HEADER LYASE 03-NOV-11 3UGV
TITLE CRYSTAL STRUCTURE OF AN ENOLASE FROM ALPHA PRETOBACTERIUM BAL199 (EFI
TITLE 2 TARGET EFI-501650) WITH BOUND MG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENOLASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ALPHA PROTEOBACTERIUM BAL199;
SOURCE 3 ORGANISM_TAXID: 331869;
SOURCE 4 GENE: BAL199_22462;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS ENOLASE, ENZYME FUNCTION INITIATIVE, EFI, LYASE, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR M.W.VETTING,R.TORO,R.BHOSLE,S.R.WASSERMAN,L.L.MORISCO,B.HILLERICH,
AUTHOR 2 E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,J.HAMMONDS,
AUTHOR 3 W.D.ZENCHECK,H.J.IMKER,J.A.GERLT,S.C.ALMO,ENZYME FUNCTION INITIATIVE
AUTHOR 4 (EFI)
REVDAT 4 13-SEP-23 3UGV 1 REMARK SEQADV LINK
REVDAT 3 24-JAN-18 3UGV 1 JRNL
REVDAT 2 22-FEB-12 3UGV 1
REVDAT 1 23-NOV-11 3UGV 0
JRNL AUTH M.W.VETTING,R.TORO,R.BHOSLE,S.R.WASSERMAN,L.L.MORISCO,
JRNL AUTH 2 B.HILLERICH,E.WASHINGTON,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,
JRNL AUTH 3 J.HAMMONDS,W.D.ZENCHECK,H.J.IMKER,J.A.GERLT,S.C.ALMO,
JRNL AUTH 4 ENZYME FUNCTION INITIATIVE (EFI)
JRNL TITL CRYSTAL STRUCTURE OF AN ENOLASE FROM ALPHA PRETOBACTERIUM
JRNL TITL 2 BAL199 (EFI TARGET EFI-501650) WITH BOUND MG
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 114.64
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 166037
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.161
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.970
REMARK 3 FREE R VALUE TEST SET COUNT : 8248
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1114.7848 - 7.1461 0.92 5581 309 0.1514 0.1648
REMARK 3 2 7.1461 - 5.6721 0.98 5709 328 0.1369 0.1877
REMARK 3 3 5.6721 - 4.9551 0.98 5696 311 0.1307 0.1766
REMARK 3 4 4.9551 - 4.5020 0.98 5631 306 0.1109 0.1532
REMARK 3 5 4.5020 - 4.1793 0.98 5677 286 0.1177 0.1630
REMARK 3 6 4.1793 - 3.9329 0.98 5599 301 0.1235 0.1571
REMARK 3 7 3.9329 - 3.7359 0.98 5597 280 0.1317 0.1583
REMARK 3 8 3.7359 - 3.5733 0.98 5581 320 0.1421 0.1907
REMARK 3 9 3.5733 - 3.4357 0.98 5544 314 0.1562 0.1929
REMARK 3 10 3.4357 - 3.3172 0.97 5475 300 0.1630 0.1940
REMARK 3 11 3.3172 - 3.2134 0.96 5488 278 0.1637 0.2196
REMARK 3 12 3.2134 - 3.1216 0.96 5497 271 0.1707 0.2132
REMARK 3 13 3.1216 - 3.0394 0.96 5430 294 0.1744 0.2402
REMARK 3 14 3.0394 - 2.9652 0.95 5405 276 0.1740 0.2110
REMARK 3 15 2.9652 - 2.8978 0.95 5383 300 0.1773 0.2489
REMARK 3 16 2.8978 - 2.8361 0.93 5328 244 0.1815 0.2298
REMARK 3 17 2.8361 - 2.7794 0.93 5257 282 0.1808 0.2530
REMARK 3 18 2.7794 - 2.7269 0.92 5227 271 0.1860 0.2564
REMARK 3 19 2.7269 - 2.6782 0.91 5175 270 0.1972 0.2727
REMARK 3 20 2.6782 - 2.6328 0.90 5081 239 0.1946 0.2614
REMARK 3 21 2.6328 - 2.5904 0.89 5069 240 0.2010 0.2691
REMARK 3 22 2.5904 - 2.5505 0.89 5073 269 0.2000 0.2752
REMARK 3 23 2.5505 - 2.5130 0.87 4918 250 0.2086 0.2811
REMARK 3 24 2.5130 - 2.4776 0.88 5000 234 0.2153 0.2604
REMARK 3 25 2.4776 - 2.4441 0.85 4863 248 0.2182 0.2850
REMARK 3 26 2.4441 - 2.4124 0.85 4795 244 0.2258 0.2945
REMARK 3 27 2.4124 - 2.3822 0.85 4803 251 0.2238 0.3055
REMARK 3 28 2.3822 - 2.3535 0.83 4697 247 0.2426 0.3103
REMARK 3 29 2.3535 - 2.3261 0.82 4632 241 0.2500 0.3238
REMARK 3 30 2.3261 - 2.3000 0.81 4578 244 0.2496 0.3190
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 34.09
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.970
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.74030
REMARK 3 B22 (A**2) : 1.87420
REMARK 3 B33 (A**2) : -2.61450
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.012 23048
REMARK 3 ANGLE : 1.054 31539
REMARK 3 CHIRALITY : 0.070 3443
REMARK 3 PLANARITY : 0.005 4065
REMARK 3 DIHEDRAL : 13.667 8334
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 4:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 90.1683 106.3253 116.8793
REMARK 3 T TENSOR
REMARK 3 T11: 0.0782 T22: 0.2072
REMARK 3 T33: 0.2251 T12: 0.0829
REMARK 3 T13: -0.0002 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 0.0179 L22: 0.0051
REMARK 3 L33: 0.0046 L12: 0.0070
REMARK 3 L13: 0.0012 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0088 S12: -0.0257 S13: 0.0160
REMARK 3 S21: 0.0023 S22: -0.0024 S23: 0.0325
REMARK 3 S31: -0.0157 S32: -0.0425 S33: -0.0023
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 120:316)
REMARK 3 ORIGIN FOR THE GROUP (A): 98.4862 91.3875 100.5480
REMARK 3 T TENSOR
REMARK 3 T11: 0.0418 T22: 0.1418
REMARK 3 T33: 0.0461 T12: -0.0208
REMARK 3 T13: -0.0809 T23: 0.0607
REMARK 3 L TENSOR
REMARK 3 L11: 0.0194 L22: 0.0163
REMARK 3 L33: 0.0163 L12: 0.0132
REMARK 3 L13: -0.0143 L23: -0.0058
REMARK 3 S TENSOR
REMARK 3 S11: 0.0171 S12: 0.0733 S13: 0.0101
REMARK 3 S21: -0.0450 S22: 0.0252 S23: 0.0519
REMARK 3 S31: 0.0212 S32: -0.0820 S33: 0.0607
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 317:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 94.5798 109.8356 101.4492
REMARK 3 T TENSOR
REMARK 3 T11: 0.0688 T22: 0.1136
REMARK 3 T33: 0.1303 T12: 0.0714
REMARK 3 T13: -0.0318 T23: 0.0340
REMARK 3 L TENSOR
REMARK 3 L11: 0.0001 L22: 0.0104
REMARK 3 L33: 0.0208 L12: -0.0000
REMARK 3 L13: 0.0007 L23: -0.0142
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: -0.0008 S13: 0.0221
REMARK 3 S21: -0.0108 S22: 0.0003 S23: 0.0216
REMARK 3 S31: -0.0157 S32: -0.0184 S33: -0.0122
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 4:139)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.2791 50.8878 121.2141
REMARK 3 T TENSOR
REMARK 3 T11: 0.2529 T22: 0.2885
REMARK 3 T33: 0.2831 T12: -0.2386
REMARK 3 T13: 0.0287 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.0507 L22: 0.0385
REMARK 3 L33: 0.0017 L12: 0.0365
REMARK 3 L13: -0.0017 L23: -0.0069
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: 0.0076 S13: 0.0123
REMARK 3 S21: 0.0240 S22: -0.0031 S23: 0.0578
REMARK 3 S31: 0.0429 S32: -0.0412 S33: -0.0088
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 140:316)
REMARK 3 ORIGIN FOR THE GROUP (A): 91.5284 58.4443 103.1355
REMARK 3 T TENSOR
REMARK 3 T11: 0.1782 T22: 0.2160
REMARK 3 T33: 0.1455 T12: -0.1672
REMARK 3 T13: -0.0530 T23: -0.0445
REMARK 3 L TENSOR
REMARK 3 L11: 0.0208 L22: 0.0275
REMARK 3 L33: 0.0057 L12: 0.0084
REMARK 3 L13: 0.0026 L23: -0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0011 S12: 0.0337 S13: -0.0519
REMARK 3 S21: -0.0560 S22: 0.0320 S23: 0.0362
REMARK 3 S31: 0.0445 S32: -0.0347 S33: 0.0261
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 317:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.0038 55.2141 109.1644
REMARK 3 T TENSOR
REMARK 3 T11: 0.1761 T22: 0.2586
REMARK 3 T33: 0.2230 T12: -0.1654
REMARK 3 T13: -0.0311 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.0070 L22: 0.0006
REMARK 3 L33: 0.0054 L12: 0.0019
REMARK 3 L13: 0.0062 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: -0.0042 S12: 0.0097 S13: 0.0079
REMARK 3 S21: -0.0018 S22: -0.0023 S23: 0.0137
REMARK 3 S31: 0.0058 S32: -0.0066 S33: -0.0026
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 4:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 137.5740 35.7140 102.4518
REMARK 3 T TENSOR
REMARK 3 T11: 0.5590 T22: 0.3789
REMARK 3 T33: 0.4633 T12: 0.1418
REMARK 3 T13: 0.0909 T23: 0.0459
REMARK 3 L TENSOR
REMARK 3 L11: 0.0133 L22: 0.0934
REMARK 3 L33: 0.0111 L12: 0.0079
REMARK 3 L13: 0.0024 L23: -0.0193
REMARK 3 S TENSOR
REMARK 3 S11: -0.0122 S12: -0.0093 S13: -0.0083
REMARK 3 S21: -0.0019 S22: 0.0031 S23: 0.0267
REMARK 3 S31: 0.0113 S32: 0.0117 S33: -0.0013
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESSEQ 43:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 125.5296 44.0166 102.4465
REMARK 3 T TENSOR
REMARK 3 T11: 0.3774 T22: 0.0665
REMARK 3 T33: 0.1904 T12: 0.0246
REMARK 3 T13: 0.0415 T23: -0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 0.0882 L22: 0.0103
REMARK 3 L33: 0.0467 L12: -0.0053
REMARK 3 L13: -0.0345 L23: -0.0071
REMARK 3 S TENSOR
REMARK 3 S11: -0.0758 S12: 0.0455 S13: -0.1737
REMARK 3 S21: -0.0511 S22: -0.0055 S23: 0.0267
REMARK 3 S31: 0.1859 S32: 0.0486 S33: -0.0557
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 4:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 145.9842 97.2665 97.4120
REMARK 3 T TENSOR
REMARK 3 T11: 0.2178 T22: 0.2359
REMARK 3 T33: 0.2791 T12: -0.0639
REMARK 3 T13: -0.0560 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.0119 L22: 0.0496
REMARK 3 L33: 0.0307 L12: 0.0185
REMARK 3 L13: 0.0009 L23: -0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0006 S12: -0.0156 S13: -0.0136
REMARK 3 S21: 0.0130 S22: -0.0192 S23: -0.0690
REMARK 3 S31: -0.0115 S32: 0.0228 S33: 0.0151
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 43:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 137.3735 85.3918 97.7827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0622 T22: 0.1104
REMARK 3 T33: 0.0687 T12: -0.0151
REMARK 3 T13: 0.0047 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.0373 L22: 0.1847
REMARK 3 L33: 0.0953 L12: -0.0272
REMARK 3 L13: -0.0329 L23: -0.0192
REMARK 3 S TENSOR
REMARK 3 S11: -0.0327 S12: 0.0624 S13: 0.0390
REMARK 3 S21: -0.0661 S22: 0.0041 S23: -0.1112
REMARK 3 S31: -0.0551 S32: 0.0557 S33: 0.0082
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 4:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 98.6289 33.5140 126.0874
REMARK 3 T TENSOR
REMARK 3 T11: 0.4664 T22: 0.1778
REMARK 3 T33: 0.3816 T12: -0.1562
REMARK 3 T13: 0.0537 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0071
REMARK 3 L33: 0.0034 L12: 0.0032
REMARK 3 L13: -0.0017 L23: -0.0047
REMARK 3 S TENSOR
REMARK 3 S11: -0.0240 S12: 0.0101 S13: -0.0472
REMARK 3 S21: -0.0211 S22: 0.0053 S23: -0.0066
REMARK 3 S31: 0.0579 S32: -0.0160 S33: 0.0010
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 120:267)
REMARK 3 ORIGIN FOR THE GROUP (A): 109.5771 51.9661 141.3185
REMARK 3 T TENSOR
REMARK 3 T11: 0.2267 T22: 0.1337
REMARK 3 T33: 0.1222 T12: 0.0019
REMARK 3 T13: 0.0461 T23: 0.0972
REMARK 3 L TENSOR
REMARK 3 L11: 0.0389 L22: 0.1118
REMARK 3 L33: 0.0371 L12: 0.0015
REMARK 3 L13: 0.0302 L23: -0.0297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.0816 S13: -0.0646
REMARK 3 S21: 0.0187 S22: -0.0279 S23: -0.0212
REMARK 3 S31: 0.0504 S32: 0.0041 S33: -0.0215
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'E' AND (RESSEQ 268:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 110.7363 37.6908 133.5808
REMARK 3 T TENSOR
REMARK 3 T11: 0.3036 T22: 0.0855
REMARK 3 T33: 0.2236 T12: -0.0352
REMARK 3 T13: 0.0304 T23: 0.0815
REMARK 3 L TENSOR
REMARK 3 L11: 0.0007 L22: 0.0186
REMARK 3 L33: 0.0124 L12: -0.0032
REMARK 3 L13: -0.0024 L23: 0.0146
REMARK 3 S TENSOR
REMARK 3 S11: -0.0050 S12: -0.0257 S13: -0.0505
REMARK 3 S21: 0.0114 S22: -0.0084 S23: 0.0016
REMARK 3 S31: 0.0429 S32: -0.0106 S33: -0.0126
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 4:119)
REMARK 3 ORIGIN FOR THE GROUP (A): 76.5849 88.3021 127.8196
REMARK 3 T TENSOR
REMARK 3 T11: 0.1544 T22: 0.3360
REMARK 3 T33: 0.2979 T12: 0.0192
REMARK 3 T13: -0.0351 T23: 0.0578
REMARK 3 L TENSOR
REMARK 3 L11: 0.0319 L22: 0.0420
REMARK 3 L33: 0.0663 L12: -0.0290
REMARK 3 L13: -0.0257 L23: 0.0023
REMARK 3 S TENSOR
REMARK 3 S11: -0.0370 S12: 0.0280 S13: 0.0007
REMARK 3 S21: -0.0245 S22: 0.0301 S23: 0.0808
REMARK 3 S31: -0.0200 S32: -0.1472 S33: 0.0025
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'F' AND (RESSEQ 120:367)
REMARK 3 ORIGIN FOR THE GROUP (A): 91.5005 80.6114 140.2482
REMARK 3 T TENSOR
REMARK 3 T11: 0.0715 T22: 0.1667
REMARK 3 T33: 0.0871 T12: -0.0180
REMARK 3 T13: 0.0364 T23: 0.0428
REMARK 3 L TENSOR
REMARK 3 L11: 0.0594 L22: 0.0827
REMARK 3 L33: 0.1496 L12: -0.0033
REMARK 3 L13: -0.0647 L23: -0.0198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0223 S12: -0.0042 S13: 0.0075
REMARK 3 S21: 0.0782 S22: 0.0679 S23: 0.0953
REMARK 3 S31: -0.0240 S32: -0.0886 S33: 0.0150
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'G' AND (RESSEQ 4:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 134.9765 111.7115 123.0168
REMARK 3 T TENSOR
REMARK 3 T11: 0.1934 T22: 0.2018
REMARK 3 T33: 0.2280 T12: -0.0478
REMARK 3 T13: -0.0176 T23: 0.0115
REMARK 3 L TENSOR
REMARK 3 L11: 0.0218 L22: 0.0080
REMARK 3 L33: 0.0051 L12: 0.0100
REMARK 3 L13: -0.0084 L23: -0.0011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: 0.0127 S13: 0.0332
REMARK 3 S21: -0.0036 S22: 0.0097 S23: 0.0088
REMARK 3 S31: -0.0021 S32: 0.0046 S33: -0.0029
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'G' AND (RESSEQ 43:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 125.6096 101.3832 127.4432
REMARK 3 T TENSOR
REMARK 3 T11: 0.0881 T22: 0.1008
REMARK 3 T33: 0.0846 T12: -0.0121
REMARK 3 T13: -0.0157 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 0.1792 L22: 0.0904
REMARK 3 L33: 0.0890 L12: 0.0367
REMARK 3 L13: -0.0182 L23: -0.0081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0472 S12: -0.0083 S13: 0.0893
REMARK 3 S21: 0.0576 S22: 0.0218 S23: -0.0323
REMARK 3 S31: -0.0270 S32: 0.1058 S33: 0.0049
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 4:42)
REMARK 3 ORIGIN FOR THE GROUP (A): 155.0483 52.7165 122.0352
REMARK 3 T TENSOR
REMARK 3 T11: 0.2162 T22: 0.2331
REMARK 3 T33: 0.2543 T12: 0.1480
REMARK 3 T13: 0.0288 T23: 0.0245
REMARK 3 L TENSOR
REMARK 3 L11: 0.0017 L22: 0.0030
REMARK 3 L33: 0.0007 L12: -0.0027
REMARK 3 L13: -0.0009 L23: 0.0014
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: 0.0116 S13: -0.0063
REMARK 3 S21: -0.0060 S22: 0.0035 S23: -0.0110
REMARK 3 S31: 0.0084 S32: 0.0115 S33: -0.0024
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'H' AND (RESSEQ 43:366)
REMARK 3 ORIGIN FOR THE GROUP (A): 145.2301 62.8204 125.4105
REMARK 3 T TENSOR
REMARK 3 T11: 0.0618 T22: 0.1050
REMARK 3 T33: 0.0899 T12: 0.1472
REMARK 3 T13: -0.0472 T23: 0.0236
REMARK 3 L TENSOR
REMARK 3 L11: 0.0480 L22: 0.0340
REMARK 3 L33: 0.0361 L12: -0.0266
REMARK 3 L13: 0.0082 L23: -0.0093
REMARK 3 S TENSOR
REMARK 3 S11: -0.0217 S12: -0.0480 S13: -0.0428
REMARK 3 S21: 0.0363 S22: 0.0188 S23: -0.0729
REMARK 3 S31: 0.0781 S32: 0.0725 S33: 0.0048
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 3UGV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068738.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 175465
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 173.535
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : 0.07700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.48100
REMARK 200 R SYM FOR SHELL (I) : 0.48100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 1MDR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (10 MM HEPES, PH 7.8, 150 MM
REMARK 280 NACL, 10% GLYCEROL, 5 MM DTT, 5 MM MGCL2); RESERVOIR (200 MM
REMARK 280 MGACETATE, 100 MM NACAC PH 6.5, 30% MPD); CRYOPROTECTION
REMARK 280 (RESERVOIR), VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K, PH
REMARK 280 4.6
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 76.35550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.76750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 76.49200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.76750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 76.35550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 76.49200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -312.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, 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 -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 SER A -15
REMARK 465 SER A -14
REMARK 465 GLY A -13
REMARK 465 VAL A -12
REMARK 465 ASP A -11
REMARK 465 LEU A -10
REMARK 465 GLY A -9
REMARK 465 THR A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 SER A -1
REMARK 465 MET A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 GLN A 3
REMARK 465 GLU A 367
REMARK 465 MET B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 SER B -15
REMARK 465 SER B -14
REMARK 465 GLY B -13
REMARK 465 VAL B -12
REMARK 465 ASP B -11
REMARK 465 LEU B -10
REMARK 465 GLY B -9
REMARK 465 THR B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 SER B -1
REMARK 465 MET B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLN B 3
REMARK 465 GLU B 367
REMARK 465 MET C -22
REMARK 465 HIS C -21
REMARK 465 HIS C -20
REMARK 465 HIS C -19
REMARK 465 HIS C -18
REMARK 465 HIS C -17
REMARK 465 HIS C -16
REMARK 465 SER C -15
REMARK 465 SER C -14
REMARK 465 GLY C -13
REMARK 465 VAL C -12
REMARK 465 ASP C -11
REMARK 465 LEU C -10
REMARK 465 GLY C -9
REMARK 465 THR C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 SER C -1
REMARK 465 MET C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLN C 3
REMARK 465 GLU C 367
REMARK 465 MET D -22
REMARK 465 HIS D -21
REMARK 465 HIS D -20
REMARK 465 HIS D -19
REMARK 465 HIS D -18
REMARK 465 HIS D -17
REMARK 465 HIS D -16
REMARK 465 SER D -15
REMARK 465 SER D -14
REMARK 465 GLY D -13
REMARK 465 VAL D -12
REMARK 465 ASP D -11
REMARK 465 LEU D -10
REMARK 465 GLY D -9
REMARK 465 THR D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 SER D -1
REMARK 465 MET D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLN D 3
REMARK 465 GLU D 367
REMARK 465 MET E -22
REMARK 465 HIS E -21
REMARK 465 HIS E -20
REMARK 465 HIS E -19
REMARK 465 HIS E -18
REMARK 465 HIS E -17
REMARK 465 HIS E -16
REMARK 465 SER E -15
REMARK 465 SER E -14
REMARK 465 GLY E -13
REMARK 465 VAL E -12
REMARK 465 ASP E -11
REMARK 465 LEU E -10
REMARK 465 GLY E -9
REMARK 465 THR E -8
REMARK 465 GLU E -7
REMARK 465 ASN E -6
REMARK 465 LEU E -5
REMARK 465 TYR E -4
REMARK 465 PHE E -3
REMARK 465 GLN E -2
REMARK 465 SER E -1
REMARK 465 MET E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 GLN E 3
REMARK 465 GLU E 367
REMARK 465 MET F -22
REMARK 465 HIS F -21
REMARK 465 HIS F -20
REMARK 465 HIS F -19
REMARK 465 HIS F -18
REMARK 465 HIS F -17
REMARK 465 HIS F -16
REMARK 465 SER F -15
REMARK 465 SER F -14
REMARK 465 GLY F -13
REMARK 465 VAL F -12
REMARK 465 ASP F -11
REMARK 465 LEU F -10
REMARK 465 GLY F -9
REMARK 465 THR F -8
REMARK 465 GLU F -7
REMARK 465 ASN F -6
REMARK 465 LEU F -5
REMARK 465 TYR F -4
REMARK 465 PHE F -3
REMARK 465 GLN F -2
REMARK 465 SER F -1
REMARK 465 MET F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLN F 3
REMARK 465 MET G -22
REMARK 465 HIS G -21
REMARK 465 HIS G -20
REMARK 465 HIS G -19
REMARK 465 HIS G -18
REMARK 465 HIS G -17
REMARK 465 HIS G -16
REMARK 465 SER G -15
REMARK 465 SER G -14
REMARK 465 GLY G -13
REMARK 465 VAL G -12
REMARK 465 ASP G -11
REMARK 465 LEU G -10
REMARK 465 GLY G -9
REMARK 465 THR G -8
REMARK 465 GLU G -7
REMARK 465 ASN G -6
REMARK 465 LEU G -5
REMARK 465 TYR G -4
REMARK 465 PHE G -3
REMARK 465 GLN G -2
REMARK 465 SER G -1
REMARK 465 MET G 0
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 GLN G 3
REMARK 465 GLU G 367
REMARK 465 MET H -22
REMARK 465 HIS H -21
REMARK 465 HIS H -20
REMARK 465 HIS H -19
REMARK 465 HIS H -18
REMARK 465 HIS H -17
REMARK 465 HIS H -16
REMARK 465 SER H -15
REMARK 465 SER H -14
REMARK 465 GLY H -13
REMARK 465 VAL H -12
REMARK 465 ASP H -11
REMARK 465 LEU H -10
REMARK 465 GLY H -9
REMARK 465 THR H -8
REMARK 465 GLU H -7
REMARK 465 ASN H -6
REMARK 465 LEU H -5
REMARK 465 TYR H -4
REMARK 465 PHE H -3
REMARK 465 GLN H -2
REMARK 465 SER H -1
REMARK 465 MET H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLN H 3
REMARK 465 GLU H 367
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 473 O HOH A 694 2.19
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 PRO E 259 C - N - CA ANGL. DEV. = 9.4 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 ARG A 8 -62.71 -102.18
REMARK 500 TYR A 55 -55.38 71.38
REMARK 500 GLN A 163 152.53 75.64
REMARK 500 GLU A 229 70.05 24.91
REMARK 500 LEU A 305 -172.91 57.03
REMARK 500 ALA A 320 129.06 -37.38
REMARK 500 HIS A 321 -85.70 -116.23
REMARK 500 ILE B 27 -86.01 -64.55
REMARK 500 TYR B 55 -57.83 71.52
REMARK 500 SER B 147 155.43 -48.74
REMARK 500 GLN B 163 146.41 67.30
REMARK 500 GLU B 229 70.53 29.91
REMARK 500 MET B 275 81.72 -152.58
REMARK 500 LEU B 305 -168.93 60.54
REMARK 500 HIS B 321 -89.09 -119.61
REMARK 500 ARG C 8 -63.23 -103.28
REMARK 500 TYR C 55 -56.64 74.32
REMARK 500 TRP C 144 -168.63 -75.20
REMARK 500 GLN C 163 155.85 69.82
REMARK 500 GLU C 229 65.07 30.05
REMARK 500 LEU C 305 -172.49 50.83
REMARK 500 ALA C 320 129.84 -34.85
REMARK 500 HIS C 321 -91.25 -117.51
REMARK 500 ASP C 348 45.13 -91.84
REMARK 500 ARG D 8 -61.19 -100.38
REMARK 500 TYR D 55 -59.32 73.40
REMARK 500 TRP D 144 -167.91 -69.42
REMARK 500 LEU D 145 47.43 -84.79
REMARK 500 GLN D 163 156.65 70.27
REMARK 500 GLN D 205 18.21 59.06
REMARK 500 GLU D 229 69.98 27.65
REMARK 500 LEU D 305 -174.03 58.18
REMARK 500 HIS D 321 -86.99 -117.57
REMARK 500 ARG E 8 -66.22 -97.62
REMARK 500 TYR E 55 -49.44 72.41
REMARK 500 GLN E 163 154.02 68.08
REMARK 500 GLN E 205 19.99 58.57
REMARK 500 GLU E 229 68.07 37.73
REMARK 500 LEU E 305 -173.00 58.45
REMARK 500 HIS E 321 -86.19 -119.34
REMARK 500 LEU E 365 160.55 -49.29
REMARK 500 ARG F 8 -60.15 -97.55
REMARK 500 TYR F 55 -58.08 77.11
REMARK 500 TRP F 144 -169.63 -78.52
REMARK 500 LEU F 145 48.74 -82.78
REMARK 500 GLN F 163 154.09 72.30
REMARK 500 GLU F 229 66.99 36.90
REMARK 500 LEU F 305 -173.16 57.45
REMARK 500 HIS F 321 -83.41 -124.70
REMARK 500 ARG G 8 -63.75 -103.31
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
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 MG A 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 202 OD2
REMARK 620 2 GLU A 228 OE2 77.8
REMARK 620 3 GLU A 254 OE1 127.6 75.7
REMARK 620 4 HOH A 394 O 65.6 76.1 64.6
REMARK 620 5 HOH A 411 O 85.0 139.9 87.3 63.9
REMARK 620 6 HOH A 429 O 110.1 125.2 122.2 158.0 94.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 243 O
REMARK 620 2 LEU A 246 O 91.3
REMARK 620 3 HOH A 370 O 85.4 81.6
REMARK 620 4 HOH A 375 O 97.0 96.1 176.7
REMARK 620 5 HOH A 382 O 86.7 174.3 92.8 89.5
REMARK 620 6 HOH D 371 O 165.1 88.2 79.8 97.8 92.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 369 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 244 NE2
REMARK 620 2 HIS B 244 NE2 97.6
REMARK 620 3 HIS C 244 NE2 162.4 82.5
REMARK 620 4 HIS D 244 NE2 84.9 177.4 95.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 374 O
REMARK 620 2 ARG B 243 O 89.1
REMARK 620 3 LEU B 246 O 86.4 99.0
REMARK 620 4 HOH B 369 O 89.9 84.1 175.1
REMARK 620 5 HOH B 370 O 174.3 96.6 92.1 91.2
REMARK 620 6 HOH B 381 O 85.1 170.3 88.4 88.1 89.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 202 OD2
REMARK 620 2 GLU B 228 OE2 81.6
REMARK 620 3 GLU B 254 OE1 163.7 91.4
REMARK 620 4 HOH B 407 O 90.6 92.1 104.4
REMARK 620 5 HOH B 486 O 92.5 173.8 93.9 89.8
REMARK 620 6 HOH B 866 O 81.4 97.0 84.9 166.8 80.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 373 O
REMARK 620 2 HOH B 380 O 89.8
REMARK 620 3 ARG C 243 O 85.0 174.7
REMARK 620 4 LEU C 246 O 87.5 88.8 91.9
REMARK 620 5 HOH C 370 O 176.2 87.0 98.3 90.4
REMARK 620 6 HOH C 378 O 89.3 86.3 92.8 174.1 92.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 202 OD2
REMARK 620 2 GLU C 228 OE2 95.1
REMARK 620 3 GLU C 254 OE1 171.5 87.2
REMARK 620 4 HOH C 667 O 93.0 101.1 94.7
REMARK 620 5 HOH C 707 O 89.3 175.4 88.3 79.8
REMARK 620 6 HOH C 782 O 94.8 106.3 76.6 150.6 72.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C 368 O
REMARK 620 2 HOH C 369 O 84.4
REMARK 620 3 ARG D 243 O 83.1 166.5
REMARK 620 4 LEU D 246 O 88.6 93.2 91.5
REMARK 620 5 HOH D 369 O 171.8 98.4 94.6 83.6
REMARK 620 6 HOH D 372 O 90.8 85.5 89.6 178.6 97.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 202 OD2
REMARK 620 2 GLU D 228 OE2 83.8
REMARK 620 3 GLU D 254 OE1 164.9 86.7
REMARK 620 4 HOH D 381 O 91.3 172.8 97.0
REMARK 620 5 HOH D 401 O 78.6 92.2 90.1 81.7
REMARK 620 6 HOH D 415 O 96.6 104.3 97.1 81.4 162.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 202 OD2
REMARK 620 2 GLU E 228 OE2 75.0
REMARK 620 3 GLU E 254 OE1 145.7 76.0
REMARK 620 4 HOH E 386 O 77.2 70.3 76.1
REMARK 620 5 HOH E 726 O 96.4 107.8 109.7 173.5
REMARK 620 6 HOH E 836 O 101.4 157.3 98.3 87.0 94.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG E 243 O
REMARK 620 2 LEU E 246 O 92.3
REMARK 620 3 HOH E 370 O 88.2 82.1
REMARK 620 4 HOH E 371 O 76.5 167.9 92.7
REMARK 620 5 HOH H 370 O 81.8 94.0 169.2 89.1
REMARK 620 6 HOH H 446 O 169.5 95.1 100.1 96.6 90.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI F 368 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 244 NE2
REMARK 620 2 HIS F 244 NE2 92.9
REMARK 620 3 HIS G 244 NE2 149.4 86.1
REMARK 620 4 HIS H 244 NE2 82.6 156.8 86.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH E 369 O
REMARK 620 2 ARG F 243 O 86.5
REMARK 620 3 LEU F 246 O 96.2 96.5
REMARK 620 4 HOH F 370 O 82.8 168.7 88.3
REMARK 620 5 HOH F 372 O 171.3 95.9 91.8 94.1
REMARK 620 6 HOH F 379 O 86.0 86.4 176.4 89.3 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 202 OD2
REMARK 620 2 GLU F 228 OE2 80.6
REMARK 620 3 GLU F 254 OE1 152.5 85.1
REMARK 620 4 HOH F 407 O 105.7 107.6 100.9
REMARK 620 5 HOH F 418 O 95.5 170.9 95.0 81.4
REMARK 620 6 HOH F 419 O 78.7 86.4 77.1 165.8 84.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH F 369 O
REMARK 620 2 ARG G 243 O 166.5
REMARK 620 3 LEU G 246 O 90.4 89.0
REMARK 620 4 HOH G 368 O 97.3 96.2 90.1
REMARK 620 5 HOH G 370 O 84.0 82.6 81.3 171.3
REMARK 620 6 HOH G 381 O 92.1 86.9 172.2 96.9 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP G 202 OD2
REMARK 620 2 GLU G 228 OE2 79.3
REMARK 620 3 GLU G 254 OE1 159.1 80.8
REMARK 620 4 HOH G 409 O 95.9 97.6 93.0
REMARK 620 5 HOH G 429 O 105.5 174.7 94.7 79.7
REMARK 620 6 HOH G 438 O 82.8 99.6 94.3 162.2 83.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH G 373 O
REMARK 620 2 ARG H 243 O 93.3
REMARK 620 3 LEU H 246 O 83.9 88.6
REMARK 620 4 HOH H 368 O 165.3 88.2 81.5
REMARK 620 5 HOH H 372 O 106.8 92.1 169.2 87.8
REMARK 620 6 HOH H 385 O 92.7 172.9 88.3 85.0 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG H 500 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 202 OD2
REMARK 620 2 GLU H 228 OE2 71.9
REMARK 620 3 GLU H 254 OE1 130.5 72.0
REMARK 620 4 HOH H 403 O 103.4 153.1 94.2
REMARK 620 5 HOH H 423 O 70.8 74.5 67.7 79.0
REMARK 620 6 HOH H 846 O 104.4 101.6 115.2 105.1 174.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI F 368
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EFI-501650 RELATED DB: TARGETTRACK
DBREF 3UGV A 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV B 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV C 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV D 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV E 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV F 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV G 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
DBREF 3UGV H 1 367 UNP A8TYI5 A8TYI5_9PROT 1 367
SEQADV 3UGV MET A -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS A -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER A -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER A -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY A -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL A -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP A -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU A -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY A -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR A -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU A -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN A -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU A -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR A -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE A -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN A -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER A -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET A 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET B -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS B -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER B -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER B -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY B -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL B -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP B -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU B -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY B -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR B -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU B -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN B -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU B -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR B -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE B -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN B -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER B -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET B 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET C -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS C -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER C -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER C -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY C -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL C -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP C -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU C -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY C -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR C -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU C -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN C -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU C -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR C -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE C -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN C -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER C -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET C 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET D -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS D -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER D -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER D -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY D -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL D -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP D -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU D -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY D -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR D -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU D -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN D -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU D -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR D -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE D -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN D -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER D -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET D 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET E -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS E -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER E -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER E -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY E -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL E -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP E -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU E -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY E -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR E -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU E -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN E -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU E -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR E -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE E -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN E -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER E -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET E 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET F -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS F -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER F -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER F -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY F -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL F -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP F -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU F -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY F -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR F -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU F -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN F -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU F -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR F -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE F -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN F -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER F -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET F 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET G -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS G -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER G -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER G -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY G -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL G -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP G -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU G -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY G -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR G -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU G -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN G -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU G -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR G -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE G -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN G -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER G -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET G 0 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET H -22 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -21 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -20 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -19 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -18 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -17 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV HIS H -16 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER H -15 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER H -14 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY H -13 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV VAL H -12 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASP H -11 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU H -10 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLY H -9 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV THR H -8 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLU H -7 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV ASN H -6 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV LEU H -5 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV TYR H -4 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV PHE H -3 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV GLN H -2 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV SER H -1 UNP A8TYI5 EXPRESSION TAG
SEQADV 3UGV MET H 0 UNP A8TYI5 EXPRESSION TAG
SEQRES 1 A 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 A 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 A 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 A 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 A 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 A 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 A 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 A 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 A 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 A 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 A 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 A 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 A 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 A 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 A 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 A 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 A 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 A 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 A 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 A 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 A 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 A 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 A 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 A 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 A 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 A 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 A 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 A 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 A 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 B 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 B 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 B 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 B 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 B 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 B 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 B 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 B 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 B 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 B 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 B 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 B 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 B 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 B 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 B 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 B 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 B 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 B 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 B 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 B 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 B 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 B 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 B 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 B 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 B 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 B 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 B 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 B 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 B 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 C 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 C 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 C 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 C 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 C 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 C 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 C 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 C 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 C 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 C 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 C 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 C 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 C 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 C 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 C 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 C 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 C 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 C 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 C 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 C 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 C 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 C 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 C 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 C 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 C 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 C 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 C 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 C 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 C 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 C 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 D 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 D 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 D 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 D 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 D 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 D 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 D 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 D 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 D 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 D 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 D 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 D 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 D 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 D 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 D 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 D 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 D 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 D 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 D 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 D 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 D 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 D 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 D 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 D 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 D 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 D 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 D 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 D 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 D 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 D 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 E 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 E 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 E 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 E 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 E 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 E 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 E 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 E 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 E 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 E 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 E 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 E 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 E 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 E 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 E 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 E 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 E 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 E 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 E 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 E 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 E 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 E 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 E 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 E 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 E 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 E 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 E 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 E 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 E 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 E 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 F 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 F 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 F 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 F 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 F 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 F 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 F 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 F 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 F 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 F 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 F 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 F 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 F 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 F 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 F 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 F 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 F 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 F 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 F 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 F 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 F 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 F 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 F 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 F 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 F 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 F 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 F 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 F 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 F 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 F 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 G 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 G 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 G 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 G 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 G 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 G 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 G 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 G 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 G 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 G 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 G 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 G 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 G 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 G 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 G 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 G 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 G 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 G 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 G 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 G 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 G 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 G 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 G 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 G 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 G 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 G 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 G 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 G 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 G 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 G 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
SEQRES 1 H 390 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 H 390 GLY THR GLU ASN LEU TYR PHE GLN SER MET MET ALA GLN
SEQRES 3 H 390 THR LEU THR PHE ARG LYS LEU THR ALA ARG PRO VAL LEU
SEQRES 4 H 390 LEU LYS LEU GLN ARG PRO VAL THR ALA ARG ILE ALA THR
SEQRES 5 H 390 ILE PRO ASP TRP PRO LEU ILE LEU ILE ASP ILE GLU THR
SEQRES 6 H 390 GLU GLU GLY VAL PRO GLY ARG ALA TYR LEU GLU PRO TYR
SEQRES 7 H 390 VAL PRO LYS ALA MET LYS TYR LEU VAL PRO ALA LEU HIS
SEQRES 8 H 390 ASP MET SER ASP MET LEU ALA GLY GLN PRO LEU ALA PRO
SEQRES 9 H 390 ALA GLU ILE TYR ASP LYS THR ARG LYS SER LEU HIS PHE
SEQRES 10 H 390 VAL GLY TYR ALA GLY LEU SER MET ILE ALA ALA SER GLY
SEQRES 11 H 390 VAL ASP MET ALA VAL TRP ASP ALA LEU ALA ARG ALA ALA
SEQRES 12 H 390 ASN MET PRO LEU CYS THR LEU LEU GLY GLY THR PRO GLY
SEQRES 13 H 390 SER VAL LYS ALA TYR ASN SER ASN GLY LEU TRP LEU LYS
SEQRES 14 H 390 SER PRO ALA GLU VAL ALA ALA GLU ALA VAL GLU LEU LYS
SEQRES 15 H 390 ALA GLU GLY GLN GLY THR GLY PHE LYS GLY LEU LYS LEU
SEQRES 16 H 390 ARG MET GLY ARG ASP ASP PRO ALA VAL ASP ILE GLU THR
SEQRES 17 H 390 ALA GLU ALA VAL TRP ASP ALA VAL GLY ARG ASP THR ALA
SEQRES 18 H 390 LEU MET VAL ASP PHE ASN GLN GLY LEU ASP MET ALA GLU
SEQRES 19 H 390 ALA MET HIS ARG THR ARG GLN ILE ASP ASP LEU GLY LEU
SEQRES 20 H 390 GLU TRP ILE GLU GLU PRO VAL VAL TYR ASP ASN PHE ASP
SEQRES 21 H 390 GLY TYR ALA GLN LEU ARG HIS ASP LEU LYS THR PRO LEU
SEQRES 22 H 390 MET ILE GLY GLU ASN PHE TYR GLY PRO ARG GLU MET HIS
SEQRES 23 H 390 GLN ALA LEU GLN ALA GLY ALA CYS ASP LEU VAL MET PRO
SEQRES 24 H 390 ASP PHE MET ARG ILE GLY GLY VAL SER GLY TRP MET ARG
SEQRES 25 H 390 ALA ALA GLY VAL ALA GLY ALA TRP GLY ILE PRO MET SER
SEQRES 26 H 390 THR HIS LEU TYR PRO GLU VAL GLY ALA HIS VAL MET ARG
SEQRES 27 H 390 VAL THR GLU THR ALA HIS TRP LEU GLU TRP GLN SER TRP
SEQRES 28 H 390 ALA ASP PRO ILE LEU GLN GLU PRO TYR ALA LEU SER ASP
SEQRES 29 H 390 GLY ASP LEU ILE VAL PRO ASP LYS PRO GLY LEU GLY LEU
SEQRES 30 H 390 ASP TRP ASP GLU ASP VAL VAL ALA ALA ASN LEU VAL GLU
HET MG A 500 1
HET MG A 501 1
HET CL A 368 1
HET NI A 369 1
HET MG B 500 1
HET MG B 501 1
HET CL B 368 1
HET MG C 500 1
HET MG C 501 1
HET MG D 500 1
HET MG D 501 1
HET CL D 368 1
HET MG E 500 1
HET MG E 501 1
HET MG F 500 1
HET MG F 501 1
HET NI F 368 1
HET MG G 500 1
HET MG G 501 1
HET MG H 500 1
HET MG H 501 1
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM NI NICKEL (II) ION
FORMUL 9 MG 16(MG 2+)
FORMUL 11 CL 3(CL 1-)
FORMUL 12 NI 2(NI 2+)
FORMUL 30 HOH *866(H2 O)
HELIX 1 1 VAL A 56 LYS A 58 5 3
HELIX 2 2 ALA A 59 ALA A 75 1 17
HELIX 3 3 ALA A 80 LEU A 92 1 13
HELIX 4 4 HIS A 93 GLY A 96 5 4
HELIX 5 5 GLY A 99 ALA A 120 1 22
HELIX 6 6 PRO A 123 LEU A 128 1 6
HELIX 7 7 SER A 147 GLU A 161 1 15
HELIX 8 8 ASP A 178 GLY A 194 1 17
HELIX 9 9 ASP A 208 ASP A 220 1 13
HELIX 10 10 ASN A 235 LEU A 246 1 12
HELIX 11 11 GLY A 258 ALA A 268 1 11
HELIX 12 12 ASP A 277 GLY A 282 1 6
HELIX 13 13 GLY A 282 GLY A 298 1 17
HELIX 14 14 TYR A 306 ARG A 315 1 10
HELIX 15 15 ALA A 329 LEU A 333 5 5
HELIX 16 16 ASP A 357 ALA A 363 1 7
HELIX 17 17 VAL B 56 LYS B 58 5 3
HELIX 18 18 ALA B 59 ALA B 75 1 17
HELIX 19 19 ALA B 80 LEU B 92 1 13
HELIX 20 20 HIS B 93 GLY B 96 5 4
HELIX 21 21 GLY B 99 ALA B 120 1 22
HELIX 22 22 PRO B 123 LEU B 128 1 6
HELIX 23 23 SER B 147 GLU B 161 1 15
HELIX 24 24 ASP B 178 GLY B 194 1 17
HELIX 25 25 ASP B 208 ILE B 219 1 12
HELIX 26 26 ASN B 235 LEU B 246 1 12
HELIX 27 27 GLY B 258 ALA B 268 1 11
HELIX 28 28 GLY B 282 GLY B 298 1 17
HELIX 29 29 TYR B 306 ARG B 315 1 10
HELIX 30 30 ALA B 329 LEU B 333 5 5
HELIX 31 31 ASP B 357 LEU B 365 1 9
HELIX 32 32 VAL C 56 LYS C 58 5 3
HELIX 33 33 ALA C 59 ALA C 75 1 17
HELIX 34 34 ALA C 80 HIS C 93 1 14
HELIX 35 35 PHE C 94 GLY C 96 5 3
HELIX 36 36 GLY C 99 ALA C 120 1 22
HELIX 37 37 PRO C 123 LEU C 128 1 6
HELIX 38 38 SER C 147 GLY C 162 1 16
HELIX 39 39 ASP C 178 GLY C 194 1 17
HELIX 40 40 ASP C 208 ILE C 219 1 12
HELIX 41 41 ASN C 235 LEU C 246 1 12
HELIX 42 42 GLY C 258 ALA C 268 1 11
HELIX 43 43 GLY C 282 GLY C 298 1 17
HELIX 44 44 TYR C 306 ARG C 315 1 10
HELIX 45 45 ALA C 329 LEU C 333 5 5
HELIX 46 46 ASP C 357 LEU C 365 1 9
HELIX 47 47 VAL D 56 LYS D 58 5 3
HELIX 48 48 ALA D 59 ALA D 75 1 17
HELIX 49 49 ALA D 80 LEU D 92 1 13
HELIX 50 50 HIS D 93 GLY D 96 5 4
HELIX 51 51 GLY D 99 ALA D 120 1 22
HELIX 52 52 PRO D 123 LEU D 128 1 6
HELIX 53 53 SER D 147 GLY D 162 1 16
HELIX 54 54 ASP D 178 GLY D 194 1 17
HELIX 55 55 ASP D 208 ASP D 220 1 13
HELIX 56 56 ASN D 235 LEU D 246 1 12
HELIX 57 57 GLY D 258 ALA D 268 1 11
HELIX 58 58 ASP D 277 GLY D 282 1 6
HELIX 59 59 GLY D 282 GLY D 298 1 17
HELIX 60 60 TYR D 306 ARG D 315 1 10
HELIX 61 61 ALA D 329 LEU D 333 5 5
HELIX 62 62 ASP D 357 LEU D 365 1 9
HELIX 63 63 VAL E 56 LYS E 58 5 3
HELIX 64 64 ALA E 59 ALA E 75 1 17
HELIX 65 65 ALA E 80 LEU E 92 1 13
HELIX 66 66 HIS E 93 GLY E 96 5 4
HELIX 67 67 GLY E 99 ALA E 119 1 21
HELIX 68 68 PRO E 123 LEU E 128 1 6
HELIX 69 69 SER E 147 GLU E 161 1 15
HELIX 70 70 ASP E 178 GLY E 194 1 17
HELIX 71 71 ASP E 208 ILE E 219 1 12
HELIX 72 72 ASN E 235 LEU E 246 1 12
HELIX 73 73 GLY E 258 ALA E 268 1 11
HELIX 74 74 ASP E 277 GLY E 282 1 6
HELIX 75 75 GLY E 282 GLY E 298 1 17
HELIX 76 76 TYR E 306 ARG E 315 1 10
HELIX 77 77 ALA E 329 LEU E 333 5 5
HELIX 78 78 ASP E 357 LEU E 365 1 9
HELIX 79 79 VAL F 56 LYS F 58 5 3
HELIX 80 80 ALA F 59 ALA F 75 1 17
HELIX 81 81 ALA F 80 LEU F 92 1 13
HELIX 82 82 HIS F 93 GLY F 96 5 4
HELIX 83 83 GLY F 99 ALA F 120 1 22
HELIX 84 84 PRO F 123 LEU F 128 1 6
HELIX 85 85 SER F 147 GLU F 161 1 15
HELIX 86 86 ASP F 178 GLY F 194 1 17
HELIX 87 87 ASP F 208 ASP F 220 1 13
HELIX 88 88 ASN F 235 LEU F 246 1 12
HELIX 89 89 GLY F 258 ALA F 268 1 11
HELIX 90 90 ASP F 277 GLY F 282 1 6
HELIX 91 91 GLY F 282 GLY F 298 1 17
HELIX 92 92 TYR F 306 ARG F 315 1 10
HELIX 93 93 ALA F 329 LEU F 333 5 5
HELIX 94 94 ASP F 357 LEU F 365 1 9
HELIX 95 95 VAL G 56 LYS G 58 5 3
HELIX 96 96 ALA G 59 ALA G 75 1 17
HELIX 97 97 ALA G 80 LEU G 92 1 13
HELIX 98 98 HIS G 93 GLY G 96 5 4
HELIX 99 99 GLY G 99 ALA G 120 1 22
HELIX 100 100 PRO G 123 LEU G 128 1 6
HELIX 101 101 SER G 147 GLU G 161 1 15
HELIX 102 102 ASP G 178 GLY G 194 1 17
HELIX 103 103 ASP G 208 ASP G 220 1 13
HELIX 104 104 ASN G 235 LEU G 246 1 12
HELIX 105 105 GLY G 258 ALA G 268 1 11
HELIX 106 106 ASP G 277 GLY G 282 1 6
HELIX 107 107 GLY G 282 GLY G 298 1 17
HELIX 108 108 TYR G 306 ARG G 315 1 10
HELIX 109 109 ALA G 329 LEU G 333 5 5
HELIX 110 110 ASP G 357 LEU G 365 1 9
HELIX 111 111 VAL H 56 LYS H 58 5 3
HELIX 112 112 ALA H 59 ALA H 75 1 17
HELIX 113 113 ALA H 80 LEU H 92 1 13
HELIX 114 114 HIS H 93 GLY H 96 5 4
HELIX 115 115 GLY H 99 ALA H 120 1 22
HELIX 116 116 PRO H 123 LEU H 128 1 6
HELIX 117 117 SER H 147 GLU H 161 1 15
HELIX 118 118 ASP H 178 GLY H 194 1 17
HELIX 119 119 ASP H 208 ASP H 220 1 13
HELIX 120 120 ASN H 235 LEU H 246 1 12
HELIX 121 121 GLY H 258 ALA H 268 1 11
HELIX 122 122 GLY H 282 GLY H 298 1 17
HELIX 123 123 TYR H 306 ARG H 315 1 10
HELIX 124 124 ALA H 329 LEU H 333 5 5
HELIX 125 125 ASP H 357 LEU H 365 1 9
SHEET 1 A 3 PHE A 7 THR A 24 0
SHEET 2 A 3 THR A 29 THR A 42 -1 O ASP A 39 N THR A 11
SHEET 3 A 3 GLY A 48 LEU A 52 -1 O GLY A 48 N ILE A 40
SHEET 1 B 4 LEU A 323 TRP A 325 0
SHEET 2 B 4 SER A 134 ASN A 139 1 N TYR A 138 O TRP A 325
SHEET 3 B 4 ASP A 343 ILE A 345 -1 O LEU A 344 N VAL A 135
SHEET 4 B 4 LEU A 339 SER A 340 -1 N SER A 340 O ASP A 343
SHEET 1 C 5 GLY A 169 ARG A 173 0
SHEET 2 C 5 ALA A 198 ASP A 202 1 O MET A 200 N LEU A 172
SHEET 3 C 5 TRP A 226 GLU A 228 1 O GLU A 228 N VAL A 201
SHEET 4 C 5 LEU A 250 ILE A 252 1 O MET A 251 N ILE A 227
SHEET 5 C 5 LEU A 273 VAL A 274 1 N LEU A 273 O LEU A 250
SHEET 1 D 3 PHE B 7 THR B 24 0
SHEET 2 D 3 THR B 29 THR B 42 -1 O PRO B 31 N LEU B 19
SHEET 3 D 3 PRO B 47 LEU B 52 -1 O GLY B 48 N ILE B 40
SHEET 1 E 4 LEU B 323 TRP B 325 0
SHEET 2 E 4 SER B 134 ASN B 139 1 N TYR B 138 O TRP B 325
SHEET 3 E 4 ASP B 343 ILE B 345 -1 O LEU B 344 N VAL B 135
SHEET 4 E 4 ALA B 338 SER B 340 -1 N ALA B 338 O ILE B 345
SHEET 1 F 5 GLY B 169 ARG B 173 0
SHEET 2 F 5 ALA B 198 ASP B 202 1 O ALA B 198 N LEU B 170
SHEET 3 F 5 TRP B 226 GLU B 228 1 O GLU B 228 N VAL B 201
SHEET 4 F 5 LEU B 250 ILE B 252 1 O MET B 251 N ILE B 227
SHEET 5 F 5 LEU B 273 VAL B 274 1 N LEU B 273 O LEU B 250
SHEET 1 G 3 PHE C 7 THR C 24 0
SHEET 2 G 3 THR C 29 THR C 42 -1 O PRO C 31 N LEU C 19
SHEET 3 G 3 GLY C 48 LEU C 52 -1 O GLY C 48 N ILE C 40
SHEET 1 H 4 LEU C 323 TRP C 325 0
SHEET 2 H 4 SER C 134 ASN C 139 1 N TYR C 138 O TRP C 325
SHEET 3 H 4 ASP C 343 ILE C 345 -1 O LEU C 344 N VAL C 135
SHEET 4 H 4 ALA C 338 SER C 340 -1 N ALA C 338 O ILE C 345
SHEET 1 I 5 GLY C 169 ARG C 173 0
SHEET 2 I 5 ALA C 198 ASP C 202 1 O ALA C 198 N LEU C 170
SHEET 3 I 5 TRP C 226 GLU C 228 1 O GLU C 228 N VAL C 201
SHEET 4 I 5 LEU C 250 ILE C 252 1 O MET C 251 N ILE C 227
SHEET 5 I 5 LEU C 273 VAL C 274 1 N LEU C 273 O LEU C 250
SHEET 1 J 3 PHE D 7 THR D 24 0
SHEET 2 J 3 THR D 29 THR D 42 -1 O ILE D 30 N VAL D 23
SHEET 3 J 3 GLY D 48 LEU D 52 -1 O GLY D 48 N ILE D 40
SHEET 1 K 4 LEU D 323 TRP D 325 0
SHEET 2 K 4 SER D 134 ASN D 139 1 N TYR D 138 O TRP D 325
SHEET 3 K 4 ASP D 343 ILE D 345 -1 O LEU D 344 N VAL D 135
SHEET 4 K 4 LEU D 339 SER D 340 -1 N SER D 340 O ASP D 343
SHEET 1 L 5 GLY D 169 ARG D 173 0
SHEET 2 L 5 ALA D 198 ASP D 202 1 O MET D 200 N LEU D 172
SHEET 3 L 5 TRP D 226 GLU D 228 1 O GLU D 228 N VAL D 201
SHEET 4 L 5 LEU D 250 ILE D 252 1 O MET D 251 N ILE D 227
SHEET 5 L 5 LEU D 273 VAL D 274 1 N LEU D 273 O LEU D 250
SHEET 1 M 3 PHE E 7 THR E 24 0
SHEET 2 M 3 THR E 29 THR E 42 -1 O GLU E 41 N ARG E 8
SHEET 3 M 3 PRO E 47 LEU E 52 -1 O GLY E 48 N ILE E 40
SHEET 1 N 4 LEU E 323 TRP E 325 0
SHEET 2 N 4 SER E 134 ASN E 139 1 N TYR E 138 O TRP E 325
SHEET 3 N 4 ASP E 343 ILE E 345 -1 O LEU E 344 N VAL E 135
SHEET 4 N 4 LEU E 339 SER E 340 -1 N SER E 340 O ASP E 343
SHEET 1 O 5 GLY E 169 ARG E 173 0
SHEET 2 O 5 ALA E 198 ASP E 202 1 O MET E 200 N LEU E 170
SHEET 3 O 5 TRP E 226 GLU E 228 1 O GLU E 228 N VAL E 201
SHEET 4 O 5 LEU E 250 ILE E 252 1 O MET E 251 N ILE E 227
SHEET 5 O 5 LEU E 273 VAL E 274 1 O LEU E 273 N ILE E 252
SHEET 1 P 3 PHE F 7 THR F 24 0
SHEET 2 P 3 THR F 29 THR F 42 -1 O PRO F 31 N LEU F 19
SHEET 3 P 3 GLY F 48 LEU F 52 -1 O GLY F 48 N ILE F 40
SHEET 1 Q 4 LEU F 323 TRP F 325 0
SHEET 2 Q 4 SER F 134 ASN F 139 1 N TYR F 138 O TRP F 325
SHEET 3 Q 4 ASP F 343 ILE F 345 -1 O LEU F 344 N VAL F 135
SHEET 4 Q 4 ALA F 338 SER F 340 -1 N ALA F 338 O ILE F 345
SHEET 1 R 5 GLY F 169 ARG F 173 0
SHEET 2 R 5 ALA F 198 ASP F 202 1 O MET F 200 N LEU F 172
SHEET 3 R 5 TRP F 226 GLU F 228 1 O GLU F 228 N VAL F 201
SHEET 4 R 5 LEU F 250 ILE F 252 1 O MET F 251 N ILE F 227
SHEET 5 R 5 LEU F 273 VAL F 274 1 N LEU F 273 O LEU F 250
SHEET 1 S 3 PHE G 7 THR G 24 0
SHEET 2 S 3 THR G 29 THR G 42 -1 O LEU G 37 N ARG G 13
SHEET 3 S 3 GLY G 48 LEU G 52 -1 O GLY G 48 N ILE G 40
SHEET 1 T 4 LEU G 323 TRP G 325 0
SHEET 2 T 4 SER G 134 ASN G 139 1 N TYR G 138 O TRP G 325
SHEET 3 T 4 ASP G 343 ILE G 345 -1 O LEU G 344 N VAL G 135
SHEET 4 T 4 ALA G 338 SER G 340 -1 N ALA G 338 O ILE G 345
SHEET 1 U 5 GLY G 169 ARG G 173 0
SHEET 2 U 5 ALA G 198 ASP G 202 1 O MET G 200 N LEU G 172
SHEET 3 U 5 TRP G 226 GLU G 228 1 O GLU G 228 N VAL G 201
SHEET 4 U 5 LEU G 250 ILE G 252 1 O MET G 251 N ILE G 227
SHEET 5 U 5 LEU G 273 VAL G 274 1 N LEU G 273 O LEU G 250
SHEET 1 V 3 PHE H 7 THR H 24 0
SHEET 2 V 3 THR H 29 THR H 42 -1 O TRP H 33 N LEU H 17
SHEET 3 V 3 PRO H 47 LEU H 52 -1 O ALA H 50 N ILE H 38
SHEET 1 W 4 LEU H 323 TRP H 325 0
SHEET 2 W 4 SER H 134 ASN H 139 1 N TYR H 138 O TRP H 325
SHEET 3 W 4 ASP H 343 ILE H 345 -1 O LEU H 344 N VAL H 135
SHEET 4 W 4 ALA H 338 SER H 340 -1 N ALA H 338 O ILE H 345
SHEET 1 X 5 GLY H 169 ARG H 173 0
SHEET 2 X 5 ALA H 198 ASP H 202 1 O MET H 200 N LEU H 172
SHEET 3 X 5 TRP H 226 GLU H 228 1 O GLU H 228 N VAL H 201
SHEET 4 X 5 LEU H 250 ILE H 252 1 O MET H 251 N ILE H 227
SHEET 5 X 5 LEU H 273 VAL H 274 1 N LEU H 273 O LEU H 250
LINK OD2 ASP A 202 MG MG A 500 1555 1555 2.30
LINK OE2 GLU A 228 MG MG A 500 1555 1555 2.07
LINK O ARG A 243 MG MG A 501 1555 1555 2.05
LINK NE2 HIS A 244 NI NI A 369 1555 1555 2.34
LINK O LEU A 246 MG MG A 501 1555 1555 2.07
LINK OE1 GLU A 254 MG MG A 500 1555 1555 2.19
LINK NI NI A 369 NE2 HIS B 244 1555 1555 2.51
LINK NI NI A 369 NE2 HIS C 244 1555 1555 2.35
LINK NI NI A 369 NE2 HIS D 244 1555 1555 2.41
LINK O HOH A 370 MG MG A 501 1555 1555 2.05
LINK O HOH A 374 MG MG B 501 1555 1555 2.13
LINK O HOH A 375 MG MG A 501 1555 1555 2.00
LINK O HOH A 382 MG MG A 501 1555 1555 2.02
LINK O HOH A 394 MG MG A 500 1555 1555 2.19
LINK O HOH A 411 MG MG A 500 1555 1555 2.09
LINK O HOH A 429 MG MG A 500 1555 1555 2.11
LINK MG MG A 501 O HOH D 371 1555 1555 2.00
LINK OD2 ASP B 202 MG MG B 500 1555 1555 2.19
LINK OE2 GLU B 228 MG MG B 500 1555 1555 2.07
LINK O ARG B 243 MG MG B 501 1555 1555 2.03
LINK O LEU B 246 MG MG B 501 1555 1555 2.01
LINK OE1 GLU B 254 MG MG B 500 1555 1555 2.01
LINK O HOH B 369 MG MG B 501 1555 1555 2.03
LINK O HOH B 370 MG MG B 501 1555 1555 2.06
LINK O HOH B 373 MG MG C 501 1555 1555 2.11
LINK O HOH B 380 MG MG C 501 1555 1555 2.07
LINK O HOH B 381 MG MG B 501 1555 1555 2.02
LINK O HOH B 407 MG MG B 500 1555 1555 2.09
LINK O HOH B 486 MG MG B 500 1555 1555 2.06
LINK MG MG B 500 O HOH B 866 1555 1555 2.01
LINK OD2 ASP C 202 MG MG C 500 1555 1555 2.17
LINK OE2 GLU C 228 MG MG C 500 1555 1555 1.97
LINK O ARG C 243 MG MG C 501 1555 1555 2.00
LINK O LEU C 246 MG MG C 501 1555 1555 2.08
LINK OE1 GLU C 254 MG MG C 500 1555 1555 2.19
LINK O HOH C 368 MG MG D 501 1555 1555 2.11
LINK O HOH C 369 MG MG D 501 1555 1555 2.09
LINK O HOH C 370 MG MG C 501 1555 1555 2.11
LINK O HOH C 378 MG MG C 501 1555 1555 2.09
LINK MG MG C 500 O HOH C 667 1555 1555 2.11
LINK MG MG C 500 O HOH C 707 1555 1555 2.06
LINK MG MG C 500 O HOH C 782 1555 1555 2.07
LINK OD2 ASP D 202 MG MG D 500 1555 1555 2.12
LINK OE2 GLU D 228 MG MG D 500 1555 1555 1.98
LINK O ARG D 243 MG MG D 501 1555 1555 2.08
LINK O LEU D 246 MG MG D 501 1555 1555 2.05
LINK OE1 GLU D 254 MG MG D 500 1555 1555 2.17
LINK O HOH D 369 MG MG D 501 1555 1555 2.11
LINK O HOH D 372 MG MG D 501 1555 1555 2.05
LINK O HOH D 381 MG MG D 500 1555 1555 2.08
LINK O HOH D 401 MG MG D 500 1555 1555 2.14
LINK O HOH D 415 MG MG D 500 1555 1555 2.12
LINK OD2 ASP E 202 MG MG E 500 1555 1555 2.13
LINK OE2 GLU E 228 MG MG E 500 1555 1555 2.09
LINK O ARG E 243 MG MG E 501 1555 1555 2.20
LINK NE2 HIS E 244 NI NI F 368 1555 1555 2.42
LINK O LEU E 246 MG MG E 501 1555 1555 2.11
LINK OE1 GLU E 254 MG MG E 500 1555 1555 2.14
LINK O HOH E 369 MG MG F 501 1555 1555 2.06
LINK O HOH E 370 MG MG E 501 1555 1555 2.04
LINK O HOH E 371 MG MG E 501 1555 1555 2.07
LINK O HOH E 386 MG MG E 500 1555 1555 2.12
LINK MG MG E 500 O HOH E 726 1555 1555 2.10
LINK MG MG E 500 O HOH E 836 1555 1555 2.05
LINK MG MG E 501 O HOH H 370 1555 1555 2.07
LINK MG MG E 501 O HOH H 446 1555 1555 2.04
LINK OD2 ASP F 202 MG MG F 500 1555 1555 1.98
LINK OE2 GLU F 228 MG MG F 500 1555 1555 1.93
LINK O ARG F 243 MG MG F 501 1555 1555 2.11
LINK NE2 HIS F 244 NI NI F 368 1555 1555 2.49
LINK O LEU F 246 MG MG F 501 1555 1555 2.02
LINK OE1 GLU F 254 MG MG F 500 1555 1555 2.20
LINK NI NI F 368 NE2 HIS G 244 1555 1555 2.37
LINK NI NI F 368 NE2 HIS H 244 1555 1555 2.26
LINK O HOH F 369 MG MG G 501 1555 1555 2.01
LINK O HOH F 370 MG MG F 501 1555 1555 2.08
LINK O HOH F 372 MG MG F 501 1555 1555 2.07
LINK O HOH F 379 MG MG F 501 1555 1555 2.06
LINK O HOH F 407 MG MG F 500 1555 1555 2.10
LINK O HOH F 418 MG MG F 500 1555 1555 2.09
LINK O HOH F 419 MG MG F 500 1555 1555 2.12
LINK OD2 ASP G 202 MG MG G 500 1555 1555 2.08
LINK OE2 GLU G 228 MG MG G 500 1555 1555 2.06
LINK O ARG G 243 MG MG G 501 1555 1555 2.16
LINK O LEU G 246 MG MG G 501 1555 1555 2.14
LINK OE1 GLU G 254 MG MG G 500 1555 1555 2.16
LINK O HOH G 368 MG MG G 501 1555 1555 2.07
LINK O HOH G 370 MG MG G 501 1555 1555 2.12
LINK O HOH G 373 MG MG H 501 1555 1555 2.07
LINK O HOH G 381 MG MG G 501 1555 1555 2.10
LINK O HOH G 409 MG MG G 500 1555 1555 2.14
LINK O HOH G 429 MG MG G 500 1555 1555 2.07
LINK O HOH G 438 MG MG G 500 1555 1555 2.08
LINK OD2 ASP H 202 MG MG H 500 1555 1555 2.16
LINK OE2 GLU H 228 MG MG H 500 1555 1555 2.16
LINK O ARG H 243 MG MG H 501 1555 1555 2.01
LINK O LEU H 246 MG MG H 501 1555 1555 2.07
LINK OE1 GLU H 254 MG MG H 500 1555 1555 2.27
LINK O HOH H 368 MG MG H 501 1555 1555 2.07
LINK O HOH H 372 MG MG H 501 1555 1555 2.04
LINK O HOH H 385 MG MG H 501 1555 1555 2.06
LINK O HOH H 403 MG MG H 500 1555 1555 2.04
LINK O HOH H 423 MG MG H 500 1555 1555 2.11
LINK MG MG H 500 O HOH H 846 1555 1555 2.06
SITE 1 AC1 7 LYS A 171 ASP A 202 GLU A 228 GLU A 254
SITE 2 AC1 7 HOH A 394 HOH A 411 HOH A 429
SITE 1 AC2 6 ARG A 243 LEU A 246 HOH A 370 HOH A 375
SITE 2 AC2 6 HOH A 382 HOH D 371
SITE 1 AC3 4 HIS A 263 TRP A 297 HIS G 263 TRP G 297
SITE 1 AC4 4 HIS A 244 HIS B 244 HIS C 244 HIS D 244
SITE 1 AC5 6 ASP B 202 GLU B 228 GLU B 254 HOH B 407
SITE 2 AC5 6 HOH B 486 HOH B 866
SITE 1 AC6 6 HOH A 374 ARG B 243 LEU B 246 HOH B 369
SITE 2 AC6 6 HOH B 370 HOH B 381
SITE 1 AC7 4 HIS B 263 TRP B 297 HIS F 263 TRP F 297
SITE 1 AC8 6 ASP C 202 GLU C 228 GLU C 254 HOH C 667
SITE 2 AC8 6 HOH C 707 HOH C 782
SITE 1 AC9 6 HOH B 373 HOH B 380 ARG C 243 LEU C 246
SITE 2 AC9 6 HOH C 370 HOH C 378
SITE 1 BC1 6 ASP D 202 GLU D 228 GLU D 254 HOH D 381
SITE 2 BC1 6 HOH D 401 HOH D 415
SITE 1 BC2 6 HOH C 368 HOH C 369 ARG D 243 LEU D 246
SITE 2 BC2 6 HOH D 369 HOH D 372
SITE 1 BC3 4 HIS D 263 TRP D 297 HIS H 263 TRP H 297
SITE 1 BC4 6 ASP E 202 GLU E 228 GLU E 254 HOH E 386
SITE 2 BC4 6 HOH E 726 HOH E 836
SITE 1 BC5 6 ARG E 243 LEU E 246 HOH E 370 HOH E 371
SITE 2 BC5 6 HOH H 370 HOH H 446
SITE 1 BC6 6 ASP F 202 GLU F 228 GLU F 254 HOH F 407
SITE 2 BC6 6 HOH F 418 HOH F 419
SITE 1 BC7 6 HOH E 369 ARG F 243 LEU F 246 HOH F 370
SITE 2 BC7 6 HOH F 372 HOH F 379
SITE 1 BC8 4 HIS E 244 HIS F 244 HIS G 244 HIS H 244
SITE 1 BC9 6 ASP G 202 GLU G 228 GLU G 254 HOH G 409
SITE 2 BC9 6 HOH G 429 HOH G 438
SITE 1 CC1 6 HOH F 369 ARG G 243 LEU G 246 HOH G 368
SITE 2 CC1 6 HOH G 370 HOH G 381
SITE 1 CC2 6 ASP H 202 GLU H 228 GLU H 254 HOH H 403
SITE 2 CC2 6 HOH H 423 HOH H 846
SITE 1 CC3 6 HOH G 373 ARG H 243 LEU H 246 HOH H 368
SITE 2 CC3 6 HOH H 372 HOH H 385
CRYST1 152.711 152.984 173.535 90.00 90.00 90.00 P 21 21 21 32
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 0.006548 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006537 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005763 0.00000
(ATOM LINES ARE NOT SHOWN.)
END