HEADER SIGNALING PROTEIN 15-AUG-11 3TF9
TITLE CRYSTAL STRUCTURE OF AN H-NOX PROTEIN FROM NOSTOC SP. PCC 7120 UNDER 1
TITLE 2 ATM OF XENON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALR2278 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HEME-BASED SENSOR DOMAIN (UNP RESIDUES 1-189);
COMPND 5 ENGINEERED: 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 2 13-SEP-23 3TF9 1 REMARK LINK
REVDAT 1 09-NOV-11 3TF9 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. 2.59 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) : 2.59
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.9
REMARK 3 NUMBER OF REFLECTIONS : 36721
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 1902
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 43.9898 - 6.2369 0.97 2538 142 0.1669 0.1744
REMARK 3 2 6.2369 - 4.9526 0.99 2624 128 0.1807 0.2354
REMARK 3 3 4.9526 - 4.3272 0.99 2586 150 0.1344 0.2274
REMARK 3 4 4.3272 - 3.9318 0.98 2619 106 0.1315 0.1479
REMARK 3 5 3.9318 - 3.6501 0.98 2547 154 0.1475 0.1514
REMARK 3 6 3.6501 - 3.4350 0.98 2538 143 0.1611 0.1854
REMARK 3 7 3.4350 - 3.2631 0.97 2529 137 0.1908 0.2363
REMARK 3 8 3.2631 - 3.1211 0.97 2517 145 0.1943 0.2520
REMARK 3 9 3.1211 - 3.0009 0.96 2549 154 0.1827 0.2093
REMARK 3 10 3.0009 - 2.8974 0.95 2422 146 0.2021 0.2247
REMARK 3 11 2.8974 - 2.8068 0.93 2467 116 0.2203 0.2514
REMARK 3 12 2.8068 - 2.7266 0.91 2354 159 0.2393 0.2944
REMARK 3 13 2.7266 - 2.6548 0.88 2317 109 0.2436 0.2669
REMARK 3 14 2.6548 - 2.5901 0.84 2212 113 0.2531 0.2871
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.90
REMARK 3 SHRINKAGE RADIUS : 0.77
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 40.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.150
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 : 0.021 3062
REMARK 3 ANGLE : 1.881 4170
REMARK 3 CHIRALITY : 0.110 429
REMARK 3 PLANARITY : 0.012 534
REMARK 3 DIHEDRAL : 14.880 1088
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 1:28)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.6063 12.1081 77.8432
REMARK 3 T TENSOR
REMARK 3 T11: 0.4887 T22: 0.4940
REMARK 3 T33: 0.6813 T12: -0.0998
REMARK 3 T13: -0.1880 T23: 0.1561
REMARK 3 L TENSOR
REMARK 3 L11: 0.2335 L22: 0.4824
REMARK 3 L33: 0.4318 L12: -0.1241
REMARK 3 L13: -0.2091 L23: 0.0708
REMARK 3 S TENSOR
REMARK 3 S11: 0.1128 S12: -0.1403 S13: -0.3113
REMARK 3 S21: 0.1270 S22: -0.3497 S23: -0.1215
REMARK 3 S31: 0.0142 S32: 0.0924 S33: 0.0613
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 29:44)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.7663 12.2868 86.1832
REMARK 3 T TENSOR
REMARK 3 T11: 0.4571 T22: 0.4588
REMARK 3 T33: 0.4529 T12: -0.1601
REMARK 3 T13: -0.0668 T23: 0.1696
REMARK 3 L TENSOR
REMARK 3 L11: 0.9455 L22: 0.7506
REMARK 3 L33: 0.7007 L12: -0.4655
REMARK 3 L13: 0.4146 L23: -0.3228
REMARK 3 S TENSOR
REMARK 3 S11: 0.1611 S12: -0.2306 S13: -0.2512
REMARK 3 S21: 0.2251 S22: -0.0749 S23: 0.1260
REMARK 3 S31: -0.2379 S32: 0.0157 S33: -0.0406
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 45:62)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4030 21.9114 79.1691
REMARK 3 T TENSOR
REMARK 3 T11: 0.6054 T22: 0.4521
REMARK 3 T33: 0.4837 T12: -0.1345
REMARK 3 T13: -0.2381 T23: 0.1394
REMARK 3 L TENSOR
REMARK 3 L11: 0.4608 L22: 0.2249
REMARK 3 L33: 0.0134 L12: 0.1949
REMARK 3 L13: 0.0074 L23: 0.0401
REMARK 3 S TENSOR
REMARK 3 S11: 0.0852 S12: -0.1533 S13: 0.0740
REMARK 3 S21: 0.3267 S22: -0.2364 S23: -0.1225
REMARK 3 S31: -0.0286 S32: 0.1165 S33: -0.0033
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 63:90)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.4745 14.4144 67.2020
REMARK 3 T TENSOR
REMARK 3 T11: 0.3980 T22: 0.4889
REMARK 3 T33: 0.4774 T12: -0.0117
REMARK 3 T13: -0.0126 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 1.2336 L22: 1.0040
REMARK 3 L33: 1.3902 L12: 0.6530
REMARK 3 L13: 0.8704 L23: 0.3268
REMARK 3 S TENSOR
REMARK 3 S11: 0.3794 S12: 0.3152 S13: -0.3790
REMARK 3 S21: 0.0109 S22: -0.2014 S23: -0.3156
REMARK 3 S31: -0.0174 S32: 0.4767 S33: -0.0850
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 91:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5067 19.4645 63.7830
REMARK 3 T TENSOR
REMARK 3 T11: 0.2287 T22: 0.5205
REMARK 3 T33: 0.4963 T12: -0.1414
REMARK 3 T13: -0.0340 T23: 0.1033
REMARK 3 L TENSOR
REMARK 3 L11: 0.1027 L22: 0.4225
REMARK 3 L33: 0.7326 L12: -0.1810
REMARK 3 L13: -0.1732 L23: 0.1070
REMARK 3 S TENSOR
REMARK 3 S11: -0.0265 S12: -0.0174 S13: 0.6430
REMARK 3 S21: 0.0461 S22: 0.1453 S23: 0.3268
REMARK 3 S31: -0.0434 S32: 0.1393 S33: -0.1241
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 112:126)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.4372 26.0524 67.9211
REMARK 3 T TENSOR
REMARK 3 T11: 0.4277 T22: 0.5223
REMARK 3 T33: 0.5524 T12: 0.0560
REMARK 3 T13: -0.0061 T23: 0.0527
REMARK 3 L TENSOR
REMARK 3 L11: 1.0205 L22: 1.0693
REMARK 3 L33: 1.2239 L12: 0.2577
REMARK 3 L13: -0.8435 L23: -0.0846
REMARK 3 S TENSOR
REMARK 3 S11: -0.1333 S12: 0.3520 S13: 0.0650
REMARK 3 S21: 0.0802 S22: 0.0665 S23: 0.4667
REMARK 3 S31: -0.0260 S32: -0.2532 S33: -0.0924
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 127:141)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1004 30.3353 64.9672
REMARK 3 T TENSOR
REMARK 3 T11: 0.4080 T22: 0.4235
REMARK 3 T33: 0.5653 T12: 0.0461
REMARK 3 T13: 0.0612 T23: 0.0451
REMARK 3 L TENSOR
REMARK 3 L11: 0.9174 L22: 0.5179
REMARK 3 L33: 0.3059 L12: -0.0597
REMARK 3 L13: -0.0479 L23: -0.2037
REMARK 3 S TENSOR
REMARK 3 S11: 0.2567 S12: -0.2254 S13: 0.4289
REMARK 3 S21: 0.0219 S22: 0.0650 S23: 0.1499
REMARK 3 S31: -0.1586 S32: -0.0946 S33: -0.2011
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 142:155)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9546 21.1254 61.9898
REMARK 3 T TENSOR
REMARK 3 T11: 0.2546 T22: 0.4530
REMARK 3 T33: 0.4680 T12: -0.0337
REMARK 3 T13: -0.0084 T23: 0.0760
REMARK 3 L TENSOR
REMARK 3 L11: 0.1607 L22: 0.3314
REMARK 3 L33: 1.0290 L12: -0.1925
REMARK 3 L13: 0.0841 L23: -0.4000
REMARK 3 S TENSOR
REMARK 3 S11: -0.1608 S12: 0.3342 S13: 0.0999
REMARK 3 S21: 0.0196 S22: -0.4334 S23: -0.2006
REMARK 3 S31: -0.0916 S32: 0.2098 S33: 0.2557
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 156:166)
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0489 25.7584 55.5987
REMARK 3 T TENSOR
REMARK 3 T11: 0.4930 T22: 0.5872
REMARK 3 T33: 0.6505 T12: -0.1553
REMARK 3 T13: 0.1279 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.4859 L22: 0.0910
REMARK 3 L33: 0.1244 L12: -0.2064
REMARK 3 L13: -0.2394 L23: 0.1099
REMARK 3 S TENSOR
REMARK 3 S11: -0.0781 S12: 0.0214 S13: -0.0314
REMARK 3 S21: -0.0337 S22: -0.0668 S23: 0.0444
REMARK 3 S31: 0.0190 S32: 0.0332 S33: 0.0505
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 167:183)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.7760 33.5579 62.1977
REMARK 3 T TENSOR
REMARK 3 T11: 0.5247 T22: 0.4504
REMARK 3 T33: 0.5052 T12: -0.0968
REMARK 3 T13: 0.0628 T23: 0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 1.4162 L22: 1.4194
REMARK 3 L33: 0.9649 L12: -1.0376
REMARK 3 L13: -0.0017 L23: -0.6261
REMARK 3 S TENSOR
REMARK 3 S11: -0.2726 S12: 0.0163 S13: 0.5652
REMARK 3 S21: 0.3505 S22: 0.0958 S23: -0.2237
REMARK 3 S31: -0.4449 S32: -0.1312 S33: 0.0347
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1:17)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9778 43.8110 77.9076
REMARK 3 T TENSOR
REMARK 3 T11: 0.3342 T22: 0.6008
REMARK 3 T33: 0.8062 T12: 0.0174
REMARK 3 T13: 0.0530 T23: 0.1339
REMARK 3 L TENSOR
REMARK 3 L11: 0.2878 L22: 0.3341
REMARK 3 L33: 0.6570 L12: 0.2738
REMARK 3 L13: 0.3491 L23: 0.2797
REMARK 3 S TENSOR
REMARK 3 S11: 0.2149 S12: 0.1197 S13: 0.8602
REMARK 3 S21: -0.0008 S22: -0.1408 S23: 0.2489
REMARK 3 S31: 0.0684 S32: -0.4756 S33: -0.0465
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 18:28)
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8163 52.7699 70.7794
REMARK 3 T TENSOR
REMARK 3 T11: 0.3584 T22: 0.2045
REMARK 3 T33: 0.9601 T12: -0.0498
REMARK 3 T13: -0.2959 T23: 0.6775
REMARK 3 L TENSOR
REMARK 3 L11: 0.0167 L22: 0.0070
REMARK 3 L33: 0.0070 L12: -0.0137
REMARK 3 L13: -0.0151 L23: 0.0061
REMARK 3 S TENSOR
REMARK 3 S11: -0.0357 S12: 0.0029 S13: 0.0072
REMARK 3 S21: 0.0042 S22: -0.0450 S23: -0.0196
REMARK 3 S31: -0.0145 S32: 0.0350 S33: -0.1021
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 29:62)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7122 44.8749 70.1840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3842 T22: 0.5326
REMARK 3 T33: 0.6486 T12: -0.1094
REMARK 3 T13: -0.1157 T23: 0.3952
REMARK 3 L TENSOR
REMARK 3 L11: 0.1358 L22: 0.1714
REMARK 3 L33: 0.0476 L12: 0.1380
REMARK 3 L13: -0.0844 L23: -0.0870
REMARK 3 S TENSOR
REMARK 3 S11: -0.1122 S12: 0.2823 S13: 0.1800
REMARK 3 S21: -0.1058 S22: -0.0460 S23: -0.0553
REMARK 3 S31: 0.0948 S32: 0.2425 S33: 0.1141
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 63:80)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.4848 43.3916 84.8941
REMARK 3 T TENSOR
REMARK 3 T11: 0.4188 T22: 0.3322
REMARK 3 T33: 0.6503 T12: 0.0287
REMARK 3 T13: -0.0191 T23: -0.0980
REMARK 3 L TENSOR
REMARK 3 L11: 1.5796 L22: 1.8183
REMARK 3 L33: 0.7987 L12: 1.0233
REMARK 3 L13: -0.0548 L23: 0.0767
REMARK 3 S TENSOR
REMARK 3 S11: -0.2645 S12: -0.1527 S13: 0.8901
REMARK 3 S21: 0.1051 S22: 0.3149 S23: 0.2065
REMARK 3 S31: -0.2900 S32: -0.0016 S33: -0.0822
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 81:100)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3562 29.6812 92.5571
REMARK 3 T TENSOR
REMARK 3 T11: 0.4223 T22: 0.3504
REMARK 3 T33: 0.4662 T12: -0.0981
REMARK 3 T13: -0.0230 T23: 0.0530
REMARK 3 L TENSOR
REMARK 3 L11: 0.9326 L22: 2.5212
REMARK 3 L33: 1.0442 L12: -0.0631
REMARK 3 L13: -0.4990 L23: -0.7345
REMARK 3 S TENSOR
REMARK 3 S11: -0.0140 S12: 0.0792 S13: 0.4619
REMARK 3 S21: 0.4958 S22: -0.0086 S23: -0.2422
REMARK 3 S31: -0.1693 S32: -0.1278 S33: 0.0874
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 101:111)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9188 25.0166 83.7596
REMARK 3 T TENSOR
REMARK 3 T11: 0.4410 T22: 0.3022
REMARK 3 T33: 0.5211 T12: 0.0180
REMARK 3 T13: 0.0053 T23: 0.0164
REMARK 3 L TENSOR
REMARK 3 L11: 2.7176 L22: 0.2778
REMARK 3 L33: 4.1194 L12: -0.7984
REMARK 3 L13: 2.9868 L23: -1.0663
REMARK 3 S TENSOR
REMARK 3 S11: 0.5302 S12: 0.0281 S13: -0.3845
REMARK 3 S21: -0.0589 S22: 0.0585 S23: -0.0866
REMARK 3 S31: 0.6761 S32: -0.0297 S33: -0.5104
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 112:126)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2503 29.5709 85.3117
REMARK 3 T TENSOR
REMARK 3 T11: 0.4766 T22: 0.4255
REMARK 3 T33: 0.5261 T12: 0.0157
REMARK 3 T13: -0.0484 T23: -0.0259
REMARK 3 L TENSOR
REMARK 3 L11: 0.2265 L22: 0.1161
REMARK 3 L33: 0.3297 L12: 0.1512
REMARK 3 L13: 0.2133 L23: 0.0933
REMARK 3 S TENSOR
REMARK 3 S11: 0.1727 S12: 0.0030 S13: -0.0615
REMARK 3 S21: 0.1414 S22: -0.0095 S23: -0.0756
REMARK 3 S31: 0.1508 S32: -0.0298 S33: -0.0949
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 127:166)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.3203 39.0132 91.2419
REMARK 3 T TENSOR
REMARK 3 T11: 0.4904 T22: 0.3149
REMARK 3 T33: 0.5239 T12: -0.0798
REMARK 3 T13: -0.0680 T23: -0.1484
REMARK 3 L TENSOR
REMARK 3 L11: 0.2044 L22: 0.1519
REMARK 3 L33: 0.2156 L12: -0.0754
REMARK 3 L13: -0.0909 L23: 0.1053
REMARK 3 S TENSOR
REMARK 3 S11: 0.0953 S12: 0.0156 S13: 0.0058
REMARK 3 S21: -0.0168 S22: -0.0365 S23: -0.0897
REMARK 3 S31: -0.0495 S32: 0.0760 S33: 0.0192
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 167:184)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.2717 39.4233 90.6571
REMARK 3 T TENSOR
REMARK 3 T11: 0.4348 T22: 0.5111
REMARK 3 T33: 0.4575 T12: -0.0685
REMARK 3 T13: -0.0364 T23: -0.0976
REMARK 3 L TENSOR
REMARK 3 L11: 0.7282 L22: 0.6238
REMARK 3 L33: 0.5384 L12: 0.0038
REMARK 3 L13: 0.4211 L23: 0.2260
REMARK 3 S TENSOR
REMARK 3 S11: 0.0947 S12: 0.2111 S13: -0.0500
REMARK 3 S21: 0.0089 S22: 0.0017 S23: -0.0965
REMARK 3 S31: 0.1044 S32: 0.1988 S33: -0.0647
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 3TF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000067408.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUL-10
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) : 1.40
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 : 36721
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.590
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 (%) : 99.5
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) : 2.59
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.62
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 (%): 68.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M DL-MALIC ACID (PH 7.0) WITH AND
REMARK 280 WITHOUT 100 MM BIS-TRIS PROPANE (PH 7.0), VAPOR DIFFUSION,
REMARK 280 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 62.20200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.20200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.20200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.20200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 62.20200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.20200
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 62.20200
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 62.20200
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 62.20200
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 62.20200
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 62.20200
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 62.20200
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 62.20200
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 62.20200
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 62.20200
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 62.20200
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 62.20200
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 62.20200
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 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 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 32 CG CD OE1 OE2
REMARK 480 ASP A 33 CG OD1 OD2
REMARK 480 LYS A 128 CD CE NZ
REMARK 480 LYS A 154 CG CD CE NZ
REMARK 480 GLN A 157 CD OE1 NE2
REMARK 480 LYS A 159 CE NZ
REMARK 480 GLU A 161 CD OE1 OE2
REMARK 480 GLU A 169 CD OE1 OE2
REMARK 480 LYS A 180 CD CE NZ
REMARK 480 GLU A 182 CG CD OE1 OE2
REMARK 480 LYS B 15 CE NZ
REMARK 480 GLU B 19 CD OE1 OE2
REMARK 480 ASP B 20 CG OD1 OD2
REMARK 480 GLN B 27 CG CD OE1 NE2
REMARK 480 LYS B 28 CD CE NZ
REMARK 480 GLU B 32 CG CD OE1 OE2
REMARK 480 ASP B 33 CG OD1 OD2
REMARK 480 ASP B 35 CG OD1 OD2
REMARK 480 GLU B 57 CG CD OE1 OE2
REMARK 480 LYS B 61 CD CE NZ
REMARK 480 GLU B 65 CD OE1 OE2
REMARK 480 LYS B 128 CG CD CE NZ
REMARK 480 GLN B 157 CD OE1 NE2
REMARK 480 GLU B 169 CG CD OE1 OE2
REMARK 480 GLU B 182 CG CD OE1 OE2
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 33 2.53 -66.45
REMARK 500 GLU A 182 133.19 -173.38
REMARK 500 SER B 126 -178.81 -178.19
REMARK 500 THR B 170 41.18 -78.08
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 NA A 191 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 44 O
REMARK 620 2 THR A 48 OG1 124.7
REMARK 620 N 1
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 98.7
REMARK 620 3 HEM A 500 NB 94.9 82.7
REMARK 620 4 HEM A 500 NC 98.4 161.2 88.1
REMARK 620 5 HEM A 500 ND 104.7 91.0 160.1 92.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 191 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 6 OD1
REMARK 620 2 SER B 44 O 140.1
REMARK 620 3 THR B 48 OG1 81.7 123.6
REMARK 620 N 1 2
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 104.3
REMARK 620 3 HEM B 501 NB 93.1 84.0
REMARK 620 4 HEM B 501 NC 92.2 163.1 91.8
REMARK 620 5 HEM B 501 ND 103.8 90.2 163.0 89.1
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 XE A 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 191
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XE B 190
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 191
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: 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 3TF9 A 1 189 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 189
DBREF 3TF9 B 1 189 UNP Q8YUQ7 Q8YUQ7_NOSS1 1 189
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 LEU LEU 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 LEU LEU 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 XE A 190 1
HET NA A 191 1
HET HEM B 501 73
HET XE B 190 1
HET NA B 191 1
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM XE XENON
HETNAM NA SODIUM ION
HETSYN HEM HEME
FORMUL 3 HEM 2(C34 H32 FE N4 O4)
FORMUL 4 XE 2(XE)
FORMUL 5 NA 2(NA 1+)
FORMUL 9 HOH *23(H2 O)
HELIX 1 1 TYR A 2 GLY A 30 1 29
HELIX 2 2 SER A 44 GLY A 60 1 17
HELIX 3 3 PRO A 62 GLU A 81 1 20
HELIX 4 4 TYR A 83 SER A 89 1 7
HELIX 5 5 SER A 93 ASN A 100 1 8
HELIX 6 6 ASN A 100 PHE A 112 1 13
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 THR A 163 O SER A 178
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 ASP B 183 -1 O PHE B 177 N LEU B 132
SHEET 4 B 4 THR B 158 ALA B 166 -1 N THR B 165 O ILE B 176
LINK O SER A 44 NA NA A 191 1555 1555 2.72
LINK OG1 THR A 48 NA NA A 191 1555 1555 2.76
LINK NE2 HIS A 105 FE HEM A 500 1555 1555 2.20
LINK OD1 ASN B 6 NA NA B 191 1555 1555 2.83
LINK O SER B 44 NA NA B 191 1555 1555 2.97
LINK OG1 THR B 48 NA NA B 191 1555 1555 2.44
LINK NE2 HIS B 105 FE HEM B 501 1555 1555 2.22
SITE 1 AC1 18 MET A 1 TYR A 2 TRP A 74 TYR A 83
SITE 2 AC1 18 PHE A 97 LEU A 101 HIS A 105 LEU A 115
SITE 3 AC1 18 ARG A 116 PRO A 118 TYR A 134 SER A 136
SITE 4 AC1 18 ARG A 138 LEU A 141 VAL A 145 LEU A 148
SITE 5 AC1 18 XE A 190 HOH A 195
SITE 1 AC2 2 TRP A 74 HEM A 500
SITE 1 AC3 5 MET A 1 ASN A 6 TYR A 43 SER A 44
SITE 2 AC3 5 THR A 48
SITE 1 AC4 17 MET B 1 TYR B 2 TRP B 74 THR B 78
SITE 2 AC4 17 LEU B 87 LEU B 101 HIS B 105 LEU B 115
SITE 3 AC4 17 ARG B 116 PRO B 118 TYR B 134 SER B 136
SITE 4 AC4 17 ARG B 138 MET B 144 VAL B 145 LEU B 148
SITE 5 AC4 17 HOH B 197
SITE 1 AC5 1 TRP B 74
SITE 1 AC6 6 MET B 1 ASN B 6 TYR B 43 SER B 44
SITE 2 AC6 6 VAL B 47 THR B 48
CRYST1 124.404 124.404 124.404 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 0.008038 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008038 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008038 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
