HEADER TRANSCRIPTION 04-MAY-22 7ZRA TITLE CRYSTAL STRUCTURE OF E.COLI LEXA IN COMPLEX WITH NANOBODY TITLE 2 NBSOS1(NB14497) COMPND MOL_ID: 1; COMPND 2 MOLECULE: LEXA REPRESSOR; COMPND 3 CHAIN: A, C, B, D; COMPND 4 EC: 3.4.21.88; COMPND 5 ENGINEERED: YES; COMPND 6 OTHER_DETAILS: N-TERMINUS IS NOT VISIBLE IN THE ELECTRON DENSITY COMPND 7 MAPS.; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: NANOBODY NBSOS1 (NB14497); COMPND 10 CHAIN: E, G, F, H; COMPND 11 ENGINEERED: YES; COMPND 12 OTHER_DETAILS: C-TERMINUS TAG IS NOT VISIBLE IN THE ELECTRON DENSITY COMPND 13 MAPS SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: STR. 'CLONE D I14'; SOURCE 5 GENE: LEXA_1, LEXA, LEXA_2, LEXA_3, LEXA_4, LEXA_5, LEXA_6, SOURCE 6 A6581_03840, A6592_09000, A6V01_14725, A8C65_05740, A9819_23115, SOURCE 7 A9P13_24790, A9R57_24265, A9X72_23540, AAW05_04940, AC067_05020, SOURCE 8 AC789_1C44530, ACN002_4144, ACN68_15885, ACN81_05765, ACU57_23725, SOURCE 9 ACU90_04800, AJ318_13980, AM270_18420, AM446_25905, AM464_13585, SOURCE 10 AM465_02855, AMK83_25365, AML07_00445, AML35_16500, APT94_01725, SOURCE 11 APU18_20100, APZ14_12275, ARC77_17360, AU473_00505, AUQ13_09675, SOURCE 12 AUS26_09870, AW059_18350, AW106_02825, AWB10_24615, AWE53_003010, SOURCE 13 AWF59_006810, AWG78_010890, AWG90_025185, AWP75_14755, AZZ83_003567, SOURCE 14 B6V57_23175, B7C53_16050, B9M99_07260, B9N33_14930, B9T59_11225, SOURCE 15 BANRA_02722, BANRA_02895, BANRA_05124, BB545_04745, BE963_11630, SOURCE 16 BEN53_25180, BER14_12995, BFD68_07790, BHF03_13425, BHF46_15090, SOURCE 17 BHJ80_01810, BHS81_24295, BHS87_22640, BIQ87_23185, BIU72_20655, SOURCE 18 BIZ41_02125, BJJ90_24770, BK248_24315, BK292_01025, BK296_23860, SOURCE 19 BK334_08815, BK373_03960, BK375_08450, BK383_21615, BMA87_07675, SOURCE 20 BMT49_20690, BMT91_12915, BN17_40181, BOH76_06090, BON63_06530, SOURCE 21 BON65_23060, BON66_03315, BON69_22095, BON71_16410, BON75_07080, SOURCE 22 BON76_04855, BON83_16235, BON86_25705, BON87_02545, BON91_12300, SOURCE 23 BON92_17725, BON94_08075, BON95_04860, BON96_03145, BON98_14025, SOURCE 24 BTQ04_27960, BTQ06_28255, BUE81_22465, BVCMS12BK_04297, SOURCE 25 BVCMS2454_00415, BVCMS28BK_01342, BVCMS35BK_01831, BVCMSC61A_01832, SOURCE 26 BVCMSHHP001_00842, BVCMSHHP019_03449, BVCMSHHP056_02653, SOURCE 27 BVCMSKKP036_01653, BVCMSKKP061_03212, BVCMSKSNP073_04428, SOURCE 28 BVCMSKSNP081_02209, BVCMSKSNP120_00016, BVCMSKSP011_01869, SOURCE 29 BVCMSKSP024_01390, BVCMSKSP026_03995, BVCMSKSP045_02606, SOURCE 30 BVCMSKSP058_01651, BVCMSKSP067_03973, BVCMSKSP076_00063, SOURCE 31 BVCMSNSNP036_01892, BVCMSNSP006_05193, BVCMSNSP007_02439, SOURCE 32 BVCMSNSP047_02150, BVCMSNSP072_02985, BVCMSOUP014_01488, SOURCE 33 BVCMSSINP011_01581, BVCMSSINP022_02516, BVCMSSIP019_02982, SOURCE 34 BVCMSSIP044_03653, BVL39_05000, BW690_17275, BWI89_17045, SOURCE 35 BWP17_09115, BXT93_20190, BZL31_27495, BZL69_04975, C2M16_18650, SOURCE 36 C2U48_12390, C4K41_22540, C4M78_06355, C5715_10070, C5F72_25480, SOURCE 37 C5F73_24600, C5N07_20195, C5P01_10950, C5P44_17630, C6669_07275, SOURCE 38 C6B13_20680, C7235_23375, C7B02_13860, C7B06_21440, C7B07_20950, SOURCE 39 C7B08_17115, C7B18_19350, C9098_11905, C9114_00185, C9141_04535, SOURCE 40 C9160_08095, C9162_23740, C9201_06385, C9306_11555, C9E25_05905, SOURCE 41 C9E67_28315, C9Z03_09215, C9Z23_10210, C9Z28_18985, C9Z29_15625, SOURCE 42 C9Z37_11110, C9Z39_12685, C9Z43_13055, C9Z68_12230, C9Z69_10275, SOURCE 43 C9Z70_15630, C9Z78_21525, C9Z89_05965, CA593_05680, CCZ14_07840, SOURCE 44 CDC27_21910, CDL37_20795, CF006_04145, CG692_11650, CI641_013760, SOURCE 45 CI693_02120, CI694_23155, CIG45_19390, CJU63_23870, CJU64_24205, SOURCE 46 CMR93_13445, CO706_19840, COD30_15395, COD46_18700, CQP61_25715, SOURCE 47 CR538_23835, CR539_02040, CRD98_27320, CRE06_21195, CRJUMX01_510039, SOURCE 48 CRM83_18295, CRT43_24270, CRX46_18555, CSB64_02010, CT146_24150, SOURCE 49 CUB99_11400, CV83915_01994, CVH05_06385, CWM24_08770, CWS33_15975, SOURCE 50 D0X26_12200, D1912_18705, D2184_21525, D2185_07080, D2188_17815, SOURCE 51 D3821_04640, D3822_08745, D3M98_15580, D3O91_19225, D3P01_12220, SOURCE 52 D3P02_10990, D4011_20000, D4023_17595, D4074_20080, D4628_12380, SOURCE 53 D4636_09720, D4638_24525, D4660_19160, D4718_13325, D4L91_18735, SOURCE 54 D4M06_19695, D4M76_10435, D4U49_11220, D4U85_19640, D4V08_08845, SOURCE 55 D5H35_01910, D5I97_18270, D6004_01850, D6C36_19740, D6D43_19725, SOURCE 56 D6T60_08900, D6T98_07050, D6W00_08775, D6X36_02250, D6X63_25780, SOURCE 57 D6X76_22790, D7K33_19360, D7K63_02835, D7K66_21305, D7W70_12300, SOURCE 58 D7Y10_01185, D7Z75_09495, D8Y65_18220, D9610_00735, D9C99_09310, SOURCE 59 D9D20_17210, D9D33_01860, D9D43_18385, D9D44_06445, D9D94_04730, SOURCE 60 D9E13_11180, D9E19_14095, D9E34_02075, D9E35_10415, D9E49_22250, SOURCE 61 D9E73_19440, D9F17_19275, D9F32_11525, D9F87_12490, D9G11_22460, SOURCE 62 D9G29_18660, D9G42_14820, D9G48_15290, D9G69_15475, D9G95_21630, SOURCE 63 D9H10_15220, D9H36_09830, D9H53_20975, D9H68_20260, D9H70_15350, SOURCE 64 D9H94_14230, D9I18_21060, D9I20_19240, D9I87_21035, D9I88_03895, SOURCE 65 D9I97_23010, D9J03_04410, D9J11_07590, D9J44_17675, D9J46_13285, SOURCE 66 D9J52_18345, D9J58_14965, D9J60_05135, D9J63_12310, D9J78_21390, SOURCE 67 D9K02_09285, D9K48_05710, D9K54_02940, D9L89_19960, D9L99_05045, SOURCE 68 D9S45_16730, D9X77_17715, D9X97_19985, D9Z28_19505, DAH18_17020, SOURCE 69 DAH26_23105, DAH30_16750, DAH32_05100, DAH34_09745, DAH37_23000, SOURCE 70 DAH43_08050, DB359_22770, DBQ99_24230, DD762_09570, DEN86_01240, SOURCE 71 DEN89_16940, DEN97_12815, DEO04_14355, DEO19_12485, DEO20_13045, SOURCE 72 DIV22_28315, DJ487_17695, DJ503_03205, DK132_10450, DL251_19160, SOURCE 73 DL257_06320, DL292_14670, DL326_18360, DL455_17780, DL479_04890, SOURCE 74 DL530_02190, DL545_23320, DL705_06290, DL800_28030, DL979_22465, SOURCE 75 DLT82_16100, DLU50_04305, DLU67_12520, DLU82_06835, DLW60_00780, SOURCE 76 DLW88_15040, DLX38_07225, DLX40_14200, DLY41_09575, DLY44_12300, SOURCE 77 DM102_07955, DM129_07275, DM155_00780, DM267_22275, DM272_08145, SOURCE 78 DM280_16450, DM296_05455, DM382_06365, DM820_11410, DM962_16745, SOURCE 79 DM973_17240, DMI04_18725, DMI53_18525, DMO02_19335, DMY83_08280, SOURCE 80 DMZ50_11405, DN627_13770, DN660_12190, DN700_09495, DN703_20325, SOURCE 81 DN808_20920, DNB37_17705, DNC98_13900, DND16_08380, DND79_11485, SOURCE 82 DNI21_02325, DNJ62_19610, DNK12_18155, DNQ45_03405, DNR35_06920, SOURCE 83 DNR41_16590, DNW42_02895, DNX19_05225, DOE35_19020, DOM23_10665, SOURCE 84 DOS18_18880, DOT81_19955, DOU81_18220, DOY22_18350, DOY56_18570, SOURCE 85 DOY61_11305, DOY67_06200, DP258_12750, DP265_01880, DP277_17730, SOURCE 86 DQE91_14650, DQF36_19215, DQF57_12540, DQF71_02370, DQF72_01950, SOURCE 87 DQG35_19915, DQO13_07445, DQP61_07285, DRP48_19990, DRW19_10040, SOURCE 88 DS143_02030, DS721_17960, DS732_01915, DS966_07340, DT034_16995, SOURCE 89 DTL43_19530, DTL90_18345, DTM10_17250, DTM45_22000, DTZ20_07940, SOURCE 90 DU309_08590, DU321_20700, DU333_20915, DVB38_00780, DW236_20350, SOURCE 91 DWB25_23105, DXT69_11240, DXT71_13455, DXT73_06680, DXX80_014420, SOURCE 92 E0I42_01715, E0K84_14705, E0L04_06555, E0L12_12475, E2112_13635, SOURCE 93 E2119_15925, E2127_04695, E2128_24955, E2129_11665, E2134_19225, SOURCE 94 E2135_15890, E2148_17730, E2855_05069, E2863_04868, E4A44_08405, SOURCE 95 E4K51_08400, E4K55_09280, E4K59_02705, E4K60_21225, E4K61_06350, SOURCE 96 E5P22_21020, E5P24_22750, E5P28_22440, E5P37_19690, E5S42_14590, SOURCE 97 E5S56_16625, E5S58_10005, E5S61_13810, E5S62_09140, EA159_09860, SOURCE 98 EA164_11895, EA167_12330, EA174_06160, EA184_14750, EA189_16420, SOURCE 99 EA191_11120, EA198_19920, EA200_15705, EA203_12170, EA213_12715, SOURCE 100 EA214_12670, EA218_06700, EA222_18665, EA223_05425, EA225_15150, SOURCE 101 EA231_21330, EA232_11815, EA233_13540, EA235_13150, EA239_14350, SOURCE 102 EA242_15215, EA245_21190, EA247_19925, EA250_22905, EA410_10735, SOURCE 103 EA429_14660, EA433_09295, EA434_07730, EA435_14070, EA834_14185, SOURCE 104 EAI42_11775, EAI46_13910, EAI52_14305, EAM59_19660, EAN70_04295, SOURCE 105 EAN77_18045, EAX79_14320, EB476_06510, EB509_23270, EB510_19485, SOURCE 106 EB515_21475, EB525_RS22295, EBA46_21785, EBA84_21540, EBJ06_20090, SOURCE 107 EBM08_00725, EC1094V2_4222, EC3234A_77C00360, EC3426_00367, SOURCE 108 EC382_06195, EC95NR1_03586, ECONIH1_23895, ECS5026, ECTO124_04687, SOURCE 109 ECTO6_04452, ED178_02160, ED225_20150, ED307_20800, ED600_11955, SOURCE 110 ED607_20180, ED611_21565, ED648_10135, ED903_21355, ED944_20920, SOURCE 111 EEA45_23665, EEP23_23665, EF082_14250, EF173_02775, EG075_18135, SOURCE 112 EG599_11110, EG796_08865, EG808_11410, EGC26_22390, EGT48_16960, SOURCE 113 EGU87_16570, EH186_18415, EH412_04435, EHD45_05640, EHD63_19000, SOURCE 114 EHD79_12175, EHH55_01035, EHJ36_05660, EHJ66_21070, EHV81_14020, SOURCE 115 EHV90_14340, EHW09_21540, EHX09_18295, EI021_16120, EI028_05870, SOURCE 116 EI032_15785, EI041_04290, EIA08_19795, EIA21_16610, EIZ93_23270, SOURCE 117 EJ366_21585, EJC75_19935, EKI52_13610, EL75_4145, EL79_4350, SOURCE 118 EL80_4257, ELT17_04335, ELT20_15125, ELT22_19765, ELT23_17595, SOURCE 119 ELT33_14365, ELT48_13885, ELT49_00210, ELT58_16885, ELU82_17295, SOURCE 120 ELU85_16290, ELU96_14010, ELV00_20075, ELV05_04290, ELV08_22365, SOURCE 121 ELV13_10080, ELV15_24385, ELV22_20245, ELV24_10490, ELV28_08325, SOURCE 122 ELX56_12745, ELX70_12445, ELX76_18040, ELX79_01350, ELX83_19330, SOURCE 123 ELY05_20415, ELY23_17950, ELY24_02305, ELY41_24075, ELY48_01785, SOURCE 124 ELY50_17875, EO241_22225, EPS91_05510, EPS94_15340, EPU41_22875, SOURCE 125 EQ820_09870, EQ823_07865, EQ825_11565, EQ830_09950, EQO00_24610, SOURCE 126 ERL57_14825, ERS085365_02976, ERS085366_03456, ERS085374_01624, SOURCE 127 ERS085379_03983, ERS085383_01448, ERS085386_02660, ERS085404_01243, SOURCE 128 ERS085406_04198, ERS085411_04446, ERS085416_00631, ERS139211_04672, SOURCE 129 ERS150873_01187, ERS150876_04135, EST51_23545, EVY14_11520, SOURCE 130 EWK56_09425, EXM29_06605, EXPECSC019_02605, EXPECSC038_04549, SOURCE 131 EXPECSC065_01920, EXX06_18435, EXX13_12090, EXX23_19315, SOURCE 132 EXX24_09955, EXX53_09260, EXX55_18970, EXX71_07865, EXX78_13230, SOURCE 133 EXX87_20000, EYD11_21280, EYX82_05305, EYX99_01640, EYY27_19365, SOURCE 134 EYY34_21065, EYY78_21440, F1E13_08855, F1E19_14155, F7F00_04830, SOURCE 135 F7F11_03715, F7F18_10310, F7F23_02515, F7F26_18655, F7F29_21255, SOURCE 136 F7F56_09730, F7G01_19665, F7G03_07710, F9040_10620, F9050_18985, SOURCE 137 F9225_08300, F9B07_06640, F9X20_06245, F9Z53_12245, F9Z74_02500, SOURCE 138 FAF34_027445, FE846_20710, FKO60_19090, FNJ67_24760, FNJ69_19430, SOURCE 139 FNJ83_25115, FORC82_4459, FPI65_24840, FQ021_13785, FQ022_13220, SOURCE 140 FQ915_20070, FQR64_21510, FQU83_25315, FQZ46_11420, FRV13_15940, SOURCE 141 FTV92_16270, FTV93_16625, FV293_00180, FV295_14155, FV438_02950, SOURCE 142 FVB16_13290, FY127_04780, FZ043_01435, FZC17_04895, FZN06_07660, SOURCE 143 FZN26_04905, FZN30_09565, G3565_23685, G3V64_10445, G5603_20840, SOURCE 144 G5608_21780, G5616_05135, G5632_08040, G5668_16270, G5670_04760, SOURCE 145 G5675_07615, G5680_02920, G5686_19405, G5688_11635, G5696_16625, SOURCE 146 G5697_10455, GFU40_20155, GFU45_18365, GFU47_11010, GHR40_03285, SOURCE 147 GII67_18535, GII91_01590, GIJ01_07080, GIY13_22705, GIY19_15100, SOURCE 148 GJ11_25525, GJ638_08800, GJD97_25670, GKE15_08795, GKE16_10270, SOURCE 149 GKE22_09815, GKE24_10940, GKE26_10295, GKE29_07830, GKE31_09080, SOURCE 150 GKE39_08675, GKE46_08475, GKE53_08285, GKE58_08305, GKE60_08375, SOURCE 151 GKE64_08350, GKE69_08185, GKE77_10555, GKE79_08190, GKE87_03580, SOURCE 152 GKE92_11980, GKE93_09555, GKE98_17470, GKF00_11225, GKF03_07640, SOURCE 153 GKF21_19525, GKF28_19545, GKF34_19920, GKF39_10130, GKF47_19635, SOURCE 154 GKF52_19185, GKF74_07005, GKF86_09530, GKF89_08240, GKG08_19925, SOURCE 155 GKG09_19795, GKG11_19965, GKG12_13240, GKG22_19630, GKG29_19840, SOURCE 156 GN312_11355, GNZ00_12570, GNZ02_08260, GNZ03_05545, GNZ05_23055, SOURCE 157 GP650_09375, GP654_14900, GP661_10840, GP662_05880, GP664_12905, SOURCE 158 GP666_14410, GP671_00680, GP678_14315, GP689_08955, GP698_02940, SOURCE 159 GP700_05045, GP711_15355, GP712_07365, GP720_18065, GP727_20045, SOURCE 160 GP892_04865, GP912_08340, GP935_16255, GP945_10980, GP946_12270, SOURCE 161 GP950_01700, GQA23_07565, GQA63_11350, GQA64_11565, GQE22_22480, SOURCE 162 GQE30_09515, GQE33_21095, GQE34_18985, GQE36_21390, GQE42_17480, SOURCE 163 GQE47_16615, GQE51_19030, GQE58_14030, GQE64_15035, GQE68_09185, SOURCE 164 GQE87_13955, GQE88_20795, GQE93_06065, GQF59_13075, GQL64_02840, SOURCE 165 GQM04_21825, GQM06_05485, GQM09_07375, GQM10_00185, GQM13_10075, SOURCE 166 GQM17_17755, GQM18_21055, GQM28_14230, GQN16_10665, GQN24_10350, SOURCE 167 GQN33_15605, GQS26_13850, GQY14_18825, GRW05_25935, GRW12_07495, SOURCE 168 GRW27_03680, GRW30_10035, GRW42_18565, GRW57_21705, GRW80_00680, SOURCE 169 GRW81_20425, GUB08_14505, GUB85_10045, GUB91_12015, GUB95_13125, SOURCE 170 GUC01_08305, GUC12_14155, GUC40_13020, GUI16_13780, GUI33_07450, SOURCE 171 GZS12_22285, HMCMS169_03196, HMCMS184_01443, HMCMSJML074_03763, SOURCE 172 HMCMSJML079_02438, HMCMSJML146_04299, HMCMSJML204_02607, SOURCE 173 HMCMSJML236_03697, HMPREF3040_01362, HW43_01890, MJ49_09110, SOURCE 174 MS6198_46970, MS8345_04507, NCTC10082_02015, NCTC10089_04675, SOURCE 175 NCTC10090_02705, NCTC10764_02888, NCTC10766_00857, NCTC10767_00646, SOURCE 176 NCTC10963_04726, NCTC10974_05266, NCTC11022_04367, NCTC11126_02097, SOURCE 177 NCTC11181_01887, NCTC11341_02866, NCTC12650_04928, NCTC12950_05138, SOURCE 178 NCTC13127_06081, NCTC13216_02170, NCTC13846_04407, NCTC7922_05075, SOURCE 179 NCTC7927_05177, NCTC7928_03743, NCTC8009_08326, NCTC8179_05022, SOURCE 180 NCTC8621_04799, NCTC8959_04132, NCTC8960_02264, NCTC8985_03936, SOURCE 181 NCTC9001_04561, NCTC9007_01043, NCTC9036_04577, NCTC9044_02378, SOURCE 182 NCTC9045_05471, NCTC9050_02746, NCTC9055_01590, NCTC9058_02211, SOURCE 183 NCTC9062_03515, NCTC9073_00755, NCTC9077_05829, NCTC9081_06397, SOURCE 184 NCTC9111_04889, NCTC9117_05822, NCTC9119_04984, NCTC9434_04602, SOURCE 185 NCTC9701_04926, NCTC9702_05565, NCTC9703_04146, NCTC9706_01937, SOURCE 186 NCTC9777_01051, NCTC9962_03719, NCTC9969_04855, PGD_03216, SOURCE 187 PU06_05790, RG28_25645, RK56_017085, RX35_03825, SAMEA3472043_01946, SOURCE 188 SAMEA3472044_04487, SAMEA3472047_04009, SAMEA3472055_01604, SOURCE 189 SAMEA3472056_04390, SAMEA3472070_04043, SAMEA3472080_00231, SOURCE 190 SAMEA3472090_02852, SAMEA3472108_01696, SAMEA3472110_00875, SOURCE 191 SAMEA3472112_01208, SAMEA3472114_02039, SAMEA3472147_04803, SOURCE 192 SAMEA3484427_03830, SAMEA3484429_02475, SAMEA3484434_03756, SOURCE 193 SAMEA3485101_02956, SAMEA3752372_01305, SAMEA3752553_02498, SOURCE 194 SAMEA3752557_02189, SAMEA3752559_00285, SAMEA3752620_03709, SOURCE 195 SAMEA3753064_01449, SAMEA3753097_04412, SAMEA3753164_04167, SOURCE 196 SAMEA3753290_01938, SAMEA3753300_00786, SK85_04379, SY51_23235, SOURCE 197 U12A_04345, U14A_04341, UC41_10590, UN86_02805, UN91_08555, SOURCE 198 WQ89_14700, WR15_07670, YDC107_2768; SOURCE 199 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 200 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 201 MOL_ID: 2; SOURCE 202 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 203 ORGANISM_TAXID: 9844; SOURCE 204 EXPRESSION_SYSTEM: ESCHERICHIA COLI W; SOURCE 205 EXPRESSION_SYSTEM_TAXID: 566546 KEYWDS TRANSCRIPTIONAL REPRESSOR DNA BINDING AUTOPROTEOLYSIS NANOBODIES, KEYWDS 2 TRANSCRIPTION EXPDTA X-RAY DIFFRACTION AUTHOR L.MASO,F.VASCON,M.CHINELLATO,E.PARDON,J.STEYAERT,A.ANGELINI,D.TONDI, AUTHOR 2 L.CENDRON JRNL AUTH L.MASO,F.VASCON,M.CHINELLATO,F.GOORMAGHTIGH,P.BELLIO, JRNL AUTH 2 E.CAMPAGNARO,L.VAN MELDEREN,M.RUZZENE,E.PARDON,A.ANGELINI, JRNL AUTH 3 G.CELENZA,J.STEYAERT,D.TONDI,L.CENDRON JRNL TITL NANOBODIES TARGETING LEXA AUTOCLEAVAGE DISCLOSE A NOVEL JRNL TITL 2 SUPPRESSION STRATEGY OF SOS-RESPONSE PATHWAY. JRNL REF STRUCTURE 2022 JRNL REFN ISSN 0969-2126 JRNL PMID 36240773 JRNL DOI 10.1016/J.STR.2022.09.004 REMARK 2 REMARK 2 RESOLUTION. 2.80 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 5.8.0267 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 : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97 REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 38473 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.259 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL REMARK 3 FREE R VALUE TEST SET COUNT : 1818 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 SOLVENT RADIUS : NULL REMARK 3 SHRINKAGE RADIUS : NULL REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.94 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL 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 7ZRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE. REMARK 100 THE DEPOSITION ID IS D_1292122770. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAR-19 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06DA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0007 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38956 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800 REMARK 200 RESOLUTION RANGE LOW (A) : 48.020 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 1.900 REMARK 200 R MERGE (I) : 0.05000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.9000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.25000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 1JHC REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.68 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M CALCIUM CHLORIDE, 0.1 M HEPES, REMARK 280 20 % W/V PEG 6000, PH 7, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 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 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 29.95900 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 115.89800 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.37500 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 115.89800 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.95900 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.37500 REMARK 290 SMTRY3 4 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 6220 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21940 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5520 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21850 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, H REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 1 REMARK 465 LYS A 2 REMARK 465 ALA A 3 REMARK 465 LEU A 4 REMARK 465 THR A 5 REMARK 465 ALA A 6 REMARK 465 ARG A 7 REMARK 465 GLN A 8 REMARK 465 GLN A 9 REMARK 465 GLU A 10 REMARK 465 VAL A 11 REMARK 465 PHE A 12 REMARK 465 ASP A 13 REMARK 465 LEU A 14 REMARK 465 ILE A 15 REMARK 465 ARG A 16 REMARK 465 ASP A 17 REMARK 465 HIS A 18 REMARK 465 ILE A 19 REMARK 465 SER A 20 REMARK 465 GLN A 21 REMARK 465 THR A 22 REMARK 465 GLY A 23 REMARK 465 MET A 24 REMARK 465 PRO A 25 REMARK 465 PRO A 26 REMARK 465 THR A 27 REMARK 465 ARG A 28 REMARK 465 ALA A 29 REMARK 465 GLU A 30 REMARK 465 ILE A 31 REMARK 465 ALA A 32 REMARK 465 GLN A 33 REMARK 465 ARG A 34 REMARK 465 LEU A 35 REMARK 465 GLY A 36 REMARK 465 PHE A 37 REMARK 465 ARG A 38 REMARK 465 SER A 39 REMARK 465 PRO A 40 REMARK 465 ASN A 41 REMARK 465 ALA A 42 REMARK 465 ALA A 43 REMARK 465 GLU A 44 REMARK 465 GLU A 45 REMARK 465 HIS A 46 REMARK 465 LEU A 47 REMARK 465 LYS A 48 REMARK 465 ALA A 49 REMARK 465 LEU A 50 REMARK 465 ALA A 51 REMARK 465 ARG A 52 REMARK 465 LYS A 53 REMARK 465 GLY A 54 REMARK 465 VAL A 55 REMARK 465 ILE A 56 REMARK 465 GLU A 57 REMARK 465 ILE A 58 REMARK 465 VAL A 59 REMARK 465 SER A 60 REMARK 465 GLY A 61 REMARK 465 ALA A 62 REMARK 465 SER A 63 REMARK 465 ARG A 64 REMARK 465 GLY A 65 REMARK 465 ILE A 66 REMARK 465 ARG A 67 REMARK 465 LEU A 68 REMARK 465 LEU A 69 REMARK 465 GLN A 70 REMARK 465 GLU A 71 REMARK 465 GLU A 72 REMARK 465 GLU A 73 REMARK 465 MET C 1 REMARK 465 LYS C 2 REMARK 465 ALA C 3 REMARK 465 LEU C 4 REMARK 465 THR C 5 REMARK 465 ALA C 6 REMARK 465 ARG C 7 REMARK 465 GLN C 8 REMARK 465 GLN C 9 REMARK 465 GLU C 10 REMARK 465 VAL C 11 REMARK 465 PHE C 12 REMARK 465 ASP C 13 REMARK 465 LEU C 14 REMARK 465 ILE C 15 REMARK 465 ARG C 16 REMARK 465 ASP C 17 REMARK 465 HIS C 18 REMARK 465 ILE C 19 REMARK 465 SER C 20 REMARK 465 GLN C 21 REMARK 465 THR C 22 REMARK 465 GLY C 23 REMARK 465 MET C 24 REMARK 465 PRO C 25 REMARK 465 PRO C 26 REMARK 465 THR C 27 REMARK 465 ARG C 28 REMARK 465 ALA C 29 REMARK 465 GLU C 30 REMARK 465 ILE C 31 REMARK 465 ALA C 32 REMARK 465 GLN C 33 REMARK 465 ARG C 34 REMARK 465 LEU C 35 REMARK 465 GLY C 36 REMARK 465 PHE C 37 REMARK 465 ARG C 38 REMARK 465 SER C 39 REMARK 465 PRO C 40 REMARK 465 ASN C 41 REMARK 465 ALA C 42 REMARK 465 ALA C 43 REMARK 465 GLU C 44 REMARK 465 GLU C 45 REMARK 465 HIS C 46 REMARK 465 LEU C 47 REMARK 465 LYS C 48 REMARK 465 ALA C 49 REMARK 465 LEU C 50 REMARK 465 ALA C 51 REMARK 465 ARG C 52 REMARK 465 LYS C 53 REMARK 465 GLY C 54 REMARK 465 VAL C 55 REMARK 465 ILE C 56 REMARK 465 GLU C 57 REMARK 465 ILE C 58 REMARK 465 VAL C 59 REMARK 465 SER C 60 REMARK 465 GLY C 61 REMARK 465 ALA C 62 REMARK 465 SER C 63 REMARK 465 ARG C 64 REMARK 465 GLY C 65 REMARK 465 ILE C 66 REMARK 465 ARG C 67 REMARK 465 LEU C 68 REMARK 465 LEU C 69 REMARK 465 GLN C 70 REMARK 465 GLU C 71 REMARK 465 GLU C 72 REMARK 465 GLU C 73 REMARK 465 SER E 121 REMARK 465 SER E 122 REMARK 465 HIS E 123 REMARK 465 HIS E 124 REMARK 465 HIS E 125 REMARK 465 HIS E 126 REMARK 465 HIS E 127 REMARK 465 HIS E 128 REMARK 465 GLU E 129 REMARK 465 PRO E 130 REMARK 465 GLU E 131 REMARK 465 ALA E 132 REMARK 465 HIS G 124 REMARK 465 HIS G 125 REMARK 465 HIS G 126 REMARK 465 HIS G 127 REMARK 465 HIS G 128 REMARK 465 GLU G 129 REMARK 465 PRO G 130 REMARK 465 GLU G 131 REMARK 465 ALA G 132 REMARK 465 MET B 1 REMARK 465 LYS B 2 REMARK 465 ALA B 3 REMARK 465 LEU B 4 REMARK 465 THR B 5 REMARK 465 ALA B 6 REMARK 465 ARG B 7 REMARK 465 GLN B 8 REMARK 465 GLN B 9 REMARK 465 GLU B 10 REMARK 465 VAL B 11 REMARK 465 PHE B 12 REMARK 465 ASP B 13 REMARK 465 LEU B 14 REMARK 465 ILE B 15 REMARK 465 ARG B 16 REMARK 465 ASP B 17 REMARK 465 HIS B 18 REMARK 465 ILE B 19 REMARK 465 SER B 20 REMARK 465 GLN B 21 REMARK 465 THR B 22 REMARK 465 GLY B 23 REMARK 465 MET B 24 REMARK 465 PRO B 25 REMARK 465 PRO B 26 REMARK 465 THR B 27 REMARK 465 ARG B 28 REMARK 465 ALA B 29 REMARK 465 GLU B 30 REMARK 465 ILE B 31 REMARK 465 ALA B 32 REMARK 465 GLN B 33 REMARK 465 ARG B 34 REMARK 465 LEU B 35 REMARK 465 GLY B 36 REMARK 465 PHE B 37 REMARK 465 ARG B 38 REMARK 465 SER B 39 REMARK 465 PRO B 40 REMARK 465 ASN B 41 REMARK 465 ALA B 42 REMARK 465 ALA B 43 REMARK 465 GLU B 44 REMARK 465 GLU B 45 REMARK 465 HIS B 46 REMARK 465 LEU B 47 REMARK 465 LYS B 48 REMARK 465 ALA B 49 REMARK 465 LEU B 50 REMARK 465 ALA B 51 REMARK 465 ARG B 52 REMARK 465 LYS B 53 REMARK 465 GLY B 54 REMARK 465 VAL B 55 REMARK 465 ILE B 56 REMARK 465 GLU B 57 REMARK 465 ILE B 58 REMARK 465 VAL B 59 REMARK 465 SER B 60 REMARK 465 GLY B 61 REMARK 465 ALA B 62 REMARK 465 SER B 63 REMARK 465 ARG B 64 REMARK 465 GLY B 65 REMARK 465 ILE B 66 REMARK 465 ARG B 67 REMARK 465 LEU B 68 REMARK 465 LEU B 69 REMARK 465 GLN B 70 REMARK 465 GLU B 71 REMARK 465 GLU B 72 REMARK 465 GLU B 73 REMARK 465 GLU B 74 REMARK 465 MET D 1 REMARK 465 LYS D 2 REMARK 465 ALA D 3 REMARK 465 LEU D 4 REMARK 465 THR D 5 REMARK 465 ALA D 6 REMARK 465 ARG D 7 REMARK 465 GLN D 8 REMARK 465 GLN D 9 REMARK 465 GLU D 10 REMARK 465 VAL D 11 REMARK 465 PHE D 12 REMARK 465 ASP D 13 REMARK 465 LEU D 14 REMARK 465 ILE D 15 REMARK 465 ARG D 16 REMARK 465 ASP D 17 REMARK 465 HIS D 18 REMARK 465 ILE D 19 REMARK 465 SER D 20 REMARK 465 GLN D 21 REMARK 465 THR D 22 REMARK 465 GLY D 23 REMARK 465 MET D 24 REMARK 465 PRO D 25 REMARK 465 PRO D 26 REMARK 465 THR D 27 REMARK 465 ARG D 28 REMARK 465 ALA D 29 REMARK 465 GLU D 30 REMARK 465 ILE D 31 REMARK 465 ALA D 32 REMARK 465 GLN D 33 REMARK 465 ARG D 34 REMARK 465 LEU D 35 REMARK 465 GLY D 36 REMARK 465 PHE D 37 REMARK 465 ARG D 38 REMARK 465 SER D 39 REMARK 465 PRO D 40 REMARK 465 ASN D 41 REMARK 465 ALA D 42 REMARK 465 ALA D 43 REMARK 465 GLU D 44 REMARK 465 GLU D 45 REMARK 465 HIS D 46 REMARK 465 LEU D 47 REMARK 465 LYS D 48 REMARK 465 ALA D 49 REMARK 465 LEU D 50 REMARK 465 ALA D 51 REMARK 465 ARG D 52 REMARK 465 LYS D 53 REMARK 465 GLY D 54 REMARK 465 VAL D 55 REMARK 465 ILE D 56 REMARK 465 GLU D 57 REMARK 465 ILE D 58 REMARK 465 VAL D 59 REMARK 465 SER D 60 REMARK 465 GLY D 61 REMARK 465 ALA D 62 REMARK 465 SER D 63 REMARK 465 ARG D 64 REMARK 465 GLY D 65 REMARK 465 ILE D 66 REMARK 465 ARG D 67 REMARK 465 LEU D 68 REMARK 465 LEU D 69 REMARK 465 GLN D 70 REMARK 465 GLU D 71 REMARK 465 GLU D 72 REMARK 465 GLU D 73 REMARK 465 SER F 122 REMARK 465 HIS F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 REMARK 465 HIS F 126 REMARK 465 HIS F 127 REMARK 465 HIS F 128 REMARK 465 GLU F 129 REMARK 465 PRO F 130 REMARK 465 GLU F 131 REMARK 465 ALA F 132 REMARK 465 HIS H 123 REMARK 465 HIS H 124 REMARK 465 HIS H 125 REMARK 465 HIS H 126 REMARK 465 HIS H 127 REMARK 465 HIS H 128 REMARK 465 GLU H 129 REMARK 465 PRO H 130 REMARK 465 GLU H 131 REMARK 465 ALA H 132 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 GLU A 95 46.48 -100.11 REMARK 500 ASP A 101 108.23 -55.33 REMARK 500 GLU A 170 68.69 -115.53 REMARK 500 ASN A 171 135.66 -170.81 REMARK 500 LEU C 89 33.26 -86.32 REMARK 500 MET C 118 31.44 -98.12 REMARK 500 TRP C 201 10.58 50.80 REMARK 500 SER E 17 91.15 -160.99 REMARK 500 LYS E 64 70.44 -106.25 REMARK 500 SER G 7 104.39 -162.49 REMARK 500 ALA G 14 150.24 -49.89 REMARK 500 LYS G 64 67.94 -104.93 REMARK 500 SER G 84 58.02 -118.90 REMARK 500 GLU B 95 42.46 -101.98 REMARK 500 GLU B 170 68.61 -115.89 REMARK 500 ASN B 171 136.83 -171.09 REMARK 500 LEU D 89 44.97 -79.42 REMARK 500 SER F 17 92.99 -163.19 REMARK 500 LYS F 64 68.85 -104.47 REMARK 500 ALA F 91 173.01 179.16 REMARK 500 SER H 7 106.23 -163.96 REMARK 500 LEU H 18 117.09 -170.83 REMARK 500 LYS H 64 65.02 -102.77 REMARK 500 SER H 84 53.67 -115.45 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 7B5G RELATED DB: PDB DBREF 7ZRA A 1 202 UNP C3SHL2 C3SHL2_ECOLX 1 202 DBREF 7ZRA C 1 202 UNP C3SHL2 C3SHL2_ECOLX 1 202 DBREF 7ZRA E 1 132 PDB 7ZRA 7ZRA 1 132 DBREF 7ZRA G 1 132 PDB 7ZRA 7ZRA 1 132 DBREF 7ZRA B 1 202 UNP C3SHL2 C3SHL2_ECOLX 1 202 DBREF 7ZRA D 1 202 UNP C3SHL2 C3SHL2_ECOLX 1 202 DBREF 7ZRA F 1 132 PDB 7ZRA 7ZRA 1 132 DBREF 7ZRA H 1 132 PDB 7ZRA 7ZRA 1 132 SEQRES 1 A 202 MET LYS ALA LEU THR ALA ARG GLN GLN GLU VAL PHE ASP SEQRES 2 A 202 LEU ILE ARG ASP HIS ILE SER GLN THR GLY MET PRO PRO SEQRES 3 A 202 THR ARG ALA GLU ILE ALA GLN ARG LEU GLY PHE ARG SER SEQRES 4 A 202 PRO ASN ALA ALA GLU GLU HIS LEU LYS ALA LEU ALA ARG SEQRES 5 A 202 LYS GLY VAL ILE GLU ILE VAL SER GLY ALA SER ARG GLY SEQRES 6 A 202 ILE ARG LEU LEU GLN GLU GLU GLU GLU GLY LEU PRO LEU SEQRES 7 A 202 VAL GLY ARG VAL ALA ALA GLY GLU PRO LEU LEU ALA GLN SEQRES 8 A 202 GLN HIS ILE GLU GLY HIS TYR GLN VAL ASP PRO SER LEU SEQRES 9 A 202 PHE LYS PRO ASN ALA ASP PHE LEU LEU ARG VAL SER GLY SEQRES 10 A 202 MET SER MET LYS ASP ILE GLY ILE MET ASP GLY ASP LEU SEQRES 11 A 202 LEU ALA VAL HIS LYS THR GLN ASP VAL ARG ASN GLY GLN SEQRES 12 A 202 VAL VAL VAL ALA ARG ILE ASP ASP GLU VAL THR VAL LYS SEQRES 13 A 202 ARG LEU LYS LYS GLN GLY ASN LYS VAL GLU LEU LEU PRO SEQRES 14 A 202 GLU ASN SER GLU PHE LYS PRO ILE VAL VAL ASP LEU ARG SEQRES 15 A 202 GLN GLN SER PHE THR ILE GLU GLY LEU ALA VAL GLY VAL SEQRES 16 A 202 ILE ARG ASN GLY ASP TRP LEU SEQRES 1 C 202 MET LYS ALA LEU THR ALA ARG GLN GLN GLU VAL PHE ASP SEQRES 2 C 202 LEU ILE ARG ASP HIS ILE SER GLN THR GLY MET PRO PRO SEQRES 3 C 202 THR ARG ALA GLU ILE ALA GLN ARG LEU GLY PHE ARG SER SEQRES 4 C 202 PRO ASN ALA ALA GLU GLU HIS LEU LYS ALA LEU ALA ARG SEQRES 5 C 202 LYS GLY VAL ILE GLU ILE VAL SER GLY ALA SER ARG GLY SEQRES 6 C 202 ILE ARG LEU LEU GLN GLU GLU GLU GLU GLY LEU PRO LEU SEQRES 7 C 202 VAL GLY ARG VAL ALA ALA GLY GLU PRO LEU LEU ALA GLN SEQRES 8 C 202 GLN HIS ILE GLU GLY HIS TYR GLN VAL ASP PRO SER LEU SEQRES 9 C 202 PHE LYS PRO ASN ALA ASP PHE LEU LEU ARG VAL SER GLY SEQRES 10 C 202 MET SER MET LYS ASP ILE GLY ILE MET ASP GLY ASP LEU SEQRES 11 C 202 LEU ALA VAL HIS LYS THR GLN ASP VAL ARG ASN GLY GLN SEQRES 12 C 202 VAL VAL VAL ALA ARG ILE ASP ASP GLU VAL THR VAL LYS SEQRES 13 C 202 ARG LEU LYS LYS GLN GLY ASN LYS VAL GLU LEU LEU PRO SEQRES 14 C 202 GLU ASN SER GLU PHE LYS PRO ILE VAL VAL ASP LEU ARG SEQRES 15 C 202 GLN GLN SER PHE THR ILE GLU GLY LEU ALA VAL GLY VAL SEQRES 16 C 202 ILE ARG ASN GLY ASP TRP LEU SEQRES 1 E 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 E 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 E 132 SER ILE PHE SER ILE ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 E 132 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 E 132 ARG ARG GLY SER THR ASN TYR ALA ASP PHE VAL LYS GLY SEQRES 6 E 132 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 E 132 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 E 132 VAL TYR TYR CYS LYS ALA ARG ILE GLU PRO ASP SER SER SEQRES 9 E 132 TRP GLY THR GLU TYR GLU TYR TRP GLY GLN GLY THR GLN SEQRES 10 E 132 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 11 E 132 GLU ALA SEQRES 1 G 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 G 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 G 132 SER ILE PHE SER ILE ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 G 132 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 G 132 ARG ARG GLY SER THR ASN TYR ALA ASP PHE VAL LYS GLY SEQRES 6 G 132 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 G 132 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 G 132 VAL TYR TYR CYS LYS ALA ARG ILE GLU PRO ASP SER SER SEQRES 9 G 132 TRP GLY THR GLU TYR GLU TYR TRP GLY GLN GLY THR GLN SEQRES 10 G 132 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 11 G 132 GLU ALA SEQRES 1 B 202 MET LYS ALA LEU THR ALA ARG GLN GLN GLU VAL PHE ASP SEQRES 2 B 202 LEU ILE ARG ASP HIS ILE SER GLN THR GLY MET PRO PRO SEQRES 3 B 202 THR ARG ALA GLU ILE ALA GLN ARG LEU GLY PHE ARG SER SEQRES 4 B 202 PRO ASN ALA ALA GLU GLU HIS LEU LYS ALA LEU ALA ARG SEQRES 5 B 202 LYS GLY VAL ILE GLU ILE VAL SER GLY ALA SER ARG GLY SEQRES 6 B 202 ILE ARG LEU LEU GLN GLU GLU GLU GLU GLY LEU PRO LEU SEQRES 7 B 202 VAL GLY ARG VAL ALA ALA GLY GLU PRO LEU LEU ALA GLN SEQRES 8 B 202 GLN HIS ILE GLU GLY HIS TYR GLN VAL ASP PRO SER LEU SEQRES 9 B 202 PHE LYS PRO ASN ALA ASP PHE LEU LEU ARG VAL SER GLY SEQRES 10 B 202 MET SER MET LYS ASP ILE GLY ILE MET ASP GLY ASP LEU SEQRES 11 B 202 LEU ALA VAL HIS LYS THR GLN ASP VAL ARG ASN GLY GLN SEQRES 12 B 202 VAL VAL VAL ALA ARG ILE ASP ASP GLU VAL THR VAL LYS SEQRES 13 B 202 ARG LEU LYS LYS GLN GLY ASN LYS VAL GLU LEU LEU PRO SEQRES 14 B 202 GLU ASN SER GLU PHE LYS PRO ILE VAL VAL ASP LEU ARG SEQRES 15 B 202 GLN GLN SER PHE THR ILE GLU GLY LEU ALA VAL GLY VAL SEQRES 16 B 202 ILE ARG ASN GLY ASP TRP LEU SEQRES 1 D 202 MET LYS ALA LEU THR ALA ARG GLN GLN GLU VAL PHE ASP SEQRES 2 D 202 LEU ILE ARG ASP HIS ILE SER GLN THR GLY MET PRO PRO SEQRES 3 D 202 THR ARG ALA GLU ILE ALA GLN ARG LEU GLY PHE ARG SER SEQRES 4 D 202 PRO ASN ALA ALA GLU GLU HIS LEU LYS ALA LEU ALA ARG SEQRES 5 D 202 LYS GLY VAL ILE GLU ILE VAL SER GLY ALA SER ARG GLY SEQRES 6 D 202 ILE ARG LEU LEU GLN GLU GLU GLU GLU GLY LEU PRO LEU SEQRES 7 D 202 VAL GLY ARG VAL ALA ALA GLY GLU PRO LEU LEU ALA GLN SEQRES 8 D 202 GLN HIS ILE GLU GLY HIS TYR GLN VAL ASP PRO SER LEU SEQRES 9 D 202 PHE LYS PRO ASN ALA ASP PHE LEU LEU ARG VAL SER GLY SEQRES 10 D 202 MET SER MET LYS ASP ILE GLY ILE MET ASP GLY ASP LEU SEQRES 11 D 202 LEU ALA VAL HIS LYS THR GLN ASP VAL ARG ASN GLY GLN SEQRES 12 D 202 VAL VAL VAL ALA ARG ILE ASP ASP GLU VAL THR VAL LYS SEQRES 13 D 202 ARG LEU LYS LYS GLN GLY ASN LYS VAL GLU LEU LEU PRO SEQRES 14 D 202 GLU ASN SER GLU PHE LYS PRO ILE VAL VAL ASP LEU ARG SEQRES 15 D 202 GLN GLN SER PHE THR ILE GLU GLY LEU ALA VAL GLY VAL SEQRES 16 D 202 ILE ARG ASN GLY ASP TRP LEU SEQRES 1 F 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 F 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 132 SER ILE PHE SER ILE ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 F 132 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 F 132 ARG ARG GLY SER THR ASN TYR ALA ASP PHE VAL LYS GLY SEQRES 6 F 132 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 F 132 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 F 132 VAL TYR TYR CYS LYS ALA ARG ILE GLU PRO ASP SER SER SEQRES 9 F 132 TRP GLY THR GLU TYR GLU TYR TRP GLY GLN GLY THR GLN SEQRES 10 F 132 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 11 F 132 GLU ALA SEQRES 1 H 132 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY SER VAL GLN SEQRES 2 H 132 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 H 132 SER ILE PHE SER ILE ASN ALA MET GLY TRP TYR ARG GLN SEQRES 4 H 132 ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 H 132 ARG ARG GLY SER THR ASN TYR ALA ASP PHE VAL LYS GLY SEQRES 6 H 132 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 H 132 TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 H 132 VAL TYR TYR CYS LYS ALA ARG ILE GLU PRO ASP SER SER SEQRES 9 H 132 TRP GLY THR GLU TYR GLU TYR TRP GLY GLN GLY THR GLN SEQRES 10 H 132 VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS GLU PRO SEQRES 11 H 132 GLU ALA HET EDO A 301 4 HET EDO C 301 4 HET EDO C 302 4 HETNAM EDO 1,2-ETHANEDIOL HETSYN EDO ETHYLENE GLYCOL FORMUL 9 EDO 3(C2 H6 O2) FORMUL 12 HOH *20(H2 O) HELIX 1 AA1 ALA A 90 GLN A 92 5 3 HELIX 2 AA2 ASP A 101 PHE A 105 5 5 HELIX 3 AA3 MET A 120 GLY A 124 5 5 HELIX 4 AA4 ALA C 90 GLN C 92 5 3 HELIX 5 AA5 ASP C 101 PHE C 105 5 5 HELIX 6 AA6 LYS E 86 THR E 90 5 5 HELIX 7 AA7 LYS G 86 THR G 90 5 5 HELIX 8 AA8 ALA B 90 GLN B 92 5 3 HELIX 9 AA9 ASP B 101 PHE B 105 5 5 HELIX 10 AB1 MET B 120 GLY B 124 5 5 HELIX 11 AB2 ALA D 90 GLN D 92 5 3 HELIX 12 AB3 ASP D 101 PHE D 105 5 5 HELIX 13 AB4 LYS F 86 THR F 90 5 5 HELIX 14 AB5 LYS H 86 THR H 90 5 5 SHEET 1 AA130 LEU A 76 VAL A 79 0 SHEET 2 AA130 ILE A 94 TYR A 98 -1 O TYR A 98 N LEU A 76 SHEET 3 AA130 PHE A 111 ARG A 114 1 O LEU A 112 N VAL A 79 SHEET 4 AA130 LEU A 130 HIS A 134 -1 O LEU A 131 N LEU A 113 SHEET 5 AA130 VAL A 144 ILE A 149 0 SHEET 6 AA130 VAL A 153 GLN A 161 -1 O LYS A 156 N VAL A 145 SHEET 7 AA130 LYS A 164 LEU A 168 -1 O LYS A 164 N GLN A 161 SHEET 8 AA130 ILE A 177 ASP A 180 -1 O ILE A 177 N LEU A 167 SHEET 9 AA130 PHE A 186 ARG A 197 -1 O ALA A 192 N VAL A 144 SHEET 10 AA130 LEU C 76 VAL C 79 0 SHEET 11 AA130 ILE C 94 TYR C 98 -1 O GLU C 95 N LEU C 78 SHEET 12 AA130 PHE C 111 ARG C 114 1 O LEU C 112 N VAL C 79 SHEET 13 AA130 LEU C 130 HIS C 134 -1 O LEU C 131 N LEU C 113 SHEET 14 AA130 VAL C 144 ILE C 149 0 SHEET 15 AA130 VAL C 153 GLN C 161 -1 O THR C 154 N ALA C 147 SHEET 16 AA130 LYS C 164 LEU C 168 -1 O LEU C 168 N ARG C 157 SHEET 17 AA130 ILE C 177 ASP C 180 -1 O VAL C 179 N VAL C 165 SHEET 18 AA130 PHE C 186 ARG C 197 -1 O ALA C 192 N VAL C 144 SHEET 19 AA130 GLY E 10 SER E 11 0 SHEET 20 AA130 ILE E 28 GLN E 39 0 SHEET 21 AA130 ARG E 45 THR E 52 -1 O GLU E 46 N ARG E 38 SHEET 22 AA130 THR E 57 TYR E 59 -1 O ASN E 58 N ALA E 50 SHEET 23 AA130 ALA E 91 PRO E 101 -1 O GLU E 100 N SER E 30 SHEET 24 AA130 TYR E 109 TRP E 112 -1 O TYR E 111 N ALA E 97 SHEET 25 AA130 THR E 116 THR E 119 -1 O THR E 116 N TYR E 93 SHEET 26 AA130 ILE G 28 GLN G 39 0 SHEET 27 AA130 ARG G 45 THR G 52 -1 O VAL G 48 N TRP G 36 SHEET 28 AA130 THR G 57 TYR G 59 -1 O ASN G 58 N ALA G 50 SHEET 29 AA130 CYS G 95 PRO G 101 -1 O GLU G 100 N SER G 30 SHEET 30 AA130 TYR G 109 TRP G 112 -1 O TYR G 111 N ALA G 97 SHEET 1 AA2 4 VAL E 2 SER E 7 0 SHEET 2 AA2 4 GLY E 15 GLY E 26 -1 O ALA E 23 N VAL E 5 SHEET 3 AA2 4 THR E 77 LEU E 85 -1 O MET E 82 N LEU E 18 SHEET 4 AA2 4 PHE E 67 ASP E 72 -1 N THR E 68 O GLN E 81 SHEET 1 AA3 4 VAL G 2 GLY G 8 0 SHEET 2 AA3 4 LEU G 18 GLY G 26 -1 O ALA G 23 N VAL G 5 SHEET 3 AA3 4 THR G 77 MET G 82 -1 O VAL G 78 N CYS G 22 SHEET 4 AA3 4 PHE G 67 ASP G 72 -1 N ASP G 72 O THR G 77 SHEET 1 AA4 3 GLY G 10 GLN G 13 0 SHEET 2 AA4 3 THR G 116 SER G 121 1 O THR G 119 N GLY G 10 SHEET 3 AA4 3 ALA G 91 TYR G 93 -1 N TYR G 93 O THR G 116 SHEET 1 AA523 LEU B 76 VAL B 79 0 SHEET 2 AA523 ILE B 94 TYR B 98 -1 O TYR B 98 N LEU B 76 SHEET 3 AA523 PHE B 111 ARG B 114 1 O LEU B 112 N VAL B 79 SHEET 4 AA523 LEU B 130 HIS B 134 -1 O LEU B 131 N LEU B 113 SHEET 5 AA523 VAL B 144 ILE B 149 0 SHEET 6 AA523 VAL B 153 GLN B 161 -1 O LYS B 156 N VAL B 145 SHEET 7 AA523 LYS B 164 LEU B 168 -1 O LYS B 164 N GLN B 161 SHEET 8 AA523 ILE B 177 ASP B 180 -1 O ILE B 177 N LEU B 167 SHEET 9 AA523 PHE B 186 ARG B 197 -1 O ALA B 192 N VAL B 144 SHEET 10 AA523 LEU D 76 VAL D 79 0 SHEET 11 AA523 ILE D 94 TYR D 98 -1 O GLU D 95 N LEU D 78 SHEET 12 AA523 PHE D 111 ARG D 114 1 O LEU D 112 N PRO D 77 SHEET 13 AA523 LEU D 130 HIS D 134 -1 O LEU D 131 N LEU D 113 SHEET 14 AA523 VAL D 144 ILE D 149 0 SHEET 15 AA523 GLU D 152 GLN D 161 -1 O GLU D 152 N ILE D 149 SHEET 16 AA523 LYS D 164 LEU D 168 -1 O LEU D 168 N ARG D 157 SHEET 17 AA523 ILE D 177 ASP D 180 -1 O VAL D 179 N VAL D 165 SHEET 18 AA523 PHE D 186 ARG D 197 -1 O ALA D 192 N VAL D 144 SHEET 19 AA523 ILE H 28 GLN H 39 0 SHEET 20 AA523 ARG H 45 THR H 52 -1 O VAL H 48 N TRP H 36 SHEET 21 AA523 THR H 57 TYR H 59 -1 O ASN H 58 N ALA H 50 SHEET 22 AA523 CYS H 95 PRO H 101 -1 O GLU H 100 N SER H 30 SHEET 23 AA523 TYR H 109 TRP H 112 -1 O TYR H 111 N ALA H 97 SHEET 1 AA6 4 VAL F 2 SER F 7 0 SHEET 2 AA6 4 GLY F 15 GLY F 26 -1 O ALA F 23 N VAL F 5 SHEET 3 AA6 4 THR F 77 LEU F 85 -1 O MET F 82 N LEU F 18 SHEET 4 AA6 4 PHE F 67 ASP F 72 -1 N ASP F 72 O THR F 77 SHEET 1 AA7 7 GLY F 10 VAL F 12 0 SHEET 2 AA7 7 ILE F 28 GLN F 39 0 SHEET 3 AA7 7 ARG F 45 THR F 52 -1 O GLU F 46 N ARG F 38 SHEET 4 AA7 7 THR F 57 TYR F 59 -1 O ASN F 58 N ALA F 50 SHEET 5 AA7 7 ALA F 91 PRO F 101 -1 O VAL F 92 N GLN F 39 SHEET 6 AA7 7 TYR F 109 TRP F 112 -1 O TYR F 111 N ALA F 97 SHEET 7 AA7 7 THR F 116 VAL F 120 -1 O THR F 116 N TYR F 93 SHEET 1 AA8 4 VAL H 2 GLY H 8 0 SHEET 2 AA8 4 LEU H 18 GLY H 26 -1 O SER H 25 N GLN H 3 SHEET 3 AA8 4 THR H 77 MET H 82 -1 O VAL H 78 N CYS H 22 SHEET 4 AA8 4 PHE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA9 3 GLY H 10 GLN H 13 0 SHEET 2 AA9 3 THR H 116 SER H 121 1 O THR H 119 N GLY H 10 SHEET 3 AA9 3 ALA H 91 TYR H 93 -1 N TYR H 93 O THR H 116 SSBOND 1 CYS E 22 CYS E 95 1555 1555 2.03 SSBOND 2 CYS G 22 CYS G 95 1555 1555 2.05 SSBOND 3 CYS F 22 CYS F 95 1555 1555 2.04 SSBOND 4 CYS H 22 CYS H 95 1555 1555 2.03 CISPEP 1 LYS A 106 PRO A 107 0 -4.34 CISPEP 2 LYS C 106 PRO C 107 0 -5.35 CISPEP 3 LYS B 106 PRO B 107 0 -4.20 CISPEP 4 LYS D 106 PRO D 107 0 -3.54 CRYST1 59.918 110.750 231.796 90.00 90.00 90.00 P 21 21 21 16 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 0.016689 0.000000 0.000000 0.00000 SCALE2 0.000000 0.009029 0.000000 0.00000 SCALE3 0.000000 0.000000 0.004314 0.00000