HEADER HYDROLASE 30-SEP-11 3U1N
TITLE STRUCTURE OF THE CATALYTIC CORE OF HUMAN SAMHD1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SAM DOMAIN AND HD DOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 120-626;
COMPND 5 SYNONYM: DENDRITIC CELL-DERIVED IFNG-INDUCED PROTEIN, DCIP, MONOCYTE
COMPND 6 PROTEIN 5, MOP-5;
COMPND 7 EC: 3.1.4.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: MOP5, SAMHD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HD-DOMAIN, DEOXYNUCLEOTIDE TRIPHOSPHOHYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.GOLDSTONE,V.ENNIS-ADENIRAN,P.A.WALKER,L.F.HAIRE,M.WEBB,I.A.TAYLOR
REVDAT 5 24-JAN-18 3U1N 1 AUTHOR
REVDAT 4 12-NOV-14 3U1N 1 AUTHOR
REVDAT 3 21-DEC-11 3U1N 1 JRNL
REVDAT 2 14-DEC-11 3U1N 1 JRNL
REVDAT 1 16-NOV-11 3U1N 0
JRNL AUTH D.C.GOLDSTONE,V.ENNIS-ADENIRAN,J.J.HEDDEN,H.C.GROOM,
JRNL AUTH 2 G.I.RICE,E.CHRISTODOULOU,P.A.WALKER,G.KELLY,L.F.HAIRE,
JRNL AUTH 3 M.W.YAP,L.P.DE CARVALHO,J.P.STOYE,Y.J.CROW,I.A.TAYLOR,M.WEBB
JRNL TITL HIV-1 RESTRICTION FACTOR SAMHD1 IS A DEOXYNUCLEOSIDE
JRNL TITL 2 TRIPHOSPHATE TRIPHOSPHOHYDROLASE
JRNL REF NATURE V. 480 379 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 22056990
JRNL DOI 10.1038/NATURE10623
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.56
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 84061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.470
REMARK 3 FREE R VALUE TEST SET COUNT : 3760
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 34.5586 - 9.2425 0.97 3053 143 0.2067 0.2107
REMARK 3 2 9.2425 - 7.3594 0.99 3076 144 0.1746 0.2255
REMARK 3 3 7.3594 - 6.4359 0.99 3115 136 0.2245 0.2509
REMARK 3 4 6.4359 - 5.8506 0.98 3102 149 0.2390 0.2052
REMARK 3 5 5.8506 - 5.4329 0.99 3096 145 0.2161 0.2340
REMARK 3 6 5.4329 - 5.1137 0.98 3106 154 0.1780 0.2289
REMARK 3 7 5.1137 - 4.8583 0.98 3085 135 0.1682 0.2135
REMARK 3 8 4.8583 - 4.6474 0.98 3161 144 0.1541 0.1705
REMARK 3 9 4.6474 - 4.4688 0.98 3052 156 0.1569 0.1845
REMARK 3 10 4.4688 - 4.3149 0.98 3058 135 0.1541 0.1875
REMARK 3 11 4.3149 - 4.1802 0.98 3062 137 0.1568 0.2037
REMARK 3 12 4.1802 - 4.0609 0.98 3086 160 0.1729 0.2054
REMARK 3 13 4.0609 - 3.9542 0.98 3137 128 0.1664 0.1782
REMARK 3 14 3.9542 - 3.8578 0.97 2997 148 0.1764 0.2154
REMARK 3 15 3.8578 - 3.7702 0.96 3101 138 0.1787 0.2057
REMARK 3 16 3.7702 - 3.6901 0.96 2926 135 0.1878 0.2063
REMARK 3 17 3.6901 - 3.6164 0.95 3080 140 0.1993 0.2752
REMARK 3 18 3.6164 - 3.5482 0.95 2820 155 0.2051 0.2663
REMARK 3 19 3.5482 - 3.4849 0.94 3064 148 0.2062 0.2736
REMARK 3 20 3.4849 - 3.4259 0.93 2911 127 0.2246 0.2880
REMARK 3 21 3.4259 - 3.3707 0.91 2929 137 0.2337 0.2407
REMARK 3 22 3.3707 - 3.3188 0.90 2822 140 0.2357 0.2921
REMARK 3 23 3.3188 - 3.2701 0.91 2821 124 0.2554 0.2570
REMARK 3 24 3.2701 - 3.2240 0.88 2791 133 0.2731 0.3245
REMARK 3 25 3.2240 - 3.1805 0.86 2717 131 0.2848 0.3091
REMARK 3 26 3.1805 - 3.1392 0.84 2653 106 0.3224 0.3991
REMARK 3 27 3.1392 - 3.1000 0.80 2480 132 0.3328 0.3345
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 38.81
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.390
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.92
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.62530
REMARK 3 B22 (A**2) : 0.29780
REMARK 3 B33 (A**2) : -3.92310
REMARK 3 B12 (A**2) : 0.88850
REMARK 3 B13 (A**2) : -1.29060
REMARK 3 B23 (A**2) : -5.54670
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 : 0.010 13893
REMARK 3 ANGLE : 1.203 18822
REMARK 3 CHIRALITY : 0.082 2038
REMARK 3 PLANARITY : 0.005 2438
REMARK 3 DIHEDRAL : 16.510 5006
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 118:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.5413 20.1669 4.9281
REMARK 3 T TENSOR
REMARK 3 T11: 0.4078 T22: 0.2669
REMARK 3 T33: 0.3430 T12: 0.0519
REMARK 3 T13: -0.0416 T23: 0.0757
REMARK 3 L TENSOR
REMARK 3 L11: 2.4801 L22: 0.9252
REMARK 3 L33: 3.0441 L12: 1.4713
REMARK 3 L13: 0.4377 L23: -0.0715
REMARK 3 S TENSOR
REMARK 3 S11: -0.0536 S12: 0.0589 S13: 0.2574
REMARK 3 S21: -0.0263 S22: -0.0204 S23: 0.3767
REMARK 3 S31: -0.3551 S32: -0.1679 S33: -0.0120
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 217:470)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5222 12.8699 2.0608
REMARK 3 T TENSOR
REMARK 3 T11: 0.3710 T22: 0.3627
REMARK 3 T33: 0.3600 T12: -0.0439
REMARK 3 T13: 0.0083 T23: 0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.9834 L22: 2.0035
REMARK 3 L33: 1.8215 L12: -0.5581
REMARK 3 L13: -0.3399 L23: 0.1811
REMARK 3 S TENSOR
REMARK 3 S11: 0.0188 S12: 0.1979 S13: 0.2531
REMARK 3 S21: -0.2358 S22: -0.0196 S23: -0.1359
REMARK 3 S31: -0.4311 S32: 0.1580 S33: 0.0005
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 471:504)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4925 -9.4546 0.4648
REMARK 3 T TENSOR
REMARK 3 T11: 0.4580 T22: 0.5300
REMARK 3 T33: 0.4565 T12: 0.1091
REMARK 3 T13: 0.0675 T23: 0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 0.9801 L22: 0.2301
REMARK 3 L33: 0.4462 L12: 0.3388
REMARK 3 L13: 0.1463 L23: -0.0349
REMARK 3 S TENSOR
REMARK 3 S11: 0.2707 S12: 0.1625 S13: 0.1679
REMARK 3 S21: -0.1953 S22: -0.1988 S23: -0.5635
REMARK 3 S31: 0.2765 S32: 0.3202 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 505:530)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5916 32.8226 18.4189
REMARK 3 T TENSOR
REMARK 3 T11: 1.1265 T22: 0.6095
REMARK 3 T33: 0.7644 T12: -0.4398
REMARK 3 T13: -0.1018 T23: -0.1025
REMARK 3 L TENSOR
REMARK 3 L11: 0.5366 L22: 0.0163
REMARK 3 L33: 0.1564 L12: -0.0779
REMARK 3 L13: 0.1995 L23: -0.0560
REMARK 3 S TENSOR
REMARK 3 S11: 0.1339 S12: 1.2215 S13: 0.0836
REMARK 3 S21: -0.5782 S22: -0.1081 S23: -0.3964
REMARK 3 S31: -0.1532 S32: -0.0055 S33: -0.0431
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 546:583)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1233 -9.8243 8.2224
REMARK 3 T TENSOR
REMARK 3 T11: 0.2654 T22: 0.5687
REMARK 3 T33: 0.4819 T12: 0.0755
REMARK 3 T13: 0.0091 T23: 0.0238
REMARK 3 L TENSOR
REMARK 3 L11: 0.7030 L22: 0.4274
REMARK 3 L33: 1.0655 L12: -0.0398
REMARK 3 L13: 0.1430 L23: -0.0087
REMARK 3 S TENSOR
REMARK 3 S11: 0.0886 S12: -0.3088 S13: -0.0957
REMARK 3 S21: -0.1019 S22: 0.1039 S23: -0.3629
REMARK 3 S31: 0.2842 S32: 0.5193 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 118:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4253 24.7058 52.3422
REMARK 3 T TENSOR
REMARK 3 T11: 0.3908 T22: 0.2586
REMARK 3 T33: 0.3145 T12: -0.0522
REMARK 3 T13: 0.0313 T23: 0.0364
REMARK 3 L TENSOR
REMARK 3 L11: 2.4328 L22: 0.9325
REMARK 3 L33: 2.7459 L12: -1.1024
REMARK 3 L13: -0.1653 L23: -0.0501
REMARK 3 S TENSOR
REMARK 3 S11: -0.0598 S12: -0.1285 S13: -0.3101
REMARK 3 S21: -0.0260 S22: 0.0424 S23: 0.4437
REMARK 3 S31: 0.4095 S32: -0.1838 S33: -0.0024
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 217:470)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4941 31.9852 55.1610
REMARK 3 T TENSOR
REMARK 3 T11: 0.3231 T22: 0.3167
REMARK 3 T33: 0.3301 T12: 0.0450
REMARK 3 T13: -0.0248 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.0177 L22: 2.0759
REMARK 3 L33: 1.8427 L12: 0.7907
REMARK 3 L13: 0.1424 L23: 0.2068
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: -0.1914 S13: -0.2117
REMARK 3 S21: 0.1986 S22: -0.0583 S23: -0.0915
REMARK 3 S31: 0.4061 S32: 0.1977 S33: 0.0007
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 471:504)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.2981 54.4539 56.9623
REMARK 3 T TENSOR
REMARK 3 T11: 0.4705 T22: 0.5025
REMARK 3 T33: 0.4240 T12: -0.1103
REMARK 3 T13: -0.0348 T23: 0.0583
REMARK 3 L TENSOR
REMARK 3 L11: 0.8963 L22: 0.2806
REMARK 3 L33: 0.5922 L12: -0.2543
REMARK 3 L13: -0.0134 L23: -0.0853
REMARK 3 S TENSOR
REMARK 3 S11: 0.1162 S12: -0.1695 S13: -0.1066
REMARK 3 S21: -0.1534 S22: -0.0199 S23: -0.5634
REMARK 3 S31: -0.3897 S32: 0.0524 S33: 0.0002
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 505:531)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5699 12.1483 38.4230
REMARK 3 T TENSOR
REMARK 3 T11: 1.2489 T22: 0.8236
REMARK 3 T33: 0.6183 T12: 0.2362
REMARK 3 T13: 0.0856 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 1.0335 L22: 0.6648
REMARK 3 L33: 0.1385 L12: 0.4383
REMARK 3 L13: 0.3500 L23: 0.0908
REMARK 3 S TENSOR
REMARK 3 S11: 0.2804 S12: -0.7406 S13: -0.5717
REMARK 3 S21: 0.2026 S22: -0.0345 S23: -0.2078
REMARK 3 S31: -0.8120 S32: -0.0467 S33: 0.0243
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 546:583)
REMARK 3 ORIGIN FOR THE GROUP (A): 22.1908 54.8850 48.9098
REMARK 3 T TENSOR
REMARK 3 T11: 0.1775 T22: 0.5670
REMARK 3 T33: 0.4485 T12: -0.0744
REMARK 3 T13: 0.0006 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4653 L22: 0.5948
REMARK 3 L33: 0.7089 L12: 0.3433
REMARK 3 L13: -0.0657 L23: -0.1250
REMARK 3 S TENSOR
REMARK 3 S11: 0.1093 S12: 0.0667 S13: -0.0387
REMARK 3 S21: -0.0760 S22: 0.1099 S23: -0.0420
REMARK 3 S31: -0.4350 S32: 0.4858 S33: 0.0070
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 117:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2554 51.0712 38.4663
REMARK 3 T TENSOR
REMARK 3 T11: 0.3143 T22: 0.2616
REMARK 3 T33: 0.3037 T12: 0.0309
REMARK 3 T13: -0.0416 T23: -0.0234
REMARK 3 L TENSOR
REMARK 3 L11: 2.0843 L22: 1.4557
REMARK 3 L33: 2.1123 L12: -0.7209
REMARK 3 L13: 1.4090 L23: 0.3707
REMARK 3 S TENSOR
REMARK 3 S11: -0.1655 S12: 0.0785 S13: 0.1244
REMARK 3 S21: -0.0730 S22: -0.0128 S23: -0.0317
REMARK 3 S31: -0.2161 S32: 0.0141 S33: 0.0001
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 217:340)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8042 54.6606 37.3496
REMARK 3 T TENSOR
REMARK 3 T11: 0.5088 T22: 0.5071
REMARK 3 T33: 0.5658 T12: 0.1432
REMARK 3 T13: -0.0456 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 1.2490 L22: 1.7766
REMARK 3 L33: 1.8207 L12: 0.5458
REMARK 3 L13: 0.0525 L23: -1.6187
REMARK 3 S TENSOR
REMARK 3 S11: -0.0124 S12: -0.0317 S13: 0.2147
REMARK 3 S21: 0.0792 S22: 0.1724 S23: 0.2752
REMARK 3 S31: -0.4477 S32: -0.3731 S33: 0.0004
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 341:504)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6915 40.3440 53.5172
REMARK 3 T TENSOR
REMARK 3 T11: 0.2362 T22: 0.5285
REMARK 3 T33: 0.4492 T12: 0.0811
REMARK 3 T13: 0.0161 T23: -0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 1.6525 L22: 1.5160
REMARK 3 L33: 1.4977 L12: 0.7285
REMARK 3 L13: -0.2139 L23: -0.5558
REMARK 3 S TENSOR
REMARK 3 S11: 0.0249 S12: -0.2556 S13: 0.1139
REMARK 3 S21: 0.0791 S22: 0.0377 S23: 0.5076
REMARK 3 S31: 0.0466 S32: -0.4842 S33: -0.0044
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 505:523)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0766 44.5578 20.7024
REMARK 3 T TENSOR
REMARK 3 T11: 1.1987 T22: 1.1157
REMARK 3 T33: 0.9061 T12: -0.0422
REMARK 3 T13: -0.2069 T23: -0.1116
REMARK 3 L TENSOR
REMARK 3 L11: 0.2913 L22: 0.2386
REMARK 3 L33: 0.0212 L12: -0.2817
REMARK 3 L13: 0.0149 L23: 0.0028
REMARK 3 S TENSOR
REMARK 3 S11: -0.6237 S12: -0.5861 S13: -0.2583
REMARK 3 S21: -0.1643 S22: 0.3729 S23: 0.0843
REMARK 3 S31: 0.0574 S32: 0.2157 S33: 0.0009
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 547:583)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7198 27.6144 55.7534
REMARK 3 T TENSOR
REMARK 3 T11: 0.4480 T22: 0.9898
REMARK 3 T33: 0.9099 T12: -0.1806
REMARK 3 T13: 0.0348 T23: 0.0788
REMARK 3 L TENSOR
REMARK 3 L11: 0.4051 L22: 0.4713
REMARK 3 L33: 0.7981 L12: 0.0593
REMARK 3 L13: -0.1994 L23: 0.3018
REMARK 3 S TENSOR
REMARK 3 S11: 0.3640 S12: -0.2524 S13: -0.6808
REMARK 3 S21: 0.1750 S22: -0.0685 S23: 0.1238
REMARK 3 S31: 0.8925 S32: -0.3204 S33: 0.0100
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 117:216)
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3064 -6.1390 18.8642
REMARK 3 T TENSOR
REMARK 3 T11: 0.2995 T22: 0.2434
REMARK 3 T33: 0.2786 T12: -0.0345
REMARK 3 T13: 0.0406 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 2.1602 L22: 1.3928
REMARK 3 L33: 1.9013 L12: 0.5645
REMARK 3 L13: -1.3208 L23: 0.3495
REMARK 3 S TENSOR
REMARK 3 S11: -0.1326 S12: -0.0700 S13: -0.0139
REMARK 3 S21: 0.1693 S22: -0.0611 S23: -0.0144
REMARK 3 S31: 0.0429 S32: 0.0220 S33: -0.0005
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN D AND RESID 217:364)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5283 -8.0062 22.7959
REMARK 3 T TENSOR
REMARK 3 T11: 0.4286 T22: 0.4747
REMARK 3 T33: 0.4897 T12: -0.1258
REMARK 3 T13: 0.0920 T23: -0.0450
REMARK 3 L TENSOR
REMARK 3 L11: 1.4506 L22: 1.9468
REMARK 3 L33: 2.3357 L12: -0.7536
REMARK 3 L13: 0.3038 L23: -1.8335
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.1158 S13: -0.0963
REMARK 3 S21: 0.1879 S22: 0.1948 S23: 0.3314
REMARK 3 S31: 0.3116 S32: -0.5342 S33: 0.0038
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN D AND RESID 365:504)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4719 4.6560 -1.0746
REMARK 3 T TENSOR
REMARK 3 T11: 0.2716 T22: 0.5688
REMARK 3 T33: 0.4355 T12: -0.0743
REMARK 3 T13: -0.0568 T23: 0.0211
REMARK 3 L TENSOR
REMARK 3 L11: 2.1032 L22: 1.3256
REMARK 3 L33: 1.4474 L12: -0.4690
REMARK 3 L13: 0.2959 L23: -0.0373
REMARK 3 S TENSOR
REMARK 3 S11: -0.0333 S12: 0.4351 S13: 0.0296
REMARK 3 S21: -0.2580 S22: -0.0165 S23: 0.4058
REMARK 3 S31: 0.0051 S32: -0.4206 S33: 0.0001
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 505:523)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.8500 0.8136 35.7951
REMARK 3 T TENSOR
REMARK 3 T11: 1.3231 T22: 1.2264
REMARK 3 T33: 0.8776 T12: 0.1607
REMARK 3 T13: 0.3822 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 0.2275 L22: 0.1678
REMARK 3 L33: 0.0470 L12: 0.0617
REMARK 3 L13: -0.0870 L23: 0.0275
REMARK 3 S TENSOR
REMARK 3 S11: -0.1320 S12: 0.8137 S13: 0.2359
REMARK 3 S21: -0.0847 S22: 0.2761 S23: -0.1693
REMARK 3 S31: -0.0850 S32: -0.2808 S33: -0.0005
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 547:583)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.7228 17.3718 1.5853
REMARK 3 T TENSOR
REMARK 3 T11: 0.3327 T22: 0.8953
REMARK 3 T33: 0.8316 T12: 0.2332
REMARK 3 T13: -0.1679 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.2624 L22: 0.6294
REMARK 3 L33: 0.6665 L12: -0.1646
REMARK 3 L13: 0.0794 L23: 0.4457
REMARK 3 S TENSOR
REMARK 3 S11: 0.1658 S12: 0.3130 S13: 0.6264
REMARK 3 S21: -0.6501 S22: 0.1184 S23: 0.1345
REMARK 3 S31: -1.0263 S32: -0.0828 S33: 0.0185
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 516:530 OR RESSEQ 548:583 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 517:531 OR RESSEQ 548:583 )
REMARK 3 ATOM PAIRS NUMBER : 3268
REMARK 3 RMSD : 0.032
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 516:530 OR RESSEQ 548:583 )
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 517:523 OR RESSEQ 548:583 )
REMARK 3 ATOM PAIRS NUMBER : 3200
REMARK 3 RMSD : 0.058
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 516:530 OR RESSEQ 548:583 )
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 118:276 OR RESSEQ
REMARK 3 284:287 OR RESSEQ 289:311 OR RESSEQ 313:
REMARK 3 460 OR RESSEQ 468:486 OR RESSEQ 491:504
REMARK 3 OR RESSEQ 516:523 OR RESSEQ 548:583 )
REMARK 3 ATOM PAIRS NUMBER : 3221
REMARK 3 RMSD : 0.054
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3U1N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068192.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 89495
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.58100
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: SAD
REMARK 200 SOFTWARE USED: SHELX, RESOLVE, SHELXD
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ALA A 99
REMARK 465 SER A 100
REMARK 465 TRP A 101
REMARK 465 SER A 102
REMARK 465 HIS A 103
REMARK 465 PRO A 104
REMARK 465 GLN A 105
REMARK 465 PHE A 106
REMARK 465 GLU A 107
REMARK 465 LYS A 108
REMARK 465 GLY A 109
REMARK 465 ALA A 110
REMARK 465 LEU A 111
REMARK 465 GLU A 112
REMARK 465 VAL A 113
REMARK 465 LEU A 114
REMARK 465 PHE A 115
REMARK 465 GLN A 116
REMARK 465 GLY A 117
REMARK 465 SER A 278
REMARK 465 PRO A 279
REMARK 465 VAL A 280
REMARK 465 GLU A 281
REMARK 465 ASP A 282
REMARK 465 SER A 283
REMARK 465 ASP A 506
REMARK 465 TYR A 507
REMARK 465 GLY A 508
REMARK 465 MSE A 509
REMARK 465 GLN A 510
REMARK 465 GLU A 511
REMARK 465 LYS A 512
REMARK 465 ASN A 513
REMARK 465 PRO A 514
REMARK 465 ILE A 515
REMARK 465 ARG A 531
REMARK 465 ILE A 532
REMARK 465 THR A 533
REMARK 465 LYS A 534
REMARK 465 ASN A 535
REMARK 465 GLN A 536
REMARK 465 VAL A 537
REMARK 465 SER A 538
REMARK 465 GLN A 539
REMARK 465 LEU A 540
REMARK 465 LEU A 541
REMARK 465 PRO A 542
REMARK 465 GLU A 543
REMARK 465 LYS A 544
REMARK 465 PHE A 545
REMARK 465 GLY A 584
REMARK 465 ASP A 585
REMARK 465 VAL A 586
REMARK 465 ILE A 587
REMARK 465 ALA A 588
REMARK 465 PRO A 589
REMARK 465 LEU A 590
REMARK 465 ILE A 591
REMARK 465 THR A 592
REMARK 465 PRO A 593
REMARK 465 GLN A 594
REMARK 465 LYS A 595
REMARK 465 LYS A 596
REMARK 465 GLU A 597
REMARK 465 TRP A 598
REMARK 465 ASN A 599
REMARK 465 ASP A 600
REMARK 465 SER A 601
REMARK 465 THR A 602
REMARK 465 SER A 603
REMARK 465 VAL A 604
REMARK 465 GLN A 605
REMARK 465 ASN A 606
REMARK 465 PRO A 607
REMARK 465 THR A 608
REMARK 465 ARG A 609
REMARK 465 LEU A 610
REMARK 465 ARG A 611
REMARK 465 GLU A 612
REMARK 465 ALA A 613
REMARK 465 SER A 614
REMARK 465 LYS A 615
REMARK 465 SER A 616
REMARK 465 ARG A 617
REMARK 465 VAL A 618
REMARK 465 GLN A 619
REMARK 465 LEU A 620
REMARK 465 PHE A 621
REMARK 465 LYS A 622
REMARK 465 ASP A 623
REMARK 465 ASP A 624
REMARK 465 PRO A 625
REMARK 465 MSE A 626
REMARK 465 ALA B 99
REMARK 465 SER B 100
REMARK 465 TRP B 101
REMARK 465 SER B 102
REMARK 465 HIS B 103
REMARK 465 PRO B 104
REMARK 465 GLN B 105
REMARK 465 PHE B 106
REMARK 465 GLU B 107
REMARK 465 LYS B 108
REMARK 465 GLY B 109
REMARK 465 ALA B 110
REMARK 465 LEU B 111
REMARK 465 GLU B 112
REMARK 465 VAL B 113
REMARK 465 LEU B 114
REMARK 465 PHE B 115
REMARK 465 GLN B 116
REMARK 465 GLY B 117
REMARK 465 GLU B 277
REMARK 465 SER B 278
REMARK 465 PRO B 279
REMARK 465 VAL B 280
REMARK 465 GLU B 281
REMARK 465 ASP B 282
REMARK 465 SER B 283
REMARK 465 ASP B 506
REMARK 465 TYR B 507
REMARK 465 GLY B 508
REMARK 465 MSE B 509
REMARK 465 GLN B 510
REMARK 465 GLU B 511
REMARK 465 LYS B 512
REMARK 465 ASN B 513
REMARK 465 PRO B 514
REMARK 465 ILE B 515
REMARK 465 ASP B 516
REMARK 465 ILE B 532
REMARK 465 THR B 533
REMARK 465 LYS B 534
REMARK 465 ASN B 535
REMARK 465 GLN B 536
REMARK 465 VAL B 537
REMARK 465 SER B 538
REMARK 465 GLN B 539
REMARK 465 LEU B 540
REMARK 465 LEU B 541
REMARK 465 PRO B 542
REMARK 465 GLU B 543
REMARK 465 LYS B 544
REMARK 465 PHE B 545
REMARK 465 GLY B 584
REMARK 465 ASP B 585
REMARK 465 VAL B 586
REMARK 465 ILE B 587
REMARK 465 ALA B 588
REMARK 465 PRO B 589
REMARK 465 LEU B 590
REMARK 465 ILE B 591
REMARK 465 THR B 592
REMARK 465 PRO B 593
REMARK 465 GLN B 594
REMARK 465 LYS B 595
REMARK 465 LYS B 596
REMARK 465 GLU B 597
REMARK 465 TRP B 598
REMARK 465 ASN B 599
REMARK 465 ASP B 600
REMARK 465 SER B 601
REMARK 465 THR B 602
REMARK 465 SER B 603
REMARK 465 VAL B 604
REMARK 465 GLN B 605
REMARK 465 ASN B 606
REMARK 465 PRO B 607
REMARK 465 THR B 608
REMARK 465 ARG B 609
REMARK 465 LEU B 610
REMARK 465 ARG B 611
REMARK 465 GLU B 612
REMARK 465 ALA B 613
REMARK 465 SER B 614
REMARK 465 LYS B 615
REMARK 465 SER B 616
REMARK 465 ARG B 617
REMARK 465 VAL B 618
REMARK 465 GLN B 619
REMARK 465 LEU B 620
REMARK 465 PHE B 621
REMARK 465 LYS B 622
REMARK 465 ASP B 623
REMARK 465 ASP B 624
REMARK 465 PRO B 625
REMARK 465 MSE B 626
REMARK 465 ALA C 99
REMARK 465 SER C 100
REMARK 465 TRP C 101
REMARK 465 SER C 102
REMARK 465 HIS C 103
REMARK 465 PRO C 104
REMARK 465 GLN C 105
REMARK 465 PHE C 106
REMARK 465 GLU C 107
REMARK 465 LYS C 108
REMARK 465 GLY C 109
REMARK 465 ALA C 110
REMARK 465 LEU C 111
REMARK 465 GLU C 112
REMARK 465 VAL C 113
REMARK 465 LEU C 114
REMARK 465 PHE C 115
REMARK 465 GLN C 116
REMARK 465 SER C 278
REMARK 465 PRO C 279
REMARK 465 VAL C 280
REMARK 465 GLU C 281
REMARK 465 ASP C 282
REMARK 465 SER C 283
REMARK 465 ASP C 506
REMARK 465 TYR C 507
REMARK 465 GLY C 508
REMARK 465 MSE C 509
REMARK 465 GLN C 510
REMARK 465 GLU C 511
REMARK 465 LYS C 512
REMARK 465 ASN C 513
REMARK 465 PRO C 514
REMARK 465 ILE C 515
REMARK 465 ASP C 516
REMARK 465 THR C 524
REMARK 465 ALA C 525
REMARK 465 PRO C 526
REMARK 465 ASN C 527
REMARK 465 ARG C 528
REMARK 465 ALA C 529
REMARK 465 ILE C 530
REMARK 465 ARG C 531
REMARK 465 ILE C 532
REMARK 465 THR C 533
REMARK 465 LYS C 534
REMARK 465 ASN C 535
REMARK 465 GLN C 536
REMARK 465 VAL C 537
REMARK 465 SER C 538
REMARK 465 GLN C 539
REMARK 465 LEU C 540
REMARK 465 LEU C 541
REMARK 465 PRO C 542
REMARK 465 GLU C 543
REMARK 465 LYS C 544
REMARK 465 PHE C 545
REMARK 465 ALA C 546
REMARK 465 GLY C 584
REMARK 465 ASP C 585
REMARK 465 VAL C 586
REMARK 465 ILE C 587
REMARK 465 ALA C 588
REMARK 465 PRO C 589
REMARK 465 LEU C 590
REMARK 465 ILE C 591
REMARK 465 THR C 592
REMARK 465 PRO C 593
REMARK 465 GLN C 594
REMARK 465 LYS C 595
REMARK 465 LYS C 596
REMARK 465 GLU C 597
REMARK 465 TRP C 598
REMARK 465 ASN C 599
REMARK 465 ASP C 600
REMARK 465 SER C 601
REMARK 465 THR C 602
REMARK 465 SER C 603
REMARK 465 VAL C 604
REMARK 465 GLN C 605
REMARK 465 ASN C 606
REMARK 465 PRO C 607
REMARK 465 THR C 608
REMARK 465 ARG C 609
REMARK 465 LEU C 610
REMARK 465 ARG C 611
REMARK 465 GLU C 612
REMARK 465 ALA C 613
REMARK 465 SER C 614
REMARK 465 LYS C 615
REMARK 465 SER C 616
REMARK 465 ARG C 617
REMARK 465 VAL C 618
REMARK 465 GLN C 619
REMARK 465 LEU C 620
REMARK 465 PHE C 621
REMARK 465 LYS C 622
REMARK 465 ASP C 623
REMARK 465 ASP C 624
REMARK 465 PRO C 625
REMARK 465 MSE C 626
REMARK 465 ALA D 99
REMARK 465 SER D 100
REMARK 465 TRP D 101
REMARK 465 SER D 102
REMARK 465 HIS D 103
REMARK 465 PRO D 104
REMARK 465 GLN D 105
REMARK 465 PHE D 106
REMARK 465 GLU D 107
REMARK 465 LYS D 108
REMARK 465 GLY D 109
REMARK 465 ALA D 110
REMARK 465 LEU D 111
REMARK 465 GLU D 112
REMARK 465 VAL D 113
REMARK 465 LEU D 114
REMARK 465 PHE D 115
REMARK 465 GLN D 116
REMARK 465 GLU D 277
REMARK 465 SER D 278
REMARK 465 PRO D 279
REMARK 465 VAL D 280
REMARK 465 GLU D 281
REMARK 465 ASP D 282
REMARK 465 SER D 283
REMARK 465 VAL D 487
REMARK 465 LEU D 488
REMARK 465 LEU D 489
REMARK 465 ASP D 506
REMARK 465 TYR D 507
REMARK 465 GLY D 508
REMARK 465 MSE D 509
REMARK 465 GLN D 510
REMARK 465 GLU D 511
REMARK 465 LYS D 512
REMARK 465 ASN D 513
REMARK 465 PRO D 514
REMARK 465 ILE D 515
REMARK 465 THR D 524
REMARK 465 ALA D 525
REMARK 465 PRO D 526
REMARK 465 ASN D 527
REMARK 465 ARG D 528
REMARK 465 ALA D 529
REMARK 465 ILE D 530
REMARK 465 ARG D 531
REMARK 465 ILE D 532
REMARK 465 THR D 533
REMARK 465 LYS D 534
REMARK 465 ASN D 535
REMARK 465 GLN D 536
REMARK 465 VAL D 537
REMARK 465 SER D 538
REMARK 465 GLN D 539
REMARK 465 LEU D 540
REMARK 465 LEU D 541
REMARK 465 PRO D 542
REMARK 465 GLU D 543
REMARK 465 LYS D 544
REMARK 465 PHE D 545
REMARK 465 ALA D 546
REMARK 465 GLY D 584
REMARK 465 ASP D 585
REMARK 465 VAL D 586
REMARK 465 ILE D 587
REMARK 465 ALA D 588
REMARK 465 PRO D 589
REMARK 465 LEU D 590
REMARK 465 ILE D 591
REMARK 465 THR D 592
REMARK 465 PRO D 593
REMARK 465 GLN D 594
REMARK 465 LYS D 595
REMARK 465 LYS D 596
REMARK 465 GLU D 597
REMARK 465 TRP D 598
REMARK 465 ASN D 599
REMARK 465 ASP D 600
REMARK 465 SER D 601
REMARK 465 THR D 602
REMARK 465 SER D 603
REMARK 465 VAL D 604
REMARK 465 GLN D 605
REMARK 465 ASN D 606
REMARK 465 PRO D 607
REMARK 465 THR D 608
REMARK 465 ARG D 609
REMARK 465 LEU D 610
REMARK 465 ARG D 611
REMARK 465 GLU D 612
REMARK 465 ALA D 613
REMARK 465 SER D 614
REMARK 465 LYS D 615
REMARK 465 SER D 616
REMARK 465 ARG D 617
REMARK 465 VAL D 618
REMARK 465 GLN D 619
REMARK 465 LEU D 620
REMARK 465 PHE D 621
REMARK 465 LYS D 622
REMARK 465 ASP D 623
REMARK 465 ASP D 624
REMARK 465 PRO D 625
REMARK 465 MSE D 626
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 185 CG CD CE NZ
REMARK 470 GLN A 190 CG CD OE1 NE2
REMARK 470 GLU A 193 CG CD OE1 OE2
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 GLU A 262 CG CD OE1 OE2
REMARK 470 GLU A 263 CG CD OE1 OE2
REMARK 470 GLU A 277 CG CD OE1 OE2
REMARK 470 LYS A 288 CD CE NZ
REMARK 470 LYS A 304 CG CD CE NZ
REMARK 470 ARG A 305 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 312 CD CE NZ
REMARK 470 LYS A 336 CE NZ
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 ASP A 344 CG OD1 OD2
REMARK 470 ASN A 345 CG OD1 ND2
REMARK 470 LYS A 354 CG CD CE NZ
REMARK 470 ARG A 372 NE CZ NH1 NH2
REMARK 470 LYS A 377 CD CE NZ
REMARK 470 GLU A 398 CG CD OE1 OE2
REMARK 470 LYS A 405 CG CD CE NZ
REMARK 470 ARG A 408 NE CZ NH1 NH2
REMARK 470 LYS A 455 CD CE NZ
REMARK 470 LYS A 467 CD CE NZ
REMARK 470 LYS A 484 CE NZ
REMARK 470 LYS A 486 CG CD CE NZ
REMARK 470 LEU A 488 CG CD1 CD2
REMARK 470 LEU A 489 CG CD1 CD2
REMARK 470 ASP A 490 CG OD1 OD2
REMARK 470 LYS A 492 CG CD CE NZ
REMARK 470 LYS A 494 CG CD CE NZ
REMARK 470 GLU A 496 CG CD OE1 OE2
REMARK 470 ASP A 516 CG OD1 OD2
REMARK 470 CYS A 522 SG
REMARK 470 LYS A 523 CG CD CE NZ
REMARK 470 LYS A 580 CD CE NZ
REMARK 470 GLN A 582 CG CD OE1 NE2
REMARK 470 ASP A 583 CG OD1 OD2
REMARK 470 HIS B 125 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 184 CG CD OE1 OE2
REMARK 470 GLN B 190 CG CD OE1 NE2
REMARK 470 GLU B 193 CG CD OE1 OE2
REMARK 470 LYS B 230 CG CD CE NZ
REMARK 470 GLU B 262 CG CD OE1 OE2
REMARK 470 LEU B 284 CG CD1 CD2
REMARK 470 LYS B 288 CG CD CE NZ
REMARK 470 GLU B 299 CG CD OE1 OE2
REMARK 470 LYS B 304 CG CD CE NZ
REMARK 470 GLU B 342 CG CD OE1 OE2
REMARK 470 ASP B 344 CG OD1 OD2
REMARK 470 ASN B 345 CG OD1 ND2
REMARK 470 GLU B 346 CG CD OE1 OE2
REMARK 470 LYS B 354 CG CD CE NZ
REMARK 470 ARG B 372 NE CZ NH1 NH2
REMARK 470 GLU B 398 CG CD OE1 OE2
REMARK 470 LYS B 405 CG CD CE NZ
REMARK 470 ASP B 440 CG OD1 OD2
REMARK 470 LYS B 455 CG CD CE NZ
REMARK 470 LYS B 484 CG CD CE NZ
REMARK 470 LYS B 486 CG CD CE NZ
REMARK 470 LEU B 488 CG CD1 CD2
REMARK 470 ASP B 490 CG OD1 OD2
REMARK 470 LYS B 492 CG CD CE NZ
REMARK 470 LYS B 494 CG CD CE NZ
REMARK 470 LYS B 523 CG CD CE NZ
REMARK 470 THR B 524 OG1 CG2
REMARK 470 ARG B 528 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 531 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 547 CG CD OE1 OE2
REMARK 470 ASP B 583 CG OD1 OD2
REMARK 470 GLU C 193 CG CD OE1 OE2
REMARK 470 LYS C 230 CG CD CE NZ
REMARK 470 GLU C 262 CG CD OE1 OE2
REMARK 470 GLU C 277 CG CD OE1 OE2
REMARK 470 LEU C 284 CG CD1 CD2
REMARK 470 LYS C 288 CG CD CE NZ
REMARK 470 LYS C 304 CG CD CE NZ
REMARK 470 ARG C 305 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 306 CG OD1 ND2
REMARK 470 ASP C 344 CG OD1 OD2
REMARK 470 ASN C 345 CG OD1 ND2
REMARK 470 GLU C 346 CG CD OE1 OE2
REMARK 470 ARG C 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 354 CG CD CE NZ
REMARK 470 GLU C 355 CG CD OE1 OE2
REMARK 470 TYR C 360 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG C 366 NE CZ NH1 NH2
REMARK 470 ARG C 372 NE CZ NH1 NH2
REMARK 470 LYS C 405 CG CD CE NZ
REMARK 470 GLN C 465 CG CD OE1 NE2
REMARK 470 LYS C 469 CG CD CE NZ
REMARK 470 LYS C 484 CG CD CE NZ
REMARK 470 LYS C 486 CG CD CE NZ
REMARK 470 VAL C 487 CG1 CG2
REMARK 470 LEU C 488 CG CD1 CD2
REMARK 470 LYS C 492 CG CD CE NZ
REMARK 470 LYS C 494 CG CD CE NZ
REMARK 470 GLU C 496 CG CD OE1 OE2
REMARK 470 HIS C 517 CG ND1 CD2 CE1 NE2
REMARK 470 LYS C 523 CG CD CE NZ
REMARK 470 GLU C 547 CG CD OE1 OE2
REMARK 470 LYS C 560 CG CD CE NZ
REMARK 470 LYS C 580 CG CD CE NZ
REMARK 470 GLN C 582 CG CD OE1 NE2
REMARK 470 ASP C 583 CG OD1 OD2
REMARK 470 GLU D 127 CG CD OE1 OE2
REMARK 470 LYS D 185 CG CD CE NZ
REMARK 470 GLU D 193 CG CD OE1 OE2
REMARK 470 LYS D 230 CG CD CE NZ
REMARK 470 GLU D 262 CG CD OE1 OE2
REMARK 470 GLU D 263 CG CD OE1 OE2
REMARK 470 LEU D 284 CG CD1 CD2
REMARK 470 LYS D 304 CG CD CE NZ
REMARK 470 ARG D 305 CG CD NE CZ NH1 NH2
REMARK 470 ASN D 306 CG OD1 ND2
REMARK 470 GLU D 342 CG CD OE1 OE2
REMARK 470 ASP D 344 CG OD1 OD2
REMARK 470 ASN D 345 CG OD1 ND2
REMARK 470 GLU D 346 CG CD OE1 OE2
REMARK 470 LYS D 354 CG CD CE NZ
REMARK 470 ARG D 366 NE CZ NH1 NH2
REMARK 470 ARG D 371 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 408 NE CZ NH1 NH2
REMARK 470 ASP D 440 CG OD1 OD2
REMARK 470 LYS D 455 CG CD CE NZ
REMARK 470 GLN D 465 CG CD OE1 NE2
REMARK 470 LYS D 484 CG CD CE NZ
REMARK 470 LYS D 486 CG CD CE NZ
REMARK 470 ASP D 490 CG OD1 OD2
REMARK 470 LYS D 492 CG CD CE NZ
REMARK 470 LYS D 494 CG CD CE NZ
REMARK 470 GLU D 496 CG CD OE1 OE2
REMARK 470 ASP D 516 CG OD1 OD2
REMARK 470 CYS D 522 SG
REMARK 470 LYS D 523 CG CD CE NZ
REMARK 470 GLU D 547 CG CD OE1 OE2
REMARK 470 LYS D 580 CG CD CE NZ
REMARK 470 ASP D 583 CG OD1 OD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 184 CD GLU A 184 OE2 0.087
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 ARG A 451 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 451 NE - CZ - NH1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 ARG A 451 NE - CZ - NH2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG B 451 NE - CZ - NH1 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ARG B 451 NE - CZ - NH2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG C 290 CD - NE - CZ ANGL. DEV. = 13.5 DEGREES
REMARK 500 ARG C 290 NE - CZ - NH1 ANGL. DEV. = -10.6 DEGREES
REMARK 500 ARG C 290 NE - CZ - NH2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 ARG C 451 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 451 NE - CZ - NH2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG D 290 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG D 451 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ARG D 451 NE - CZ - NH2 ANGL. DEV. = -6.5 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 SER A 214 -119.34 52.46
REMARK 500 ARG A 220 -47.30 -135.23
REMARK 500 LEU A 276 44.46 -95.67
REMARK 500 ARG A 305 -70.35 -62.94
REMARK 500 ASP A 344 61.31 62.86
REMARK 500 ALA A 373 -54.82 -130.33
REMARK 500 ARG A 451 31.64 72.01
REMARK 500 PRO A 462 47.42 -94.08
REMARK 500 ASP A 490 7.34 -69.22
REMARK 500 HIS A 517 58.05 -91.30
REMARK 500 ALA A 525 73.30 -109.13
REMARK 500 PRO A 526 -171.98 -67.46
REMARK 500 ASN A 527 4.05 58.54
REMARK 500 GLN B 142 -19.75 -49.88
REMARK 500 SER B 214 -119.26 55.43
REMARK 500 ARG B 220 -47.74 -134.26
REMARK 500 ALA B 373 -54.52 -130.40
REMARK 500 ARG B 451 31.93 74.00
REMARK 500 PRO B 462 47.90 -91.39
REMARK 500 ALA B 525 72.97 -108.53
REMARK 500 PRO B 526 -171.83 -67.03
REMARK 500 ASN B 527 4.54 58.56
REMARK 500 SER C 214 -119.30 53.73
REMARK 500 ARG C 220 -47.85 -134.53
REMARK 500 LEU C 276 53.22 -96.42
REMARK 500 ARG C 305 -72.67 -62.00
REMARK 500 ASP C 344 62.25 62.18
REMARK 500 ASN C 345 32.88 39.81
REMARK 500 ALA C 373 -54.95 -126.46
REMARK 500 ARG C 451 32.68 74.93
REMARK 500 SER D 214 -120.23 55.40
REMARK 500 ARG D 220 -48.33 -134.74
REMARK 500 ARG D 305 -71.08 -62.76
REMARK 500 ASP D 344 62.04 61.63
REMARK 500 ALA D 373 -57.24 -127.60
REMARK 500 THR D 423 -159.48 -135.57
REMARK 500 ARG D 451 32.18 74.64
REMARK 500 HIS D 517 57.27 -91.70
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 ZN C 627 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 C 3 O2
REMARK 620 2 HIS C 167 NE2 134.9
REMARK 620 3 HIS C 206 NE2 122.3 97.5
REMARK 620 4 ASP C 311 OD1 85.4 84.7 75.9
REMARK 620 5 ASP C 207 OD2 110.8 89.3 87.7 161.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 627 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 167 NE2
REMARK 620 2 PO4 A 1 O2 137.0
REMARK 620 3 HIS A 206 NE2 107.1 114.5
REMARK 620 4 ASP A 311 OD1 91.1 85.7 80.6
REMARK 620 5 ASP A 207 OD2 91.6 102.2 84.5 165.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PO4 D 4 O4
REMARK 620 2 HIS D 167 NE2 142.4
REMARK 620 3 HIS D 206 NE2 114.1 101.3
REMARK 620 4 ASP D 311 OD1 84.3 90.6 79.2
REMARK 620 5 ASP D 207 OD2 106.9 87.6 84.9 163.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 4 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 167 NE2
REMARK 620 2 HIS B 206 NE2 108.8
REMARK 620 3 PO4 B 2 O3 126.6 122.9
REMARK 620 4 ASP B 311 OD1 91.9 82.3 83.0
REMARK 620 5 ASP B 207 OD2 89.6 87.1 104.6 169.2
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 PO4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 4
DBREF 3U1N A 120 626 UNP Q9Y3Z3 SAMH1_HUMAN 120 626
DBREF 3U1N B 120 626 UNP Q9Y3Z3 SAMH1_HUMAN 120 626
DBREF 3U1N C 120 626 UNP Q9Y3Z3 SAMH1_HUMAN 120 626
DBREF 3U1N D 120 626 UNP Q9Y3Z3 SAMH1_HUMAN 120 626
SEQADV 3U1N ALA A 99 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER A 100 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N TRP A 101 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER A 102 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N HIS A 103 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO A 104 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN A 105 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE A 106 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU A 107 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LYS A 108 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY A 109 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA A 110 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU A 111 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU A 112 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N VAL A 113 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU A 114 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE A 115 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN A 116 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY A 117 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO A 118 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY A 119 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA B 99 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER B 100 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N TRP B 101 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER B 102 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N HIS B 103 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO B 104 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN B 105 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE B 106 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU B 107 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LYS B 108 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY B 109 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA B 110 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU B 111 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU B 112 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N VAL B 113 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU B 114 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE B 115 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN B 116 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY B 117 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO B 118 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY B 119 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA C 99 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER C 100 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N TRP C 101 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER C 102 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N HIS C 103 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO C 104 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN C 105 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE C 106 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU C 107 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LYS C 108 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY C 109 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA C 110 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU C 111 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU C 112 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N VAL C 113 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU C 114 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE C 115 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN C 116 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY C 117 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO C 118 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY C 119 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA D 99 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER D 100 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N TRP D 101 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N SER D 102 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N HIS D 103 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO D 104 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN D 105 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE D 106 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU D 107 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LYS D 108 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY D 109 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N ALA D 110 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU D 111 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLU D 112 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N VAL D 113 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N LEU D 114 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PHE D 115 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLN D 116 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY D 117 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N PRO D 118 UNP Q9Y3Z3 EXPRESSION TAG
SEQADV 3U1N GLY D 119 UNP Q9Y3Z3 EXPRESSION TAG
SEQRES 1 A 528 ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA LEU
SEQRES 2 A 528 GLU VAL LEU PHE GLN GLY PRO GLY ASP PRO ILE HIS GLY
SEQRES 3 A 528 HIS ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP
SEQRES 4 A 528 THR PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU
SEQRES 5 A 528 GLY GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN
SEQRES 6 A 528 ARG PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY
SEQRES 7 A 528 CYS LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU
SEQRES 8 A 528 GLN ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA
SEQRES 9 A 528 GLY LEU CYS HIS ASP LEU GLY HIS GLY PRO PHE SER HIS
SEQRES 10 A 528 MSE PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU
SEQRES 11 A 528 VAL LYS TRP THR HIS GLU GLN GLY SER VAL MSE MSE PHE
SEQRES 12 A 528 GLU HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MSE
SEQRES 13 A 528 GLU GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE
SEQRES 14 A 528 ILE LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL
SEQRES 15 A 528 GLU ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN
SEQRES 16 A 528 LYS SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN
SEQRES 17 A 528 GLY ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP
SEQRES 18 A 528 CYS HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS
SEQRES 19 A 528 ARG PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN
SEQRES 20 A 528 GLU LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN
SEQRES 21 A 528 LEU TYR ASP MSE PHE HIS THR ARG ASN SER LEU HIS ARG
SEQRES 22 A 528 ARG ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR
SEQRES 23 A 528 MSE ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE
SEQRES 24 A 528 GLU ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER
SEQRES 25 A 528 THR ALA ILE ASP ASP MSE GLU ALA TYR THR LYS LEU THR
SEQRES 26 A 528 ASP ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO
SEQRES 27 A 528 LYS LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU
SEQRES 28 A 528 TYR ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO
SEQRES 29 A 528 THR GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER
SEQRES 30 A 528 LEU PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU
SEQRES 31 A 528 LEU ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP
SEQRES 32 A 528 VAL ILE ASN MSE ASP TYR GLY MSE GLN GLU LYS ASN PRO
SEQRES 33 A 528 ILE ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN
SEQRES 34 A 528 ARG ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU
SEQRES 35 A 528 LEU PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR
SEQRES 36 A 528 CYS LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG
SEQRES 37 A 528 GLN TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR
SEQRES 38 A 528 LYS PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR
SEQRES 39 A 528 PRO GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN
SEQRES 40 A 528 ASN PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL
SEQRES 41 A 528 GLN LEU PHE LYS ASP ASP PRO MSE
SEQRES 1 B 528 ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA LEU
SEQRES 2 B 528 GLU VAL LEU PHE GLN GLY PRO GLY ASP PRO ILE HIS GLY
SEQRES 3 B 528 HIS ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP
SEQRES 4 B 528 THR PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU
SEQRES 5 B 528 GLY GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN
SEQRES 6 B 528 ARG PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY
SEQRES 7 B 528 CYS LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU
SEQRES 8 B 528 GLN ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA
SEQRES 9 B 528 GLY LEU CYS HIS ASP LEU GLY HIS GLY PRO PHE SER HIS
SEQRES 10 B 528 MSE PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU
SEQRES 11 B 528 VAL LYS TRP THR HIS GLU GLN GLY SER VAL MSE MSE PHE
SEQRES 12 B 528 GLU HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MSE
SEQRES 13 B 528 GLU GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE
SEQRES 14 B 528 ILE LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL
SEQRES 15 B 528 GLU ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN
SEQRES 16 B 528 LYS SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN
SEQRES 17 B 528 GLY ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP
SEQRES 18 B 528 CYS HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS
SEQRES 19 B 528 ARG PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN
SEQRES 20 B 528 GLU LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN
SEQRES 21 B 528 LEU TYR ASP MSE PHE HIS THR ARG ASN SER LEU HIS ARG
SEQRES 22 B 528 ARG ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR
SEQRES 23 B 528 MSE ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE
SEQRES 24 B 528 GLU ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER
SEQRES 25 B 528 THR ALA ILE ASP ASP MSE GLU ALA TYR THR LYS LEU THR
SEQRES 26 B 528 ASP ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO
SEQRES 27 B 528 LYS LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU
SEQRES 28 B 528 TYR ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO
SEQRES 29 B 528 THR GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER
SEQRES 30 B 528 LEU PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU
SEQRES 31 B 528 LEU ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP
SEQRES 32 B 528 VAL ILE ASN MSE ASP TYR GLY MSE GLN GLU LYS ASN PRO
SEQRES 33 B 528 ILE ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN
SEQRES 34 B 528 ARG ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU
SEQRES 35 B 528 LEU PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR
SEQRES 36 B 528 CYS LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG
SEQRES 37 B 528 GLN TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR
SEQRES 38 B 528 LYS PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR
SEQRES 39 B 528 PRO GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN
SEQRES 40 B 528 ASN PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL
SEQRES 41 B 528 GLN LEU PHE LYS ASP ASP PRO MSE
SEQRES 1 C 528 ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA LEU
SEQRES 2 C 528 GLU VAL LEU PHE GLN GLY PRO GLY ASP PRO ILE HIS GLY
SEQRES 3 C 528 HIS ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP
SEQRES 4 C 528 THR PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU
SEQRES 5 C 528 GLY GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN
SEQRES 6 C 528 ARG PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY
SEQRES 7 C 528 CYS LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU
SEQRES 8 C 528 GLN ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA
SEQRES 9 C 528 GLY LEU CYS HIS ASP LEU GLY HIS GLY PRO PHE SER HIS
SEQRES 10 C 528 MSE PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU
SEQRES 11 C 528 VAL LYS TRP THR HIS GLU GLN GLY SER VAL MSE MSE PHE
SEQRES 12 C 528 GLU HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MSE
SEQRES 13 C 528 GLU GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE
SEQRES 14 C 528 ILE LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL
SEQRES 15 C 528 GLU ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN
SEQRES 16 C 528 LYS SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN
SEQRES 17 C 528 GLY ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP
SEQRES 18 C 528 CYS HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS
SEQRES 19 C 528 ARG PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN
SEQRES 20 C 528 GLU LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN
SEQRES 21 C 528 LEU TYR ASP MSE PHE HIS THR ARG ASN SER LEU HIS ARG
SEQRES 22 C 528 ARG ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR
SEQRES 23 C 528 MSE ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE
SEQRES 24 C 528 GLU ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER
SEQRES 25 C 528 THR ALA ILE ASP ASP MSE GLU ALA TYR THR LYS LEU THR
SEQRES 26 C 528 ASP ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO
SEQRES 27 C 528 LYS LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU
SEQRES 28 C 528 TYR ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO
SEQRES 29 C 528 THR GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER
SEQRES 30 C 528 LEU PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU
SEQRES 31 C 528 LEU ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP
SEQRES 32 C 528 VAL ILE ASN MSE ASP TYR GLY MSE GLN GLU LYS ASN PRO
SEQRES 33 C 528 ILE ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN
SEQRES 34 C 528 ARG ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU
SEQRES 35 C 528 LEU PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR
SEQRES 36 C 528 CYS LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG
SEQRES 37 C 528 GLN TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR
SEQRES 38 C 528 LYS PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR
SEQRES 39 C 528 PRO GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN
SEQRES 40 C 528 ASN PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL
SEQRES 41 C 528 GLN LEU PHE LYS ASP ASP PRO MSE
SEQRES 1 D 528 ALA SER TRP SER HIS PRO GLN PHE GLU LYS GLY ALA LEU
SEQRES 2 D 528 GLU VAL LEU PHE GLN GLY PRO GLY ASP PRO ILE HIS GLY
SEQRES 3 D 528 HIS ILE GLU LEU HIS PRO LEU LEU VAL ARG ILE ILE ASP
SEQRES 4 D 528 THR PRO GLN PHE GLN ARG LEU ARG TYR ILE LYS GLN LEU
SEQRES 5 D 528 GLY GLY GLY TYR TYR VAL PHE PRO GLY ALA SER HIS ASN
SEQRES 6 D 528 ARG PHE GLU HIS SER LEU GLY VAL GLY TYR LEU ALA GLY
SEQRES 7 D 528 CYS LEU VAL HIS ALA LEU GLY GLU LYS GLN PRO GLU LEU
SEQRES 8 D 528 GLN ILE SER GLU ARG ASP VAL LEU CYS VAL GLN ILE ALA
SEQRES 9 D 528 GLY LEU CYS HIS ASP LEU GLY HIS GLY PRO PHE SER HIS
SEQRES 10 D 528 MSE PHE ASP GLY ARG PHE ILE PRO LEU ALA ARG PRO GLU
SEQRES 11 D 528 VAL LYS TRP THR HIS GLU GLN GLY SER VAL MSE MSE PHE
SEQRES 12 D 528 GLU HIS LEU ILE ASN SER ASN GLY ILE LYS PRO VAL MSE
SEQRES 13 D 528 GLU GLN TYR GLY LEU ILE PRO GLU GLU ASP ILE CYS PHE
SEQRES 14 D 528 ILE LYS GLU GLN ILE VAL GLY PRO LEU GLU SER PRO VAL
SEQRES 15 D 528 GLU ASP SER LEU TRP PRO TYR LYS GLY ARG PRO GLU ASN
SEQRES 16 D 528 LYS SER PHE LEU TYR GLU ILE VAL SER ASN LYS ARG ASN
SEQRES 17 D 528 GLY ILE ASP VAL ASP LYS TRP ASP TYR PHE ALA ARG ASP
SEQRES 18 D 528 CYS HIS HIS LEU GLY ILE GLN ASN ASN PHE ASP TYR LYS
SEQRES 19 D 528 ARG PHE ILE LYS PHE ALA ARG VAL CYS GLU VAL ASP ASN
SEQRES 20 D 528 GLU LEU ARG ILE CYS ALA ARG ASP LYS GLU VAL GLY ASN
SEQRES 21 D 528 LEU TYR ASP MSE PHE HIS THR ARG ASN SER LEU HIS ARG
SEQRES 22 D 528 ARG ALA TYR GLN HIS LYS VAL GLY ASN ILE ILE ASP THR
SEQRES 23 D 528 MSE ILE THR ASP ALA PHE LEU LYS ALA ASP ASP TYR ILE
SEQRES 24 D 528 GLU ILE THR GLY ALA GLY GLY LYS LYS TYR ARG ILE SER
SEQRES 25 D 528 THR ALA ILE ASP ASP MSE GLU ALA TYR THR LYS LEU THR
SEQRES 26 D 528 ASP ASN ILE PHE LEU GLU ILE LEU TYR SER THR ASP PRO
SEQRES 27 D 528 LYS LEU LYS ASP ALA ARG GLU ILE LEU LYS GLN ILE GLU
SEQRES 28 D 528 TYR ARG ASN LEU PHE LYS TYR VAL GLY GLU THR GLN PRO
SEQRES 29 D 528 THR GLY GLN ILE LYS ILE LYS ARG GLU ASP TYR GLU SER
SEQRES 30 D 528 LEU PRO LYS GLU VAL ALA SER ALA LYS PRO LYS VAL LEU
SEQRES 31 D 528 LEU ASP VAL LYS LEU LYS ALA GLU ASP PHE ILE VAL ASP
SEQRES 32 D 528 VAL ILE ASN MSE ASP TYR GLY MSE GLN GLU LYS ASN PRO
SEQRES 33 D 528 ILE ASP HIS VAL SER PHE TYR CYS LYS THR ALA PRO ASN
SEQRES 34 D 528 ARG ALA ILE ARG ILE THR LYS ASN GLN VAL SER GLN LEU
SEQRES 35 D 528 LEU PRO GLU LYS PHE ALA GLU GLN LEU ILE ARG VAL TYR
SEQRES 36 D 528 CYS LYS LYS VAL ASP ARG LYS SER LEU TYR ALA ALA ARG
SEQRES 37 D 528 GLN TYR PHE VAL GLN TRP CYS ALA ASP ARG ASN PHE THR
SEQRES 38 D 528 LYS PRO GLN ASP GLY ASP VAL ILE ALA PRO LEU ILE THR
SEQRES 39 D 528 PRO GLN LYS LYS GLU TRP ASN ASP SER THR SER VAL GLN
SEQRES 40 D 528 ASN PRO THR ARG LEU ARG GLU ALA SER LYS SER ARG VAL
SEQRES 41 D 528 GLN LEU PHE LYS ASP ASP PRO MSE
MODRES 3U1N MSE A 216 MET SELENOMETHIONINE
MODRES 3U1N MSE A 239 MET SELENOMETHIONINE
MODRES 3U1N MSE A 240 MET SELENOMETHIONINE
MODRES 3U1N MSE A 254 MET SELENOMETHIONINE
MODRES 3U1N MSE A 362 MET SELENOMETHIONINE
MODRES 3U1N MSE A 385 MET SELENOMETHIONINE
MODRES 3U1N MSE A 416 MET SELENOMETHIONINE
MODRES 3U1N MSE A 505 MET SELENOMETHIONINE
MODRES 3U1N MSE B 216 MET SELENOMETHIONINE
MODRES 3U1N MSE B 239 MET SELENOMETHIONINE
MODRES 3U1N MSE B 240 MET SELENOMETHIONINE
MODRES 3U1N MSE B 254 MET SELENOMETHIONINE
MODRES 3U1N MSE B 362 MET SELENOMETHIONINE
MODRES 3U1N MSE B 385 MET SELENOMETHIONINE
MODRES 3U1N MSE B 416 MET SELENOMETHIONINE
MODRES 3U1N MSE B 505 MET SELENOMETHIONINE
MODRES 3U1N MSE C 216 MET SELENOMETHIONINE
MODRES 3U1N MSE C 239 MET SELENOMETHIONINE
MODRES 3U1N MSE C 240 MET SELENOMETHIONINE
MODRES 3U1N MSE C 254 MET SELENOMETHIONINE
MODRES 3U1N MSE C 362 MET SELENOMETHIONINE
MODRES 3U1N MSE C 385 MET SELENOMETHIONINE
MODRES 3U1N MSE C 416 MET SELENOMETHIONINE
MODRES 3U1N MSE C 505 MET SELENOMETHIONINE
MODRES 3U1N MSE D 216 MET SELENOMETHIONINE
MODRES 3U1N MSE D 239 MET SELENOMETHIONINE
MODRES 3U1N MSE D 240 MET SELENOMETHIONINE
MODRES 3U1N MSE D 254 MET SELENOMETHIONINE
MODRES 3U1N MSE D 362 MET SELENOMETHIONINE
MODRES 3U1N MSE D 385 MET SELENOMETHIONINE
MODRES 3U1N MSE D 416 MET SELENOMETHIONINE
MODRES 3U1N MSE D 505 MET SELENOMETHIONINE
HET MSE A 216 8
HET MSE A 239 8
HET MSE A 240 8
HET MSE A 254 8
HET MSE A 362 8
HET MSE A 385 8
HET MSE A 416 8
HET MSE A 505 8
HET MSE B 216 8
HET MSE B 239 8
HET MSE B 240 8
HET MSE B 254 8
HET MSE B 362 8
HET MSE B 385 8
HET MSE B 416 8
HET MSE B 505 8
HET MSE C 216 8
HET MSE C 239 8
HET MSE C 240 8
HET MSE C 254 8
HET MSE C 362 8
HET MSE C 385 8
HET MSE C 416 8
HET MSE C 505 8
HET MSE D 216 8
HET MSE D 239 8
HET MSE D 240 8
HET MSE D 254 8
HET MSE D 362 8
HET MSE D 385 8
HET MSE D 416 8
HET MSE D 505 8
HET PO4 A 1 5
HET ZN A 627 1
HET PO4 B 2 5
HET ZN B 4 1
HET PO4 C 3 5
HET ZN C 627 1
HET PO4 D 4 5
HET ZN D 2 1
HETNAM MSE SELENOMETHIONINE
HETNAM PO4 PHOSPHATE ION
HETNAM ZN ZINC ION
FORMUL 1 MSE 32(C5 H11 N O2 SE)
FORMUL 5 PO4 4(O4 P 3-)
FORMUL 6 ZN 4(ZN 2+)
FORMUL 13 HOH *28(H2 O)
HELIX 1 1 HIS A 129 ASP A 137 1 9
HELIX 2 2 THR A 138 ARG A 143 1 6
HELIX 3 3 LEU A 144 ILE A 147 5 4
HELIX 4 4 LEU A 150 TYR A 154 5 5
HELIX 5 5 ASN A 163 GLN A 186 1 24
HELIX 6 6 PRO A 187 GLN A 190 5 4
HELIX 7 7 SER A 192 HIS A 206 1 15
HELIX 8 8 SER A 214 ARG A 220 1 7
HELIX 9 9 ARG A 220 ARG A 226 1 7
HELIX 10 10 THR A 232 ASN A 248 1 17
HELIX 11 11 ILE A 250 TYR A 257 1 8
HELIX 12 12 ILE A 260 GLY A 274 1 15
HELIX 13 13 PRO A 291 ILE A 300 5 10
HELIX 14 14 ASP A 309 GLY A 324 1 16
HELIX 15 15 ASP A 330 PHE A 337 1 8
HELIX 16 16 GLU A 355 ALA A 373 1 19
HELIX 17 17 HIS A 376 LYS A 392 1 17
HELIX 18 18 ALA A 402 GLY A 404 5 3
HELIX 19 19 ARG A 408 ASP A 414 5 7
HELIX 20 20 ASP A 415 THR A 420 1 6
HELIX 21 21 LYS A 421 THR A 423 5 3
HELIX 22 22 ASP A 424 SER A 433 1 10
HELIX 23 23 LEU A 438 ARG A 451 1 14
HELIX 24 24 LYS A 469 GLU A 474 5 6
HELIX 25 25 SER A 475 SER A 482 1 8
HELIX 26 26 LYS A 494 GLU A 496 5 3
HELIX 27 27 ASP A 558 ASP A 575 1 18
HELIX 28 28 HIS B 129 ASP B 137 1 9
HELIX 29 29 THR B 138 ARG B 143 1 6
HELIX 30 30 LEU B 144 ILE B 147 5 4
HELIX 31 31 LEU B 150 TYR B 154 5 5
HELIX 32 32 ASN B 163 GLN B 186 1 24
HELIX 33 33 PRO B 187 GLN B 190 5 4
HELIX 34 34 SER B 192 HIS B 206 1 15
HELIX 35 35 SER B 214 ARG B 220 1 7
HELIX 36 36 ARG B 220 ARG B 226 1 7
HELIX 37 37 THR B 232 ASN B 248 1 17
HELIX 38 38 ILE B 250 TYR B 257 1 8
HELIX 39 39 ILE B 260 GLY B 274 1 15
HELIX 40 40 PRO B 291 ILE B 300 5 10
HELIX 41 41 ASP B 309 GLY B 324 1 16
HELIX 42 42 ASP B 330 PHE B 337 1 8
HELIX 43 43 GLU B 355 ALA B 373 1 19
HELIX 44 44 HIS B 376 LYS B 392 1 17
HELIX 45 45 ALA B 402 GLY B 404 5 3
HELIX 46 46 ARG B 408 ASP B 414 5 7
HELIX 47 47 ASP B 415 THR B 420 1 6
HELIX 48 48 LYS B 421 THR B 423 5 3
HELIX 49 49 ASP B 424 SER B 433 1 10
HELIX 50 50 LEU B 438 ARG B 451 1 14
HELIX 51 51 LYS B 469 GLU B 474 5 6
HELIX 52 52 SER B 475 SER B 482 1 8
HELIX 53 53 LYS B 494 GLU B 496 5 3
HELIX 54 54 ASP B 558 ASP B 575 1 18
HELIX 55 55 HIS C 129 ASP C 137 1 9
HELIX 56 56 THR C 138 ARG C 143 1 6
HELIX 57 57 LEU C 144 ILE C 147 5 4
HELIX 58 58 LEU C 150 TYR C 154 5 5
HELIX 59 59 ASN C 163 GLN C 186 1 24
HELIX 60 60 PRO C 187 GLN C 190 5 4
HELIX 61 61 SER C 192 HIS C 206 1 15
HELIX 62 62 SER C 214 ARG C 220 1 7
HELIX 63 63 ARG C 220 ARG C 226 1 7
HELIX 64 64 THR C 232 ASN C 248 1 17
HELIX 65 65 ILE C 250 TYR C 257 1 8
HELIX 66 66 ILE C 260 GLY C 274 1 15
HELIX 67 67 PRO C 291 ILE C 300 5 10
HELIX 68 68 ASP C 309 GLY C 324 1 16
HELIX 69 69 ASP C 330 PHE C 337 1 8
HELIX 70 70 GLU C 355 ALA C 373 1 19
HELIX 71 71 HIS C 376 LYS C 392 1 17
HELIX 72 72 ALA C 402 GLY C 404 5 3
HELIX 73 73 ARG C 408 ASP C 414 5 7
HELIX 74 74 ASP C 415 THR C 420 1 6
HELIX 75 75 LYS C 421 THR C 423 5 3
HELIX 76 76 ASP C 424 SER C 433 1 10
HELIX 77 77 LEU C 438 ARG C 451 1 14
HELIX 78 78 LYS C 469 GLU C 474 5 6
HELIX 79 79 SER C 475 SER C 482 1 8
HELIX 80 80 LYS C 494 GLU C 496 5 3
HELIX 81 81 ASP C 558 ASP C 575 1 18
HELIX 82 82 HIS D 129 ASP D 137 1 9
HELIX 83 83 THR D 138 ARG D 143 1 6
HELIX 84 84 LEU D 144 ILE D 147 5 4
HELIX 85 85 LEU D 150 VAL D 156 5 7
HELIX 86 86 ASN D 163 GLN D 186 1 24
HELIX 87 87 PRO D 187 GLN D 190 5 4
HELIX 88 88 SER D 192 HIS D 206 1 15
HELIX 89 89 SER D 214 ARG D 220 1 7
HELIX 90 90 ARG D 220 ARG D 226 1 7
HELIX 91 91 THR D 232 ASN D 248 1 17
HELIX 92 92 ILE D 250 TYR D 257 1 8
HELIX 93 93 ILE D 260 GLY D 274 1 15
HELIX 94 94 PRO D 291 ILE D 300 5 10
HELIX 95 95 ASP D 309 GLY D 324 1 16
HELIX 96 96 ASP D 330 PHE D 337 1 8
HELIX 97 97 GLU D 355 ALA D 373 1 19
HELIX 98 98 HIS D 376 LYS D 392 1 17
HELIX 99 99 ALA D 402 GLY D 404 5 3
HELIX 100 100 ARG D 408 ASP D 414 5 7
HELIX 101 101 ASP D 415 THR D 420 1 6
HELIX 102 102 LYS D 421 THR D 423 5 3
HELIX 103 103 ASP D 424 SER D 433 1 10
HELIX 104 104 LEU D 438 ARG D 451 1 14
HELIX 105 105 LYS D 469 GLU D 474 5 6
HELIX 106 106 SER D 475 SER D 482 1 8
HELIX 107 107 LYS D 494 GLU D 496 5 3
HELIX 108 108 ASP D 558 ASP D 575 1 18
SHEET 1 A 3 ALA A 338 GLU A 342 0
SHEET 2 A 3 LEU A 347 ARG A 352 -1 O CYS A 350 N ARG A 339
SHEET 3 A 3 PHE A 520 TYR A 521 1 O TYR A 521 N ALA A 351
SHEET 1 B 2 ILE A 399 THR A 400 0
SHEET 2 B 2 LYS A 406 TYR A 407 -1 O TYR A 407 N ILE A 399
SHEET 1 C 3 LYS A 455 THR A 460 0
SHEET 2 C 3 GLN A 548 CYS A 554 -1 O ILE A 550 N THR A 460
SHEET 3 C 3 PHE A 498 ASN A 504 -1 N ILE A 499 O TYR A 553
SHEET 1 D 3 ALA B 338 GLU B 342 0
SHEET 2 D 3 LEU B 347 ARG B 352 -1 O CYS B 350 N ARG B 339
SHEET 3 D 3 PHE B 520 TYR B 521 1 O TYR B 521 N ALA B 351
SHEET 1 E 2 ILE B 399 THR B 400 0
SHEET 2 E 2 LYS B 406 TYR B 407 -1 O TYR B 407 N ILE B 399
SHEET 1 F 3 LYS B 455 THR B 460 0
SHEET 2 F 3 GLN B 548 CYS B 554 -1 O ILE B 550 N THR B 460
SHEET 3 F 3 PHE B 498 ASN B 504 -1 N ILE B 499 O TYR B 553
SHEET 1 G 3 ALA C 338 GLU C 342 0
SHEET 2 G 3 LEU C 347 ARG C 352 -1 O CYS C 350 N ARG C 339
SHEET 3 G 3 PHE C 520 TYR C 521 1 O TYR C 521 N ALA C 351
SHEET 1 H 2 ILE C 399 THR C 400 0
SHEET 2 H 2 LYS C 406 TYR C 407 -1 O TYR C 407 N ILE C 399
SHEET 1 I 3 LYS C 455 THR C 460 0
SHEET 2 I 3 GLN C 548 CYS C 554 -1 O ILE C 550 N THR C 460
SHEET 3 I 3 PHE C 498 ASN C 504 -1 N ILE C 499 O TYR C 553
SHEET 1 J 3 ALA D 338 GLU D 342 0
SHEET 2 J 3 LEU D 347 ARG D 352 -1 O CYS D 350 N ARG D 339
SHEET 3 J 3 PHE D 520 TYR D 521 1 O TYR D 521 N ALA D 351
SHEET 1 K 2 ILE D 399 THR D 400 0
SHEET 2 K 2 LYS D 406 TYR D 407 -1 O TYR D 407 N ILE D 399
SHEET 1 L 3 LYS D 455 THR D 460 0
SHEET 2 L 3 GLN D 548 CYS D 554 -1 O ILE D 550 N THR D 460
SHEET 3 L 3 PHE D 498 ASN D 504 -1 N ILE D 499 O TYR D 553
SSBOND 1 CYS A 341 CYS A 350 1555 1555 2.08
SSBOND 2 CYS B 341 CYS B 350 1555 1555 2.07
SSBOND 3 CYS C 341 CYS C 350 1555 1555 2.06
SSBOND 4 CYS D 341 CYS D 350 1555 1555 2.05
LINK C HIS A 215 N MSE A 216 1555 1555 1.31
LINK C MSE A 216 N PHE A 217 1555 1555 1.33
LINK C VAL A 238 N MSE A 239 1555 1555 1.33
LINK C MSE A 239 N MSE A 240 1555 1555 1.32
LINK C MSE A 240 N PHE A 241 1555 1555 1.33
LINK C VAL A 253 N MSE A 254 1555 1555 1.32
LINK C MSE A 254 N GLU A 255 1555 1555 1.33
LINK C ASP A 361 N MSE A 362 1555 1555 1.33
LINK C MSE A 362 N PHE A 363 1555 1555 1.32
LINK C THR A 384 N MSE A 385 1555 1555 1.33
LINK C MSE A 385 N ILE A 386 1555 1555 1.33
LINK C ASP A 415 N MSE A 416 1555 1555 1.33
LINK C MSE A 416 N GLU A 417 1555 1555 1.32
LINK C ASN A 504 N MSE A 505 1555 1555 1.34
LINK C HIS B 215 N MSE B 216 1555 1555 1.31
LINK C MSE B 216 N PHE B 217 1555 1555 1.33
LINK C VAL B 238 N MSE B 239 1555 1555 1.32
LINK C MSE B 239 N MSE B 240 1555 1555 1.32
LINK C MSE B 240 N PHE B 241 1555 1555 1.32
LINK C VAL B 253 N MSE B 254 1555 1555 1.32
LINK C MSE B 254 N GLU B 255 1555 1555 1.33
LINK C ASP B 361 N MSE B 362 1555 1555 1.32
LINK C MSE B 362 N PHE B 363 1555 1555 1.32
LINK C THR B 384 N MSE B 385 1555 1555 1.33
LINK C MSE B 385 N ILE B 386 1555 1555 1.33
LINK C ASP B 415 N MSE B 416 1555 1555 1.33
LINK C MSE B 416 N GLU B 417 1555 1555 1.32
LINK C ASN B 504 N MSE B 505 1555 1555 1.34
LINK C HIS C 215 N MSE C 216 1555 1555 1.32
LINK C MSE C 216 N PHE C 217 1555 1555 1.32
LINK C VAL C 238 N MSE C 239 1555 1555 1.32
LINK C MSE C 239 N MSE C 240 1555 1555 1.32
LINK C MSE C 240 N PHE C 241 1555 1555 1.33
LINK C VAL C 253 N MSE C 254 1555 1555 1.32
LINK C MSE C 254 N GLU C 255 1555 1555 1.33
LINK C ASP C 361 N MSE C 362 1555 1555 1.33
LINK C MSE C 362 N PHE C 363 1555 1555 1.33
LINK C THR C 384 N MSE C 385 1555 1555 1.33
LINK C MSE C 385 N ILE C 386 1555 1555 1.33
LINK C ASP C 415 N MSE C 416 1555 1555 1.32
LINK C MSE C 416 N GLU C 417 1555 1555 1.33
LINK C ASN C 504 N MSE C 505 1555 1555 1.33
LINK C HIS D 215 N MSE D 216 1555 1555 1.32
LINK C MSE D 216 N PHE D 217 1555 1555 1.32
LINK C VAL D 238 N MSE D 239 1555 1555 1.32
LINK C MSE D 239 N MSE D 240 1555 1555 1.32
LINK C MSE D 240 N PHE D 241 1555 1555 1.33
LINK C VAL D 253 N MSE D 254 1555 1555 1.33
LINK C MSE D 254 N GLU D 255 1555 1555 1.33
LINK C ASP D 361 N MSE D 362 1555 1555 1.33
LINK C MSE D 362 N PHE D 363 1555 1555 1.33
LINK C THR D 384 N MSE D 385 1555 1555 1.33
LINK C MSE D 385 N ILE D 386 1555 1555 1.32
LINK C ASP D 415 N MSE D 416 1555 1555 1.32
LINK C MSE D 416 N GLU D 417 1555 1555 1.33
LINK C ASN D 504 N MSE D 505 1555 1555 1.33
LINK O2 PO4 C 3 ZN ZN C 627 1555 1555 2.09
LINK NE2 HIS A 167 ZN ZN A 627 1555 1555 2.14
LINK O4 PO4 D 4 ZN ZN D 2 1555 1555 2.16
LINK NE2 HIS B 167 ZN ZN B 4 1555 1555 2.17
LINK NE2 HIS B 206 ZN ZN B 4 1555 1555 2.18
LINK NE2 HIS D 167 ZN ZN D 2 1555 1555 2.20
LINK O2 PO4 A 1 ZN ZN A 627 1555 1555 2.20
LINK NE2 HIS A 206 ZN ZN A 627 1555 1555 2.25
LINK NE2 HIS D 206 ZN ZN D 2 1555 1555 2.27
LINK NE2 HIS C 167 ZN ZN C 627 1555 1555 2.30
LINK O3 PO4 B 2 ZN ZN B 4 1555 1555 2.31
LINK OD1 ASP B 311 ZN ZN B 4 1555 1555 2.31
LINK NE2 HIS C 206 ZN ZN C 627 1555 1555 2.32
LINK OD1 ASP D 311 ZN ZN D 2 1555 1555 2.36
LINK OD1 ASP A 311 ZN ZN A 627 1555 1555 2.36
LINK OD1 ASP C 311 ZN ZN C 627 1555 1555 2.47
LINK OD2 ASP A 207 ZN ZN A 627 1555 1555 2.72
LINK OD2 ASP B 207 ZN ZN B 4 1555 1555 2.75
LINK OD2 ASP C 207 ZN ZN C 627 1555 1555 2.65
LINK OD2 ASP D 207 ZN ZN D 2 1555 1555 2.78
SITE 1 AC1 8 HOH A 18 ARG A 164 ASP A 207 HIS A 210
SITE 2 AC1 8 HIS A 215 HIS A 233 ASP A 311 ZN A 627
SITE 1 AC2 8 ZN B 4 HOH B 25 ARG B 164 ASP B 207
SITE 2 AC2 8 HIS B 210 HIS B 215 HIS B 233 ASP B 311
SITE 1 AC3 8 HOH C 7 ARG C 164 ASP C 207 HIS C 210
SITE 2 AC3 8 HIS C 215 HIS C 233 ASP C 311 ZN C 627
SITE 1 AC4 7 ZN D 2 HOH D 11 ARG D 164 ASP D 207
SITE 2 AC4 7 HIS D 210 HIS D 215 ASP D 311
SITE 1 AC5 5 PO4 A 1 HIS A 167 HIS A 206 ASP A 207
SITE 2 AC5 5 ASP A 311
SITE 1 AC6 5 PO4 D 4 HIS D 167 HIS D 206 ASP D 207
SITE 2 AC6 5 ASP D 311
SITE 1 AC7 5 PO4 C 3 HIS C 167 HIS C 206 ASP C 207
SITE 2 AC7 5 ASP C 311
SITE 1 AC8 5 PO4 B 2 HIS B 167 HIS B 206 ASP B 207
SITE 2 AC8 5 ASP B 311
CRYST1 81.516 95.818 96.661 91.18 109.24 115.20 P 1 4
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 0.012268 0.005773 0.005467 0.00000
SCALE2 0.000000 0.011534 0.002213 0.00000
SCALE3 0.000000 0.000000 0.011157 0.00000
MTRIX1 1 0.999999 0.000651 -0.001344 0.05058 1
MTRIX2 1 0.000645 -0.999988 -0.004929 45.09030 1
MTRIX3 1 -0.001347 0.004928 -0.999987 57.12400 1
MTRIX1 2 -0.982077 -0.072405 -0.174019 -6.16191 1
MTRIX2 2 0.090620 0.628172 -0.772780 19.24390 1
MTRIX3 2 0.165267 -0.774699 -0.610351 70.28590 1
MTRIX1 3 -0.981869 0.073510 0.174729 -19.40400 1
MTRIX2 3 0.091406 -0.623911 0.776131 3.00954 1
MTRIX3 3 0.166069 0.778030 0.605880 0.56273 1
(ATOM LINES ARE NOT SHOWN.)
END
