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HEADER OXIDOREDUCTASE 10-JAN-13 4IQ4
TITLE STRUCTURE OF A 16 NM PROTEIN CAGE DESIGNED BY FUSING SYMMETRIC
TITLE 2 OLIGOMERIC DOMAINS, TRIPLE MUTANT, P21212 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-HAEM BROMOPEROXIDASE BPO-A2, MATRIX PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: BPO2, BROMIDE PEROXIDASE, M1;
COMPND 5 EC: 1.11.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES AUREOFACIENS, INFLUENZA A VIRUS;
SOURCE 3 ORGANISM_TAXID: 1894, 211044;
SOURCE 4 STRAIN: A/PUERTO RICO/8/1934 H1N1;
SOURCE 5 GENE: BPOA2, BROMOPEROXIDASE A2 AND M1 MATRIX FUSION, M;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS PROTEIN DESIGN, BIONANOTECHNOLOGY, PROTEIN ASSEMBLY, SYMMETRIC
KEYWDS 2 OLIGOMERIC DOMAINS, BIOMATERIALS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-T.LAI,M.R.SAWAYA,T.O.YEATES
REVDAT 1 24-JUL-13 4IQ4 0
JRNL AUTH Y.T.LAI,K.L.TSAI,M.R.SAWAYA,F.J.ASTURIAS,T.O.YEATES
JRNL TITL STRUCTURE AND FLEXIBILITY OF NANOSCALE PROTEIN CAGES
JRNL TITL 2 DESIGNED BY SYMMETRIC SELF-ASSEMBLY.
JRNL REF J.AM.CHEM.SOC. V. 135 7738 2013
JRNL REFN ISSN 0002-7863
JRNL PMID 23621606
JRNL DOI 10.1021/JA402277F
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 93.29
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 37833
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1893
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 93.3270 - 8.4226 0.95 2692 143 0.1816 0.1849
REMARK 3 2 8.4226 - 6.6858 0.96 2563 135 0.2036 0.2180
REMARK 3 3 6.6858 - 5.8409 0.98 2621 138 0.2188 0.2604
REMARK 3 4 5.8409 - 5.3069 0.99 2605 137 0.2046 0.2599
REMARK 3 5 5.3069 - 4.9265 0.97 2551 135 0.1916 0.2103
REMARK 3 6 4.9265 - 4.6361 0.97 2548 134 0.1760 0.2459
REMARK 3 7 4.6361 - 4.4039 0.99 2583 136 0.1879 0.2170
REMARK 3 8 4.4039 - 4.2122 0.99 2583 136 0.1812 0.2319
REMARK 3 9 4.2122 - 4.0500 0.99 2586 136 0.1951 0.2282
REMARK 3 10 4.0500 - 3.9103 1.00 2582 136 0.2078 0.2328
REMARK 3 11 3.9103 - 3.7880 0.98 2552 134 0.2067 0.2431
REMARK 3 12 3.7880 - 3.6797 0.97 2507 132 0.2188 0.2525
REMARK 3 13 3.6797 - 3.5829 0.99 2577 135 0.2386 0.2764
REMARK 3 14 3.5829 - 3.4954 0.93 2390 126 0.2586 0.3154
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 : 0.80
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.660
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 71.07
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 103.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 20850
REMARK 3 ANGLE : 0.723 28374
REMARK 3 CHIRALITY : 0.059 3204
REMARK 3 PLANARITY : 0.003 3696
REMARK 3 DIHEDRAL : 15.187 7404
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain A and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7971 45.8201 202.6478
REMARK 3 T TENSOR
REMARK 3 T11: 0.5538 T22: 0.4636
REMARK 3 T33: 0.7155 T12: -0.0037
REMARK 3 T13: 0.0215 T23: -0.0685
REMARK 3 L TENSOR
REMARK 3 L11: 1.3263 L22: 2.4359
REMARK 3 L33: 3.3280 L12: 0.3396
REMARK 3 L13: 0.0964 L23: -0.5480
REMARK 3 S TENSOR
REMARK 3 S11: 0.0919 S12: -0.1154 S13: 0.4745
REMARK 3 S21: 0.3945 S22: -0.0917 S23: -0.0348
REMARK 3 S31: -0.4077 S32: 0.0954 S33: 0.0231
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain A and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): 49.1595 30.8972 221.6766
REMARK 3 T TENSOR
REMARK 3 T11: 1.4414 T22: 0.9537
REMARK 3 T33: 1.4268 T12: -0.2323
REMARK 3 T13: -0.3286 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 1.1300 L22: 3.7673
REMARK 3 L33: 1.4647 L12: 2.0648
REMARK 3 L13: -1.2931 L23: -2.3497
REMARK 3 S TENSOR
REMARK 3 S11: 0.5897 S12: -0.6849 S13: -0.2226
REMARK 3 S21: 0.6455 S22: -0.2247 S23: -0.4896
REMARK 3 S31: -0.0588 S32: 0.3185 S33: -0.3292
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain A and resid 286:440
REMARK 3 ORIGIN FOR THE GROUP (A): 45.9678 9.9118 224.3894
REMARK 3 T TENSOR
REMARK 3 T11: 0.9692 T22: 0.7051
REMARK 3 T33: 0.6648 T12: -0.1231
REMARK 3 T13: 0.0049 T23: -0.0208
REMARK 3 L TENSOR
REMARK 3 L11: 4.4549 L22: 4.8266
REMARK 3 L33: 4.1545 L12: -0.3201
REMARK 3 L13: 2.7822 L23: -0.1452
REMARK 3 S TENSOR
REMARK 3 S11: -0.2345 S12: 0.1824 S13: 0.2183
REMARK 3 S21: 0.3061 S22: -0.0439 S23: -0.2383
REMARK 3 S31: -0.4740 S32: 0.3322 S33: 0.2728
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain B and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7415 39.4986 174.5345
REMARK 3 T TENSOR
REMARK 3 T11: 0.4513 T22: 0.7199
REMARK 3 T33: 0.7757 T12: 0.0927
REMARK 3 T13: -0.0694 T23: -0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 1.9279 L22: 2.9821
REMARK 3 L33: 2.6789 L12: -0.0534
REMARK 3 L13: 0.0487 L23: 1.0537
REMARK 3 S TENSOR
REMARK 3 S11: -0.0342 S12: -0.0248 S13: 0.2903
REMARK 3 S21: -0.3274 S22: -0.1450 S23: 0.7206
REMARK 3 S31: -0.3704 S32: -0.8793 S33: 0.2161
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain B and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8192 55.4872 184.1686
REMARK 3 T TENSOR
REMARK 3 T11: 1.1007 T22: 1.7247
REMARK 3 T33: 1.1778 T12: 0.4451
REMARK 3 T13: 0.2589 T23: 0.2358
REMARK 3 L TENSOR
REMARK 3 L11: 3.2107 L22: 1.3175
REMARK 3 L33: 4.6481 L12: -1.1803
REMARK 3 L13: -3.3581 L23: 0.5463
REMARK 3 S TENSOR
REMARK 3 S11: 0.6092 S12: 0.7252 S13: 0.4801
REMARK 3 S21: 0.0586 S22: -0.3834 S23: 0.0415
REMARK 3 S31: -0.3269 S32: -0.9828 S33: -0.2075
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain B and resid 286:352
REMARK 3 ORIGIN FOR THE GROUP (A): -20.4107 61.8982 194.3592
REMARK 3 T TENSOR
REMARK 3 T11: 1.0394 T22: 1.7536
REMARK 3 T33: 1.6348 T12: -0.0152
REMARK 3 T13: -0.0425 T23: 0.1028
REMARK 3 L TENSOR
REMARK 3 L11: 6.5211 L22: 3.8244
REMARK 3 L33: 5.6317 L12: -1.3327
REMARK 3 L13: -2.6118 L23: -1.9966
REMARK 3 S TENSOR
REMARK 3 S11: 0.1922 S12: 1.9818 S13: 0.6814
REMARK 3 S21: -0.3101 S22: 0.2485 S23: 1.5957
REMARK 3 S31: -0.5210 S32: -1.2153 S33: -0.3974
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain B and resid 353:388
REMARK 3 ORIGIN FOR THE GROUP (A): -13.4980 54.8020 209.4729
REMARK 3 T TENSOR
REMARK 3 T11: 1.4955 T22: 1.7646
REMARK 3 T33: 0.9734 T12: 0.5153
REMARK 3 T13: 0.2703 T23: 0.2060
REMARK 3 L TENSOR
REMARK 3 L11: 6.9058 L22: 4.7905
REMARK 3 L33: 5.0609 L12: -1.7877
REMARK 3 L13: -1.2726 L23: -1.0757
REMARK 3 S TENSOR
REMARK 3 S11: -0.8252 S12: -1.5201 S13: -0.3861
REMARK 3 S21: 0.4761 S22: 0.0543 S23: -1.0507
REMARK 3 S31: 1.0451 S32: 1.6113 S33: 0.8164
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain B and resid 389:440
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9080 48.4022 200.7364
REMARK 3 T TENSOR
REMARK 3 T11: 1.8374 T22: 1.7061
REMARK 3 T33: 1.6113 T12: 0.6462
REMARK 3 T13: 0.5811 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 7.1804 L22: 7.3912
REMARK 3 L33: 8.7124 L12: -1.6098
REMARK 3 L13: -3.8325 L23: -1.0051
REMARK 3 S TENSOR
REMARK 3 S11: -1.1285 S12: -1.4655 S13: -1.2038
REMARK 3 S21: -0.1407 S22: -0.1507 S23: 0.6970
REMARK 3 S31: 2.7804 S32: 2.0748 S33: 1.2878
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain C and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): 40.6488 13.9330 182.9218
REMARK 3 T TENSOR
REMARK 3 T11: 0.4401 T22: 0.4213
REMARK 3 T33: 0.5972 T12: 0.0335
REMARK 3 T13: 0.0105 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.9686 L22: 3.0113
REMARK 3 L33: 4.1428 L12: 0.3796
REMARK 3 L13: -0.2604 L23: 0.2141
REMARK 3 S TENSOR
REMARK 3 S11: 0.0934 S12: 0.0549 S13: -0.1753
REMARK 3 S21: 0.0565 S22: -0.0375 S23: 0.0307
REMARK 3 S31: 0.5469 S32: 0.1975 S33: -0.0493
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain C and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4123 -5.6489 172.6894
REMARK 3 T TENSOR
REMARK 3 T11: 1.4108 T22: 0.9110
REMARK 3 T33: 1.2703 T12: 0.0096
REMARK 3 T13: -0.0823 T23: -0.0984
REMARK 3 L TENSOR
REMARK 3 L11: 5.1791 L22: 2.9930
REMARK 3 L33: 3.9477 L12: 2.0594
REMARK 3 L13: -2.5773 L23: -0.8439
REMARK 3 S TENSOR
REMARK 3 S11: -0.0367 S12: -0.0904 S13: 0.3834
REMARK 3 S21: 0.2681 S22: 0.0922 S23: 0.2707
REMARK 3 S31: 0.2013 S32: -0.4952 S33: -0.0437
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain C and resid 286:352
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2299 -17.2186 171.1644
REMARK 3 T TENSOR
REMARK 3 T11: 1.7694 T22: 1.1202
REMARK 3 T33: 1.4853 T12: 0.1594
REMARK 3 T13: 0.5996 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 4.5049 L22: 7.5861
REMARK 3 L33: 5.9403 L12: 1.8266
REMARK 3 L13: -2.1446 L23: 0.5262
REMARK 3 S TENSOR
REMARK 3 S11: 1.1770 S12: 0.2060 S13: 1.7257
REMARK 3 S21: 0.7608 S22: -0.5934 S23: 0.8079
REMARK 3 S31: -2.0058 S32: -1.4560 S33: -0.5496
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain C and resid 353:388
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2467 -11.3221 187.1248
REMARK 3 T TENSOR
REMARK 3 T11: 3.6149 T22: 3.0246
REMARK 3 T33: 3.0612 T12: -0.2634
REMARK 3 T13: 1.9098 T23: -0.7679
REMARK 3 L TENSOR
REMARK 3 L11: 1.0413 L22: 0.1001
REMARK 3 L33: 0.4200 L12: 0.0955
REMARK 3 L13: 0.0798 L23: 0.2018
REMARK 3 S TENSOR
REMARK 3 S11: 1.2377 S12: -0.2850 S13: 1.6367
REMARK 3 S21: 0.6431 S22: -0.9859 S23: 0.6279
REMARK 3 S31: -0.7037 S32: -0.8178 S33: -0.2581
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain C and resid 389:440
REMARK 3 ORIGIN FOR THE GROUP (A): 13.2147 -13.6285 187.1715
REMARK 3 T TENSOR
REMARK 3 T11: 2.6636 T22: 1.6042
REMARK 3 T33: 1.8935 T12: -0.5310
REMARK 3 T13: 1.0149 T23: -0.3489
REMARK 3 L TENSOR
REMARK 3 L11: 6.6441 L22: 4.4074
REMARK 3 L33: 5.9712 L12: 2.4843
REMARK 3 L13: 0.5716 L23: 0.5691
REMARK 3 S TENSOR
REMARK 3 S11: 1.2458 S12: -1.7629 S13: 1.4157
REMARK 3 S21: 1.1543 S22: -0.6940 S23: 1.4075
REMARK 3 S31: -0.9606 S32: -0.0206 S33: -0.4766
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain D and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -40.9160 14.7526 247.0440
REMARK 3 T TENSOR
REMARK 3 T11: 0.5530 T22: 0.5367
REMARK 3 T33: 0.6452 T12: 0.0057
REMARK 3 T13: -0.0365 T23: -0.0353
REMARK 3 L TENSOR
REMARK 3 L11: 2.0292 L22: 3.3368
REMARK 3 L33: 2.4425 L12: 0.2572
REMARK 3 L13: -0.0586 L23: 0.2344
REMARK 3 S TENSOR
REMARK 3 S11: 0.0682 S12: -0.1702 S13: 0.0086
REMARK 3 S21: -0.2767 S22: -0.0333 S23: 0.1963
REMARK 3 S31: 0.1762 S32: -0.1660 S33: -0.0316
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain D and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): -28.2151 -5.9754 257.0403
REMARK 3 T TENSOR
REMARK 3 T11: 1.2152 T22: 1.2094
REMARK 3 T33: 1.4295 T12: 0.3972
REMARK 3 T13: -0.1152 T23: 0.1427
REMARK 3 L TENSOR
REMARK 3 L11: 5.9057 L22: 6.9569
REMARK 3 L33: 0.7205 L12: -4.6126
REMARK 3 L13: -1.9976 L23: 1.9527
REMARK 3 S TENSOR
REMARK 3 S11: -0.2273 S12: -0.6434 S13: -0.5303
REMARK 3 S21: -0.2948 S22: 0.1222 S23: -0.8022
REMARK 3 S31: 0.4803 S32: 1.0160 S33: 0.1015
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain D and resid 286:352
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1394 -15.0529 259.1197
REMARK 3 T TENSOR
REMARK 3 T11: 1.5575 T22: 1.3654
REMARK 3 T33: 2.0011 T12: -0.0012
REMARK 3 T13: 0.5394 T23: -0.2244
REMARK 3 L TENSOR
REMARK 3 L11: 7.6495 L22: 6.6775
REMARK 3 L33: 6.5971 L12: -0.1656
REMARK 3 L13: -2.9577 L23: 0.7368
REMARK 3 S TENSOR
REMARK 3 S11: 1.2762 S12: -1.3800 S13: 0.7466
REMARK 3 S21: -0.9514 S22: -0.4766 S23: -1.5665
REMARK 3 S31: -1.8198 S32: 0.5056 S33: -0.8741
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain D and resid 353:388
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5412 -9.1007 243.1697
REMARK 3 T TENSOR
REMARK 3 T11: 4.1305 T22: 3.2764
REMARK 3 T33: 2.9818 T12: 1.3550
REMARK 3 T13: 1.5244 T23: 1.2376
REMARK 3 L TENSOR
REMARK 3 L11: 0.5237 L22: 0.0071
REMARK 3 L33: 1.1380 L12: 0.1111
REMARK 3 L13: -0.7508 L23: -0.1669
REMARK 3 S TENSOR
REMARK 3 S11: 0.8925 S12: 1.0938 S13: 0.7393
REMARK 3 S21: -1.3804 S22: -1.8342 S23: -1.0427
REMARK 3 S31: -0.3183 S32: 0.5841 S33: 0.8327
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain D and resid 389:440
REMARK 3 ORIGIN FOR THE GROUP (A): -13.9903 -12.5372 242.6851
REMARK 3 T TENSOR
REMARK 3 T11: 3.3286 T22: 1.9111
REMARK 3 T33: 2.1104 T12: 0.9402
REMARK 3 T13: 0.9202 T23: 0.2313
REMARK 3 L TENSOR
REMARK 3 L11: 4.7011 L22: 4.3745
REMARK 3 L33: 5.1531 L12: -0.7377
REMARK 3 L13: 0.9501 L23: -0.6737
REMARK 3 S TENSOR
REMARK 3 S11: 2.0233 S12: 1.9144 S13: 0.9317
REMARK 3 S21: -2.4214 S22: -0.6376 S23: -1.0799
REMARK 3 S31: -2.0176 S32: 0.1419 S33: -1.3206
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain E and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -34.4095 46.3015 227.6304
REMARK 3 T TENSOR
REMARK 3 T11: 0.9336 T22: 0.5170
REMARK 3 T33: 0.7007 T12: 0.0418
REMARK 3 T13: 0.0334 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 1.2886 L22: 1.2428
REMARK 3 L33: 1.9247 L12: 0.2947
REMARK 3 L13: 0.1674 L23: 0.6926
REMARK 3 S TENSOR
REMARK 3 S11: 0.0463 S12: 0.0983 S13: 0.4168
REMARK 3 S21: -0.4476 S22: 0.0970 S23: 0.0134
REMARK 3 S31: -0.6156 S32: -0.0594 S33: -0.1236
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain E and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): -45.8769 32.7007 208.1010
REMARK 3 T TENSOR
REMARK 3 T11: 1.7275 T22: 0.7894
REMARK 3 T33: 1.3366 T12: 0.0445
REMARK 3 T13: -0.3759 T23: 0.0791
REMARK 3 L TENSOR
REMARK 3 L11: 0.3288 L22: 1.4997
REMARK 3 L33: 1.5829 L12: -0.0425
REMARK 3 L13: -0.1350 L23: 1.2906
REMARK 3 S TENSOR
REMARK 3 S11: 0.4048 S12: 0.1982 S13: -0.2345
REMARK 3 S21: -0.3714 S22: -0.1006 S23: -0.3876
REMARK 3 S31: -0.6932 S32: -0.3558 S33: -0.2767
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: chain E and resid 286:440
REMARK 3 ORIGIN FOR THE GROUP (A): -44.4026 11.2512 205.2651
REMARK 3 T TENSOR
REMARK 3 T11: 1.0138 T22: 0.6427
REMARK 3 T33: 0.7266 T12: 0.0189
REMARK 3 T13: 0.1137 T23: 0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 4.1727 L22: 4.8030
REMARK 3 L33: 4.1366 L12: -1.1866
REMARK 3 L13: 3.6281 L23: -0.7764
REMARK 3 S TENSOR
REMARK 3 S11: -0.2115 S12: -0.0178 S13: 0.1961
REMARK 3 S21: -0.0491 S22: 0.0036 S23: 0.1205
REMARK 3 S31: -0.5902 S32: -0.1121 S33: 0.2582
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: chain F and resid 1:276
REMARK 3 ORIGIN FOR THE GROUP (A): -12.4755 37.1641 256.6588
REMARK 3 T TENSOR
REMARK 3 T11: 0.6977 T22: 0.6735
REMARK 3 T33: 0.6005 T12: -0.1490
REMARK 3 T13: 0.1098 T23: -0.1059
REMARK 3 L TENSOR
REMARK 3 L11: 2.3559 L22: 2.8083
REMARK 3 L33: 2.9279 L12: 0.1251
REMARK 3 L13: -0.3562 L23: -0.3501
REMARK 3 S TENSOR
REMARK 3 S11: 0.2445 S12: -0.3123 S13: 0.3398
REMARK 3 S21: 0.3568 S22: -0.0648 S23: -0.3216
REMARK 3 S31: -0.6869 S32: 0.4662 S33: -0.1889
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: chain F and resid 277:285
REMARK 3 ORIGIN FOR THE GROUP (A): 6.1535 50.5225 243.7748
REMARK 3 T TENSOR
REMARK 3 T11: 0.9663 T22: 1.8989
REMARK 3 T33: 1.4437 T12: -0.3188
REMARK 3 T13: -0.1064 T23: -0.1267
REMARK 3 L TENSOR
REMARK 3 L11: 1.9837 L22: 1.3914
REMARK 3 L33: 1.1320 L12: 0.4750
REMARK 3 L13: -0.8283 L23: -1.2041
REMARK 3 S TENSOR
REMARK 3 S11: 0.1199 S12: 0.3980 S13: -0.1922
REMARK 3 S21: 0.0697 S22: -0.3676 S23: -0.3385
REMARK 3 S31: -0.3828 S32: 0.3303 S33: 0.2549
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: chain F and resid 286:440
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2946 49.0443 223.1726
REMARK 3 T TENSOR
REMARK 3 T11: 0.7587 T22: 1.0755
REMARK 3 T33: 0.9416 T12: -0.0098
REMARK 3 T13: 0.1771 T23: -0.1265
REMARK 3 L TENSOR
REMARK 3 L11: 5.5522 L22: 4.3035
REMARK 3 L33: 4.8727 L12: 3.1772
REMARK 3 L13: -2.1965 L23: -0.9969
REMARK 3 S TENSOR
REMARK 3 S11: 0.1568 S12: 0.3663 S13: 0.2690
REMARK 3 S21: 0.0175 S22: -0.2222 S23: 0.6540
REMARK 3 S31: -0.2661 S32: -0.9155 S33: -0.0315
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 4IQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-13.
REMARK 100 THE RCSB ID CODE IS RCSB077067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97910
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37857
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.495
REMARK 200 RESOLUTION RANGE LOW (A) : 93.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.60600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.420
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: 1BRO AND 1AA7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NA CITRATE PH 4.4, 10% PEG 3,000,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 63.35500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 68.93500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 63.35500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 68.93500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 186480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, D, C, B, 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 0
REMARK 465 GLN A 441
REMARK 465 HIS A 442
REMARK 465 ARG A 443
REMARK 465 SER A 444
REMARK 465 HIS A 445
REMARK 465 ARG A 446
REMARK 465 GLN A 447
REMARK 465 LEU A 448
REMARK 465 GLU A 449
REMARK 465 HIS A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 MET B 0
REMARK 465 GLN B 441
REMARK 465 HIS B 442
REMARK 465 ARG B 443
REMARK 465 SER B 444
REMARK 465 HIS B 445
REMARK 465 ARG B 446
REMARK 465 GLN B 447
REMARK 465 LEU B 448
REMARK 465 GLU B 449
REMARK 465 HIS B 450
REMARK 465 HIS B 451
REMARK 465 HIS B 452
REMARK 465 HIS B 453
REMARK 465 HIS B 454
REMARK 465 HIS B 455
REMARK 465 MET C 0
REMARK 465 GLN C 441
REMARK 465 HIS C 442
REMARK 465 ARG C 443
REMARK 465 SER C 444
REMARK 465 HIS C 445
REMARK 465 ARG C 446
REMARK 465 GLN C 447
REMARK 465 LEU C 448
REMARK 465 GLU C 449
REMARK 465 HIS C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 465 MET D 0
REMARK 465 GLN D 441
REMARK 465 HIS D 442
REMARK 465 ARG D 443
REMARK 465 SER D 444
REMARK 465 HIS D 445
REMARK 465 ARG D 446
REMARK 465 GLN D 447
REMARK 465 LEU D 448
REMARK 465 GLU D 449
REMARK 465 HIS D 450
REMARK 465 HIS D 451
REMARK 465 HIS D 452
REMARK 465 HIS D 453
REMARK 465 HIS D 454
REMARK 465 HIS D 455
REMARK 465 MET E 0
REMARK 465 GLN E 441
REMARK 465 HIS E 442
REMARK 465 ARG E 443
REMARK 465 SER E 444
REMARK 465 HIS E 445
REMARK 465 ARG E 446
REMARK 465 GLN E 447
REMARK 465 LEU E 448
REMARK 465 GLU E 449
REMARK 465 HIS E 450
REMARK 465 HIS E 451
REMARK 465 HIS E 452
REMARK 465 HIS E 453
REMARK 465 HIS E 454
REMARK 465 HIS E 455
REMARK 465 MET F 0
REMARK 465 GLN F 441
REMARK 465 HIS F 442
REMARK 465 ARG F 443
REMARK 465 SER F 444
REMARK 465 HIS F 445
REMARK 465 ARG F 446
REMARK 465 GLN F 447
REMARK 465 LEU F 448
REMARK 465 GLU F 449
REMARK 465 HIS F 450
REMARK 465 HIS F 451
REMARK 465 HIS F 452
REMARK 465 HIS F 453
REMARK 465 HIS F 454
REMARK 465 HIS F 455
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 ASN A 9 -131.06 60.92
REMARK 500 PRO A 33 47.01 -109.43
REMARK 500 LEU A 34 -146.70 -100.74
REMARK 500 GLN A 66 75.01 -117.19
REMARK 500 SER A 98 -110.90 49.61
REMARK 500 THR A 113 37.70 -87.58
REMARK 500 PHE A 128 118.74 -160.18
REMARK 500 ASP A 155 99.33 -162.16
REMARK 500 TYR A 206 39.77 -87.65
REMARK 500 THR A 236 -87.82 -120.45
REMARK 500 HIS A 263 43.62 -106.05
REMARK 500 THR A 320 -32.78 55.75
REMARK 500 ARG A 355 -141.03 60.91
REMARK 500 ASN A 370 -8.07 78.38
REMARK 500 ILE A 390 -39.40 -133.29
REMARK 500 ARG A 417 20.23 80.86
REMARK 500 ASN B 9 -130.27 60.07
REMARK 500 PRO B 33 46.67 -108.91
REMARK 500 LEU B 34 -146.50 -100.90
REMARK 500 GLN B 66 75.55 -117.05
REMARK 500 SER B 98 -111.58 50.65
REMARK 500 THR B 113 38.02 -87.82
REMARK 500 GLU B 126 150.40 -43.59
REMARK 500 PHE B 128 118.63 -160.15
REMARK 500 ASP B 155 98.88 -162.03
REMARK 500 TYR B 206 39.32 -87.78
REMARK 500 THR B 236 -88.22 -119.79
REMARK 500 HIS B 263 44.34 -105.95
REMARK 500 ASN B 319 95.61 -48.18
REMARK 500 ILE B 334 -10.94 52.53
REMARK 500 PRO B 352 -78.54 -62.97
REMARK 500 SER B 353 85.93 -61.29
REMARK 500 ARG B 355 -31.18 65.97
REMARK 500 ASN B 370 -9.46 39.89
REMARK 500 ILE B 390 -40.02 -134.00
REMARK 500 ASP B 439 -70.69 -87.41
REMARK 500 ASN C 9 -131.05 59.97
REMARK 500 PRO C 33 47.25 -108.98
REMARK 500 LEU C 34 -147.04 -100.20
REMARK 500 GLN C 66 75.18 -118.13
REMARK 500 SER C 98 -109.85 50.78
REMARK 500 THR C 113 37.18 -88.25
REMARK 500 GLU C 126 150.09 -43.06
REMARK 500 PHE C 128 118.72 -160.37
REMARK 500 ASP C 155 99.47 -162.39
REMARK 500 TYR C 206 40.02 -87.57
REMARK 500 THR C 236 -88.17 -120.38
REMARK 500 HIS C 263 43.82 -105.67
REMARK 500 ASN C 319 87.07 -55.21
REMARK 500 ARG C 355 -25.86 62.19
REMARK 500
REMARK 500 THIS ENTRY HAS 108 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VDX RELATED DB: PDB
REMARK 900 RELATED ID: 4D9J RELATED DB: PDB
DBREF 4IQ4 A 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 A 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IQ4 B 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 B 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IQ4 C 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 C 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IQ4 D 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 D 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IQ4 E 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 E 286 448 UNP P03485 M1_I34A1 3 165
DBREF 4IQ4 F 0 277 UNP P29715 BPOA2_STRAU 1 278
DBREF 4IQ4 F 286 448 UNP P03485 M1_I34A1 3 165
SEQADV 4IQ4 THR A 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA A 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA A 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN A 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU A 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA A 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN A 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS A 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN A 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS A 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU A 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU A 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS A 455 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 THR B 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA B 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA B 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN B 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU B 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA B 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN B 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS B 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN B 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS B 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU B 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU B 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS B 455 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 THR C 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA C 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA C 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN C 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU C 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA C 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN C 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS C 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN C 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS C 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU C 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU C 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS C 455 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 THR D 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA D 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA D 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN D 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU D 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA D 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN D 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS D 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN D 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS D 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU D 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU D 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS D 455 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 THR E 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA E 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA E 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN E 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU E 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA E 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN E 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS E 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN E 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS E 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU E 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU E 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS E 455 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 THR F 24 UNP P29715 GLN 25 ENGINEERED MUTATION
SEQADV 4IQ4 ALA F 118 UNP P29715 LYS 119 ENGINEERED MUTATION
SEQADV 4IQ4 ALA F 278 UNP P03485 LINKER
SEQADV 4IQ4 GLN F 279 UNP P03485 LINKER
SEQADV 4IQ4 GLU F 280 UNP P03485 LINKER
SEQADV 4IQ4 ALA F 281 UNP P03485 LINKER
SEQADV 4IQ4 GLN F 282 UNP P03485 LINKER
SEQADV 4IQ4 LYS F 283 UNP P03485 LINKER
SEQADV 4IQ4 GLN F 284 UNP P03485 LINKER
SEQADV 4IQ4 LYS F 285 UNP P03485 LINKER
SEQADV 4IQ4 LEU F 448 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 GLU F 449 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 450 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 451 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 452 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 453 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 454 UNP P03485 EXPRESSION TAG
SEQADV 4IQ4 HIS F 455 UNP P03485 EXPRESSION TAG
SEQRES 1 A 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 A 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 A 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 A 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 A 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 A 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 A 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 A 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 A 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 A 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 A 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 A 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 A 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 A 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 A 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 A 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 A 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 A 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 A 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 A 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 A 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 A 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 A 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 A 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 A 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 A 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 A 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 A 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 A 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 A 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 A 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 A 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 A 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 A 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 A 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 A 456 HIS
SEQRES 1 B 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 B 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 B 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 B 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 B 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 B 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 B 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 B 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 B 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 B 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 B 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 B 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 B 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 B 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 B 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 B 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 B 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 B 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 B 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 B 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 B 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 B 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 B 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 B 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 B 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 B 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 B 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 B 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 B 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 B 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 B 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 B 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 B 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 B 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 B 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 B 456 HIS
SEQRES 1 C 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 C 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 C 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 C 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 C 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 C 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 C 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 C 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 C 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 C 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 C 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 C 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 C 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 C 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 C 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 C 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 C 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 C 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 C 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 C 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 C 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 C 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 C 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 C 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 C 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 C 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 C 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 C 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 C 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 C 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 C 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 C 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 C 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 C 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 C 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 C 456 HIS
SEQRES 1 D 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 D 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 D 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 D 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 D 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 D 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 D 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 D 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 D 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 D 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 D 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 D 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 D 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 D 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 D 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 D 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 D 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 D 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 D 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 D 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 D 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 D 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 D 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 D 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 D 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 D 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 D 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 D 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 D 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 D 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 D 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 D 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 D 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 D 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 D 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 D 456 HIS
SEQRES 1 E 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 E 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 E 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 E 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 E 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 E 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 E 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 E 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 E 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 E 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 E 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 E 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 E 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 E 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 E 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 E 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 E 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 E 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 E 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 E 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 E 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 E 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 E 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 E 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 E 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 E 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 E 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 E 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 E 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 E 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 E 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 E 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 E 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 E 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 E 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 E 456 HIS
SEQRES 1 F 456 MET PRO PHE ILE THR VAL GLY GLN GLU ASN SER THR SER
SEQRES 2 F 456 ILE ASP LEU TYR TYR GLU ASP HIS GLY THR GLY THR PRO
SEQRES 3 F 456 VAL VAL LEU ILE HIS GLY PHE PRO LEU SER GLY HIS SER
SEQRES 4 F 456 TRP GLU ARG GLN SER ALA ALA LEU LEU ASP ALA GLY TYR
SEQRES 5 F 456 ARG VAL ILE THR TYR ASP ARG ARG GLY PHE GLY GLN SER
SEQRES 6 F 456 SER GLN PRO THR THR GLY TYR ASP TYR ASP THR PHE ALA
SEQRES 7 F 456 ALA ASP LEU ASN THR VAL LEU GLU THR LEU ASP LEU GLN
SEQRES 8 F 456 ASP ALA VAL LEU VAL GLY PHE SER MET GLY THR GLY GLU
SEQRES 9 F 456 VAL ALA ARG TYR VAL SER SER TYR GLY THR ALA ARG ILE
SEQRES 10 F 456 ALA ALA VAL ALA PHE LEU ALA SER LEU GLU PRO PHE LEU
SEQRES 11 F 456 LEU LYS THR ASP ASP ASN PRO ASP GLY ALA ALA PRO GLN
SEQRES 12 F 456 GLU PHE PHE ASP GLY ILE VAL ALA ALA VAL LYS ALA ASP
SEQRES 13 F 456 ARG TYR ALA PHE TYR THR GLY PHE PHE ASN ASP PHE TYR
SEQRES 14 F 456 ASN LEU ASP GLU ASN LEU GLY THR ARG ILE SER GLU GLU
SEQRES 15 F 456 ALA VAL ARG ASN SER TRP ASN THR ALA ALA SER GLY GLY
SEQRES 16 F 456 PHE PHE ALA ALA ALA ALA ALA PRO THR THR TRP TYR THR
SEQRES 17 F 456 ASP PHE ARG ALA ASP ILE PRO ARG ILE ASP VAL PRO ALA
SEQRES 18 F 456 LEU ILE LEU HIS GLY THR GLY ASP ARG THR LEU PRO ILE
SEQRES 19 F 456 GLU ASN THR ALA ARG VAL PHE HIS LYS ALA LEU PRO SER
SEQRES 20 F 456 ALA GLU TYR VAL GLU VAL GLU GLY ALA PRO HIS GLY LEU
SEQRES 21 F 456 LEU TRP THR HIS ALA GLU GLU VAL ASN THR ALA LEU LEU
SEQRES 22 F 456 ALA PHE LEU ALA LYS ALA GLN GLU ALA GLN LYS GLN LYS
SEQRES 23 F 456 LEU LEU THR GLU VAL GLU THR TYR VAL LEU SER ILE ILE
SEQRES 24 F 456 PRO SER GLY PRO LEU LYS ALA GLU ILE ALA GLN ARG LEU
SEQRES 25 F 456 GLU ASP VAL PHE ALA GLY LYS ASN THR ASP LEU GLU VAL
SEQRES 26 F 456 LEU MET GLU TRP LEU LYS THR ARG PRO ILE LEU SER PRO
SEQRES 27 F 456 LEU THR LYS GLY ILE LEU GLY PHE VAL PHE THR LEU THR
SEQRES 28 F 456 VAL PRO SER GLU ARG GLY LEU GLN ARG ARG ARG PHE VAL
SEQRES 29 F 456 GLN ASN ALA LEU ASN GLY ASN GLY ASP PRO ASN ASN MET
SEQRES 30 F 456 ASP LYS ALA VAL LYS LEU TYR ARG LYS LEU LYS ARG GLU
SEQRES 31 F 456 ILE THR PHE HIS GLY ALA LYS GLU ILE SER LEU SER TYR
SEQRES 32 F 456 SER ALA GLY ALA LEU ALA SER CYS MET GLY LEU ILE TYR
SEQRES 33 F 456 ASN ARG MET GLY ALA VAL THR THR GLU VAL ALA PHE GLY
SEQRES 34 F 456 LEU VAL CYS ALA THR CYS GLU GLN ILE ALA ASP SER GLN
SEQRES 35 F 456 HIS ARG SER HIS ARG GLN LEU GLU HIS HIS HIS HIS HIS
SEQRES 36 F 456 HIS
HELIX 1 1 SER A 35 SER A 38 5 4
HELIX 2 2 TRP A 39 ALA A 49 1 11
HELIX 3 3 ASP A 72 LEU A 87 1 16
HELIX 4 4 MET A 99 GLY A 112 1 14
HELIX 5 5 PRO A 141 ASP A 155 1 15
HELIX 6 6 ASP A 155 TYR A 168 1 14
HELIX 7 7 ASN A 169 LEU A 174 1 6
HELIX 8 8 SER A 179 SER A 192 1 14
HELIX 9 9 GLY A 194 ALA A 201 1 8
HELIX 10 10 ALA A 201 TYR A 206 1 6
HELIX 11 11 ASP A 212 ILE A 216 5 5
HELIX 12 12 THR A 236 LEU A 244 1 9
HELIX 13 13 GLY A 258 HIS A 263 1 6
HELIX 14 14 HIS A 263 SER A 296 1 34
HELIX 15 15 GLY A 301 GLY A 317 1 17
HELIX 16 16 LEU A 322 THR A 331 1 10
HELIX 17 17 SER A 336 VAL A 351 1 16
HELIX 18 18 ARG A 360 ASN A 368 1 9
HELIX 19 19 GLY A 369 GLY A 371 5 3
HELIX 20 20 ASP A 372 GLU A 389 1 18
HELIX 21 21 THR A 391 LEU A 400 1 10
HELIX 22 22 SER A 403 ASN A 416 1 14
HELIX 23 23 THR A 422 SER A 440 1 19
HELIX 24 24 SER B 35 SER B 38 5 4
HELIX 25 25 TRP B 39 ALA B 49 1 11
HELIX 26 26 ASP B 72 LEU B 87 1 16
HELIX 27 27 MET B 99 GLY B 112 1 14
HELIX 28 28 PRO B 141 ASP B 155 1 15
HELIX 29 29 ASP B 155 TYR B 168 1 14
HELIX 30 30 ASN B 169 LEU B 174 1 6
HELIX 31 31 SER B 179 SER B 192 1 14
HELIX 32 32 GLY B 194 ALA B 201 1 8
HELIX 33 33 PRO B 202 TRP B 205 5 4
HELIX 34 34 ASP B 212 ILE B 216 5 5
HELIX 35 35 PRO B 232 ASN B 235 5 4
HELIX 36 36 THR B 236 LEU B 244 1 9
HELIX 37 37 GLY B 258 HIS B 263 1 6
HELIX 38 38 HIS B 263 ILE B 298 1 36
HELIX 39 39 GLY B 301 GLY B 317 1 17
HELIX 40 40 ASP B 321 THR B 331 1 11
HELIX 41 41 SER B 336 VAL B 351 1 16
HELIX 42 42 ARG B 360 ASN B 368 1 9
HELIX 43 43 MET B 376 GLU B 389 1 14
HELIX 44 44 THR B 391 LEU B 400 1 10
HELIX 45 45 SER B 403 ARG B 417 1 15
HELIX 46 46 THR B 422 SER B 440 1 19
HELIX 47 47 SER C 35 SER C 38 5 4
HELIX 48 48 TRP C 39 ALA C 49 1 11
HELIX 49 49 ASP C 72 LEU C 87 1 16
HELIX 50 50 MET C 99 GLY C 112 1 14
HELIX 51 51 PRO C 141 ASP C 155 1 15
HELIX 52 52 ASP C 155 TYR C 168 1 14
HELIX 53 53 ASN C 169 LEU C 174 1 6
HELIX 54 54 SER C 179 SER C 192 1 14
HELIX 55 55 GLY C 194 ALA C 201 1 8
HELIX 56 56 ALA C 201 TYR C 206 1 6
HELIX 57 57 ASP C 212 ILE C 216 5 5
HELIX 58 58 PRO C 232 ASN C 235 5 4
HELIX 59 59 THR C 236 LEU C 244 1 9
HELIX 60 60 GLY C 258 HIS C 263 1 6
HELIX 61 61 HIS C 263 ILE C 298 1 36
HELIX 62 62 GLY C 301 GLY C 317 1 17
HELIX 63 63 ASP C 321 THR C 331 1 11
HELIX 64 64 SER C 336 VAL C 351 1 16
HELIX 65 65 ARG C 360 GLY C 369 1 10
HELIX 66 66 ASP C 372 GLU C 389 1 18
HELIX 67 67 THR C 391 LEU C 400 1 10
HELIX 68 68 SER C 403 ASN C 416 1 14
HELIX 69 69 THR C 422 SER C 440 1 19
HELIX 70 70 SER D 35 SER D 38 5 4
HELIX 71 71 TRP D 39 ALA D 49 1 11
HELIX 72 72 ASP D 72 LEU D 87 1 16
HELIX 73 73 MET D 99 GLY D 112 1 14
HELIX 74 74 PRO D 141 ASP D 155 1 15
HELIX 75 75 ASP D 155 TYR D 168 1 14
HELIX 76 76 ASN D 169 LEU D 174 1 6
HELIX 77 77 SER D 179 GLY D 193 1 15
HELIX 78 78 GLY D 194 ALA D 201 1 8
HELIX 79 79 PRO D 202 TRP D 205 5 4
HELIX 80 80 ASP D 212 ILE D 216 5 5
HELIX 81 81 PRO D 232 ASN D 235 5 4
HELIX 82 82 THR D 236 LEU D 244 1 9
HELIX 83 83 GLY D 258 HIS D 263 1 6
HELIX 84 84 HIS D 263 ILE D 298 1 36
HELIX 85 85 GLY D 301 GLY D 317 1 17
HELIX 86 86 ASP D 321 THR D 331 1 11
HELIX 87 87 SER D 336 VAL D 351 1 16
HELIX 88 88 ARG D 360 ASN D 368 1 9
HELIX 89 89 GLY D 369 GLY D 371 5 3
HELIX 90 90 ASP D 372 GLU D 389 1 18
HELIX 91 91 THR D 391 LEU D 400 1 10
HELIX 92 92 SER D 403 ASN D 416 1 14
HELIX 93 93 THR D 422 SER D 440 1 19
HELIX 94 94 SER E 35 SER E 38 5 4
HELIX 95 95 TRP E 39 ALA E 49 1 11
HELIX 96 96 ASP E 72 LEU E 87 1 16
HELIX 97 97 MET E 99 GLY E 112 1 14
HELIX 98 98 PRO E 141 ASP E 155 1 15
HELIX 99 99 ASP E 155 TYR E 168 1 14
HELIX 100 100 ASN E 169 LEU E 174 1 6
HELIX 101 101 SER E 179 GLY E 193 1 15
HELIX 102 102 GLY E 194 ALA E 201 1 8
HELIX 103 103 PRO E 202 TRP E 205 5 4
HELIX 104 104 ASP E 212 ILE E 216 5 5
HELIX 105 105 PRO E 232 ASN E 235 5 4
HELIX 106 106 THR E 236 LEU E 244 1 9
HELIX 107 107 GLY E 258 HIS E 263 1 6
HELIX 108 108 HIS E 263 ILE E 298 1 36
HELIX 109 109 GLY E 301 GLY E 317 1 17
HELIX 110 110 ASP E 321 THR E 331 1 11
HELIX 111 111 SER E 336 VAL E 351 1 16
HELIX 112 112 ARG E 360 ASN E 368 1 9
HELIX 113 113 ASP E 372 GLU E 389 1 18
HELIX 114 114 THR E 391 LEU E 400 1 10
HELIX 115 115 SER E 403 ASN E 416 1 14
HELIX 116 116 THR E 422 SER E 440 1 19
HELIX 117 117 SER F 35 SER F 38 5 4
HELIX 118 118 TRP F 39 ALA F 49 1 11
HELIX 119 119 ASP F 72 LEU F 87 1 16
HELIX 120 120 SER F 98 GLY F 112 1 15
HELIX 121 121 PRO F 141 ASP F 155 1 15
HELIX 122 122 ASP F 155 TYR F 168 1 14
HELIX 123 123 ASN F 169 LEU F 174 1 6
HELIX 124 124 SER F 179 SER F 192 1 14
HELIX 125 125 GLY F 194 ALA F 201 1 8
HELIX 126 126 ALA F 201 TYR F 206 1 6
HELIX 127 127 ASP F 212 ILE F 216 5 5
HELIX 128 128 PRO F 232 ASN F 235 5 4
HELIX 129 129 THR F 236 LEU F 244 1 9
HELIX 130 130 GLY F 258 HIS F 263 1 6
HELIX 131 131 HIS F 263 ILE F 298 1 36
HELIX 132 132 GLY F 301 GLY F 317 1 17
HELIX 133 133 ASP F 321 THR F 331 1 11
HELIX 134 134 SER F 336 VAL F 351 1 16
HELIX 135 135 ARG F 360 GLY F 369 1 10
HELIX 136 136 ASP F 372 GLU F 389 1 18
HELIX 137 137 THR F 391 LEU F 400 1 10
HELIX 138 138 SER F 403 ASN F 416 1 14
HELIX 139 139 THR F 422 ASP F 439 1 18
SHEET 1 A 8 PHE A 2 GLU A 8 0
SHEET 2 A 8 THR A 11 HIS A 20 -1 O ILE A 13 N VAL A 5
SHEET 3 A 8 ARG A 52 TYR A 56 -1 O THR A 55 N GLU A 18
SHEET 4 A 8 PRO A 25 ILE A 29 1 N VAL A 26 O ARG A 52
SHEET 5 A 8 ALA A 92 PHE A 97 1 O VAL A 95 N VAL A 27
SHEET 6 A 8 ILE A 116 LEU A 122 1 O ALA A 117 N ALA A 92
SHEET 7 A 8 ALA A 220 GLY A 225 1 O LEU A 221 N PHE A 121
SHEET 8 A 8 GLU A 248 VAL A 252 1 O GLU A 248 N ILE A 222
SHEET 1 B 8 PHE B 2 GLU B 8 0
SHEET 2 B 8 THR B 11 HIS B 20 -1 O ILE B 13 N VAL B 5
SHEET 3 B 8 ARG B 52 TYR B 56 -1 O THR B 55 N GLU B 18
SHEET 4 B 8 PRO B 25 ILE B 29 1 N VAL B 26 O ARG B 52
SHEET 5 B 8 ALA B 92 PHE B 97 1 O VAL B 95 N VAL B 27
SHEET 6 B 8 ILE B 116 LEU B 122 1 O ALA B 117 N ALA B 92
SHEET 7 B 8 ALA B 220 GLY B 225 1 O LEU B 221 N PHE B 121
SHEET 8 B 8 GLU B 248 VAL B 252 1 O GLU B 248 N ILE B 222
SHEET 1 C 8 PHE C 2 GLU C 8 0
SHEET 2 C 8 THR C 11 HIS C 20 -1 O LEU C 15 N ILE C 3
SHEET 3 C 8 ARG C 52 TYR C 56 -1 O THR C 55 N GLU C 18
SHEET 4 C 8 PRO C 25 ILE C 29 1 N VAL C 26 O ARG C 52
SHEET 5 C 8 ALA C 92 PHE C 97 1 O VAL C 95 N ILE C 29
SHEET 6 C 8 ILE C 116 LEU C 122 1 O ALA C 117 N ALA C 92
SHEET 7 C 8 ALA C 220 GLY C 225 1 O LEU C 221 N PHE C 121
SHEET 8 C 8 GLU C 248 VAL C 252 1 O GLU C 248 N ILE C 222
SHEET 1 D 8 PHE D 2 GLU D 8 0
SHEET 2 D 8 THR D 11 HIS D 20 -1 O ILE D 13 N VAL D 5
SHEET 3 D 8 ARG D 52 TYR D 56 -1 O THR D 55 N GLU D 18
SHEET 4 D 8 PRO D 25 ILE D 29 1 N VAL D 26 O ARG D 52
SHEET 5 D 8 ALA D 92 PHE D 97 1 O VAL D 95 N ILE D 29
SHEET 6 D 8 ILE D 116 LEU D 122 1 O ALA D 117 N ALA D 92
SHEET 7 D 8 ALA D 220 GLY D 225 1 O LEU D 221 N PHE D 121
SHEET 8 D 8 GLU D 248 VAL D 252 1 O GLU D 248 N ILE D 222
SHEET 1 E 8 PHE E 2 GLU E 8 0
SHEET 2 E 8 THR E 11 HIS E 20 -1 O ILE E 13 N VAL E 5
SHEET 3 E 8 ARG E 52 TYR E 56 -1 O THR E 55 N GLU E 18
SHEET 4 E 8 PRO E 25 ILE E 29 1 N VAL E 26 O ARG E 52
SHEET 5 E 8 ALA E 92 PHE E 97 1 O VAL E 95 N VAL E 27
SHEET 6 E 8 ILE E 116 LEU E 122 1 O ALA E 117 N ALA E 92
SHEET 7 E 8 ALA E 220 GLY E 225 1 O LEU E 221 N PHE E 121
SHEET 8 E 8 GLU E 248 VAL E 252 1 O GLU E 248 N ILE E 222
SHEET 1 F 8 PHE F 2 GLU F 8 0
SHEET 2 F 8 THR F 11 HIS F 20 -1 O ILE F 13 N VAL F 5
SHEET 3 F 8 ARG F 52 TYR F 56 -1 O THR F 55 N GLU F 18
SHEET 4 F 8 PRO F 25 ILE F 29 1 N VAL F 26 O ARG F 52
SHEET 5 F 8 ALA F 92 PHE F 97 1 O VAL F 95 N ILE F 29
SHEET 6 F 8 ILE F 116 LEU F 122 1 O ALA F 117 N ALA F 92
SHEET 7 F 8 ALA F 220 GLY F 225 1 O LEU F 221 N PHE F 121
SHEET 8 F 8 GLU F 248 VAL F 252 1 O GLU F 248 N ILE F 222
CISPEP 1 PHE A 32 PRO A 33 0 -6.70
CISPEP 2 GLU A 126 PRO A 127 0 -0.30
CISPEP 3 PHE B 32 PRO B 33 0 -6.32
CISPEP 4 GLU B 126 PRO B 127 0 -0.02
CISPEP 5 PHE C 32 PRO C 33 0 -6.61
CISPEP 6 GLU C 126 PRO C 127 0 -0.18
CISPEP 7 PHE D 32 PRO D 33 0 -6.43
CISPEP 8 GLU D 126 PRO D 127 0 -0.14
CISPEP 9 PHE E 32 PRO E 33 0 -6.38
CISPEP 10 GLU E 126 PRO E 127 0 -0.33
CISPEP 11 PHE F 32 PRO F 33 0 -5.96
CISPEP 12 GLU F 126 PRO F 127 0 0.04
CRYST1 126.710 137.870 171.780 90.00 90.00 90.00 P 21 21 2 24
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 0.007892 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007253 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005821 0.00000
TER 3399 SER A 440
TER 6798 SER B 440
TER 10197 SER C 440
TER 13596 SER D 440
TER 16995 SER E 440
TER 20394 SER F 440
MASTER 745 0 0 139 48 0 0 620388 6 0 216
END |