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HEADER HYDROLASE 11-APR-14 4Q3L
TITLE CRYSTAL STRUCTURE OF MGS-M2, AN ALPHA/BETA HYDROLASE ENZYME FROM A
TITLE 2 MEDEE BASIN DEEP-SEA METAGENOME LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGS-M2;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 FRAGMENT: MGS-M2;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNIDENTIFIED;
SOURCE 3 ORGANISM_TAXID: 32644;
SOURCE 4 GENE: MGS-M2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIL;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P15-TV LIC
KEYWDS METAGENOME, METAGENOMIC LIBRARY, ALPHA AND BETA PROTEINS, ALPHA/BETA
KEYWDS 2 HYDROLASE SUPERFAMILY, ESTERASE/LIPASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.STOGIOS,X.XU,H.CUI,M.ALCAIDE,M.FERRER,A.SAVCHENKO
REVDAT 1 25-FEB-15 4Q3L 0
JRNL AUTH M.ALCAIDE,P.J.STOGIOS,A.LAFRAYA,A.TCHIGVINTSEV,R.FLICK,
JRNL AUTH 2 R.BARGIELA,T.N.CHERNIKOVA,O.N.REVA,T.HAI,C.C.LEGGEWIE,
JRNL AUTH 3 N.KATZKE,V.LA CONO,R.MATESANZ,M.JEBBAR,K.E.JAEGER,
JRNL AUTH 4 M.M.YAKIMOV,A.F.YAKUNIN,P.N.GOLYSHIN,O.V.GOLYSHINA,
JRNL AUTH 5 A.SAVCHENKO,M.FERRER
JRNL TITL PRESSURE ADAPTATION IS LINKED TO THERMAL ADAPTATION IN
JRNL TITL 2 SALT-SATURATED MARINE HABITATS.
JRNL REF ENVIRON MICROBIOL 2014
JRNL REFN
JRNL PMID 25330254
JRNL DOI 10.1111/1462-2920.12660
REMARK 2
REMARK 2 RESOLUTION. 3.01 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9PRE_1669)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.01
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.67
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 63067
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.160
REMARK 3 FREE R VALUE TEST SET COUNT : 1992
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 31.6708 - 7.2284 0.99 4462 147 0.1922 0.1992
REMARK 3 2 7.2284 - 5.7486 1.00 4427 144 0.2161 0.2436
REMARK 3 3 5.7486 - 5.0252 1.00 4383 146 0.1842 0.2233
REMARK 3 4 5.0252 - 4.5672 1.00 4444 139 0.1638 0.1952
REMARK 3 5 4.5672 - 4.2407 1.00 4350 138 0.1685 0.2279
REMARK 3 6 4.2407 - 3.9912 1.00 4406 146 0.1780 0.2315
REMARK 3 7 3.9912 - 3.7916 1.00 4359 148 0.1878 0.2678
REMARK 3 8 3.7916 - 3.6268 1.00 4388 144 0.1954 0.2680
REMARK 3 9 3.6268 - 3.4874 1.00 4358 136 0.2121 0.2935
REMARK 3 10 3.4874 - 3.3672 1.00 4367 141 0.2332 0.3174
REMARK 3 11 3.3672 - 3.2620 1.00 4431 131 0.2363 0.3096
REMARK 3 12 3.2620 - 3.1689 1.00 4338 154 0.2419 0.3443
REMARK 3 13 3.1689 - 3.0855 1.00 4368 145 0.2709 0.3465
REMARK 3 14 3.0855 - 3.0103 0.92 3994 133 0.2736 0.3639
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 18357
REMARK 3 ANGLE : 0.711 24935
REMARK 3 CHIRALITY : 0.029 2817
REMARK 3 PLANARITY : 0.003 3138
REMARK 3 DIHEDRAL : 12.686 6717
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 32
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 2:8 )
REMARK 3 ORIGIN FOR THE GROUP (A): 103.4580 -8.3299 34.8223
REMARK 3 T TENSOR
REMARK 3 T11: 0.6930 T22: 0.8956
REMARK 3 T33: 0.3949 T12: 0.0393
REMARK 3 T13: -0.1185 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 4.5065 L22: 8.2249
REMARK 3 L33: 2.7440 L12: -4.6529
REMARK 3 L13: -3.1555 L23: 1.9092
REMARK 3 S TENSOR
REMARK 3 S11: 1.5920 S12: 0.1762 S13: 0.3400
REMARK 3 S21: -0.6852 S22: -1.0445 S23: 0.5633
REMARK 3 S31: 0.2157 S32: -1.9097 S33: -0.5743
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 9:48 )
REMARK 3 ORIGIN FOR THE GROUP (A): 119.7014 -12.5434 33.5314
REMARK 3 T TENSOR
REMARK 3 T11: 0.4822 T22: 0.2762
REMARK 3 T33: 0.4492 T12: 0.0236
REMARK 3 T13: -0.0056 T23: 0.0327
REMARK 3 L TENSOR
REMARK 3 L11: 8.3607 L22: 4.5954
REMARK 3 L33: 5.2250 L12: -1.3484
REMARK 3 L13: 0.8967 L23: 3.0446
REMARK 3 S TENSOR
REMARK 3 S11: 0.1591 S12: 0.2686 S13: 0.7652
REMARK 3 S21: -0.1390 S22: 0.0673 S23: 0.1579
REMARK 3 S31: -0.6400 S32: 0.2090 S33: -0.2411
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 49:232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 113.3072 -26.7576 34.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.3062 T22: 0.3085
REMARK 3 T33: 0.3633 T12: -0.0132
REMARK 3 T13: -0.0248 T23: -0.0015
REMARK 3 L TENSOR
REMARK 3 L11: 1.0246 L22: 2.8499
REMARK 3 L33: 2.6813 L12: -0.2874
REMARK 3 L13: -0.3348 L23: -0.4659
REMARK 3 S TENSOR
REMARK 3 S11: -0.0109 S12: 0.1676 S13: 0.1156
REMARK 3 S21: -0.1870 S22: -0.0145 S23: 0.0124
REMARK 3 S31: -0.1408 S32: -0.2573 S33: 0.0327
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 233:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 127.1117 -26.3988 22.9324
REMARK 3 T TENSOR
REMARK 3 T11: 0.4219 T22: 0.3159
REMARK 3 T33: 0.3585 T12: 0.0235
REMARK 3 T13: 0.0544 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 6.3917 L22: 4.9154
REMARK 3 L33: 2.8034 L12: 0.0972
REMARK 3 L13: -0.3071 L23: 1.2307
REMARK 3 S TENSOR
REMARK 3 S11: 0.1429 S12: 0.6243 S13: 0.0975
REMARK 3 S21: -0.7056 S22: -0.2562 S23: -0.1690
REMARK 3 S31: 0.4168 S32: -0.2145 S33: 0.0996
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 2:9 )
REMARK 3 ORIGIN FOR THE GROUP (A): 116.7561 -70.7595 61.3303
REMARK 3 T TENSOR
REMARK 3 T11: 0.4933 T22: 0.7058
REMARK 3 T33: 0.5451 T12: -0.0363
REMARK 3 T13: -0.0562 T23: 0.1939
REMARK 3 L TENSOR
REMARK 3 L11: 1.9948 L22: 7.2676
REMARK 3 L33: 8.4653 L12: -0.4712
REMARK 3 L13: -3.4493 L23: 1.9585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: -1.1270 S13: -0.5659
REMARK 3 S21: 1.6252 S22: 0.2714 S23: -0.3029
REMARK 3 S31: 0.8363 S32: 0.7263 S33: -0.1724
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 10:45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 117.2169 -71.2337 44.1727
REMARK 3 T TENSOR
REMARK 3 T11: 0.4287 T22: 0.3659
REMARK 3 T33: 0.6387 T12: 0.0078
REMARK 3 T13: -0.0016 T23: 0.0624
REMARK 3 L TENSOR
REMARK 3 L11: 2.2985 L22: 3.5963
REMARK 3 L33: 7.0857 L12: 1.8157
REMARK 3 L13: -0.3478 L23: -0.5788
REMARK 3 S TENSOR
REMARK 3 S11: -0.2864 S12: -0.2450 S13: -0.6627
REMARK 3 S21: -0.1061 S22: -0.0053 S23: -0.0127
REMARK 3 S31: 0.5754 S32: 0.1830 S33: 0.2463
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 46:232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 119.9535 -56.4465 46.3834
REMARK 3 T TENSOR
REMARK 3 T11: 0.2804 T22: 0.3348
REMARK 3 T33: 0.3307 T12: -0.0325
REMARK 3 T13: -0.0254 T23: 0.0528
REMARK 3 L TENSOR
REMARK 3 L11: 1.5206 L22: 2.7529
REMARK 3 L33: 1.3637 L12: -0.2700
REMARK 3 L13: -0.5077 L23: 0.2423
REMARK 3 S TENSOR
REMARK 3 S11: 0.0460 S12: -0.1625 S13: -0.1425
REMARK 3 S21: 0.0287 S22: -0.0006 S23: -0.0135
REMARK 3 S31: 0.0664 S32: 0.0745 S33: -0.0408
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 233:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 129.1952 -62.2100 32.5221
REMARK 3 T TENSOR
REMARK 3 T11: 0.3909 T22: 0.3218
REMARK 3 T33: 0.4237 T12: -0.0052
REMARK 3 T13: 0.0405 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 3.4663 L22: 4.8965
REMARK 3 L33: 3.8932 L12: -0.4195
REMARK 3 L13: -1.0037 L23: -0.2977
REMARK 3 S TENSOR
REMARK 3 S11: -0.0212 S12: -0.2958 S13: -0.1015
REMARK 3 S21: -0.2842 S22: -0.0881 S23: -0.5827
REMARK 3 S31: 0.2403 S32: 0.2768 S33: 0.1155
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID -1:37 )
REMARK 3 ORIGIN FOR THE GROUP (A): 153.8998 -17.7750 12.6429
REMARK 3 T TENSOR
REMARK 3 T11: 0.4999 T22: 0.4375
REMARK 3 T33: 0.4835 T12: -0.0770
REMARK 3 T13: 0.0054 T23: 0.1227
REMARK 3 L TENSOR
REMARK 3 L11: 8.9977 L22: 2.4179
REMARK 3 L33: 7.6119 L12: 1.2102
REMARK 3 L13: -0.5932 L23: 1.0776
REMARK 3 S TENSOR
REMARK 3 S11: 0.2093 S12: 0.0194 S13: 0.5263
REMARK 3 S21: 0.1106 S22: 0.2113 S23: -0.0582
REMARK 3 S31: -0.6089 S32: 0.6526 S33: -0.3859
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 38:121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 152.3323 -23.4320 18.3008
REMARK 3 T TENSOR
REMARK 3 T11: 0.4133 T22: 0.3672
REMARK 3 T33: 0.3662 T12: -0.0911
REMARK 3 T13: 0.0015 T23: 0.0457
REMARK 3 L TENSOR
REMARK 3 L11: 5.2541 L22: 4.5429
REMARK 3 L33: 3.3774 L12: 0.5316
REMARK 3 L13: -0.7511 L23: 0.1960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0097 S12: -0.0878 S13: 0.4218
REMARK 3 S21: 0.3164 S22: 0.0687 S23: 0.0456
REMARK 3 S31: -0.1487 S32: 0.2412 S33: -0.0533
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 122:197 )
REMARK 3 ORIGIN FOR THE GROUP (A): 147.0923 -40.5905 6.1230
REMARK 3 T TENSOR
REMARK 3 T11: 0.4069 T22: 0.3400
REMARK 3 T33: 0.3304 T12: 0.0026
REMARK 3 T13: -0.0644 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 5.6968 L22: 1.7147
REMARK 3 L33: 1.9692 L12: 0.5370
REMARK 3 L13: -0.7182 L23: -0.7890
REMARK 3 S TENSOR
REMARK 3 S11: -0.1371 S12: 0.3413 S13: 0.4929
REMARK 3 S21: -0.0239 S22: -0.0871 S23: 0.1375
REMARK 3 S31: 0.0715 S32: 0.1494 S33: 0.2051
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 198:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 140.7366 -31.6583 26.1873
REMARK 3 T TENSOR
REMARK 3 T11: 0.4663 T22: 0.3837
REMARK 3 T33: 0.3336 T12: -0.0678
REMARK 3 T13: 0.0776 T23: 0.0768
REMARK 3 L TENSOR
REMARK 3 L11: 2.5034 L22: 3.8324
REMARK 3 L33: 1.5276 L12: -0.8414
REMARK 3 L13: 0.9362 L23: 0.6656
REMARK 3 S TENSOR
REMARK 3 S11: 0.0092 S12: -0.2012 S13: 0.1775
REMARK 3 S21: 0.2061 S22: -0.0846 S23: 0.2151
REMARK 3 S31: -0.0322 S32: 0.1628 S33: 0.0911
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN D AND RESID 2:31 )
REMARK 3 ORIGIN FOR THE GROUP (A): 132.6357 -79.7264 8.0195
REMARK 3 T TENSOR
REMARK 3 T11: 0.5825 T22: 0.4588
REMARK 3 T33: 0.5048 T12: -0.0586
REMARK 3 T13: 0.0447 T23: -0.0467
REMARK 3 L TENSOR
REMARK 3 L11: 5.3677 L22: 5.4184
REMARK 3 L33: 2.1891 L12: -3.2191
REMARK 3 L13: -1.1103 L23: 3.2601
REMARK 3 S TENSOR
REMARK 3 S11: 0.1290 S12: 0.4197 S13: -0.6418
REMARK 3 S21: 0.1877 S22: -0.3760 S23: 0.4709
REMARK 3 S31: 0.7913 S32: -0.4212 S33: 0.1945
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN D AND RESID 32:68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 137.7943 -73.1135 11.0829
REMARK 3 T TENSOR
REMARK 3 T11: 0.4913 T22: 0.3121
REMARK 3 T33: 0.4828 T12: -0.0177
REMARK 3 T13: -0.0017 T23: -0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 5.0598 L22: 2.6570
REMARK 3 L33: 6.3226 L12: -0.1238
REMARK 3 L13: -3.4139 L23: -0.3897
REMARK 3 S TENSOR
REMARK 3 S11: -0.4180 S12: 0.1627 S13: -0.2610
REMARK 3 S21: -0.2465 S22: 0.2405 S23: 0.1620
REMARK 3 S31: 0.8853 S32: -0.4947 S33: 0.2513
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN D AND RESID 69:217 )
REMARK 3 ORIGIN FOR THE GROUP (A): 135.8466 -61.8169 8.1860
REMARK 3 T TENSOR
REMARK 3 T11: 0.3468 T22: 0.3478
REMARK 3 T33: 0.3612 T12: 0.0247
REMARK 3 T13: -0.0060 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 1.8465 L22: 2.4992
REMARK 3 L33: 2.0362 L12: 0.6885
REMARK 3 L13: -0.5244 L23: 0.2238
REMARK 3 S TENSOR
REMARK 3 S11: -0.0462 S12: 0.2687 S13: -0.0181
REMARK 3 S21: -0.0605 S22: -0.0038 S23: 0.1116
REMARK 3 S31: 0.2279 S32: -0.1149 S33: 0.0511
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 218:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 126.8855 -59.5958 21.2425
REMARK 3 T TENSOR
REMARK 3 T11: 0.3477 T22: 0.3372
REMARK 3 T33: 0.5078 T12: 0.0385
REMARK 3 T13: 0.0211 T23: -0.0058
REMARK 3 L TENSOR
REMARK 3 L11: 1.5364 L22: 4.6953
REMARK 3 L33: 4.8944 L12: 1.4308
REMARK 3 L13: -1.5152 L23: -0.9957
REMARK 3 S TENSOR
REMARK 3 S11: 0.1343 S12: 0.0454 S13: 0.4172
REMARK 3 S21: -0.0185 S22: -0.0966 S23: 0.6398
REMARK 3 S31: -0.0233 S32: -0.4561 S33: -0.0679
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN E AND RESID 2:24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 185.7389 -42.3133 48.9905
REMARK 3 T TENSOR
REMARK 3 T11: 0.5823 T22: 0.3976
REMARK 3 T33: 0.5636 T12: -0.0004
REMARK 3 T13: 0.0595 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 7.7900 L22: 6.8572
REMARK 3 L33: 8.7029 L12: 0.9697
REMARK 3 L13: 3.8314 L23: 2.8120
REMARK 3 S TENSOR
REMARK 3 S11: 0.2303 S12: -0.6178 S13: 0.7415
REMARK 3 S21: -0.5031 S22: -0.2230 S23: 0.1784
REMARK 3 S31: -0.3039 S32: -0.7091 S33: -0.0796
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN E AND RESID 25:115 )
REMARK 3 ORIGIN FOR THE GROUP (A): 184.3345 -52.0829 47.1281
REMARK 3 T TENSOR
REMARK 3 T11: 0.3606 T22: 0.3535
REMARK 3 T33: 0.4581 T12: -0.0310
REMARK 3 T13: -0.0334 T23: -0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 2.7559 L22: 4.0826
REMARK 3 L33: 6.5130 L12: -0.4714
REMARK 3 L13: -0.3689 L23: -0.4208
REMARK 3 S TENSOR
REMARK 3 S11: -0.3769 S12: -0.1589 S13: 0.1994
REMARK 3 S21: 0.1185 S22: 0.0522 S23: 0.2578
REMARK 3 S31: -0.6223 S32: -0.2165 S33: 0.3560
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN E AND RESID 116:213 )
REMARK 3 ORIGIN FOR THE GROUP (A): 193.5140 -66.2759 46.7345
REMARK 3 T TENSOR
REMARK 3 T11: 0.3602 T22: 0.3626
REMARK 3 T33: 0.3698 T12: -0.0314
REMARK 3 T13: 0.0130 T23: 0.0469
REMARK 3 L TENSOR
REMARK 3 L11: 1.3925 L22: 2.0728
REMARK 3 L33: 1.2319 L12: -0.1139
REMARK 3 L13: 0.4903 L23: 0.1158
REMARK 3 S TENSOR
REMARK 3 S11: 0.1105 S12: -0.1826 S13: 0.0235
REMARK 3 S21: 0.0496 S22: -0.1366 S23: 0.0844
REMARK 3 S31: -0.0793 S32: -0.0199 S33: 0.0227
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN E AND RESID 214:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 179.6731 -64.3943 34.4300
REMARK 3 T TENSOR
REMARK 3 T11: 0.3472 T22: 0.3282
REMARK 3 T33: 0.5602 T12: -0.0406
REMARK 3 T13: -0.0214 T23: -0.0889
REMARK 3 L TENSOR
REMARK 3 L11: 1.6940 L22: 4.2537
REMARK 3 L33: 4.5194 L12: -1.7551
REMARK 3 L13: 0.3424 L23: -1.3353
REMARK 3 S TENSOR
REMARK 3 S11: 0.0419 S12: 0.0002 S13: -0.2741
REMARK 3 S21: 0.3045 S22: -0.1571 S23: 0.5934
REMARK 3 S31: 0.0416 S32: -0.2370 S33: 0.1096
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN F AND RESID 2:25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 165.2107-117.0410 23.2276
REMARK 3 T TENSOR
REMARK 3 T11: 0.6846 T22: 0.5906
REMARK 3 T33: 0.4934 T12: -0.0762
REMARK 3 T13: 0.0198 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 2.3015 L22: 9.6746
REMARK 3 L33: 2.2323 L12: 0.5819
REMARK 3 L13: 0.0288 L23: 1.8016
REMARK 3 S TENSOR
REMARK 3 S11: -0.2207 S12: -0.8246 S13: -0.7323
REMARK 3 S21: 0.2379 S22: -0.1653 S23: 0.1604
REMARK 3 S31: 1.2765 S32: -0.8277 S33: 0.2653
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN F AND RESID 26:134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 166.0030-104.3756 25.3434
REMARK 3 T TENSOR
REMARK 3 T11: 0.4464 T22: 0.3831
REMARK 3 T33: 0.3578 T12: -0.0242
REMARK 3 T13: -0.0144 T23: 0.0289
REMARK 3 L TENSOR
REMARK 3 L11: 2.2843 L22: 4.3981
REMARK 3 L33: 2.0631 L12: 0.2940
REMARK 3 L13: -0.2778 L23: -0.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.0371 S12: -0.1390 S13: -0.3681
REMARK 3 S21: 0.3448 S22: 0.1075 S23: 0.2388
REMARK 3 S31: 0.2157 S32: -0.2059 S33: -0.0625
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN F AND RESID 135:173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 171.4610 -89.7727 8.9717
REMARK 3 T TENSOR
REMARK 3 T11: 0.3586 T22: 0.3979
REMARK 3 T33: 0.3269 T12: 0.0558
REMARK 3 T13: 0.0235 T23: 0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.6117 L22: 2.9445
REMARK 3 L33: 1.6746 L12: 1.4844
REMARK 3 L13: 1.2516 L23: 0.0372
REMARK 3 S TENSOR
REMARK 3 S11: 0.2846 S12: -0.0952 S13: -0.3566
REMARK 3 S21: 0.0114 S22: -0.1795 S23: -0.2586
REMARK 3 S31: 0.2378 S32: -0.0789 S33: -0.1372
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN F AND RESID 174:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 171.7960 -95.2257 26.8053
REMARK 3 T TENSOR
REMARK 3 T11: 0.4937 T22: 0.3444
REMARK 3 T33: 0.4568 T12: -0.0456
REMARK 3 T13: 0.0226 T23: 0.0324
REMARK 3 L TENSOR
REMARK 3 L11: 1.8954 L22: 1.9471
REMARK 3 L33: 1.6434 L12: -0.6004
REMARK 3 L13: 0.4665 L23: 0.2015
REMARK 3 S TENSOR
REMARK 3 S11: 0.0037 S12: -0.3803 S13: 0.0152
REMARK 3 S21: 0.4930 S22: 0.0516 S23: 0.0016
REMARK 3 S31: -0.0258 S32: -0.1659 S33: -0.0434
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN G AND RESID -1:24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 209.3064-109.9124 42.7530
REMARK 3 T TENSOR
REMARK 3 T11: 0.6640 T22: 0.6434
REMARK 3 T33: 0.8132 T12: 0.3069
REMARK 3 T13: -0.0975 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 3.9219 L22: 3.7691
REMARK 3 L33: 7.0805 L12: 2.5811
REMARK 3 L13: 1.0245 L23: 0.2876
REMARK 3 S TENSOR
REMARK 3 S11: 0.3939 S12: 0.1852 S13: -0.5541
REMARK 3 S21: -0.5873 S22: -0.0238 S23: -0.0200
REMARK 3 S31: 0.4691 S32: 0.6815 S33: -0.3427
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN G AND RESID 25:114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 205.1616-100.4588 38.5645
REMARK 3 T TENSOR
REMARK 3 T11: 0.4264 T22: 0.3900
REMARK 3 T33: 0.4138 T12: 0.1037
REMARK 3 T13: -0.0235 T23: 0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 4.6383 L22: 4.2829
REMARK 3 L33: 2.8607 L12: -0.2982
REMARK 3 L13: -0.2078 L23: -0.2598
REMARK 3 S TENSOR
REMARK 3 S11: 0.0211 S12: 0.0537 S13: -0.5011
REMARK 3 S21: -0.0709 S22: 0.0152 S23: -0.0570
REMARK 3 S31: 0.2667 S32: 0.3324 S33: -0.0533
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN G AND RESID 115:209 )
REMARK 3 ORIGIN FOR THE GROUP (A): 200.6122 -85.0783 45.0677
REMARK 3 T TENSOR
REMARK 3 T11: 0.3272 T22: 0.3052
REMARK 3 T33: 0.3795 T12: -0.0188
REMARK 3 T13: 0.0212 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.6654 L22: 1.7961
REMARK 3 L33: 1.9633 L12: -0.0062
REMARK 3 L13: 0.5462 L23: -0.3773
REMARK 3 S TENSOR
REMARK 3 S11: -0.0987 S12: -0.1297 S13: -0.1332
REMARK 3 S21: 0.0527 S22: -0.0664 S23: -0.0061
REMARK 3 S31: 0.0102 S32: 0.1184 S33: 0.1790
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN G AND RESID 210:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 191.0432 -93.1312 30.0636
REMARK 3 T TENSOR
REMARK 3 T11: 0.4672 T22: 0.3358
REMARK 3 T33: 0.4250 T12: 0.0708
REMARK 3 T13: -0.1329 T23: 0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 2.3185 L22: 5.3724
REMARK 3 L33: 1.9991 L12: 0.4874
REMARK 3 L13: -0.9549 L23: 2.2637
REMARK 3 S TENSOR
REMARK 3 S11: -0.0450 S12: 0.1260 S13: -0.1334
REMARK 3 S21: -0.3522 S22: -0.1325 S23: 0.3262
REMARK 3 S31: 0.2291 S32: 0.1494 S33: 0.2016
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN H AND RESID -3:68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 169.2201 -53.5513 6.3965
REMARK 3 T TENSOR
REMARK 3 T11: 0.3910 T22: 0.3745
REMARK 3 T33: 0.5993 T12: 0.0646
REMARK 3 T13: -0.0078 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 3.1605 L22: 2.3836
REMARK 3 L33: 2.9968 L12: 0.1821
REMARK 3 L13: 0.4643 L23: -0.1803
REMARK 3 S TENSOR
REMARK 3 S11: -0.0529 S12: 0.2339 S13: 0.3794
REMARK 3 S21: -0.0697 S22: 0.1498 S23: -0.0579
REMARK 3 S31: -0.4236 S32: 0.0504 S33: -0.0805
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN H AND RESID 69:166 )
REMARK 3 ORIGIN FOR THE GROUP (A): 174.0105 -67.6539 8.4840
REMARK 3 T TENSOR
REMARK 3 T11: 0.3087 T22: 0.3311
REMARK 3 T33: 0.3559 T12: 0.0495
REMARK 3 T13: 0.0383 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 1.0450 L22: 3.0430
REMARK 3 L33: 1.3397 L12: -0.0995
REMARK 3 L13: 0.7424 L23: -0.7386
REMARK 3 S TENSOR
REMARK 3 S11: 0.0789 S12: 0.2611 S13: 0.0709
REMARK 3 S21: -0.0743 S22: -0.1717 S23: -0.1815
REMARK 3 S31: -0.0075 S32: 0.1564 S33: 0.1176
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: (CHAIN H AND RESID 167:205 )
REMARK 3 ORIGIN FOR THE GROUP (A): 164.6326 -71.8256 7.4353
REMARK 3 T TENSOR
REMARK 3 T11: 0.3674 T22: 0.2856
REMARK 3 T33: 0.3656 T12: 0.0898
REMARK 3 T13: 0.0750 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 4.1206 L22: 4.7592
REMARK 3 L33: 2.8197 L12: 0.8359
REMARK 3 L13: 1.9869 L23: -0.9453
REMARK 3 S TENSOR
REMARK 3 S11: -0.1596 S12: 0.1944 S13: -0.2379
REMARK 3 S21: -0.0829 S22: -0.0281 S23: 0.1090
REMARK 3 S31: 0.0751 S32: -0.2314 S33: 0.1576
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: (CHAIN H AND RESID 206:276 )
REMARK 3 ORIGIN FOR THE GROUP (A): 182.6228 -65.2378 20.6372
REMARK 3 T TENSOR
REMARK 3 T11: 0.3403 T22: 0.3075
REMARK 3 T33: 0.4778 T12: 0.0119
REMARK 3 T13: -0.0954 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 2.6846 L22: 3.3724
REMARK 3 L33: 4.3027 L12: -1.2902
REMARK 3 L13: -0.8832 L23: 0.7063
REMARK 3 S TENSOR
REMARK 3 S11: 0.0690 S12: 0.1535 S13: 0.3426
REMARK 3 S21: 0.2430 S22: -0.1073 S23: -0.5876
REMARK 3 S31: -0.2609 S32: 0.2643 S33: 0.0273
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 4Q3L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085560.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63183
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 32.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.09300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.53600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (PHENIX.PHASER)
REMARK 200 STARTING MODEL: PDB ENTRY 1CR6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN TREATED WITH THERMOLYSIN IN 1/
REMARK 280 10 MOLAR RATIO CRYSTALLIZATION IN: 0.1 M SODIUM HEPES, 1.4 M
REMARK 280 SODIUM CITRATE, CRYOPROTECTANT: 15% ETHYLENE GLYCOL, PH 7.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 69.56700
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, F, 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 450
REMARK 450 SOURCE
REMARK 450 THE SAMPLE WAS EXTRACTED FROM MEDEE BASIN DEEP-SEA AND ANALYZED BY
REMARK 450 USING METAGENOME LIBRARY TECHNIQUE
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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 VAL A 1
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 ASN C -5
REMARK 465 LEU C -4
REMARK 465 TYR C -3
REMARK 465 PHE C -2
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 465 GLN D -1
REMARK 465 GLY D 0
REMARK 465 VAL D 1
REMARK 465 MET E -20
REMARK 465 GLY E -19
REMARK 465 SER E -18
REMARK 465 SER E -17
REMARK 465 HIS E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 SER E -10
REMARK 465 SER E -9
REMARK 465 GLY E -8
REMARK 465 ARG E -7
REMARK 465 GLU E -6
REMARK 465 ASN E -5
REMARK 465 LEU E -4
REMARK 465 TYR E -3
REMARK 465 PHE E -2
REMARK 465 GLN E -1
REMARK 465 GLY E 0
REMARK 465 VAL E 1
REMARK 465 MET F -20
REMARK 465 GLY F -19
REMARK 465 SER F -18
REMARK 465 SER F -17
REMARK 465 HIS F -16
REMARK 465 HIS F -15
REMARK 465 HIS F -14
REMARK 465 HIS F -13
REMARK 465 HIS F -12
REMARK 465 HIS F -11
REMARK 465 SER F -10
REMARK 465 SER F -9
REMARK 465 GLY F -8
REMARK 465 ARG F -7
REMARK 465 GLU F -6
REMARK 465 ASN F -5
REMARK 465 LEU F -4
REMARK 465 TYR F -3
REMARK 465 PHE F -2
REMARK 465 GLN F -1
REMARK 465 GLY F 0
REMARK 465 VAL F 1
REMARK 465 MET G -20
REMARK 465 GLY G -19
REMARK 465 SER G -18
REMARK 465 SER G -17
REMARK 465 HIS G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 SER G -10
REMARK 465 SER G -9
REMARK 465 GLY G -8
REMARK 465 ARG G -7
REMARK 465 GLU G -6
REMARK 465 ASN G -5
REMARK 465 LEU G -4
REMARK 465 TYR G -3
REMARK 465 PHE G -2
REMARK 465 MET H -20
REMARK 465 GLY H -19
REMARK 465 SER H -18
REMARK 465 SER H -17
REMARK 465 HIS H -16
REMARK 465 HIS H -15
REMARK 465 HIS H -14
REMARK 465 HIS H -13
REMARK 465 HIS H -12
REMARK 465 HIS H -11
REMARK 465 SER H -10
REMARK 465 SER H -9
REMARK 465 GLY H -8
REMARK 465 ARG H -7
REMARK 465 GLU H -6
REMARK 465 ASN H -5
REMARK 465 LEU H -4
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 THR A 5 84.61 -68.67
REMARK 500 GLN A 7 -138.41 55.93
REMARK 500 SER A 97 -112.21 54.97
REMARK 500 LYS A 115 -73.54 -83.27
REMARK 500 HIS A 166 51.62 -107.87
REMARK 500 ASP A 201 103.50 -161.56
REMARK 500 ASN A 238 60.84 -108.49
REMARK 500 ALA A 250 66.32 -100.95
REMARK 500 GLN A 275 54.65 -100.88
REMARK 500 SER B 97 -112.51 57.02
REMARK 500 THR B 153 -61.20 -120.91
REMARK 500 HIS B 166 57.56 -99.20
REMARK 500 PRO B 212 100.34 -58.79
REMARK 500 ASN B 238 40.20 -109.99
REMARK 500 SER C 97 -113.51 55.25
REMARK 500 LYS C 115 -63.29 -90.22
REMARK 500 THR C 153 -54.58 -120.91
REMARK 500 PRO C 155 3.95 -69.96
REMARK 500 ASP C 201 104.88 -160.90
REMARK 500 GLU D 8 -6.55 83.32
REMARK 500 THR D 71 -168.92 -102.08
REMARK 500 SER D 97 -109.30 54.68
REMARK 500 THR D 153 -55.52 -121.84
REMARK 500 LEU D 223 -55.30 -128.17
REMARK 500 THR D 224 79.37 -119.48
REMARK 500 ASN D 238 74.50 -117.18
REMARK 500 ALA D 250 76.65 -102.52
REMARK 500 GLU E 8 -4.68 82.02
REMARK 500 ASP E 20 -156.79 -114.65
REMARK 500 SER E 97 -112.88 56.02
REMARK 500 LYS E 115 -72.52 -78.27
REMARK 500 THR E 153 -56.65 -123.63
REMARK 500 HIS E 166 48.42 -108.31
REMARK 500 PRO E 212 107.37 -56.97
REMARK 500 LEU E 223 -53.72 -126.99
REMARK 500 THR E 224 77.14 -118.99
REMARK 500 ASN E 238 51.75 -117.66
REMARK 500 GLN F 7 -132.96 58.57
REMARK 500 SER F 97 -108.15 55.56
REMARK 500 LYS F 115 -73.11 -84.47
REMARK 500 HIS F 166 50.31 -106.55
REMARK 500 ASP F 201 94.86 -161.29
REMARK 500 ASN F 238 67.43 -105.81
REMARK 500 ALA F 250 67.95 -102.24
REMARK 500 GLN G 7 -127.44 57.48
REMARK 500 SER G 97 -112.80 55.83
REMARK 500 LYS G 115 -77.14 -82.55
REMARK 500 THR G 153 -58.02 -124.31
REMARK 500 HIS G 166 53.76 -96.31
REMARK 500 ASP G 201 99.24 -160.86
REMARK 500
REMARK 500 THIS ENTRY HAS 58 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY C 0 VAL C 1 144.04
REMARK 500 TYR H -3 PHE H -2 -35.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH F 329 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH G 434 DISTANCE = 5.57 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4Q3K RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3M RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3N RELATED DB: PDB
REMARK 900 RELATED ID: 4Q3O RELATED DB: PDB
DBREF 4Q3L A -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L B -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L C -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L D -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L E -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L F -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L G -20 276 PDB 4Q3L 4Q3L -20 276
DBREF 4Q3L H -20 276 PDB 4Q3L 4Q3L -20 276
SEQRES 1 A 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 A 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 A 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 A 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 A 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 A 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 A 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 A 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 A 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 A 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 A 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 A 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 A 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 A 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 A 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 A 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 A 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 A 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 A 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 A 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 A 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 A 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 B 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 B 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 B 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 B 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 B 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 B 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 B 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 B 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 B 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 B 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 B 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 B 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 B 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 B 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 B 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 B 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 B 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 B 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 B 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 B 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 B 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 B 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 C 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 C 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 C 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 C 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 C 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 C 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 C 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 C 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 C 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 C 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 C 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 C 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 C 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 C 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 C 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 C 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 C 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 C 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 C 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 C 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 C 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 C 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 D 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 D 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 D 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 D 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 D 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 D 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 D 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 D 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 D 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 D 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 D 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 D 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 D 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 D 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 D 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 D 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 D 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 D 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 D 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 D 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 D 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 D 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 E 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 E 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 E 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 E 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 E 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 E 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 E 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 E 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 E 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 E 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 E 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 E 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 E 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 E 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 E 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 E 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 E 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 E 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 E 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 E 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 E 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 E 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 E 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 F 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 F 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 F 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 F 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 F 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 F 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 F 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 F 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 F 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 F 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 F 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 F 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 F 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 F 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 F 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 F 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 F 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 F 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 F 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 F 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 F 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 F 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 F 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 G 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 G 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 G 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 G 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 G 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 G 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 G 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 G 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 G 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 G 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 G 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 G 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 G 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 G 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 G 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 G 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 G 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 G 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 G 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 G 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 G 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 G 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 G 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
SEQRES 1 H 297 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 297 ARG GLU ASN LEU TYR PHE GLN GLY VAL SER ILE PHE THR
SEQRES 3 H 297 TYR GLN GLU LYS ASP ILE TYR TYR GLU ILE ASP GLY THR
SEQRES 4 H 297 LEU ASP ILE ASN SER ASP VAL ILE VAL ILE LEU ASN GLY
SEQRES 5 H 297 ILE MET MET SER THR LYS SER TRP ASP ALA PHE VAL GLU
SEQRES 6 H 297 ASN PHE SER LYS ASN HIS VAL LEU LEU ARG TYR ASP MET
SEQRES 7 H 297 PHE ASP GLN GLY GLN SER SER LYS ILE GLU GLU SER TYR
SEQRES 8 H 297 THR GLN THR ILE GLN VAL GLU LEU LEU LYS ASN LEU LEU
SEQRES 9 H 297 GLU HIS LEU GLY ILE ALA GLN ALA ASN ILE VAL GLY ILE
SEQRES 10 H 297 SER TYR GLY ALA SER ILE ALA LEU GLN PHE ALA ALA LYS
SEQRES 11 H 297 TYR PRO THR MET ILE LYS ARG MET VAL VAL ALA ASN VAL
SEQRES 12 H 297 VAL ALA LYS THR SER PRO TRP LEU LYS ASP ILE GLY ASP
SEQRES 13 H 297 GLY TRP ASN GLU VAL ALA LYS THR GLY ASN GLY LEU ALA
SEQRES 14 H 297 TYR TYR HIS ILE THR ILE PRO TYR ILE TYR SER PRO GLN
SEQRES 15 H 297 PHE TYR THR LEU HIS ASN ASP TRP MET GLU LYS ARG LYS
SEQRES 16 H 297 GLU LEU LEU VAL PRO LEU PHE SER THR ARG THR PHE LEU
SEQRES 17 H 297 ASP ARG MET ILE ARG LEU THR LYS SER ALA GLU THR HIS
SEQRES 18 H 297 ASP VAL ILE LYS ASP LEU PRO ASN ILE LYS THR PRO THR
SEQRES 19 H 297 LEU ILE ILE SER SER GLU GLU ASP TYR LEU THR PRO PRO
SEQRES 20 H 297 PHE GLU GLN LYS TYR LEU GLN GLU HIS LEU GLN ASN ALA
SEQRES 21 H 297 GLU LEU VAL SER ILE PRO ASN CYS GLY HIS ALA SER MET
SEQRES 22 H 297 TYR GLU VAL PRO LYS THR PHE THR ALA LEU VAL LEU GLY
SEQRES 23 H 297 PHE PHE GLY GLN THR LYS LEU ASP TYR GLN ILE
HET GOL B 301 6
HET GOL G 301 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 11 HOH *292(H2 O)
HELIX 1 1 SER A 35 ALA A 41 5 7
HELIX 2 2 PHE A 42 SER A 47 1 6
HELIX 3 3 GLN A 72 LEU A 86 1 15
HELIX 4 4 SER A 97 TYR A 110 1 14
HELIX 5 5 SER A 127 LYS A 142 1 16
HELIX 6 6 ASN A 145 ILE A 154 1 10
HELIX 7 7 PRO A 155 ILE A 157 5 3
HELIX 8 8 SER A 159 HIS A 166 1 8
HELIX 9 9 HIS A 166 THR A 183 1 18
HELIX 10 10 THR A 183 ALA A 197 1 15
HELIX 11 11 GLU A 198 HIS A 200 5 3
HELIX 12 12 VAL A 202 ILE A 209 5 8
HELIX 13 13 PRO A 225 LEU A 236 1 12
HELIX 14 14 ALA A 250 VAL A 255 1 6
HELIX 15 15 VAL A 255 GLN A 269 1 15
HELIX 16 16 SER B 35 SER B 38 5 4
HELIX 17 17 TRP B 39 SER B 47 1 9
HELIX 18 18 GLN B 72 LEU B 86 1 15
HELIX 19 19 SER B 97 TYR B 110 1 14
HELIX 20 20 SER B 127 THR B 143 1 17
HELIX 21 21 ASN B 145 ILE B 152 1 8
HELIX 22 22 THR B 153 ILE B 157 5 5
HELIX 23 23 SER B 159 HIS B 166 1 8
HELIX 24 24 HIS B 166 PHE B 181 1 16
HELIX 25 25 THR B 183 ALA B 197 1 15
HELIX 26 26 GLU B 198 HIS B 200 5 3
HELIX 27 27 ASP B 205 ILE B 209 5 5
HELIX 28 28 PRO B 225 LEU B 236 1 12
HELIX 29 29 ALA B 250 VAL B 255 1 6
HELIX 30 30 VAL B 255 GLN B 269 1 15
HELIX 31 31 SER C 35 ALA C 41 5 7
HELIX 32 32 PHE C 42 SER C 47 1 6
HELIX 33 33 GLN C 72 LEU C 86 1 15
HELIX 34 34 SER C 97 TYR C 110 1 14
HELIX 35 35 SER C 127 LYS C 142 1 16
HELIX 36 36 ASN C 145 ILE C 152 1 8
HELIX 37 37 THR C 153 TYR C 158 1 6
HELIX 38 38 SER C 159 HIS C 166 1 8
HELIX 39 39 HIS C 166 LYS C 172 1 7
HELIX 40 40 LEU C 176 PHE C 181 1 6
HELIX 41 41 THR C 183 ALA C 197 1 15
HELIX 42 42 GLU C 198 HIS C 200 5 3
HELIX 43 43 PRO C 225 LEU C 236 1 12
HELIX 44 44 ALA C 250 VAL C 255 1 6
HELIX 45 45 VAL C 255 GLN C 269 1 15
HELIX 46 46 SER D 35 ALA D 41 5 7
HELIX 47 47 PHE D 42 SER D 47 1 6
HELIX 48 48 GLN D 72 LEU D 86 1 15
HELIX 49 49 SER D 97 TYR D 110 1 14
HELIX 50 50 SER D 127 LYS D 142 1 16
HELIX 51 51 ASN D 145 ILE D 152 1 8
HELIX 52 52 THR D 153 TYR D 158 1 6
HELIX 53 53 SER D 159 HIS D 166 1 8
HELIX 54 54 HIS D 166 SER D 182 1 17
HELIX 55 55 THR D 183 SER D 196 1 14
HELIX 56 56 ALA D 197 HIS D 200 5 4
HELIX 57 57 ASP D 205 ILE D 209 5 5
HELIX 58 58 PRO D 225 LEU D 236 1 12
HELIX 59 59 ALA D 250 VAL D 255 1 6
HELIX 60 60 VAL D 255 GLN D 269 1 15
HELIX 61 61 SER E 35 ALA E 41 5 7
HELIX 62 62 PHE E 42 SER E 47 1 6
HELIX 63 63 GLN E 72 LEU E 86 1 15
HELIX 64 64 SER E 97 TYR E 110 1 14
HELIX 65 65 SER E 127 THR E 143 1 17
HELIX 66 66 ASN E 145 ILE E 152 1 8
HELIX 67 67 THR E 153 ILE E 157 5 5
HELIX 68 68 SER E 159 HIS E 166 1 8
HELIX 69 69 HIS E 166 SER E 182 1 17
HELIX 70 70 THR E 183 ALA E 197 1 15
HELIX 71 71 GLU E 198 HIS E 200 5 3
HELIX 72 72 ASP E 205 ILE E 209 5 5
HELIX 73 73 PRO E 225 LEU E 236 1 12
HELIX 74 74 ALA E 250 VAL E 255 1 6
HELIX 75 75 VAL E 255 GLN E 269 1 15
HELIX 76 76 SER F 35 SER F 38 5 4
HELIX 77 77 TRP F 39 SER F 47 1 9
HELIX 78 78 GLN F 72 GLY F 87 1 16
HELIX 79 79 SER F 97 TYR F 110 1 14
HELIX 80 80 SER F 127 LYS F 142 1 16
HELIX 81 81 ASN F 145 ILE F 152 1 8
HELIX 82 82 THR F 153 ILE F 157 5 5
HELIX 83 83 SER F 159 HIS F 166 1 8
HELIX 84 84 HIS F 166 THR F 183 1 18
HELIX 85 85 THR F 183 ALA F 197 1 15
HELIX 86 86 GLU F 198 HIS F 200 5 3
HELIX 87 87 VAL F 202 ILE F 209 5 8
HELIX 88 88 PRO F 225 LEU F 236 1 12
HELIX 89 89 ALA F 250 VAL F 255 1 6
HELIX 90 90 VAL F 255 GLN F 269 1 15
HELIX 91 91 SER G 35 ALA G 41 5 7
HELIX 92 92 PHE G 42 SER G 47 1 6
HELIX 93 93 GLN G 72 LEU G 86 1 15
HELIX 94 94 SER G 97 TYR G 110 1 14
HELIX 95 95 SER G 127 GLY G 144 1 18
HELIX 96 96 ASN G 145 ILE G 152 1 8
HELIX 97 97 THR G 153 TYR G 158 1 6
HELIX 98 98 SER G 159 HIS G 166 1 8
HELIX 99 99 HIS G 166 PHE G 181 1 16
HELIX 100 100 THR G 183 ALA G 197 1 15
HELIX 101 101 GLU G 198 HIS G 200 5 3
HELIX 102 102 ASP G 205 ILE G 209 5 5
HELIX 103 103 PRO G 225 GLU G 234 1 10
HELIX 104 104 ALA G 250 VAL G 255 1 6
HELIX 105 105 VAL G 255 GLN G 269 1 15
HELIX 106 106 THR H 36 ASP H 40 5 5
HELIX 107 107 PHE H 42 SER H 47 1 6
HELIX 108 108 GLN H 72 LEU H 86 1 15
HELIX 109 109 SER H 97 TYR H 110 1 14
HELIX 110 110 SER H 127 LYS H 142 1 16
HELIX 111 111 ASN H 145 TYR H 158 1 14
HELIX 112 112 SER H 159 HIS H 166 1 8
HELIX 113 113 TRP H 169 PHE H 181 1 13
HELIX 114 114 THR H 183 ALA H 197 1 15
HELIX 115 115 GLU H 198 HIS H 200 5 3
HELIX 116 116 ASP H 205 ILE H 209 5 5
HELIX 117 117 PRO H 225 LEU H 236 1 12
HELIX 118 118 ALA H 250 VAL H 255 1 6
HELIX 119 119 VAL H 255 GLN H 269 1 15
SHEET 1 A 8 ILE A 3 TYR A 6 0
SHEET 2 A 8 LYS A 9 ASP A 16 -1 O ILE A 11 N PHE A 4
SHEET 3 A 8 VAL A 51 TYR A 55 -1 O ARG A 54 N GLU A 14
SHEET 4 A 8 VAL A 25 LEU A 29 1 N ILE A 26 O LEU A 53
SHEET 5 A 8 ALA A 91 ILE A 96 1 O ASN A 92 N VAL A 25
SHEET 6 A 8 ILE A 114 ALA A 120 1 O VAL A 118 N ILE A 93
SHEET 7 A 8 THR A 213 SER A 218 1 O ILE A 216 N VAL A 119
SHEET 8 A 8 ALA A 239 ILE A 244 1 O GLU A 240 N ILE A 215
SHEET 1 B 8 ILE B 3 TYR B 6 0
SHEET 2 B 8 LYS B 9 ASP B 16 -1 O LYS B 9 N TYR B 6
SHEET 3 B 8 VAL B 51 TYR B 55 -1 O ARG B 54 N GLU B 14
SHEET 4 B 8 VAL B 25 LEU B 29 1 N ILE B 26 O LEU B 53
SHEET 5 B 8 ALA B 91 ILE B 96 1 O ASN B 92 N VAL B 27
SHEET 6 B 8 ILE B 114 ALA B 120 1 O VAL B 118 N ILE B 93
SHEET 7 B 8 THR B 213 SER B 218 1 O ILE B 216 N VAL B 119
SHEET 8 B 8 ALA B 239 ILE B 244 1 O GLU B 240 N ILE B 215
SHEET 1 C 8 ILE C 3 THR C 5 0
SHEET 2 C 8 ASP C 10 ASP C 16 -1 O ILE C 11 N PHE C 4
SHEET 3 C 8 VAL C 51 TYR C 55 -1 O ARG C 54 N GLU C 14
SHEET 4 C 8 VAL C 25 LEU C 29 1 N ILE C 26 O LEU C 53
SHEET 5 C 8 ALA C 91 ILE C 96 1 O ASN C 92 N VAL C 25
SHEET 6 C 8 ILE C 114 ALA C 120 1 O VAL C 118 N ILE C 93
SHEET 7 C 8 THR C 213 SER C 218 1 O ILE C 216 N VAL C 119
SHEET 8 C 8 ALA C 239 ILE C 244 1 O GLU C 240 N ILE C 215
SHEET 1 D 8 ILE D 3 TYR D 6 0
SHEET 2 D 8 LYS D 9 ASP D 16 -1 O ILE D 11 N PHE D 4
SHEET 3 D 8 VAL D 51 TYR D 55 -1 O ARG D 54 N GLU D 14
SHEET 4 D 8 VAL D 25 LEU D 29 1 N ILE D 26 O LEU D 53
SHEET 5 D 8 ALA D 91 ILE D 96 1 O ASN D 92 N VAL D 27
SHEET 6 D 8 ILE D 114 ALA D 120 1 O VAL D 118 N ILE D 93
SHEET 7 D 8 THR D 213 SER D 218 1 O ILE D 216 N VAL D 119
SHEET 8 D 8 ALA D 239 ILE D 244 1 O GLU D 240 N ILE D 215
SHEET 1 E 8 ILE E 3 TYR E 6 0
SHEET 2 E 8 LYS E 9 ASP E 16 -1 O LYS E 9 N TYR E 6
SHEET 3 E 8 VAL E 51 TYR E 55 -1 O ARG E 54 N GLU E 14
SHEET 4 E 8 VAL E 25 LEU E 29 1 N ILE E 26 O LEU E 53
SHEET 5 E 8 ALA E 91 ILE E 96 1 O ASN E 92 N VAL E 25
SHEET 6 E 8 ILE E 114 ALA E 120 1 O ALA E 120 N GLY E 95
SHEET 7 E 8 THR E 213 SER E 218 1 O ILE E 216 N VAL E 119
SHEET 8 E 8 ALA E 239 ILE E 244 1 O GLU E 240 N THR E 213
SHEET 1 F 8 ILE F 3 TYR F 6 0
SHEET 2 F 8 LYS F 9 ASP F 16 -1 O ILE F 11 N PHE F 4
SHEET 3 F 8 VAL F 51 TYR F 55 -1 O ARG F 54 N GLU F 14
SHEET 4 F 8 VAL F 25 LEU F 29 1 N ILE F 26 O LEU F 53
SHEET 5 F 8 ALA F 91 ILE F 96 1 O ASN F 92 N VAL F 25
SHEET 6 F 8 ILE F 114 ALA F 120 1 O VAL F 118 N ILE F 93
SHEET 7 F 8 THR F 213 SER F 218 1 O ILE F 216 N VAL F 119
SHEET 8 F 8 ALA F 239 ILE F 244 1 O GLU F 240 N ILE F 215
SHEET 1 G 8 ILE G 3 TYR G 6 0
SHEET 2 G 8 LYS G 9 ASP G 16 -1 O ILE G 11 N PHE G 4
SHEET 3 G 8 VAL G 51 TYR G 55 -1 O ARG G 54 N GLU G 14
SHEET 4 G 8 VAL G 25 LEU G 29 1 N ILE G 26 O LEU G 53
SHEET 5 G 8 ALA G 91 ILE G 96 1 O ASN G 92 N VAL G 27
SHEET 6 G 8 ILE G 114 ALA G 120 1 O VAL G 118 N ILE G 93
SHEET 7 G 8 THR G 213 SER G 218 1 O ILE G 216 N VAL G 119
SHEET 8 G 8 ALA G 239 ILE G 244 1 O GLU G 240 N ILE G 215
SHEET 1 H 8 ILE H 3 TYR H 6 0
SHEET 2 H 8 LYS H 9 ASP H 16 -1 O ILE H 11 N PHE H 4
SHEET 3 H 8 VAL H 51 TYR H 55 -1 O ARG H 54 N GLU H 14
SHEET 4 H 8 VAL H 25 LEU H 29 1 N ILE H 26 O LEU H 53
SHEET 5 H 8 ALA H 91 ILE H 96 1 O ASN H 92 N VAL H 27
SHEET 6 H 8 ILE H 114 ALA H 120 1 O VAL H 118 N GLY H 95
SHEET 7 H 8 THR H 213 SER H 218 1 O ILE H 216 N VAL H 119
SHEET 8 H 8 ALA H 239 ILE H 244 1 O GLU H 240 N ILE H 215
SITE 1 AC1 2 LYS B 115 ARG B 116
SITE 1 AC2 3 LYS G 115 ARG G 116 LYS G 271
CRYST1 105.568 139.134 111.109 90.00 89.94 90.00 P 1 21 1 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 0.009473 0.000000 -0.000010 0.00000
SCALE2 0.000000 0.007187 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009000 0.00000
TER 2224 ILE A 276
TER 4491 ILE B 276
TER 6735 ILE C 276
TER 8967 ILE D 276
TER 11191 ILE E 276
TER 13415 ILE F 276
TER 15659 ILE G 276
TER 17926 ILE H 276
MASTER 972 0 2 119 64 0 2 618214 8 12 184
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