HEADER SIGNALING PROTEIN 15-AUG-11 3TFG
TITLE CRYSTAL STRUCTURE OF AN H-NOX PROTEIN FROM NOSTOC SP. PCC 7120,
TITLE 2 L66W/L67W DOUBLE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALR2278 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NOSTOC SP. PCC 7120;
SOURCE 3 ORGANISM_TAXID: 103690;
SOURCE 4 STRAIN: PCC 7120 / UTEX 2576;
SOURCE 5 GENE: ALR2278;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HEME-BASED SENSOR DOMAIN, GAS BINDING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.B.WINTER,M.A.HERZIK JR.,J.KURIYAN,M.A.MARLETTA
REVDAT 3 13-SEP-23 3TFG 1 REMARK SEQADV LINK
REVDAT 2 29-APR-15 3TFG 1 HETSYN
REVDAT 1 09-NOV-11 3TFG 0
JRNL AUTH M.B.WINTER,M.A.HERZIK,J.KURIYAN,M.A.MARLETTA
JRNL TITL TUNNELS MODULATE LIGAND FLUX IN A HEME NITRIC OXIDE/OXYGEN
JRNL TITL 2 BINDING (H-NOX) DOMAIN.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 E881 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21997213
JRNL DOI 10.1073/PNAS.1114038108
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.53
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 47646
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2412
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 43.5420 - 4.8840 1.00 2878 160 0.1764 0.1761
REMARK 3 2 4.8840 - 3.8773 1.00 2751 155 0.1267 0.1379
REMARK 3 3 3.8773 - 3.3874 1.00 2783 135 0.1514 0.1743
REMARK 3 4 3.3874 - 3.0778 1.00 2727 153 0.1611 0.1863
REMARK 3 5 3.0778 - 2.8573 0.99 2731 151 0.1687 0.1980
REMARK 3 6 2.8573 - 2.6888 0.99 2744 111 0.1682 0.2102
REMARK 3 7 2.6888 - 2.5542 0.99 2702 162 0.1643 0.2046
REMARK 3 8 2.5542 - 2.4430 0.98 2695 130 0.1610 0.2100
REMARK 3 9 2.4430 - 2.3490 0.98 2666 145 0.1621 0.2052
REMARK 3 10 2.3490 - 2.2679 0.98 2659 143 0.1501 0.1765
REMARK 3 11 2.2679 - 2.1970 0.97 2638 125 0.1497 0.1601
REMARK 3 12 2.1970 - 2.1342 0.97 2644 130 0.1597 0.1602
REMARK 3 13 2.1342 - 2.0780 0.95 2614 163 0.1699 0.2284
REMARK 3 14 2.0780 - 2.0273 0.95 2528 137 0.1883 0.2265
REMARK 3 15 2.0273 - 1.9812 0.94 2557 130 0.1841 0.2223
REMARK 3 16 1.9812 - 1.9391 0.92 2478 134 0.2010 0.2146
REMARK 3 17 1.9391 - 1.9003 0.90 2439 148 0.2173 0.2324
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.89
REMARK 3 K_SOL : 0.43
REMARK 3 B_SOL : 45.50
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.990
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.018 3125
REMARK 3 ANGLE : 1.667 4267
REMARK 3 CHIRALITY : 0.117 430
REMARK 3 PLANARITY : 0.008 546
REMARK 3 DIHEDRAL : 16.353 1111
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 21
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:17)
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5534 45.7785 43.0909
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: 0.4916
REMARK 3 T33: 0.2725 T12: -0.0104
REMARK 3 T13: -0.0380 T23: 0.0705
REMARK 3 L TENSOR
REMARK 3 L11: 0.0219 L22: 0.6489
REMARK 3 L33: 0.6384 L12: -0.1034
REMARK 3 L13: -0.0378 L23: -0.0344
REMARK 3 S TENSOR
REMARK 3 S11: -0.0166 S12: 0.2374 S13: 0.0533
REMARK 3 S21: -0.1545 S22: 0.1337 S23: 0.2961
REMARK 3 S31: -0.0750 S32: -0.6105 S33: -0.1019
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 18:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0583 52.5834 41.6380
REMARK 3 T TENSOR
REMARK 3 T11: 0.2548 T22: 0.9115
REMARK 3 T33: 0.5229 T12: 0.3163
REMARK 3 T13: 0.0305 T23: 0.2318
REMARK 3 L TENSOR
REMARK 3 L11: 0.1821 L22: 0.0672
REMARK 3 L33: 0.0152 L12: 0.0291
REMARK 3 L13: -0.0191 L23: -0.0304
REMARK 3 S TENSOR
REMARK 3 S11: 0.0120 S12: 0.1007 S13: 0.0098
REMARK 3 S21: -0.0266 S22: 0.0752 S23: 0.0694
REMARK 3 S31: 0.0088 S32: -0.1094 S33: 0.0187
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 29:44)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8044 56.4733 42.8387
REMARK 3 T TENSOR
REMARK 3 T11: 0.4054 T22: 0.4726
REMARK 3 T33: 0.3247 T12: 0.1738
REMARK 3 T13: 0.0744 T23: 0.1177
REMARK 3 L TENSOR
REMARK 3 L11: 0.9463 L22: 0.4408
REMARK 3 L33: 0.0554 L12: -0.5100
REMARK 3 L13: 0.0849 L23: -0.0347
REMARK 3 S TENSOR
REMARK 3 S11: 0.1477 S12: 0.2388 S13: 0.1930
REMARK 3 S21: 0.2330 S22: 0.0825 S23: 0.0840
REMARK 3 S31: -0.5949 S32: -0.6815 S33: -0.1130
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 45:62)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.4824 50.0235 52.1659
REMARK 3 T TENSOR
REMARK 3 T11: 0.3731 T22: 0.7387
REMARK 3 T33: 0.3910 T12: 0.2848
REMARK 3 T13: 0.1082 T23: 0.1324
REMARK 3 L TENSOR
REMARK 3 L11: 1.3334 L22: 0.2727
REMARK 3 L33: 0.2109 L12: -0.2627
REMARK 3 L13: -0.2831 L23: -0.1297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0598 S12: 0.1091 S13: -0.0624
REMARK 3 S21: 0.2338 S22: 0.2063 S23: 0.3456
REMARK 3 S31: -0.3411 S32: -0.5443 S33: -0.0749
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 63:93)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5280 37.1874 46.2524
REMARK 3 T TENSOR
REMARK 3 T11: 0.1838 T22: 0.3952
REMARK 3 T33: 0.2402 T12: -0.0188
REMARK 3 T13: 0.0085 T23: 0.0003
REMARK 3 L TENSOR
REMARK 3 L11: 0.1675 L22: 1.4119
REMARK 3 L33: 0.5260 L12: -0.3906
REMARK 3 L13: -0.1869 L23: 0.2821
REMARK 3 S TENSOR
REMARK 3 S11: -0.0313 S12: 0.1424 S13: -0.1449
REMARK 3 S21: -0.0872 S22: 0.0105 S23: 0.3017
REMARK 3 S31: 0.0876 S32: -0.5539 S33: 0.0528
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 94:111)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3070 35.4653 51.8475
REMARK 3 T TENSOR
REMARK 3 T11: 0.1792 T22: 0.2484
REMARK 3 T33: 0.2623 T12: 0.0040
REMARK 3 T13: 0.0388 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 0.1503 L22: 0.7109
REMARK 3 L33: 0.1708 L12: 0.0340
REMARK 3 L13: 0.0833 L23: -0.1111
REMARK 3 S TENSOR
REMARK 3 S11: 0.1191 S12: -0.0475 S13: 0.1160
REMARK 3 S21: -0.0865 S22: -0.1490 S23: -0.2411
REMARK 3 S31: -0.0333 S32: 0.0252 S33: 0.0614
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 112:126)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6802 38.6028 57.7379
REMARK 3 T TENSOR
REMARK 3 T11: 0.2345 T22: 0.2899
REMARK 3 T33: 0.2792 T12: -0.0318
REMARK 3 T13: 0.0043 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 0.5162 L22: 1.3587
REMARK 3 L33: 0.4897 L12: 0.3461
REMARK 3 L13: -0.0333 L23: -0.5724
REMARK 3 S TENSOR
REMARK 3 S11: 0.0259 S12: -0.0124 S13: -0.1524
REMARK 3 S21: -0.0451 S22: -0.1882 S23: -0.3521
REMARK 3 S31: -0.1181 S32: 0.2945 S33: 0.1414
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 127:141)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0585 36.1357 61.8636
REMARK 3 T TENSOR
REMARK 3 T11: 0.2219 T22: 0.2988
REMARK 3 T33: 0.2617 T12: -0.0300
REMARK 3 T13: 0.0260 T23: 0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 1.0254 L22: 0.3136
REMARK 3 L33: 0.5324 L12: 0.5621
REMARK 3 L13: -0.1959 L23: -0.1630
REMARK 3 S TENSOR
REMARK 3 S11: 0.1096 S12: -0.2736 S13: -0.1588
REMARK 3 S21: 0.1235 S22: -0.1533 S23: -0.1901
REMARK 3 S31: -0.0876 S32: 0.0213 S33: 0.0116
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 142:166)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.1500 30.2502 54.9784
REMARK 3 T TENSOR
REMARK 3 T11: 0.2158 T22: 0.3179
REMARK 3 T33: 0.2890 T12: -0.0865
REMARK 3 T13: 0.0403 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.1853 L22: 0.1338
REMARK 3 L33: 0.2031 L12: -0.0040
REMARK 3 L13: -0.0991 L23: -0.0924
REMARK 3 S TENSOR
REMARK 3 S11: 0.0151 S12: 0.0262 S13: -0.1457
REMARK 3 S21: 0.0003 S22: 0.0153 S23: 0.2247
REMARK 3 S31: 0.0496 S32: -0.2692 S33: -0.0074
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 167:174)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8857 42.0781 69.6989
REMARK 3 T TENSOR
REMARK 3 T11: 0.3258 T22: 0.3356
REMARK 3 T33: 0.2804 T12: -0.0570
REMARK 3 T13: 0.0299 T23: -0.0156
REMARK 3 L TENSOR
REMARK 3 L11: 0.0171 L22: 0.3260
REMARK 3 L33: 0.4484 L12: 0.0435
REMARK 3 L13: -0.0029 L23: -0.2186
REMARK 3 S TENSOR
REMARK 3 S11: 0.0477 S12: -0.0471 S13: 0.1218
REMARK 3 S21: 0.2843 S22: 0.1359 S23: 0.0320
REMARK 3 S31: -0.2261 S32: 0.1443 S33: -0.0254
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 175:183)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8956 26.1432 60.4843
REMARK 3 T TENSOR
REMARK 3 T11: 0.2492 T22: 0.2713
REMARK 3 T33: 0.3573 T12: -0.0427
REMARK 3 T13: 0.0604 T23: 0.0285
REMARK 3 L TENSOR
REMARK 3 L11: 0.8029 L22: 0.4966
REMARK 3 L33: 0.6009 L12: -0.1090
REMARK 3 L13: -0.3043 L23: 0.0282
REMARK 3 S TENSOR
REMARK 3 S11: 0.0373 S12: -0.0275 S13: -0.3948
REMARK 3 S21: -0.0508 S22: -0.2457 S23: 0.0194
REMARK 3 S31: 0.0080 S32: 0.1082 S33: 0.0948
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1:17)
REMARK 3 ORIGIN FOR THE GROUP (A): 49.7570 48.5198 75.5153
REMARK 3 T TENSOR
REMARK 3 T11: 0.2151 T22: 0.3086
REMARK 3 T33: 0.1843 T12: 0.0496
REMARK 3 T13: 0.0034 T23: -0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 1.3890 L22: 1.2011
REMARK 3 L33: 0.8282 L12: 0.4520
REMARK 3 L13: 1.0341 L23: 0.4339
REMARK 3 S TENSOR
REMARK 3 S11: -0.0752 S12: -0.2329 S13: -0.1438
REMARK 3 S21: 0.1423 S22: 0.0728 S23: -0.1756
REMARK 3 S31: 0.0060 S32: 0.2102 S33: -0.0319
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 18:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.9528 41.9523 84.9225
REMARK 3 T TENSOR
REMARK 3 T11: 0.3438 T22: 0.5730
REMARK 3 T33: 0.0774 T12: 0.3816
REMARK 3 T13: -0.0078 T23: 0.4156
REMARK 3 L TENSOR
REMARK 3 L11: 0.1968 L22: 0.2130
REMARK 3 L33: 0.1311 L12: 0.0097
REMARK 3 L13: 0.0183 L23: -0.0642
REMARK 3 S TENSOR
REMARK 3 S11: -0.0015 S12: -0.0772 S13: -0.1427
REMARK 3 S21: 0.0866 S22: 0.0424 S23: 0.0122
REMARK 3 S31: 0.1195 S32: 0.1033 S33: 0.0458
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 29:44)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.2449 37.7340 72.4244
REMARK 3 T TENSOR
REMARK 3 T11: 0.3044 T22: 0.3434
REMARK 3 T33: 0.3450 T12: 0.1427
REMARK 3 T13: 0.0924 T23: 0.0787
REMARK 3 L TENSOR
REMARK 3 L11: 0.0895 L22: 0.7986
REMARK 3 L33: 1.4373 L12: 0.1440
REMARK 3 L13: 0.0329 L23: -0.8017
REMARK 3 S TENSOR
REMARK 3 S11: -0.2069 S12: -0.2656 S13: -0.4429
REMARK 3 S21: 0.0020 S22: 0.0062 S23: 0.1429
REMARK 3 S31: 0.2780 S32: 0.3570 S33: 0.0488
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 45:62)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5964 44.5351 81.2192
REMARK 3 T TENSOR
REMARK 3 T11: 0.3308 T22: 0.3298
REMARK 3 T33: 0.2728 T12: 0.0694
REMARK 3 T13: 0.0718 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 0.9220 L22: 1.2058
REMARK 3 L33: 1.0093 L12: -0.5239
REMARK 3 L13: -0.2582 L23: -0.6280
REMARK 3 S TENSOR
REMARK 3 S11: -0.2665 S12: -0.2872 S13: -0.2638
REMARK 3 S21: 0.3827 S22: 0.1564 S23: 0.2012
REMARK 3 S31: -0.0831 S32: 0.0494 S33: -0.0163
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 63:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3330 56.2066 70.7461
REMARK 3 T TENSOR
REMARK 3 T11: 0.2358 T22: 0.2974
REMARK 3 T33: 0.1958 T12: 0.0024
REMARK 3 T13: 0.0358 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 0.3001 L22: 0.6308
REMARK 3 L33: 0.5935 L12: 0.1756
REMARK 3 L13: -0.2547 L23: -0.5876
REMARK 3 S TENSOR
REMARK 3 S11: 0.0108 S12: -0.2105 S13: -0.0192
REMARK 3 S21: 0.1974 S22: -0.1059 S23: -0.0279
REMARK 3 S31: -0.1986 S32: 0.3314 S33: 0.0141
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 91:100)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0181 66.1914 60.6922
REMARK 3 T TENSOR
REMARK 3 T11: 0.2972 T22: 0.2811
REMARK 3 T33: 0.2250 T12: 0.0317
REMARK 3 T13: 0.0548 T23: 0.0212
REMARK 3 L TENSOR
REMARK 3 L11: 0.1273 L22: 0.6097
REMARK 3 L33: 0.7009 L12: -0.2464
REMARK 3 L13: -0.0272 L23: 0.3159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0164 S12: -0.0519 S13: 0.0426
REMARK 3 S21: 0.1495 S22: 0.2302 S23: -0.0499
REMARK 3 S31: -0.1240 S32: -0.0939 S33: -0.0787
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 101:111)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4760 53.8809 56.3683
REMARK 3 T TENSOR
REMARK 3 T11: 0.2869 T22: 0.2869
REMARK 3 T33: 0.2036 T12: 0.0299
REMARK 3 T13: 0.0845 T23: 0.0546
REMARK 3 L TENSOR
REMARK 3 L11: 0.9278 L22: 0.7785
REMARK 3 L33: 0.2496 L12: -0.0512
REMARK 3 L13: 0.2451 L23: 0.3487
REMARK 3 S TENSOR
REMARK 3 S11: -0.1693 S12: 0.4113 S13: 0.1268
REMARK 3 S21: -0.3686 S22: -0.1984 S23: -0.2028
REMARK 3 S31: 0.2085 S32: 0.2029 S33: 0.1213
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 112:126)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9475 55.7102 60.5910
REMARK 3 T TENSOR
REMARK 3 T11: 0.2399 T22: 0.2515
REMARK 3 T33: 0.2188 T12: 0.0625
REMARK 3 T13: 0.0219 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 1.1955 L22: 1.3424
REMARK 3 L33: 0.4865 L12: -1.0347
REMARK 3 L13: -0.0635 L23: 0.2683
REMARK 3 S TENSOR
REMARK 3 S11: 0.1593 S12: 0.2451 S13: -0.1765
REMARK 3 S21: -0.2517 S22: -0.1127 S23: 0.1033
REMARK 3 S31: -0.0659 S32: -0.1605 S33: -0.0110
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 127:166)
REMARK 3 ORIGIN FOR THE GROUP (A): 35.9129 62.1682 69.7126
REMARK 3 T TENSOR
REMARK 3 T11: 0.2885 T22: 0.2593
REMARK 3 T33: 0.2055 T12: 0.0093
REMARK 3 T13: 0.0555 T23: -0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 0.4463 L22: 0.1526
REMARK 3 L33: 0.5651 L12: -0.0316
REMARK 3 L13: 0.0979 L23: 0.0462
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: -0.1007 S13: -0.0073
REMARK 3 S21: 0.0115 S22: 0.0275 S23: -0.0117
REMARK 3 S31: -0.2388 S32: -0.1385 S33: -0.0146
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 167:182)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.7591 60.3209 69.9046
REMARK 3 T TENSOR
REMARK 3 T11: 0.2566 T22: 0.3017
REMARK 3 T33: 0.2584 T12: 0.0056
REMARK 3 T13: 0.0560 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.5535 L22: 1.3628
REMARK 3 L33: 1.9942 L12: -0.6099
REMARK 3 L13: 0.3869 L23: 0.6709
REMARK 3 S TENSOR
REMARK 3 S11: -0.0654 S12: -0.0673 S13: 0.0799
REMARK 3 S21: -0.0414 S22: 0.0575 S23: 0.2089
REMARK 3 S31: -0.1277 S32: -0.4474 S33: -0.0249
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 3TFG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067415.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : KHOZU DOUBLE FLAT CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47646
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PDB ENTRY 3TF8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.9-2.1 M MALONIC ACID (PH 7.0), VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
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 61.56150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.56150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.56150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.56150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 61.56150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.56150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 61.56150
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 61.56150
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 61.56150
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 61.56150
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 61.56150
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 61.56150
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 61.56150
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 61.56150
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 61.56150
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 61.56150
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 61.56150
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 61.56150
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 262 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 263 LIES ON A SPECIAL POSITION.
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 SER A 184
REMARK 465 ASN A 185
REMARK 465 LEU A 186
REMARK 465 TYR A 187
REMARK 465 ASP A 188
REMARK 465 ASP A 189
REMARK 465 ASP B 183
REMARK 465 SER B 184
REMARK 465 ASN B 185
REMARK 465 LEU B 186
REMARK 465 TYR B 187
REMARK 465 ASP B 188
REMARK 465 ASP B 189
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 15 CE NZ
REMARK 480 GLU A 19 CG CD OE1 OE2
REMARK 480 GLN A 27 CD OE1 NE2
REMARK 480 LYS A 28 CD CE NZ
REMARK 480 GLU A 32 CG CD OE1 OE2
REMARK 480 GLU A 57 CD OE1 OE2
REMARK 480 LYS A 128 CE NZ
REMARK 480 GLU A 182 CD OE1 OE2
REMARK 480 GLN B 27 OE1 NE2
REMARK 480 LYS B 28 CE NZ
REMARK 480 GLU B 32 CD OE1 OE2
REMARK 480 LYS B 128 CD CE NZ
REMARK 480 LYS B 154 CD CE NZ
REMARK 480 GLN B 157 CD OE1 NE2
REMARK 480 GLU B 169 CD OE1 OE2
REMARK 480 LYS B 180 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 234 O HOH A 285 2.05
REMARK 500 O HOH A 238 O HOH B 246 2.15
REMARK 500 OE1 GLU B 19 O HOH B 308 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 45 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ILE A 34 105.25 -58.31
REMARK 500 THR A 170 -169.02 -74.82
REMARK 500
REMARK 500 REMARK: NULL
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 HEM A 500 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 105 NE2
REMARK 620 2 HEM A 500 NA 98.5
REMARK 620 3 HEM A 500 NB 93.9 85.3
REMARK 620 4 HEM A 500 NC 103.2 157.6 87.7
REMARK 620 5 HEM A 500 ND 105.1 90.4 160.9 89.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 105 NE2
REMARK 620 2 HEM B 501 NA 106.7
REMARK 620 3 HEM B 501 NB 100.7 87.8
REMARK 620 4 HEM B 501 NC 93.9 159.4 88.7
REMARK 620 5 HEM B 501 ND 99.4 88.8 159.8 87.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O09 RELATED DB: PDB
REMARK 900 RELATED ID: 2O0C RELATED DB: PDB
REMARK 900 RELATED ID: 2O0G RELATED DB: PDB
REMARK 900 RELATED ID: 3TF0 RELATED DB: PDB
REMARK 900 RELATED ID: 3TF1 RELATED DB: PDB
REMARK 900 RELATED ID: 3TF8 RELATED DB: PDB
REMARK 900 RELATED ID: 3TF9 RELATED DB: PDB
REMARK 900 RELATED ID: 3TFA RELATED DB: PDB
REMARK 900 RELATED ID: 3TFD RELATED DB: PDB
REMARK 900 RELATED ID: 3TFE RELATED DB: PDB
REMARK 900 RELATED ID: 3TFF RELATED DB: PDB
REMARK 900 RELATED ID: 3TFG RELATED DB: PDB
DBREF 3TFG A 1 189 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 189
DBREF 3TFG B 1 189 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 189
SEQADV 3TFG TRP A 66 UNP Q8YUQ7 LEU 66 ENGINEERED MUTATION
SEQADV 3TFG TRP A 67 UNP Q8YUQ7 LEU 67 ENGINEERED MUTATION
SEQADV 3TFG TRP B 66 UNP Q8YUQ7 LEU 66 ENGINEERED MUTATION
SEQADV 3TFG TRP B 67 UNP Q8YUQ7 LEU 67 ENGINEERED MUTATION
SEQRES 1 A 189 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 A 189 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 A 189 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 A 189 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 A 189 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 A 189 TRP TRP ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 A 189 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 A 189 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 A 189 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 A 189 PRO ALA PHE GLU CYS GLN HIS THR SER SER LYS SER MET
SEQRES 11 A 189 GLU LEU HIS TYR GLN SER THR ARG CYS GLY LEU ALA PRO
SEQRES 12 A 189 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 A 189 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 A 189 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
SEQRES 15 A 189 ASP SER ASN LEU TYR ASP ASP
SEQRES 1 B 189 MET TYR GLY LEU VAL ASN LYS ALA ILE GLN ASP MET ILE
SEQRES 2 B 189 SER LYS HIS HIS GLY GLU ASP THR TRP GLU ALA ILE LYS
SEQRES 3 B 189 GLN LYS ALA GLY LEU GLU ASP ILE ASP PHE PHE VAL GLY
SEQRES 4 B 189 MET GLU ALA TYR SER ASP ASP VAL THR TYR HIS LEU VAL
SEQRES 5 B 189 GLY ALA ALA SER GLU VAL LEU GLY LYS PRO ALA GLU GLU
SEQRES 6 B 189 TRP TRP ILE ALA PHE GLY GLU TYR TRP VAL THR TYR THR
SEQRES 7 B 189 SER GLU GLU GLY TYR GLY GLU LEU LEU ALA SER ALA GLY
SEQRES 8 B 189 ASP SER LEU PRO GLU PHE MET GLU ASN LEU ASP ASN LEU
SEQRES 9 B 189 HIS ALA ARG VAL GLY LEU SER PHE PRO GLN LEU ARG PRO
SEQRES 10 B 189 PRO ALA PHE GLU CYS GLN HIS THR SER SER LYS SER MET
SEQRES 11 B 189 GLU LEU HIS TYR GLN SER THR ARG CYS GLY LEU ALA PRO
SEQRES 12 B 189 MET VAL LEU GLY LEU LEU HIS GLY LEU GLY LYS ARG PHE
SEQRES 13 B 189 GLN THR LYS VAL GLU VAL THR GLN THR ALA PHE ARG GLU
SEQRES 14 B 189 THR GLY GLU ASP HIS ASP ILE PHE SER ILE LYS TYR GLU
SEQRES 15 B 189 ASP SER ASN LEU TYR ASP ASP
HET HEM A 500 73
HET MLA A 501 7
HET HEM B 501 73
HET MLA B 502 7
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM MLA MALONIC ACID
HETSYN HEM HEME
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 MLA 2(C3 H4 O4)
FORMUL 7 HOH *262(H2 O)
HELIX 1 1 TYR A 2 GLY A 18 1 17
HELIX 2 2 GLY A 18 ALA A 29 1 12
HELIX 3 3 SER A 44 GLY A 60 1 17
HELIX 4 4 PRO A 62 GLU A 81 1 20
HELIX 5 5 TYR A 83 ALA A 90 1 8
HELIX 6 6 SER A 93 PHE A 112 1 20
HELIX 7 7 LEU A 141 PHE A 156 1 16
HELIX 8 8 TYR B 2 GLY B 18 1 17
HELIX 9 9 GLY B 18 ALA B 29 1 12
HELIX 10 10 SER B 44 GLY B 60 1 17
HELIX 11 11 PRO B 62 GLU B 81 1 20
HELIX 12 12 TYR B 83 ALA B 90 1 8
HELIX 13 13 SER B 93 PHE B 112 1 20
HELIX 14 14 LEU B 141 PHE B 156 1 16
SHEET 1 A 4 ALA A 119 SER A 126 0
SHEET 2 A 4 SER A 129 GLN A 135 -1 O HIS A 133 N GLU A 121
SHEET 3 A 4 ASP A 175 GLU A 182 -1 O PHE A 177 N LEU A 132
SHEET 4 A 4 LYS A 159 ALA A 166 -1 N GLU A 161 O LYS A 180
SHEET 1 B 4 ALA B 119 SER B 126 0
SHEET 2 B 4 SER B 129 GLN B 135 -1 O GLN B 135 N ALA B 119
SHEET 3 B 4 ASP B 175 TYR B 181 -1 O PHE B 177 N LEU B 132
SHEET 4 B 4 VAL B 160 ALA B 166 -1 N THR B 163 O SER B 178
LINK NE2 HIS A 105 FE HEM A 500 1555 1555 2.23
LINK NE2 HIS B 105 FE HEM B 501 1555 1555 2.21
SITE 1 AC1 19 MET A 1 TYR A 2 LEU A 4 TRP A 74
SITE 2 AC1 19 TYR A 83 LEU A 87 PHE A 97 LEU A 101
SITE 3 AC1 19 HIS A 105 VAL A 108 LEU A 115 ARG A 116
SITE 4 AC1 19 PRO A 118 TYR A 134 SER A 136 ARG A 138
SITE 5 AC1 19 LEU A 141 LEU A 148 HOH A 212
SITE 1 AC2 23 MET B 1 TYR B 2 VAL B 5 TRP B 74
SITE 2 AC2 23 THR B 78 TYR B 83 LEU B 86 LEU B 87
SITE 3 AC2 23 PHE B 97 LEU B 101 HIS B 105 LEU B 115
SITE 4 AC2 23 ARG B 116 PRO B 118 PHE B 120 TYR B 134
SITE 5 AC2 23 SER B 136 ARG B 138 LEU B 141 VAL B 145
SITE 6 AC2 23 LEU B 148 HOH B 194 HOH B 203
SITE 1 AC3 8 HIS B 16 HIS B 17 LYS B 61 ALA B 69
SITE 2 AC3 8 HOH B 236 HOH B 238 HOH B 271 HOH B 321
SITE 1 AC4 5 HIS A 16 HIS A 17 LYS A 61 TRP A 66
SITE 2 AC4 5 ALA A 69
CRYST1 123.123 123.123 123.123 90.00 90.00 90.00 P 21 3 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 0.008122 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
