIANT: SHUFFLE;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS PROTEIN ENGINEERING, MHETASE, PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.W.SAUNDERS,R.L.FRKIC,C.J.JACKSON
REVDAT 1 18-OCT-23 8EKG 0
JRNL AUTH J.W.SAUNDERS,A.D.DAMRY,V.VONGSOUTHI,R.L.FRKIC,M.A.SPENCE,
JRNL AUTH 2 P.M.YATES,M.D.MCLEOD,N.TOKURIKI,C.J.JACKSON
JRNL TITL MHETASE PROTEIN ENGINEERING USING A NOVEL COLORIMETRIC ASSAY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1_4487
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.87
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 104701
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670
REMARK 3 FREE R VALUE TEST SET COUNT : 4885
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 43.8700 - 8.2200 0.95 3284 177 0.1405 0.1794
REMARK 3 2 8.2200 - 6.5300 0.96 3330 125 0.1438 0.1755
REMARK 3 3 6.5300 - 5.7100 0.95 3302 160 0.1534 0.1889
REMARK 3 4 5.7100 - 5.1800 0.96 3340 167 0.1418 0.1865
REMARK 3 5 5.1800 - 4.8100 0.95 3310 170 0.1360 0.2034
REMARK 3 6 4.8100 - 4.5300 0.96 3327 110 0.1260 0.1635
REMARK 3 7 4.5300 - 4.3000 0.95 3313 141 0.1248 0.1708
REMARK 3 8 4.3000 - 4.1200 0.96 3363 164 0.1368 0.1914
REMARK 3 9 4.1200 - 3.9600 0.96 3336 154 0.1470 0.1813
REMARK 3 10 3.9600 - 3.8200 0.95 3326 145 0.1517 0.2006
REMARK 3 11 3.8200 - 3.7000 0.96 3340 147 0.1616 0.2153
REMARK 3 12 3.7000 - 3.6000 0.97 3317 166 0.1656 0.2573
REMARK 3 13 3.6000 - 3.5000 0.95 3339 137 0.1777 0.2248
REMARK 3 14 3.5000 - 3.4200 0.96 3362 128 0.1820 0.2358
REMARK 3 15 3.4200 - 3.3400 0.96 3314 185 0.1915 0.2542
REMARK 3 16 3.3400 - 3.2700 0.97 3367 174 0.2248 0.2784
REMARK 3 17 3.2700 - 3.2000 0.97 3361 162 0.2379 0.2679
REMARK 3 18 3.2000 - 3.1400 0.95 3308 163 0.2464 0.3424
REMARK 3 19 3.1400 - 3.0900 0.97 3298 195 0.2493 0.3213
REMARK 3 20 3.0900 - 3.0300 0.96 3300 192 0.2492 0.3235
REMARK 3 21 3.0300 - 2.9800 0.95 3356 174 0.2574 0.3252
REMARK 3 22 2.9800 - 2.9400 0.96 3301 140 0.2711 0.3687
REMARK 3 23 2.9400 - 2.9000 0.96 3304 196 0.2793 0.3675
REMARK 3 24 2.9000 - 2.8500 0.95 3318 179 0.2736 0.3368
REMARK 3 25 2.8500 - 2.8200 0.96 3315 184 0.2724 0.3404
REMARK 3 26 2.8200 - 2.7800 0.98 3294 179 0.2839 0.3183
REMARK 3 27 2.7800 - 2.7400 0.95 3373 150 0.3098 0.3727
REMARK 3 28 2.7400 - 2.7100 0.96 3371 174 0.3174 0.3610
REMARK 3 29 2.7100 - 2.6800 0.97 3268 163 0.3335 0.3856
REMARK 3 30 2.6800 - 2.6500 0.96 3379 184 0.3375 0.3894
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.110
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.24
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 17
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 47 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.6969 -4.9443 58.1698
REMARK 3 T TENSOR
REMARK 3 T11: 0.3783 T22: 0.3289
REMARK 3 T33: 0.4935 T12: 0.0502
REMARK 3 T13: -0.0415 T23: -0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 2.7333 L22: 0.8356
REMARK 3 L33: 1.3890 L12: -0.2734
REMARK 3 L13: 1.0366 L23: -0.4120
REMARK 3 S TENSOR
REMARK 3 S11: 0.0417 S12: -0.1616 S13: 0.1392
REMARK 3 S21: -0.1477 S22: -0.0785 S23: -0.0214
REMARK 3 S31: -0.0973 S32: 0.0004 S33: 0.0486
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 213 THROUGH 533 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0427 -33.1504 55.5166
REMARK 3 T TENSOR
REMARK 3 T11: 0.4054 T22: 0.2122
REMARK 3 T33: 0.4630 T12: 0.0338
REMARK 3 T13: -0.0793 T23: 0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 1.2877 L22: 0.6906
REMARK 3 L33: 1.4390 L12: -0.0978
REMARK 3 L13: 0.1531 L23: 0.5691
REMARK 3 S TENSOR
REMARK 3 S11: 0.0560 S12: -0.1873 S13: -0.2162
REMARK 3 S21: -0.0073 S22: -0.0142 S23: -0.1257
REMARK 3 S31: 0.2217 S32: 0.0518 S33: -0.0183
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 534 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6088 -25.8559 53.5778
REMARK 3 T TENSOR
REMARK 3 T11: 0.2614 T22: 0.3609
REMARK 3 T33: 0.4468 T12: 0.0352
REMARK 3 T13: -0.0224 T23: -0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 1.8357 L22: 1.9675
REMARK 3 L33: 4.3118 L12: 1.5719
REMARK 3 L13: 1.9464 L23: 0.5233
REMARK 3 S TENSOR
REMARK 3 S11: 0.0746 S12: -0.2606 S13: 0.0668
REMARK 3 S21: 0.0383 S22: -0.3225 S23: 0.4202
REMARK 3 S31: 0.2020 S32: -0.3271 S33: 0.2567
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 46 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2225 34.8974 69.7411
REMARK 3 T TENSOR
REMARK 3 T11: 0.3294 T22: 0.3885
REMARK 3 T33: 0.4934 T12: 0.0381
REMARK 3 T13: -0.0818 T23: -0.1154
REMARK 3 L TENSOR
REMARK 3 L11: 3.2385 L22: 1.0541
REMARK 3 L33: 2.4911 L12: -0.5388
REMARK 3 L13: -1.5160 L23: 0.7831
REMARK 3 S TENSOR
REMARK 3 S11: -0.0205 S12: 0.0141 S13: 0.1333
REMARK 3 S21: -0.0397 S22: -0.0095 S23: 0.0308
REMARK 3 S31: 0.0765 S32: -0.1635 S33: 0.0407
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 213 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.9624 56.8169 84.5108
REMARK 3 T TENSOR
REMARK 3 T11: 0.4700 T22: 0.5616
REMARK 3 T33: 0.7221 T12: 0.0509
REMARK 3 T13: -0.0718 T23: -0.2706
REMARK 3 L TENSOR
REMARK 3 L11: 0.7136 L22: 1.9011
REMARK 3 L33: 0.5115 L12: -0.1890
REMARK 3 L13: -0.2869 L23: 0.3138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: -0.2699 S13: 0.3098
REMARK 3 S21: 0.0341 S22: 0.0205 S23: 0.0045
REMARK 3 S31: -0.1835 S32: 0.0173 S33: -0.0532
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 47 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.7991 12.0819 -35.2319
REMARK 3 T TENSOR
REMARK 3 T11: 0.4045 T22: 0.5131
REMARK 3 T33: 0.6963 T12: 0.0253
REMARK 3 T13: 0.0621 T23: -0.0941
REMARK 3 L TENSOR
REMARK 3 L11: 4.2179 L22: 2.9102
REMARK 3 L33: 1.6181 L12: 1.6195
REMARK 3 L13: -0.5221 L23: -1.2725
REMARK 3 S TENSOR
REMARK 3 S11: -0.3739 S12: 0.3308 S13: 0.0294
REMARK 3 S21: -0.2619 S22: 0.1006 S23: -0.3936
REMARK 3 S31: 0.3185 S32: -0.0316 S33: 0.2780
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 111 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.3588 28.0945 -12.4375
REMARK 3 T TENSOR
REMARK 3 T11: 0.4431 T22: 0.4378
REMARK 3 T33: 0.6395 T12: 0.0580
REMARK 3 T13: -0.2022 T23: -0.1186
REMARK 3 L TENSOR
REMARK 3 L11: 0.5518 L22: 1.1907
REMARK 3 L33: 1.0506 L12: -0.4588
REMARK 3 L13: -0.3977 L23: 0.1831
REMARK 3 S TENSOR
REMARK 3 S11: -0.1856 S12: -0.1324 S13: 0.3119
REMARK 3 S21: 0.3475 S22: 0.1522 S23: -0.3880
REMARK 3 S31: -0.1448 S32: 0.1361 S33: 0.0804
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 46 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.3585 9.6084 -38.5266
REMARK 3 T TENSOR
REMARK 3 T11: 0.4362 T22: 0.4065
REMARK 3 T33: 0.5257 T12: 0.0888
REMARK 3 T13: -0.0607 T23: -0.0547
REMARK 3 L TENSOR
REMARK 3 L11: 1.5743 L22: 2.0642
REMARK 3 L33: 1.4888 L12: 0.1513
REMARK 3 L13: -0.0135 L23: 0.0657
REMARK 3 S TENSOR
REMARK 3 S11: -0.1564 S12: 0.0505 S13: 0.2091
REMARK 3 S21: -0.0413 S22: 0.1544 S23: -0.0362
REMARK 3 S31: -0.4123 S32: -0.2199 S33: 0.0392
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 111 THROUGH 333 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2389 -10.3263 -26.9980
REMARK 3 T TENSOR
REMARK 3 T11: 0.2646 T22: 0.3467
REMARK 3 T33: 0.4021 T12: 0.0521
REMARK 3 T13: -0.0212 T23: -0.0394
REMARK 3 L TENSOR
REMARK 3 L11: 0.2057 L22: 0.2840
REMARK 3 L33: 0.7536 L12: 0.1038
REMARK 3 L13: -0.0581 L23: -0.1169
REMARK 3 S TENSOR
REMARK 3 S11: -0.0014 S12: 0.0506 S13: 0.0113
REMARK 3 S21: 0.0034 S22: -0.0184 S23: 0.0067
REMARK 3 S31: 0.0346 S32: 0.0062 S33: 0.0134
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 334 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2185 -20.2342 -22.3703
REMARK 3 T TENSOR
REMARK 3 T11: 0.2935 T22: 0.3383
REMARK 3 T33: 0.4652 T12: 0.0554
REMARK 3 T13: -0.0513 T23: -0.0896
REMARK 3 L TENSOR
REMARK 3 L11: 0.7021 L22: 0.8605
REMARK 3 L33: 1.5819 L12: 0.2636
REMARK 3 L13: -0.2914 L23: -0.3799
REMARK 3 S TENSOR
REMARK 3 S11: -0.0534 S12: 0.1120 S13: -0.0861
REMARK 3 S21: 0.0382 S22: -0.0367 S23: -0.0011
REMARK 3 S31: 0.1697 S32: -0.0618 S33: 0.0916
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 549 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.0715 -11.6011 -21.4404
REMARK 3 T TENSOR
REMARK 3 T11: 0.3185 T22: 0.3764
REMARK 3 T33: 0.5051 T12: 0.0353
REMARK 3 T13: -0.0132 T23: -0.0358
REMARK 3 L TENSOR
REMARK 3 L11: 1.7138 L22: 0.3637
REMARK 3 L33: 4.5691 L12: -0.2442
REMARK 3 L13: 0.9476 L23: 0.0368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: -0.0262 S13: -0.2002
REMARK 3 S21: -0.0165 S22: -0.1285 S23: 0.1001
REMARK 3 S31: 0.0279 S32: 0.5135 S33: 0.0708
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 47 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.2693 0.2663 55.0420
REMARK 3 T TENSOR
REMARK 3 T11: 0.3725 T22: 0.3740
REMARK 3 T33: 0.4810 T12: 0.0787
REMARK 3 T13: -0.0293 T23: -0.0721
REMARK 3 L TENSOR
REMARK 3 L11: 3.8128 L22: 2.5830
REMARK 3 L33: 1.3981 L12: -1.8534
REMARK 3 L13: 0.9924 L23: -0.7853
REMARK 3 S TENSOR
REMARK 3 S11: -0.1003 S12: -0.2228 S13: -0.3205
REMARK 3 S21: 0.2401 S22: 0.3675 S23: 0.0163
REMARK 3 S31: 0.0246 S32: -0.0009 S33: -0.2058
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 326 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8318 0.9414 32.8978
REMARK 3 T TENSOR
REMARK 3 T11: 0.3081 T22: 0.3742
REMARK 3 T33: 0.4728 T12: 0.0560
REMARK 3 T13: -0.0572 T23: -0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 0.1097 L22: 0.3523
REMARK 3 L33: 0.8074 L12: -0.0634
REMARK 3 L13: -0.1516 L23: 0.0523
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: -0.0790 S13: -0.0091
REMARK 3 S21: 0.0076 S22: 0.0283 S23: 0.0260
REMARK 3 S31: 0.0188 S32: 0.0026 S33: 0.0426
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 327 THROUGH 382 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.6826 -5.6678 6.5541
REMARK 3 T TENSOR
REMARK 3 T11: 0.2346 T22: 0.3311
REMARK 3 T33: 0.2511 T12: 0.0369
REMARK 3 T13: -0.0009 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 3.3690 L22: 1.2542
REMARK 3 L33: 4.3308 L12: 2.0518
REMARK 3 L13: 1.3204 L23: 0.9235
REMARK 3 S TENSOR
REMARK 3 S11: 0.0327 S12: 0.4708 S13: -0.2029
REMARK 3 S21: -0.1339 S22: 0.1069 S23: -0.1862
REMARK 3 S31: 0.1812 S32: 0.1550 S33: -0.1206
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.7211 2.0375 25.6738
REMARK 3 T TENSOR
REMARK 3 T11: 0.3022 T22: 0.3418
REMARK 3 T33: 0.3425 T12: 0.0365
REMARK 3 T13: -0.0112 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 2.0337 L22: 1.1751
REMARK 3 L33: 0.8637 L12: 0.2198
REMARK 3 L13: 0.5300 L23: 0.3998
REMARK 3 S TENSOR
REMARK 3 S11: -0.0151 S12: 0.0455 S13: 0.0621
REMARK 3 S21: -0.0444 S22: -0.0058 S23: -0.0058
REMARK 3 S31: 0.0115 S32: 0.0578 S33: 0.0155
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 47 THROUGH 212 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5040 32.7749 57.4275
REMARK 3 T TENSOR
REMARK 3 T11: 0.3098 T22: 0.4677
REMARK 3 T33: 0.5380 T12: 0.0284
REMARK 3 T13: -0.0843 T23: -0.1658
REMARK 3 L TENSOR
REMARK 3 L11: 2.8151 L22: 1.3078
REMARK 3 L33: 2.5785 L12: 0.3904
REMARK 3 L13: -1.8742 L23: -0.2426
REMARK 3 S TENSOR
REMARK 3 S11: 0.0352 S12: -0.2792 S13: 0.1556
REMARK 3 S21: 0.0508 S22: 0.1211 S23: -0.0617
REMARK 3 S31: -0.0512 S32: 0.4498 S33: -0.1245
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 213 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7747 47.3971 35.5895
REMARK 3 T TENSOR
REMARK 3 T11: 0.4555 T22: 0.2911
REMARK 3 T33: 0.4995 T12: -0.0060
REMARK 3 T13: -0.0406 T23: -0.1063
REMARK 3 L TENSOR
REMARK 3 L11: 0.6921 L22: 0.8410
REMARK 3 L33: 0.7133 L12: -0.3644
REMARK 3 L13: -0.3283 L23: 0.1940
REMARK 3 S TENSOR
REMARK 3 S11: 0.1140 S12: -0.0581 S13: 0.1373
REMARK 3 S21: -0.2269 S22: 0.0079 S23: 0.0459
REMARK 3 S31: -0.2721 S32: 0.0736 S33: -0.1265
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 8EKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-22.
REMARK 100 THE DEPOSITION ID IS D_1000268412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAR-22
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
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 0.7.7
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104762
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 43.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 200 DATA REDUNDANCY : 1.800
REMARK 200 R MERGE (I) : 0.11200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.83600
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: 6QZ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.2 M MGCL2, 0.1 M HEPES
REMARK 280 PH 7.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 12
REMARK 465 GLU A 13
REMARK 465 ASN A 14
REMARK 465 LEU A 15
REMARK 465 TYR A 16
REMARK 465 PHE A 17
REMARK 465 GLN A 18
REMARK 465 GLY A 19
REMARK 465 GLY A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 SER A 23
REMARK 465 THR A 24
REMARK 465 PRO A 25
REMARK 465 LEU A 26
REMARK 465 PRO A 27
REMARK 465 LEU A 28
REMARK 465 PRO A 29
REMARK 465 GLN A 30
REMARK 465 GLN A 31
REMARK 465 GLN A 32
REMARK 465 PRO A 33
REMARK 465 PRO A 34
REMARK 465 GLN A 35
REMARK 465 GLN A 36
REMARK 465 GLU A 37
REMARK 465 PRO A 38
REMARK 465 PRO A 39
REMARK 465 PRO A 40
REMARK 465 PRO A 41
REMARK 465 PRO A 42
REMARK 465 VAL A 43
REMARK 465 PRO A 44
REMARK 465 LEU A 45
REMARK 465 MET B 12
REMARK 465 GLU B 13
REMARK 465 ASN B 14
REMARK 465 LEU B 15
REMARK 465 TYR B 16
REMARK 465 PHE B 17
REMARK 465 GLN B 18
REMARK 465 GLY B 19
REMARK 465 GLY B 20
REMARK 465 GLY B 21
REMARK 465 GLY B 22
REMARK 465 SER B 23
REMARK 465 THR B 24
REMARK 465 PRO B 25
REMARK 465 LEU B 26
REMARK 465 PRO B 27
REMARK 465 LEU B 28
REMARK 465 PRO B 29
REMARK 465 GLN B 30
REMARK 465 GLN B 31
REMARK 465 GLN B 32
REMARK 465 PRO B 33
REMARK 465 PRO B 34
REMARK 465 GLN B 35
REMARK 465 GLN B 36
REMARK 465 GLU B 37
REMARK 465 PRO B 38
REMARK 465 PRO B 39
REMARK 465 PRO B 40
REMARK 465 PRO B 41
REMARK 465 PRO B 42
REMARK 465 VAL B 43
REMARK 465 PRO B 44
REMARK 465 LEU B 45
REMARK 465 ALA B 46
REMARK 465 MET C 12
REMARK 465 GLU C 13
REMARK 465 ASN C 14
REMARK 465 LEU C 15
REMARK 465 TYR C 16
REMARK 465 PHE C 17
REMARK 465 GLN C 18
REMARK 465 GLY C 19
REMARK 465 GLY C 20
REMARK 465 GLY C 21
REMARK 465 GLY C 22
REMARK 465 SER C 23
REMARK 465 THR C 24
REMARK 465 PRO C 25
REMARK 465 LEU C 26
REMARK 465 PRO C 27
REMARK 465 LEU C 28
REMARK 465 PRO C 29
REMARK 465 GLN C 30
REMARK 465 GLN C 31
REMARK 465 GLN C 32
REMARK 465 PRO C 33
REMARK 465 PRO C 34
REMARK 465 GLN C 35
REMARK 465 GLN C 36
REMARK 465 GLU C 37
REMARK 465 PRO C 38
REMARK 465 PRO C 39
REMARK 465 PRO C 40
REMARK 465 PRO C 41
REMARK 465 PRO C 42
REMARK 465 VAL C 43
REMARK 465 PRO C 44
REMARK 465 LEU C 45
REMARK 465 ALA C 46
REMARK 465 MET D 12
REMARK 465 GLU D 13
REMARK 465 ASN D 14
REMARK 465 LEU D 15
REMARK 465 TYR D 16
REMARK 465 PHE D 17
REMARK 465 GLN D 18
REMARK 465 GLY D 19
REMARK 465 GLY D 20
REMARK 465 GLY D 21
REMARK 465 GLY D 22
REMARK 465 SER D 23
REMARK 465 THR D 24
REMARK 465 PRO D 25
REMARK 465 LEU D 26
REMARK 465 PRO D 27
REMARK 465 LEU D 28
REMARK 465 PRO D 29
REMARK 465 GLN D 30
REMARK 465 GLN D 31
REMARK 465 GLN D 32
REMARK 465 PRO D 33
REMARK 465 PRO D 34
REMARK 465 GLN D 35
REMARK 465 GLN D 36
REMARK 465 GLU D 37
REMARK 465 PRO D 38
REMARK 465 PRO D 39
REMARK 465 PRO D 40
REMARK 465 PRO D 41
REMARK 465 PRO D 42
REMARK 465 VAL D 43
REMARK 465 PRO D 44
REMARK 465 LEU D 45
REMARK 465 ALA D 46
REMARK 465 MET E 12
REMARK 465 GLU E 13
REMARK 465 ASN E 14
REMARK 465 LEU E 15
REMARK 465 TYR E 16
REMARK 465 PHE E 17
REMARK 465 GLN E 18
REMARK 465 GLY E 19
REMARK 465 GLY E 20
REMARK 465 GLY E 21
REMARK 465 GLY E 22
REMARK 465 SER E 23
REMARK 465 THR E 24
REMARK 465 PRO E 25
REMARK 465 LEU E 26
REMARK 465 PRO E 27
REMARK 465 LEU E 28
REMARK 465 PRO E 29
REMARK 465 GLN E 30
REMARK 465 GLN E 31
REMARK 465 GLN E 32
REMARK 465 PRO E 33
REMARK 465 PRO E 34
REMARK 465 GLN E 35
REMARK 465 GLN E 36
REMARK 465 GLU E 37
REMARK 465 PRO E 38
REMARK 465 PRO E 39
REMARK 465 PRO E 40
REMARK 465 PRO E 41
REMARK 465 PRO E 42
REMARK 465 VAL E 43
REMARK 465 PRO E 44
REMARK 465 LEU E 45
REMARK 465 MET F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 LEU F 15
REMARK 465 TYR F 16
REMARK 465 PHE F 17
REMARK 465 GLN F 18
REMARK 465 GLY F 19
REMARK 465 GLY F 20
REMARK 465 GLY F 21
REMARK 465 GLY F 22
REMARK 465 SER F 23
REMARK 465 THR F 24
REMARK 465 PRO F 25
REMARK 465 LEU F 26
REMARK 465 PRO F 27
REMARK 465 LEU F 28
REMARK 465 PRO F 29
REMARK 465 GLN F 30
REMARK 465 GLN F 31
REMARK 465 GLN F 32
REMARK 465 PRO F 33
REMARK 465 PRO F 34
REMARK 465 GLN F 35
REMARK 465 GLN F 36
REMARK 465 GLU F 37
REMARK 465 PRO F 38
REMARK 465 PRO F 39
REMARK 465 PRO F 40
REMARK 465 PRO F 41
REMARK 465 PRO F 42
REMARK 465 VAL F 43
REMARK 465 PRO F 44
REMARK 465 LEU F 45
REMARK 465 ALA F 46
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 ASP A 56 -125.72 59.17
REMARK 500 ASP A 60 32.68 -96.13
REMARK 500 ASN A 134 -141.24 60.47
REMARK 500 ASN A 171 44.55 -86.79
REMARK 500 TYR A 194 -29.55 -149.09
REMARK 500 SEP A 225 -111.21 61.20
REMARK 500 ALA A 249 56.84 35.67
REMARK 500 ASP A 311 13.28 -143.80
REMARK 500 ASN A 316 75.45 -107.68
REMARK 500 ASN A 334 1.32 -159.52
REMARK 500 TYR A 373 -92.29 -134.52
REMARK 500 SER A 383 -153.51 -140.93
REMARK 500 SER A 413 -10.09 -144.23
REMARK 500 ALA A 469 43.74 -140.11
REMARK 500 SER A 491 36.79 -96.45
REMARK 500 CYS A 529 -27.23 68.25
REMARK 500 ARG A 550 -18.50 68.06
REMARK 500 ALA B 67 35.19 -86.39
REMARK 500 ALA B 73 83.49 -154.55
REMARK 500 GLU B 90 132.58 -39.71
REMARK 500 ASN B 134 -140.58 59.70
REMARK 500 TYR B 194 -33.21 -158.08
REMARK 500 SEP B 225 -112.43 66.32
REMARK 500 ALA B 249 59.14 38.06
REMARK 500 ASP B 276 -167.98 -100.40
REMARK 500 TYR B 373 -102.38 -144.36
REMARK 500 SER B 383 -144.28 -133.04
REMARK 500 ILE B 447 -49.93 -135.25
REMARK 500 SER B 491 41.85 -95.29
REMARK 500 ASN B 527 -137.75 -84.83
REMARK 500 CYS B 529 -36.84 68.82
REMARK 500 ASN C 58 55.99 -100.22
REMARK 500 ASP C 60 -15.97 69.84
REMARK 500 MET C 61 80.89 -66.77
REMARK 500 ALA C 67 45.85 -97.82
REMARK 500 ASN C 134 -147.99 59.07
REMARK 500 ASP C 172 78.04 -115.28
REMARK 500 ALA C 176 33.47 -96.38
REMARK 500 TYR C 194 -23.95 -159.85
REMARK 500 SEP C 225 -108.87 55.43
REMARK 500 ASP C 276 -156.97 -96.48
REMARK 500 ASN C 316 74.06 -100.21
REMARK 500 TYR C 373 -93.90 -137.35
REMARK 500 SER C 383 -143.55 -138.47
REMARK 500 SER C 456 118.73 -162.32
REMARK 500 ALA C 469 51.19 -147.67
REMARK 500 PHE C 517 -8.23 -150.34
REMARK 500 ASN C 527 -144.85 -84.00
REMARK 500 CYS C 529 -25.23 68.18
REMARK 500 ASN D 58 42.77 -103.93
REMARK 500
REMARK 500 THIS ENTRY HAS 94 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 868 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH A 869 DISTANCE = 8.30 ANGSTROMS
REMARK 525 HOH A 870 DISTANCE = 11.32 ANGSTROMS
REMARK 525 HOH B 890 DISTANCE = 6.14 ANGSTROMS
REMARK 525 HOH B 891 DISTANCE = 6.27 ANGSTROMS
REMARK 525 HOH C 865 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH C 866 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 867 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH C 868 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH C 869 DISTANCE = 8.44 ANGSTROMS
REMARK 525 HOH C 870 DISTANCE = 8.51 ANGSTROMS
REMARK 525 HOH C 871 DISTANCE = 8.87 ANGSTROMS
REMARK 525 HOH E 849 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH E 850 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH E 851 DISTANCE = 7.78 ANGSTROMS
REMARK 525 HOH E 852 DISTANCE = 8.58 ANGSTROMS
REMARK 525 HOH F 851 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH F 852 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH F 853 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH F 854 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH F 855 DISTANCE = 9.18 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 304 O
REMARK 620 2 ASP A 304 OD1 58.1
REMARK 620 3 ASP A 307 OD1 60.8 115.0
REMARK 620 4 ASP A 307 OD2 105.8 162.7 47.7
REMARK 620 5 LEU A 309 O 61.8 68.6 65.0 99.1
REMARK 620 6 ASP A 311 OD1 115.2 71.5 119.8 114.8 63.6
REMARK 620 7 ILE A 313 O 99.4 75.1 135.6 116.5 143.7 104.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 304 O
REMARK 620 2 ASP B 304 OD1 70.2
REMARK 620 3 ASP B 307 OD1 86.3 153.3
REMARK 620 4 ASP B 307 OD2 62.7 124.4 47.9
REMARK 620 5 LEU B 309 O 70.0 83.4 76.4 105.5
REMARK 620 6 ASP B 311 OD1 140.0 76.4 118.4 157.0 85.1
REMARK 620 7 ILE B 313 O 103.2 75.4 124.0 87.7 158.8 88.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 304 O
REMARK 620 2 ASP C 304 OD1 69.0
REMARK 620 3 ASP C 307 OD1 79.5 146.8
REMARK 620 4 ASP C 307 OD2 69.4 110.1 46.1
REMARK 620 5 LEU C 309 O 73.7 95.8 84.9 122.1
REMARK 620 6 ASP C 311 OD1 136.5 72.6 140.6 145.5 90.8
REMARK 620 7 ILE C 313 O 98.8 60.8 116.4 73.4 156.3 79.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 304 O
REMARK 620 2 ASP D 304 OD1 61.1
REMARK 620 3 ASP D 307 OD1 73.7 133.0
REMARK 620 4 ASP D 307 OD2 60.8 109.1 52.6
REMARK 620 5 LEU D 309 O 66.6 72.3 78.9 115.2
REMARK 620 6 ASP D 311 OD1 126.4 66.9 147.6 156.2 86.6
REMARK 620 7 ILE D 313 O 97.0 73.2 127.2 77.1 145.5 79.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 304 O
REMARK 620 2 ASP E 304 OD1 66.7
REMARK 620 3 ASP E 307 OD1 69.5 135.4
REMARK 620 4 ASP E 307 OD2 60.8 111.4 49.7
REMARK 620 5 LEU E 309 O 73.7 87.9 72.2 114.5
REMARK 620 6 ASP E 311 OD1 135.8 70.2 148.9 149.8 95.6
REMARK 620 7 ILE E 313 O 101.1 72.2 125.1 77.8 159.7 74.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 701 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 304 O
REMARK 620 2 ASP F 304 OD1 69.9
REMARK 620 3 ASP F 307 OD1 80.1 145.9
REMARK 620 4 ASP F 307 OD2 65.3 123.2 51.7
REMARK 620 5 LEU F 309 O 78.2 83.5 74.7 117.9
REMARK 620 6 ASP F 311 OD1 142.3 75.6 126.0 151.2 83.4
REMARK 620 7 ILE F 313 O 103.5 77.9 126.1 80.5 159.3 83.2
REMARK 620 N 1 2 3 4 5 6
DBREF1 8EKG A 20 603 UNP MHETH_IDESA
DBREF2 8EKG A A0A0K8P8E7 20 603
DBREF1 8EKG B 20 603 UNP MHETH_IDESA
DBREF2 8EKG B A0A0K8P8E7 20 603
DBREF1 8EKG C 20 603 UNP MHETH_IDESA
DBREF2 8EKG C A0A0K8P8E7 20 603
DBREF1 8EKG D 20 603 UNP MHETH_IDESA
DBREF2 8EKG D A0A0K8P8E7 20 603
DBREF1 8EKG E 20 603 UNP MHETH_IDESA
DBREF2 8EKG E A0A0K8P8E7 20 603
DBREF1 8EKG F 20 603 UNP MHETH_IDESA
DBREF2 8EKG F A0A0K8P8E7 20 603
SEQADV 8EKG MET A 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU A 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN A 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU A 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR A 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE A 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN A 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY A 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL A 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR A 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE A 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP A 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQADV 8EKG MET B 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU B 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN B 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU B 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR B 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE B 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN B 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY B 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL B 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR B 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE B 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP B 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQADV 8EKG MET C 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU C 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN C 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU C 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR C 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE C 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN C 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY C 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL C 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR C 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE C 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP C 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQADV 8EKG MET D 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU D 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN D 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU D 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR D 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE D 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN D 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY D 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL D 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR D 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE D 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP D 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQADV 8EKG MET E 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU E 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN E 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU E 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR E 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE E 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN E 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY E 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL E 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR E 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE E 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP E 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQADV 8EKG MET F 12 UNP A0A0K8P8E INITIATING METHIONINE
SEQADV 8EKG GLU F 13 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG ASN F 14 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG LEU F 15 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG TYR F 16 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG PHE F 17 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLN F 18 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG GLY F 19 UNP A0A0K8P8E EXPRESSION TAG
SEQADV 8EKG VAL F 159 UNP A0A0K8P8E THR 159 ENGINEERED MUTATION
SEQADV 8EKG TYR F 192 UNP A0A0K8P8E MET 192 ENGINEERED MUTATION
SEQADV 8EKG PHE F 252 UNP A0A0K8P8E TYR 252 ENGINEERED MUTATION
SEQADV 8EKG TRP F 503 UNP A0A0K8P8E TYR 503 ENGINEERED MUTATION
SEQRES 1 A 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 A 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 A 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 A 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 A 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 A 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 A 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 A 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 A 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 A 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 A 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 A 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 A 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 A 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 A 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 A 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 A 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 A 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 A 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 A 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 A 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 A 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 A 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 A 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 A 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 A 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 A 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 A 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 A 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 A 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 A 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 A 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 A 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 A 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 A 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 A 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 A 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 A 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 A 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 A 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 A 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 A 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 A 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 A 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 A 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 A 592 PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 B 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 B 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 B 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 B 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 B 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 B 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 B 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 B 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 B 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 B 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 B 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 B 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 B 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 B 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 B 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 B 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 B 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 B 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 B 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 B 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 B 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 B 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 B 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 B 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 B 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 B 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 B 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 B 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 B 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 B 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 B 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 B 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 B 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 B 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 B 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 B 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 B 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 B 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 B 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 B 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 B 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 B 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 B 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 B 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 B 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 B 592 PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 C 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 C 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 C 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 C 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 C 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 C 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 C 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 C 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 C 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 C 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 C 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 C 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 C 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 C 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 C 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 C 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 C 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 C 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 C 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 C 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 C 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 C 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 C 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 C 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 C 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 C 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 C 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 C 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 C 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 C 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 C 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 C 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 C 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 C 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 C 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 C 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 C 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 C 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 C 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 C 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 C 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 C 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 C 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 C 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 C 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 C 592 PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 D 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 D 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 D 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 D 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 D 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 D 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 D 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 D 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 D 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 D 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 D 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 D 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 D 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 D 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 D 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 D 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 D 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 D 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 D 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 D 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 D 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 D 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 D 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 D 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 D 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 D 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 D 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 D 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 D 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 D 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 D 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 D 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 D 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 D 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 D 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 D 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 D 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 D 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 D 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 D 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 D 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 D 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 D 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 D 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 D 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 D 592 PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 E 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 E 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 E 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 E 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 E 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 E 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 E 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 E 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 E 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 E 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 E 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 E 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 E 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 E 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 E 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 E 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 E 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 E 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 E 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 E 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 E 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 E 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 E 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 E 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 E 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 E 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 E 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 E 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 E 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 E 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 E 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 E 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 E 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 E 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 E 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 E 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 E 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 E 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 E 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 E 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 E 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 E 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 E 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 E 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 E 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 E 592 PHE ALA CYS ALA ALA PRO PRO
SEQRES 1 F 592 MET GLU ASN LEU TYR PHE GLN GLY GLY GLY GLY SER THR
SEQRES 2 F 592 PRO LEU PRO LEU PRO GLN GLN GLN PRO PRO GLN GLN GLU
SEQRES 3 F 592 PRO PRO PRO PRO PRO VAL PRO LEU ALA SER ARG ALA ALA
SEQRES 4 F 592 CYS GLU ALA LEU LYS ASP GLY ASN GLY ASP MET VAL TRP
SEQRES 5 F 592 PRO ASN ALA ALA THR VAL VAL GLU VAL ALA ALA TRP ARG
SEQRES 6 F 592 ASP ALA ALA PRO ALA THR ALA SER ALA ALA ALA LEU PRO
SEQRES 7 F 592 GLU HIS CYS GLU VAL SER GLY ALA ILE ALA LYS ARG THR
SEQRES 8 F 592 GLY ILE ASP GLY TYR PRO TYR GLU ILE LYS PHE ARG LEU
SEQRES 9 F 592 ARG MET PRO ALA GLU TRP ASN GLY ARG PHE PHE MET GLU
SEQRES 10 F 592 GLY GLY SER GLY THR ASN GLY SER LEU SER ALA ALA THR
SEQRES 11 F 592 GLY SER ILE GLY GLY GLY GLN ILE ALA SER ALA LEU SER
SEQRES 12 F 592 ARG ASN PHE ALA VAL ILE ALA THR ASP GLY GLY HIS ASP
SEQRES 13 F 592 ASN ALA VAL ASN ASP ASN PRO ASP ALA LEU GLY THR VAL
SEQRES 14 F 592 ALA PHE GLY LEU ASP PRO GLN ALA ARG LEU ASP TYR GLY
SEQRES 15 F 592 TYR ASN SER TYR ASP GLN VAL THR GLN ALA GLY LYS ALA
SEQRES 16 F 592 ALA VAL ALA ARG PHE TYR GLY ARG ALA ALA ASP LYS SER
SEQRES 17 F 592 TYR PHE ILE GLY CYS SEP GLU GLY GLY ARG GLU GLY MET
SEQRES 18 F 592 MET LEU SER GLN ARG PHE PRO SER HIS TYR ASP GLY ILE
SEQRES 19 F 592 VAL ALA GLY ALA PRO GLY PHE GLN LEU PRO LYS ALA GLY
SEQRES 20 F 592 ILE SER GLY ALA TRP THR THR GLN SER LEU ALA PRO ALA
SEQRES 21 F 592 ALA VAL GLY LEU ASP ALA GLN GLY VAL PRO LEU ILE ASN
SEQRES 22 F 592 LYS SER PHE SER ASP ALA ASP LEU HIS LEU LEU SER GLN
SEQRES 23 F 592 ALA ILE LEU GLY THR CYS ASP ALA LEU ASP GLY LEU ALA
SEQRES 24 F 592 ASP GLY ILE VAL ASP ASN TYR ARG ALA CYS GLN ALA ALA
SEQRES 25 F 592 PHE ASP PRO ALA THR ALA ALA ASN PRO ALA ASN GLY GLN
SEQRES 26 F 592 ALA LEU GLN CYS VAL GLY ALA LYS THR ALA ASP CYS LEU
SEQRES 27 F 592 SER PRO VAL GLN VAL THR ALA ILE LYS ARG ALA MET ALA
SEQRES 28 F 592 GLY PRO VAL ASN SER ALA GLY THR PRO LEU TYR ASN ARG
SEQRES 29 F 592 TRP ALA TRP ASP ALA GLY MET SER GLY LEU SER GLY THR
SEQRES 30 F 592 THR TYR ASN GLN GLY TRP ARG SER TRP TRP LEU GLY SER
SEQRES 31 F 592 PHE ASN SER SER ALA ASN ASN ALA GLN ARG VAL SER GLY
SEQRES 32 F 592 PHE SER ALA ARG SER TRP LEU VAL ASP PHE ALA THR PRO
SEQRES 33 F 592 PRO GLU PRO MET PRO MET THR GLN VAL ALA ALA ARG MET
SEQRES 34 F 592 MET LYS PHE ASP PHE ASP ILE ASP PRO LEU LYS ILE TRP
SEQRES 35 F 592 ALA THR SER GLY GLN PHE THR GLN SER SER MET ASP TRP
SEQRES 36 F 592 HIS GLY ALA THR SER THR ASP LEU ALA ALA PHE ARG ASP
SEQRES 37 F 592 ARG GLY GLY LYS MET ILE LEU TYR HIS GLY MET SER ASP
SEQRES 38 F 592 ALA ALA PHE SER ALA LEU ASP THR ALA ASP TRP TYR GLU
SEQRES 39 F 592 ARG LEU GLY ALA ALA MET PRO GLY ALA ALA GLY PHE ALA
SEQRES 40 F 592 ARG LEU PHE LEU VAL PRO GLY MET ASN HIS CYS SER GLY
SEQRES 41 F 592 GLY PRO GLY THR ASP ARG PHE ASP MET LEU THR PRO LEU
SEQRES 42 F 592 VAL ALA TRP VAL GLU ARG GLY GLU ALA PRO ASP GLN ILE
SEQRES 43 F 592 SER ALA TRP SER GLY THR PRO GLY TYR PHE GLY VAL ALA
SEQRES 44 F 592 ALA ARG THR ARG PRO LEU CYS PRO TYR PRO GLN ILE ALA
SEQRES 45 F 592 ARG TYR LYS GLY SER GLY ASP ILE ASN THR GLU ALA ASN
SEQRES 46 F 592 PHE ALA CYS ALA ALA PRO PRO
MODRES 8EKG SEP A 225 SER MODIFIED RESIDUE
MODRES 8EKG SEP B 225 SER MODIFIED RESIDUE
MODRES 8EKG SEP C 225 SER MODIFIED RESIDUE
MODRES 8EKG SEP D 225 SER MODIFIED RESIDUE
MODRES 8EKG SEP E 225 SER MODIFIED RESIDUE
MODRES 8EKG SEP F 225 SER MODIFIED RESIDUE
HET SEP A 225 10
HET SEP B 225 10
HET SEP C 225 10
HET SEP D 225 10
HET SEP E 225 10
HET SEP F 225 10
HET CA A 701 1
HET PEG A 702 7
HET EDO A 703 4
HET CA B 701 1
HET SO4 B 702 5
HET SO4 B 703 5
HET EDO B 704 4
HET EDO B 705 4
HET EDO B 706 4
HET EDO B 707 4
HET EDO B 708 4
HET EDO B 709 4
HET CA C 701 1
HET EDO C 702 4
HET CA D 701 1
HET EDO D 702 4
HET EDO D 703 4
HET CA E 701 1
HET SO4 E 702 5
HET SO4 E 703 5
HET EDO E 704 4
HET CA F 701 1
HETNAM SEP PHOSPHOSERINE
HETNAM CA CALCIUM ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETSYN SEP PHOSPHONOSERINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEP 6(C3 H8 N O6 P)
FORMUL 7 CA 6(CA 2+)
FORMUL 8 PEG C4 H10 O3
FORMUL 9 EDO 11(C2 H6 O2)
FORMUL 11 SO4 4(O4 S 2-)
FORMUL 29 HOH *403(H2 O)
HELIX 1 AA1 SER A 47 ALA A 53 1 7
HELIX 2 AA2 ALA A 152 ASN A 156 5 5
HELIX 3 AA3 LEU A 177 LEU A 184 5 8
HELIX 4 AA4 ASP A 185 TYR A 194 1 10
HELIX 5 AA5 TYR A 194 GLY A 213 1 20
HELIX 6 AA6 SEP A 225 PHE A 238 1 14
HELIX 7 AA7 GLN A 253 PRO A 255 5 3
HELIX 8 AA8 LYS A 256 ALA A 269 1 14
HELIX 9 AA9 PRO A 270 ALA A 272 5 3
HELIX 10 AB1 LEU A 282 SER A 286 5 5
HELIX 11 AB2 SER A 288 ASP A 304 1 17
HELIX 12 AB3 ALA A 305 GLY A 308 5 4
HELIX 13 AB4 ASN A 316 PHE A 324 1 9
HELIX 14 AB5 SER A 350 GLY A 363 1 14
HELIX 15 AB6 ASP A 379 SER A 383 5 5
HELIX 16 AB7 TRP A 394 LEU A 399 1 6
HELIX 17 AB8 GLY A 414 ASP A 423 1 10
HELIX 18 AB9 PRO A 432 THR A 434 5 3
HELIX 19 AC1 GLN A 435 LYS A 442 1 8
HELIX 20 AC2 ILE A 447 TRP A 453 5 7
HELIX 21 AC3 SER A 462 HIS A 467 1 6
HELIX 22 AC4 LEU A 474 ARG A 480 1 7
HELIX 23 AC5 SER A 496 MET A 511 1 16
HELIX 24 AC6 GLY A 513 GLY A 516 5 4
HELIX 25 AC7 MET A 540 GLU A 549 1 10
HELIX 26 AC8 THR A 563 PHE A 567 5 5
HELIX 27 AC9 THR A 593 ALA A 595 5 3
HELIX 28 AD1 ARG B 48 ALA B 53 1 6
HELIX 29 AD2 LEU B 54 ASP B 56 5 3
HELIX 30 AD3 ALA B 152 ASN B 156 5 5
HELIX 31 AD4 LEU B 177 LEU B 184 5 8
HELIX 32 AD5 ASP B 185 TYR B 194 1 10
HELIX 33 AD6 TYR B 194 GLY B 213 1 20
HELIX 34 AD7 SEP B 225 PHE B 238 1 14
HELIX 35 AD8 GLN B 253 PRO B 255 5 3
HELIX 36 AD9 LYS B 256 ALA B 269 1 14
HELIX 37 AE1 LEU B 282 SER B 286 5 5
HELIX 38 AE2 SER B 288 ASP B 304 1 17
HELIX 39 AE3 ALA B 305 GLY B 308 5 4
HELIX 40 AE4 ASN B 316 ALA B 322 1 7
HELIX 41 AE5 SER B 350 GLY B 363 1 14
HELIX 42 AE6 ASP B 379 SER B 383 5 5
HELIX 43 AE7 TRP B 394 LEU B 399 1 6
HELIX 44 AE8 GLY B 414 ASP B 423 1 10
HELIX 45 AE9 PRO B 432 THR B 434 5 3
HELIX 46 AF1 GLN B 435 LYS B 442 1 8
HELIX 47 AF2 ASP B 448 TRP B 453 5 6
HELIX 48 AF3 SER B 462 GLY B 468 1 7
HELIX 49 AF4 LEU B 474 ARG B 480 1 7
HELIX 50 AF5 SER B 496 MET B 511 1 16
HELIX 51 AF6 GLY B 513 GLY B 516 5 4
HELIX 52 AF7 MET B 540 GLY B 551 1 12
HELIX 53 AF8 THR B 563 GLY B 568 5 6
HELIX 54 AF9 THR B 593 ALA B 595 5 3
HELIX 55 AG1 ARG C 48 ALA C 53 1 6
HELIX 56 AG2 ALA C 152 ASN C 156 5 5
HELIX 57 AG3 LEU C 177 LEU C 184 5 8
HELIX 58 AG4 ASP C 185 TYR C 194 1 10
HELIX 59 AG5 TYR C 194 GLY C 213 1 20
HELIX 60 AG6 SEP C 225 PHE C 238 1 14
HELIX 61 AG7 GLN C 253 PRO C 255 5 3
HELIX 62 AG8 LYS C 256 ALA C 269 1 14
HELIX 63 AG9 LEU C 282 SER C 286 5 5
HELIX 64 AH1 SER C 288 ASP C 304 1 17
HELIX 65 AH2 ALA C 305 GLY C 308 5 4
HELIX 66 AH3 ASN C 316 PHE C 324 1 9
HELIX 67 AH4 SER C 350 GLY C 363 1 14
HELIX 68 AH5 ASP C 379 SER C 383 5 5
HELIX 69 AH6 TRP C 394 LEU C 399 1 6
HELIX 70 AH7 GLY C 414 PHE C 424 1 11
HELIX 71 AH8 PRO C 432 THR C 434 5 3
HELIX 72 AH9 GLN C 435 LYS C 442 1 8
HELIX 73 AI1 ILE C 447 TRP C 453 5 7
HELIX 74 AI2 SER C 462 HIS C 467 1 6
HELIX 75 AI3 LEU C 474 ARG C 480 1 7
HELIX 76 AI4 SER C 496 MET C 511 1 16
HELIX 77 AI5 GLY C 513 GLY C 516 5 4
HELIX 78 AI6 MET C 540 GLU C 549 1 10
HELIX 79 AI7 THR C 563 GLY C 568 5 6
HELIX 80 AI8 THR C 593 ALA C 595 5 3
HELIX 81 AI9 ARG D 48 ALA D 53 1 6
HELIX 82 AJ1 ALA D 152 ASN D 156 5 5
HELIX 83 AJ2 ASN D 173 LEU D 184 5 12
HELIX 84 AJ3 ASP D 185 TYR D 194 1 10
HELIX 85 AJ4 TYR D 194 GLY D 213 1 20
HELIX 86 AJ5 SEP D 225 PHE D 238 1 14
HELIX 87 AJ6 GLN D 253 PRO D 255 5 3
HELIX 88 AJ7 LYS D 256 ALA D 269 1 14
HELIX 89 AJ8 PRO D 270 ALA D 272 5 3
HELIX 90 AJ9 LEU D 282 SER D 286 5 5
HELIX 91 AK1 SER D 288 ASP D 304 1 17
HELIX 92 AK2 ALA D 305 GLY D 308 5 4
HELIX 93 AK3 ASN D 316 PHE D 324 1 9
HELIX 94 AK4 SER D 350 GLY D 363 1 14
HELIX 95 AK5 ASP D 379 SER D 383 5 5
HELIX 96 AK6 TRP D 394 LEU D 399 1 6
HELIX 97 AK7 ALA D 409 GLY D 414 1 6
HELIX 98 AK8 GLY D 414 PHE D 424 1 11
HELIX 99 AK9 PRO D 432 THR D 434 5 3
HELIX 100 AL1 GLN D 435 LYS D 442 1 8
HELIX 101 AL2 ASP D 448 TRP D 453 5 6
HELIX 102 AL3 SER D 462 GLY D 468 1 7
HELIX 103 AL4 LEU D 474 ARG D 480 1 7
HELIX 104 AL5 SER D 496 MET D 511 1 16
HELIX 105 AL6 GLY D 513 GLY D 516 5 4
HELIX 106 AL7 MET D 540 ARG D 550 1 11
HELIX 107 AL8 THR D 563 PHE D 567 5 5
HELIX 108 AL9 SER E 47 ALA E 53 1 7
HELIX 109 AM1 LEU E 54 ASP E 56 5 3
HELIX 110 AM2 ALA E 152 ASN E 156 5 5
HELIX 111 AM3 ASN E 173 LEU E 177 5 5
HELIX 112 AM4 VAL E 180 LEU E 184 5 5
HELIX 113 AM5 ASP E 185 TYR E 194 1 10
HELIX 114 AM6 TYR E 194 GLY E 213 1 20
HELIX 115 AM7 SEP E 225 PHE E 238 1 14
HELIX 116 AM8 GLN E 253 PRO E 255 5 3
HELIX 117 AM9 LYS E 256 ALA E 269 1 14
HELIX 118 AN1 PRO E 270 ALA E 272 5 3
HELIX 119 AN2 LEU E 282 SER E 286 5 5
HELIX 120 AN3 SER E 288 ASP E 304 1 17
HELIX 121 AN4 ALA E 305 GLY E 308 5 4
HELIX 122 AN5 ASN E 316 PHE E 324 1 9
HELIX 123 AN6 SER E 350 GLY E 363 1 14
HELIX 124 AN7 ASP E 379 SER E 383 5 5
HELIX 125 AN8 TRP E 394 LEU E 399 1 6
HELIX 126 AN9 GLY E 414 ASP E 423 1 10
HELIX 127 AO1 GLN E 435 LYS E 442 1 8
HELIX 128 AO2 ASP E 448 TRP E 453 5 6
HELIX 129 AO3 SER E 462 GLY E 468 1 7
HELIX 130 AO4 LEU E 474 ARG E 480 1 7
HELIX 131 AO5 SER E 496 MET E 511 1 16
HELIX 132 AO6 GLY E 513 GLY E 516 5 4
HELIX 133 AO7 MET E 540 GLU E 549 1 10
HELIX 134 AO8 THR E 563 GLY E 568 5 6
HELIX 135 AO9 THR E 593 ALA E 595 5 3
HELIX 136 AP1 ARG F 48 ALA F 53 1 6
HELIX 137 AP2 ASN F 173 LEU F 184 5 12
HELIX 138 AP3 ASP F 185 TYR F 194 1 10
HELIX 139 AP4 TYR F 194 GLY F 213 1 20
HELIX 140 AP5 SEP F 225 PHE F 238 1 14
HELIX 141 AP6 GLN F 253 PRO F 255 5 3
HELIX 142 AP7 LYS F 256 ALA F 269 1 14
HELIX 143 AP8 ILE F 283 PHE F 287 5 5
HELIX 144 AP9 SER F 288 ASP F 304 1 17
HELIX 145 AQ1 ALA F 305 GLY F 308 5 4
HELIX 146 AQ2 ASN F 316 PHE F 324 1 9
HELIX 147 AQ3 SER F 350 GLY F 363 1 14
HELIX 148 AQ4 ASP F 379 SER F 383 5 5
HELIX 149 AQ5 TRP F 394 LEU F 399 1 6
HELIX 150 AQ6 ALA F 409 GLY F 414 1 6
HELIX 151 AQ7 GLY F 414 ASP F 423 1 10
HELIX 152 AQ8 PRO F 432 THR F 434 5 3
HELIX 153 AQ9 GLN F 435 MET F 440 1 6
HELIX 154 AR1 ASP F 448 TRP F 453 5 6
HELIX 155 AR2 SER F 462 HIS F 467 1 6
HELIX 156 AR3 LEU F 474 ARG F 480 1 7
HELIX 157 AR4 SER F 496 MET F 511 1 16
HELIX 158 AR5 GLY F 513 GLY F 516 5 4
HELIX 159 AR6 MET F 540 GLY F 551 1 12
HELIX 160 AR7 THR F 563 GLY F 568 5 6
SHEET 1 AA1 9 THR A 68 ARG A 76 0
SHEET 2 AA1 9 HIS A 91 THR A 102 -1 O HIS A 91 N ARG A 76
SHEET 3 AA1 9 PRO A 108 PRO A 118 -1 O LEU A 115 N VAL A 94
SHEET 4 AA1 9 ALA A 158 THR A 162 -1 O VAL A 159 N ARG A 116
SHEET 5 AA1 9 ARG A 124 GLU A 128 1 N PHE A 126 O ALA A 158
SHEET 6 AA1 9 LYS A 218 CYS A 224 1 O LYS A 218 N PHE A 125
SHEET 7 AA1 9 GLY A 244 GLY A 248 1 O GLY A 248 N GLY A 223
SHEET 8 AA1 9 LYS A 483 GLY A 489 1 O ILE A 485 N ILE A 245
SHEET 9 AA1 9 ALA A 518 VAL A 523 1 O PHE A 521 N LEU A 486
SHEET 1 AA2 2 LEU A 385 SER A 386 0
SHEET 2 AA2 2 THR A 389 TYR A 390 -1 O THR A 389 N SER A 386
SHEET 1 AA3 3 ARG A 537 PHE A 538 0
SHEET 2 AA3 3 ILE A 557 TRP A 560 -1 O TRP A 560 N ARG A 537
SHEET 3 AA3 3 THR A 573 LEU A 576 -1 O LEU A 576 N ILE A 557
SHEET 1 AA4 2 ILE A 582 TYR A 585 0
SHEET 2 AA4 2 PHE A 597 ALA A 600 -1 O ALA A 598 N ARG A 584
SHEET 1 AA5 9 THR B 68 ARG B 76 0
SHEET 2 AA5 9 HIS B 91 THR B 102 -1 O ALA B 97 N VAL B 69
SHEET 3 AA5 9 PRO B 108 PRO B 118 -1 O ILE B 111 N ILE B 98
SHEET 4 AA5 9 ALA B 158 THR B 162 -1 O VAL B 159 N ARG B 116
SHEET 5 AA5 9 ARG B 124 GLU B 128 1 N PHE B 126 O ALA B 158
SHEET 6 AA5 9 LYS B 218 CYS B 224 1 O TYR B 220 N PHE B 125
SHEET 7 AA5 9 GLY B 244 GLY B 248 1 O GLY B 248 N GLY B 223
SHEET 8 AA5 9 LYS B 483 GLY B 489 1 O ILE B 485 N ILE B 245
SHEET 9 AA5 9 ALA B 518 VAL B 523 1 O PHE B 521 N LEU B 486
SHEET 1 AA6 2 ALA B 330 ASN B 331 0
SHEET 2 AA6 2 GLN B 336 ALA B 337 -1 O GLN B 336 N ASN B 331
SHEET 1 AA7 2 LEU B 385 SER B 386 0
SHEET 2 AA7 2 THR B 389 TYR B 390 -1 O THR B 389 N SER B 386
SHEET 1 AA8 3 ARG B 537 PHE B 538 0
SHEET 2 AA8 3 ILE B 557 TRP B 560 -1 O TRP B 560 N ARG B 537
SHEET 3 AA8 3 THR B 573 LEU B 576 -1 O ARG B 574 N ALA B 559
SHEET 1 AA9 2 ILE B 582 TYR B 585 0
SHEET 2 AA9 2 PHE B 597 ALA B 600 -1 O ALA B 600 N ILE B 582
SHEET 1 AB1 9 THR C 68 ARG C 76 0
SHEET 2 AB1 9 HIS C 91 THR C 102 -1 O ALA C 97 N VAL C 69
SHEET 3 AB1 9 PRO C 108 PRO C 118 -1 O LEU C 115 N VAL C 94
SHEET 4 AB1 9 ALA C 158 THR C 162 -1 O VAL C 159 N ARG C 116
SHEET 5 AB1 9 ARG C 124 GLU C 128 1 N PHE C 126 O ALA C 158
SHEET 6 AB1 9 LYS C 218 CYS C 224 1 O LYS C 218 N PHE C 125
SHEET 7 AB1 9 GLY C 244 GLY C 248 1 O GLY C 244 N PHE C 221
SHEET 8 AB1 9 LYS C 483 GLY C 489 1 O ILE C 485 N ILE C 245
SHEET 9 AB1 9 ALA C 518 VAL C 523 1 O VAL C 523 N HIS C 488
SHEET 1 AB2 2 LEU C 385 SER C 386 0
SHEET 2 AB2 2 THR C 389 TYR C 390 -1 O THR C 389 N SER C 386
SHEET 1 AB3 2 ILE C 557 TRP C 560 0
SHEET 2 AB3 2 THR C 573 LEU C 576 -1 O LEU C 576 N ILE C 557
SHEET 1 AB4 2 ILE C 582 TYR C 585 0
SHEET 2 AB4 2 PHE C 597 ALA C 600 -1 O ALA C 598 N ARG C 584
SHEET 1 AB5 9 THR D 68 ARG D 76 0
SHEET 2 AB5 9 HIS D 91 THR D 102 -1 O GLU D 93 N ALA D 74
SHEET 3 AB5 9 PRO D 108 PRO D 118 -1 O LEU D 115 N VAL D 94
SHEET 4 AB5 9 ALA D 158 THR D 162 -1 O VAL D 159 N ARG D 116
SHEET 5 AB5 9 ARG D 124 GLU D 128 1 N PHE D 126 O ALA D 158
SHEET 6 AB5 9 LYS D 218 CYS D 224 1 O TYR D 220 N PHE D 125
SHEET 7 AB5 9 GLY D 244 GLY D 248 1 O VAL D 246 N PHE D 221
SHEET 8 AB5 9 LYS D 483 GLY D 489 1 O ILE D 485 N ILE D 245
SHEET 9 AB5 9 ALA D 518 VAL D 523 1 O ARG D 519 N LEU D 486
SHEET 1 AB6 2 LEU D 385 SER D 386 0
SHEET 2 AB6 2 THR D 389 TYR D 390 -1 O THR D 389 N SER D 386
SHEET 1 AB7 2 ILE D 557 TRP D 560 0
SHEET 2 AB7 2 THR D 573 LEU D 576 -1 O LEU D 576 N ILE D 557
SHEET 1 AB8 2 ILE D 582 TYR D 585 0
SHEET 2 AB8 2 PHE D 597 ALA D 600 -1 O ALA D 598 N ARG D 584
SHEET 1 AB9 9 THR E 68 ARG E 76 0
SHEET 2 AB9 9 HIS E 91 THR E 102 -1 O HIS E 91 N ARG E 76
SHEET 3 AB9 9 PRO E 108 PRO E 118 -1 O LEU E 115 N VAL E 94
SHEET 4 AB9 9 ALA E 158 THR E 162 -1 O VAL E 159 N ARG E 116
SHEET 5 AB9 9 ARG E 124 GLU E 128 1 N PHE E 126 O ALA E 158
SHEET 6 AB9 9 LYS E 218 CYS E 224 1 O TYR E 220 N PHE E 125
SHEET 7 AB9 9 GLY E 244 GLY E 248 1 O GLY E 248 N GLY E 223
SHEET 8 AB9 9 LYS E 483 GLY E 489 1 O ILE E 485 N ILE E 245
SHEET 9 AB9 9 ALA E 518 VAL E 523 1 O VAL E 523 N HIS E 488
SHEET 1 AC1 2 LEU E 385 SER E 386 0
SHEET 2 AC1 2 THR E 389 TYR E 390 -1 O THR E 389 N SER E 386
SHEET 1 AC2 3 ARG E 537 PHE E 538 0
SHEET 2 AC2 3 ILE E 557 TRP E 560 -1 O TRP E 560 N ARG E 537
SHEET 3 AC2 3 THR E 573 LEU E 576 -1 O LEU E 576 N ILE E 557
SHEET 1 AC3 2 ILE E 582 TYR E 585 0
SHEET 2 AC3 2 PHE E 597 ALA E 600 -1 O ALA E 598 N ARG E 584
SHEET 1 AC4 9 THR F 68 ARG F 76 0
SHEET 2 AC4 9 HIS F 91 THR F 102 -1 O ALA F 97 N VAL F 69
SHEET 3 AC4 9 PRO F 108 PRO F 118 -1 O TYR F 109 N ARG F 101
SHEET 4 AC4 9 ALA F 158 THR F 162 -1 O VAL F 159 N ARG F 116
SHEET 5 AC4 9 ARG F 124 GLU F 128 1 N PHE F 126 O ALA F 158
SHEET 6 AC4 9 LYS F 218 CYS F 224 1 O LYS F 218 N PHE F 125
SHEET 7 AC4 9 GLY F 244 GLY F 248 1 O GLY F 248 N GLY F 223
SHEET 8 AC4 9 LYS F 483 GLY F 489 1 O ILE F 485 N ILE F 245
SHEET 9 AC4 9 ALA F 518 VAL F 523 1 O VAL F 523 N HIS F 488
SHEET 1 AC5 2 LEU F 275 ASP F 276 0
SHEET 2 AC5 2 VAL F 280 PRO F 281 -1 O VAL F 280 N ASP F 276
SHEET 1 AC6 2 LEU F 385 SER F 386 0
SHEET 2 AC6 2 THR F 389 TYR F 390 -1 O THR F 389 N SER F 386
SHEET 1 AC7 3 ARG F 537 PHE F 538 0
SHEET 2 AC7 3 ILE F 557 TRP F 560 -1 O TRP F 560 N ARG F 537
SHEET 3 AC7 3 THR F 573 LEU F 576 -1 O LEU F 576 N ILE F 557
SHEET 1 AC8 2 ILE F 582 TYR F 585 0
SHEET 2 AC8 2 PHE F 597 ALA F 600 -1 O ALA F 598 N ARG F 584
SSBOND 1 CYS A 51 CYS A 92 1555 1555 2.03
SSBOND 2 CYS A 224 CYS A 529 1555 1555 2.03
SSBOND 3 CYS A 303 CYS A 320 1555 1555 2.03
SSBOND 4 CYS A 340 CYS A 348 1555 1555 2.03
SSBOND 5 CYS A 577 CYS A 599 1555 1555 2.03
SSBOND 6 CYS B 51 CYS B 92 1555 1555 2.03
SSBOND 7 CYS B 224 CYS B 529 1555 1555 2.03
SSBOND 8 CYS B 303 CYS B 320 1555 1555 2.03
SSBOND 9 CYS B 340 CYS B 348 1555 1555 2.03
SSBOND 10 CYS B 577 CYS B 599 1555 1555 2.03
SSBOND 11 CYS C 51 CYS C 92 1555 1555 2.03
SSBOND 12 CYS C 224 CYS C 529 1555 1555 2.03
SSBOND 13 CYS C 303 CYS C 320 1555 1555 2.03
SSBOND 14 CYS C 340 CYS C 348 1555 1555 2.03
SSBOND 15 CYS C 577 CYS C 599 1555 1555 2.03
SSBOND 16 CYS D 51 CYS D 92 1555 1555 2.03
SSBOND 17 CYS D 224 CYS D 529 1555 1555 2.03
SSBOND 18 CYS D 303 CYS D 320 1555 1555 2.03
SSBOND 19 CYS D 340 CYS D 348 1555 1555 2.03
SSBOND 20 CYS D 577 CYS D 599 1555 1555 2.03
SSBOND 21 CYS E 51 CYS E 92 1555 1555 2.03
SSBOND 22 CYS E 224 CYS E 529 1555 1555 2.03
SSBOND 23 CYS E 303 CYS E 320 1555 1555 2.03
SSBOND 24 CYS E 340 CYS E 348 1555 1555 2.03
SSBOND 25 CYS E 577 CYS E 599 1555 1555 2.03
SSBOND 26 CYS F 51 CYS F 92 1555 1555 2.03
SSBOND 27 CYS F 224 CYS F 529 1555 1555 2.03
SSBOND 28 CYS F 303 CYS F 320 1555 1555 2.03
SSBOND 29 CYS F 340 CYS F 348 1555 1555 2.03
SSBOND 30 CYS F 577 CYS F 599 1555 1555 2.03
LINK C CYS A 224 N SEP A 225 1555 1555 1.33
LINK C SEP A 225 N GLU A 226 1555 1555 1.33
LINK C CYS B 224 N SEP B 225 1555 1555 1.33
LINK C SEP B 225 N GLU B 226 1555 1555 1.32
LINK C CYS C 224 N SEP C 225 1555 1555 1.33
LINK C SEP C 225 N GLU C 226 1555 1555 1.33
LINK C CYS D 224 N SEP D 225 1555 1555 1.33
LINK C SEP D 225 N GLU D 226 1555 1555 1.33
LINK C CYS E 224 N SEP E 225 1555 1555 1.33
LINK C SEP E 225 N GLU E 226 1555 1555 1.33
LINK C CYS F 224 N SEP F 225 1555 1555 1.33
LINK C SEP F 225 N GLU F 226 1555 1555 1.33
LINK O ASP A 304 CA CA A 701 1555 1555 2.75
LINK OD1 ASP A 304 CA CA A 701 1555 1555 2.56
LINK OD1 ASP A 307 CA CA A 701 1555 1555 2.62
LINK OD2 ASP A 307 CA CA A 701 1555 1555 2.79
LINK O LEU A 309 CA CA A 701 1555 1555 2.74
LINK OD1 ASP A 311 CA CA A 701 1555 1555 2.37
LINK O ILE A 313 CA CA A 701 1555 1555 2.31
LINK O ASP B 304 CA CA B 701 1555 1555 2.59
LINK OD1 ASP B 304 CA CA B 701 1555 1555 2.50
LINK OD1 ASP B 307 CA CA B 701 1555 1555 2.87
LINK OD2 ASP B 307 CA CA B 701 1555 1555 2.46
LINK O LEU B 309 CA CA B 701 1555 1555 2.44
LINK OD1 ASP B 311 CA CA B 701 1555 1555 2.30
LINK O ILE B 313 CA CA B 701 1555 1555 2.31
LINK O ASP C 304 CA CA C 701 1555 1555 2.47
LINK OD1 ASP C 304 CA CA C 701 1555 1555 2.63
LINK OD1 ASP C 307 CA CA C 701 1555 1555 2.37
LINK OD2 ASP C 307 CA CA C 701 1555 1555 3.03
LINK O LEU C 309 CA CA C 701 1555 1555 2.24
LINK OD1 ASP C 311 CA CA C 701 1555 1555 2.51
LINK O ILE C 313 CA CA C 701 1555 1555 2.67
LINK O ASP D 304 CA CA D 701 1555 1555 2.98
LINK OD1 ASP D 304 CA CA D 701 1555 1555 2.80
LINK OD1 ASP D 307 CA CA D 701 1555 1555 2.35
LINK OD2 ASP D 307 CA CA D 701 1555 1555 2.58
LINK O LEU D 309 CA CA D 701 1555 1555 2.41
LINK OD1 ASP D 311 CA CA D 701 1555 1555 2.28
LINK O ILE D 313 CA CA D 701 1555 1555 2.37
LINK O ASP E 304 CA CA E 701 1555 1555 2.83
LINK OD1 ASP E 304 CA CA E 701 1555 1555 2.57
LINK OD1 ASP E 307 CA CA E 701 1555 1555 2.36
LINK OD2 ASP E 307 CA CA E 701 1555 1555 2.78
LINK O LEU E 309 CA CA E 701 1555 1555 2.34
LINK OD1 ASP E 311 CA CA E 701 1555 1555 2.33
LINK O ILE E 313 CA CA E 701 1555 1555 2.60
LINK O ASP F 304 CA CA F 701 1555 1555 2.75
LINK OD1 ASP F 304 CA CA F 701 1555 1555 2.76
LINK OD1 ASP F 307 CA CA F 701 1555 1555 2.54
LINK OD2 ASP F 307 CA CA F 701 1555 1555 2.50
LINK O LEU F 309 CA CA F 701 1555 1555 2.34
LINK OD1 ASP F 311 CA CA F 701 1555 1555 2.34
LINK O ILE F 313 CA CA F 701 1555 1555 2.46
CISPEP 1 THR A 426 PRO A 427 0 -1.44
CISPEP 2 TYR A 579 PRO A 580 0 2.13
CISPEP 3 THR B 426 PRO B 427 0 -0.68
CISPEP 4 TYR B 579 PRO B 580 0 0.31
CISPEP 5 THR C 426 PRO C 427 0 -1.06
CISPEP 6 TYR C 579 PRO C 580 0 2.05
CISPEP 7 THR D 426 PRO D 427 0 -0.84
CISPEP 8 TYR D 579 PRO D 580 0 2.50
CISPEP 9 THR E 426 PRO E 427 0 -0.32
CISPEP 10 TYR E 579 PRO E 580 0 -1.95
CISPEP 11 THR F 426 PRO F 427 0 -2.95
CISPEP 12 TYR F 579 PRO F 580 0 1.58
CRYST1 63.967 120.514 126.290 90.44 95.15 90.20 P 1 6
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 0.015633 0.000055 0.001409 0.00000
SCALE2 0.000000 0.008298 0.000067 0.00000
SCALE3 0.000000 0.000000 0.007951 0.00000
TER 4129 PRO A 603
TER 8253 PRO B 603
TER 12377 PRO C 603
TER 16501 PRO D 603
TER 20630 PRO E 603
TER 24754 PRO F 603
MASTER 887 0 28 160 98 0 0 625228 6 257 276
END |