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HEADER HYDROLASE 11-AUG-20 7JQY
TITLE CRYSTAL STRUCTURE OF CFL1-D123S FROM BURKHOLDERIA CENOCEPACIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CIF-LIKE 1;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA CENOCEPACIA (STRAIN ATCC BAA-245 /
SOURCE 3 DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610);
SOURCE 4 ORGANISM_TAXID: 216591;
SOURCE 5 STRAIN: ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 /
SOURCE 6 CF5610;
SOURCE 7 GENE: BCAM1529;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OCTAMER, ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.TAHER,D.R.MADDEN
REVDAT 1 17-MAR-21 7JQY 0
JRNL AUTH N.M.TAHER,K.L.HVORECNY,C.M.BURKE,M.S.A.GILMAN,G.E.HEUSSLER,
JRNL AUTH 2 J.ADOLF-BRYFOGLE,C.D.BAHL,G.A.O'TOOLE,D.R.MADDEN
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF TWO CIF-LIKE
JRNL TITL 2 EPOXIDE HYDROLASES FROM BURKHOLDERIA CENOCEPACIA
JRNL REF CURR RES STRUCT BIOL 2021
JRNL REFN ESSN 2665-928X
JRNL DOI 10.1016/J.CRSTBI.2021.02.002
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.17.1_3660
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.71
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 152005
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 7615
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 2.1800 - 2.1500 0.90 4177 379 0.3516 0.4105
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) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 31
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 11 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7933 8.4865 72.5960
REMARK 3 T TENSOR
REMARK 3 T11: 0.4480 T22: 0.3357
REMARK 3 T33: 0.3222 T12: 0.0208
REMARK 3 T13: -0.0533 T23: 0.0176
REMARK 3 L TENSOR
REMARK 3 L11: 0.0256 L22: -0.0018
REMARK 3 L33: 0.0071 L12: -0.0007
REMARK 3 L13: -0.0255 L23: 0.0079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: -0.0077 S13: -0.1349
REMARK 3 S21: 0.1216 S22: -0.0195 S23: -0.0096
REMARK 3 S31: 0.0692 S32: -0.0310 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 33 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4753 16.0157 73.9595
REMARK 3 T TENSOR
REMARK 3 T11: 0.2964 T22: 0.2898
REMARK 3 T33: 0.3155 T12: 0.0440
REMARK 3 T13: -0.0462 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.0287 L22: 0.0024
REMARK 3 L33: 0.0152 L12: -0.0002
REMARK 3 L13: -0.0186 L23: -0.0279
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: -0.0248 S13: 0.0269
REMARK 3 S21: 0.0140 S22: -0.0224 S23: -0.1328
REMARK 3 S31: -0.0186 S32: 0.1162 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 61 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.3591 24.5523 65.2504
REMARK 3 T TENSOR
REMARK 3 T11: 0.3115 T22: 0.2661
REMARK 3 T33: 0.3037 T12: -0.0001
REMARK 3 T13: -0.0037 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.1036 L22: 0.1180
REMARK 3 L33: 0.1473 L12: 0.0586
REMARK 3 L13: -0.0097 L23: 0.0839
REMARK 3 S TENSOR
REMARK 3 S11: 0.0017 S12: 0.0593 S13: 0.0848
REMARK 3 S21: 0.0031 S22: 0.0070 S23: -0.0488
REMARK 3 S31: 0.0374 S32: 0.0075 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 244 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.8043 14.4483 54.0608
REMARK 3 T TENSOR
REMARK 3 T11: 0.3213 T22: 0.3279
REMARK 3 T33: 0.2803 T12: 0.0182
REMARK 3 T13: 0.0012 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.0136 L22: 0.0262
REMARK 3 L33: 0.0289 L12: -0.0145
REMARK 3 L13: -0.0044 L23: 0.0230
REMARK 3 S TENSOR
REMARK 3 S11: -0.0101 S12: 0.0741 S13: 0.0689
REMARK 3 S21: -0.1059 S22: 0.0238 S23: -0.0728
REMARK 3 S31: 0.0658 S32: 0.0623 S33: -0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 11 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -39.0805 8.4792 91.9389
REMARK 3 T TENSOR
REMARK 3 T11: 0.4380 T22: 0.3571
REMARK 3 T33: 0.3052 T12: -0.0202
REMARK 3 T13: -0.0407 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.0149 L22: 0.0090
REMARK 3 L33: 0.0164 L12: 0.0135
REMARK 3 L13: 0.0243 L23: 0.0152
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: -0.0933 S13: -0.0338
REMARK 3 S21: -0.0578 S22: -0.0536 S23: 0.0020
REMARK 3 S31: 0.1583 S32: -0.0131 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.8290 12.0375 101.5094
REMARK 3 T TENSOR
REMARK 3 T11: 0.3395 T22: 0.3302
REMARK 3 T33: 0.1708 T12: -0.0297
REMARK 3 T13: -0.0282 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.0282 L22: 0.0103
REMARK 3 L33: 0.0396 L12: 0.0287
REMARK 3 L13: 0.0252 L23: -0.0196
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: -0.1987 S13: -0.0460
REMARK 3 S21: 0.0627 S22: -0.0586 S23: -0.0393
REMARK 3 S31: -0.0105 S32: -0.0636 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.8443 25.9548 101.9820
REMARK 3 T TENSOR
REMARK 3 T11: 0.2410 T22: 0.3597
REMARK 3 T33: 0.1964 T12: 0.0222
REMARK 3 T13: -0.0361 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 0.1153 L22: 0.0805
REMARK 3 L33: 0.0787 L12: 0.0686
REMARK 3 L13: 0.0421 L23: -0.0701
REMARK 3 S TENSOR
REMARK 3 S11: 0.0387 S12: -0.2813 S13: 0.2473
REMARK 3 S21: -0.0186 S22: -0.0117 S23: -0.0159
REMARK 3 S31: 0.0276 S32: -0.0148 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 244 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.0908 13.0608 105.4027
REMARK 3 T TENSOR
REMARK 3 T11: 0.3785 T22: 0.4749
REMARK 3 T33: 0.2974 T12: 0.0127
REMARK 3 T13: -0.0761 T23: 0.0170
REMARK 3 L TENSOR
REMARK 3 L11: 0.0233 L22: -0.0009
REMARK 3 L33: 0.0111 L12: -0.0098
REMARK 3 L13: 0.0053 L23: 0.0112
REMARK 3 S TENSOR
REMARK 3 S11: 0.0508 S12: -0.2624 S13: -0.0380
REMARK 3 S21: -0.0050 S22: -0.0564 S23: -0.2358
REMARK 3 S31: 0.1032 S32: 0.1551 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 12 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2671 -2.1111 32.4628
REMARK 3 T TENSOR
REMARK 3 T11: 0.4238 T22: 0.5882
REMARK 3 T33: 0.3833 T12: 0.0256
REMARK 3 T13: -0.0269 T23: -0.0665
REMARK 3 L TENSOR
REMARK 3 L11: 0.0090 L22: 0.0012
REMARK 3 L33: 0.0007 L12: 0.0102
REMARK 3 L13: -0.0197 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0181 S12: -0.0626 S13: -0.0185
REMARK 3 S21: 0.0454 S22: -0.0574 S23: -0.1066
REMARK 3 S31: 0.0028 S32: 0.1719 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 33 THROUGH 60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2600 -9.7887 32.0732
REMARK 3 T TENSOR
REMARK 3 T11: 0.3933 T22: 0.3278
REMARK 3 T33: 0.2818 T12: 0.0348
REMARK 3 T13: -0.0069 T23: 0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.0099 L22: 0.0050
REMARK 3 L33: 0.0048 L12: -0.0035
REMARK 3 L13: -0.0090 L23: -0.0232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0208 S12: -0.0369 S13: -0.1155
REMARK 3 S21: 0.0274 S22: 0.0614 S23: -0.0262
REMARK 3 S31: 0.1228 S32: 0.0401 S33: 0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 61 THROUGH 186 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.3348 -4.4174 30.3394
REMARK 3 T TENSOR
REMARK 3 T11: 0.3943 T22: 0.3516
REMARK 3 T33: 0.3178 T12: 0.0129
REMARK 3 T13: 0.0309 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.0468 L22: 0.0866
REMARK 3 L33: 0.1558 L12: -0.0224
REMARK 3 L13: -0.1113 L23: 0.0798
REMARK 3 S TENSOR
REMARK 3 S11: 0.0335 S12: 0.0565 S13: -0.0387
REMARK 3 S21: 0.0530 S22: 0.0304 S23: 0.0619
REMARK 3 S31: 0.0442 S32: -0.0388 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 187 THROUGH 259 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0996 2.1965 27.5282
REMARK 3 T TENSOR
REMARK 3 T11: 0.3691 T22: 0.3835
REMARK 3 T33: 0.3297 T12: -0.0254
REMARK 3 T13: 0.0156 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.0217 L22: 0.0400
REMARK 3 L33: 0.0830 L12: -0.0955
REMARK 3 L13: -0.0155 L23: 0.0319
REMARK 3 S TENSOR
REMARK 3 S11: 0.0070 S12: 0.0467 S13: 0.0236
REMARK 3 S21: 0.0093 S22: 0.0268 S23: 0.0131
REMARK 3 S31: 0.0236 S32: -0.1117 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 260 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): -11.4325 3.8890 43.4623
REMARK 3 T TENSOR
REMARK 3 T11: 0.3928 T22: 0.3563
REMARK 3 T33: 0.2901 T12: 0.0088
REMARK 3 T13: 0.0188 T23: -0.0061
REMARK 3 L TENSOR
REMARK 3 L11: 0.0097 L22: 0.0188
REMARK 3 L33: 0.0149 L12: -0.0096
REMARK 3 L13: -0.0148 L23: 0.0175
REMARK 3 S TENSOR
REMARK 3 S11: -0.0459 S12: -0.0644 S13: -0.0210
REMARK 3 S21: 0.1910 S22: 0.0677 S23: 0.0246
REMARK 3 S31: 0.0553 S32: 0.0092 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 11 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.2200 -4.9152 17.4798
REMARK 3 T TENSOR
REMARK 3 T11: 0.3681 T22: 0.9113
REMARK 3 T33: 0.3792 T12: 0.0728
REMARK 3 T13: -0.0600 T23: -0.0266
REMARK 3 L TENSOR
REMARK 3 L11: 0.0155 L22: 0.0045
REMARK 3 L33: 0.0130 L12: 0.0041
REMARK 3 L13: 0.0188 L23: 0.0097
REMARK 3 S TENSOR
REMARK 3 S11: 0.0035 S12: -0.0609 S13: 0.0334
REMARK 3 S21: 0.0960 S22: 0.1015 S23: -0.0787
REMARK 3 S31: -0.0274 S32: 0.0370 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 33 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.1184 -12.9370 10.8021
REMARK 3 T TENSOR
REMARK 3 T11: 0.3698 T22: 0.8019
REMARK 3 T33: 0.3089 T12: 0.2008
REMARK 3 T13: -0.0156 T23: -0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.0087 L22: 0.0315
REMARK 3 L33: -0.0053 L12: 0.0015
REMARK 3 L13: 0.0021 L23: -0.0020
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: 0.0349 S13: 0.0016
REMARK 3 S21: -0.0202 S22: 0.0763 S23: -0.1401
REMARK 3 S31: 0.1031 S32: 0.2439 S33: 0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 83 THROUGH 230 )
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4265 -16.6732 3.8118
REMARK 3 T TENSOR
REMARK 3 T11: 0.4128 T22: 0.4860
REMARK 3 T33: 0.2390 T12: 0.1270
REMARK 3 T13: 0.0594 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0476 L22: 0.0260
REMARK 3 L33: 0.1622 L12: -0.0219
REMARK 3 L13: -0.0554 L23: -0.0318
REMARK 3 S TENSOR
REMARK 3 S11: -0.1374 S12: -0.0863 S13: 0.1693
REMARK 3 S21: -0.0134 S22: 0.0803 S23: 0.1032
REMARK 3 S31: 0.1934 S32: 0.4103 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 231 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8253 -28.1981 12.3701
REMARK 3 T TENSOR
REMARK 3 T11: 0.6335 T22: 0.5701
REMARK 3 T33: 0.3695 T12: 0.2720
REMARK 3 T13: 0.0401 T23: 0.0780
REMARK 3 L TENSOR
REMARK 3 L11: 0.0242 L22: 0.0072
REMARK 3 L33: 0.0193 L12: 0.0104
REMARK 3 L13: 0.0033 L23: -0.0190
REMARK 3 S TENSOR
REMARK 3 S11: -0.0735 S12: -0.2336 S13: -0.1652
REMARK 3 S21: 0.0337 S22: -0.0044 S23: -0.0428
REMARK 3 S31: 0.3230 S32: 0.2431 S33: -0.0000
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 11 THROUGH 36 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8769 17.6528 72.0540
REMARK 3 T TENSOR
REMARK 3 T11: 0.4583 T22: 0.2771
REMARK 3 T33: 1.2416 T12: 0.0688
REMARK 3 T13: -0.1266 T23: 0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 0.0093 L22: 0.0081
REMARK 3 L33: 0.0233 L12: -0.0194
REMARK 3 L13: -0.0032 L23: 0.0079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0386 S12: -0.0329 S13: 0.1371
REMARK 3 S21: 0.1141 S22: -0.1205 S23: -0.1263
REMARK 3 S31: 0.0696 S32: -0.1429 S33: 0.0000
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 37 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0590 12.0842 67.8907
REMARK 3 T TENSOR
REMARK 3 T11: -0.1896 T22: -0.4084
REMARK 3 T33: 0.9926 T12: 0.5384
REMARK 3 T13: -0.1867 T23: 0.1525
REMARK 3 L TENSOR
REMARK 3 L11: 0.0047 L22: -0.0022
REMARK 3 L33: 0.0355 L12: 0.0036
REMARK 3 L13: 0.0219 L23: -0.0121
REMARK 3 S TENSOR
REMARK 3 S11: -0.1858 S12: -0.0528 S13: 0.4926
REMARK 3 S21: 0.0661 S22: -0.1147 S23: -0.1361
REMARK 3 S31: 0.4914 S32: -0.4400 S33: -0.0000
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 136 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8529 0.2577 59.3480
REMARK 3 T TENSOR
REMARK 3 T11: 0.3003 T22: 0.2650
REMARK 3 T33: 0.6477 T12: 0.0110
REMARK 3 T13: -0.0131 T23: 0.1329
REMARK 3 L TENSOR
REMARK 3 L11: 0.0385 L22: 0.0706
REMARK 3 L33: -0.0204 L12: -0.0666
REMARK 3 L13: -0.0295 L23: 0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0476 S12: 0.1917 S13: 0.3465
REMARK 3 S21: 0.0252 S22: -0.0963 S23: -0.0652
REMARK 3 S31: 0.0718 S32: -0.0478 S33: 0.0000
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 244 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.6365 15.2135 51.1471
REMARK 3 T TENSOR
REMARK 3 T11: 0.3180 T22: 0.2648
REMARK 3 T33: 1.1590 T12: 0.1641
REMARK 3 T13: -0.1107 T23: 0.4622
REMARK 3 L TENSOR
REMARK 3 L11: 0.0134 L22: 0.0287
REMARK 3 L33: 0.0284 L12: 0.0045
REMARK 3 L13: 0.0158 L23: -0.0104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0332 S12: 0.1136 S13: 0.1365
REMARK 3 S21: -0.1028 S22: -0.0397 S23: -0.1912
REMARK 3 S31: -0.0230 S32: -0.1482 S33: -0.0000
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 11 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): -30.3055 19.3184 -14.9088
REMARK 3 T TENSOR
REMARK 3 T11: 0.5501 T22: 0.8598
REMARK 3 T33: 0.4775 T12: 0.1941
REMARK 3 T13: 0.0218 T23: 0.2276
REMARK 3 L TENSOR
REMARK 3 L11: 0.0033 L22: 0.0032
REMARK 3 L33: 0.0001 L12: 0.0019
REMARK 3 L13: 0.0005 L23: -0.0069
REMARK 3 S TENSOR
REMARK 3 S11: 0.1034 S12: 0.0474 S13: -0.0596
REMARK 3 S21: -0.0205 S22: 0.0479 S23: 0.0624
REMARK 3 S31: -0.1587 S32: -0.1413 S33: -0.0000
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 33 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0849 24.8967 -6.8397
REMARK 3 T TENSOR
REMARK 3 T11: 0.4787 T22: 0.9132
REMARK 3 T33: 0.1574 T12: 0.6459
REMARK 3 T13: -0.0285 T23: 0.4208
REMARK 3 L TENSOR
REMARK 3 L11: 0.0214 L22: 0.0117
REMARK 3 L33: 0.0165 L12: -0.0114
REMARK 3 L13: -0.0205 L23: -0.0097
REMARK 3 S TENSOR
REMARK 3 S11: 0.1712 S12: 0.0581 S13: 0.0676
REMARK 3 S21: 0.0290 S22: 0.1353 S23: -0.0374
REMARK 3 S31: -0.3079 S32: -0.1703 S33: -0.0000
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 83 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.0356 20.0098 7.0935
REMARK 3 T TENSOR
REMARK 3 T11: 0.4300 T22: 0.6539
REMARK 3 T33: 0.2309 T12: 0.2120
REMARK 3 T13: 0.1534 T23: 0.1213
REMARK 3 L TENSOR
REMARK 3 L11: 0.0322 L22: 0.0444
REMARK 3 L33: 0.0955 L12: 0.0289
REMARK 3 L13: -0.0517 L23: -0.0003
REMARK 3 S TENSOR
REMARK 3 S11: 0.2532 S12: 0.1957 S13: -0.1805
REMARK 3 S21: 0.0455 S22: 0.0858 S23: -0.1021
REMARK 3 S31: -0.2701 S32: -0.5361 S33: -0.0000
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 244 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.5670 14.2628 3.4335
REMARK 3 T TENSOR
REMARK 3 T11: 0.2231 T22: 1.3608
REMARK 3 T33: 0.4588 T12: 0.3120
REMARK 3 T13: 0.0775 T23: 0.1845
REMARK 3 L TENSOR
REMARK 3 L11: 0.0232 L22: 0.0124
REMARK 3 L33: 0.0117 L12: 0.0029
REMARK 3 L13: -0.0107 L23: -0.0121
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: 0.0904 S13: 0.0152
REMARK 3 S21: -0.0219 S22: 0.1358 S23: 0.0420
REMARK 3 S31: 0.0122 S32: -0.1741 S33: -0.0000
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 11 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -35.7130 -31.2919 50.8253
REMARK 3 T TENSOR
REMARK 3 T11: -0.1530 T22: -1.1100
REMARK 3 T33: 1.2779 T12: 0.7720
REMARK 3 T13: -0.5030 T23: 1.3782
REMARK 3 L TENSOR
REMARK 3 L11: 0.0008 L22: 0.0172
REMARK 3 L33: 0.0019 L12: -0.0150
REMARK 3 L13: 0.0026 L23: -0.0202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: 0.0991 S13: 0.2468
REMARK 3 S21: -0.0480 S22: -0.0867 S23: -0.1257
REMARK 3 S31: -0.0332 S32: -0.1053 S33: -0.0000
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 82 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1906 -46.4032 48.3554
REMARK 3 T TENSOR
REMARK 3 T11: 0.1847 T22: -1.2995
REMARK 3 T33: 0.2110 T12: -0.1880
REMARK 3 T13: 0.0603 T23: 1.7175
REMARK 3 L TENSOR
REMARK 3 L11: -0.0245 L22: 0.0749
REMARK 3 L33: 0.0005 L12: -0.0106
REMARK 3 L13: 0.0584 L23: -0.0251
REMARK 3 S TENSOR
REMARK 3 S11: -0.2398 S12: 0.4618 S13: 0.8357
REMARK 3 S21: 0.1227 S22: -0.0265 S23: -0.2071
REMARK 3 S31: 0.1801 S32: -0.0805 S33: 0.0000
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 244 THROUGH 303 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.2130 -33.6781 46.1005
REMARK 3 T TENSOR
REMARK 3 T11: -0.0189 T22: -0.0614
REMARK 3 T33: 1.3777 T12: -0.5824
REMARK 3 T13: 0.2330 T23: 1.1976
REMARK 3 L TENSOR
REMARK 3 L11: 0.0040 L22: 0.0137
REMARK 3 L33: 0.0027 L12: 0.0205
REMARK 3 L13: -0.0282 L23: -0.0141
REMARK 3 S TENSOR
REMARK 3 S11: -0.1049 S12: 0.0626 S13: 0.2456
REMARK 3 S21: -0.0460 S22: 0.0838 S23: -0.0813
REMARK 3 S31: -0.0046 S32: 0.1485 S33: -0.0000
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 11 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6150 28.8632 30.6691
REMARK 3 T TENSOR
REMARK 3 T11: 0.8034 T22: 0.5123
REMARK 3 T33: 0.2597 T12: -0.2531
REMARK 3 T13: 0.1897 T23: -0.2217
REMARK 3 L TENSOR
REMARK 3 L11: -0.0039 L22: 0.0601
REMARK 3 L33: 0.0357 L12: -0.0022
REMARK 3 L13: 0.0147 L23: 0.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.1434 S12: -0.1838 S13: -0.1860
REMARK 3 S21: 0.0607 S22: 0.1349 S23: 0.0129
REMARK 3 S31: -0.2378 S32: 0.2149 S33: -0.0000
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 83 THROUGH 243 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3576 36.0832 16.8436
REMARK 3 T TENSOR
REMARK 3 T11: 0.9448 T22: 0.2233
REMARK 3 T33: 0.1933 T12: -0.1371
REMARK 3 T13: 0.5074 T23: -0.0002
REMARK 3 L TENSOR
REMARK 3 L11: 0.0394 L22: 0.0262
REMARK 3 L33: 0.0493 L12: -0.0107
REMARK 3 L13: 0.0215 L23: -0.0095
REMARK 3 S TENSOR
REMARK 3 S11: 0.5764 S12: 0.1095 S13: -0.1687
REMARK 3 S21: -0.0242 S22: 0.3319 S23: 0.1884
REMARK 3 S31: -0.6102 S32: 0.2658 S33: 0.0000
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 244 THROUGH 304 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.0520 46.0090 23.2627
REMARK 3 T TENSOR
REMARK 3 T11: 1.3923 T22: -0.1012
REMARK 3 T33: 0.3020 T12: -0.8448
REMARK 3 T13: 0.3896 T23: -0.6138
REMARK 3 L TENSOR
REMARK 3 L11: -0.0059 L22: 0.0190
REMARK 3 L33: -0.0020 L12: 0.0082
REMARK 3 L13: -0.0024 L23: -0.0018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0881 S12: 0.0107 S13: 0.0562
REMARK 3 S21: 0.0010 S22: 0.1076 S23: -0.0174
REMARK 3 S31: -0.1136 S32: 0.0764 S33: -0.0000
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 7JQY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-20.
REMARK 100 THE DEPOSITION ID IS D_1000248876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS-II
REMARK 200 BEAMLINE : 17-ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9201
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152155
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 49.367
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.9600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3KD2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% ETHYLENE GLYCOL, 8% PEG 8000, 100
REMARK 280 MM HEPES PH 7.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 97.50000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 97.50000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 49.20000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -103.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -81.37762
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 149.25711
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 98.40000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 -81.37762
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 98.40000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 149.25711
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 -97.50000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 49.20000
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 6 -1.000000 0.000000 0.000000 16.12238
REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 49.20000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 149.25711
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 18110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 79450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH D 426 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 445 LIES ON A SPECIAL POSITION.
REMARK 375 HOH H 429 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 ASN A 3
REMARK 465 GLU A 4
REMARK 465 ARG A 5
REMARK 465 SER A 6
REMARK 465 GLU A 7
REMARK 465 GLN A 8
REMARK 465 SER A 9
REMARK 465 MET A 10
REMARK 465 GLU A 304
REMARK 465 ALA A 305
REMARK 465 ALA A 306
REMARK 465 SER A 307
REMARK 465 GLY A 308
REMARK 465 ARG A 309
REMARK 465 MET B 1
REMARK 465 GLN B 2
REMARK 465 ASN B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 SER B 6
REMARK 465 GLU B 7
REMARK 465 GLN B 8
REMARK 465 SER B 9
REMARK 465 MET B 10
REMARK 465 ALA B 305
REMARK 465 ALA B 306
REMARK 465 SER B 307
REMARK 465 GLY B 308
REMARK 465 ARG B 309
REMARK 465 MET C 1
REMARK 465 GLN C 2
REMARK 465 ASN C 3
REMARK 465 GLU C 4
REMARK 465 ARG C 5
REMARK 465 SER C 6
REMARK 465 GLU C 7
REMARK 465 GLN C 8
REMARK 465 SER C 9
REMARK 465 MET C 10
REMARK 465 PRO C 11
REMARK 465 ALA C 305
REMARK 465 ALA C 306
REMARK 465 SER C 307
REMARK 465 GLY C 308
REMARK 465 ARG C 309
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 ASN D 3
REMARK 465 GLU D 4
REMARK 465 ARG D 5
REMARK 465 SER D 6
REMARK 465 GLU D 7
REMARK 465 GLN D 8
REMARK 465 SER D 9
REMARK 465 MET D 10
REMARK 465 ALA D 305
REMARK 465 ALA D 306
REMARK 465 SER D 307
REMARK 465 GLY D 308
REMARK 465 ARG D 309
REMARK 465 MET E 1
REMARK 465 GLN E 2
REMARK 465 ASN E 3
REMARK 465 GLU E 4
REMARK 465 ARG E 5
REMARK 465 SER E 6
REMARK 465 GLU E 7
REMARK 465 GLN E 8
REMARK 465 SER E 9
REMARK 465 MET E 10
REMARK 465 ALA E 305
REMARK 465 ALA E 306
REMARK 465 SER E 307
REMARK 465 GLY E 308
REMARK 465 ARG E 309
REMARK 465 MET F 1
REMARK 465 GLN F 2
REMARK 465 ASN F 3
REMARK 465 GLU F 4
REMARK 465 ARG F 5
REMARK 465 SER F 6
REMARK 465 GLU F 7
REMARK 465 GLN F 8
REMARK 465 SER F 9
REMARK 465 MET F 10
REMARK 465 GLU F 304
REMARK 465 ALA F 305
REMARK 465 ALA F 306
REMARK 465 SER F 307
REMARK 465 GLY F 308
REMARK 465 ARG F 309
REMARK 465 MET G 1
REMARK 465 GLN G 2
REMARK 465 ASN G 3
REMARK 465 GLU G 4
REMARK 465 ARG G 5
REMARK 465 SER G 6
REMARK 465 GLU G 7
REMARK 465 GLN G 8
REMARK 465 SER G 9
REMARK 465 MET G 10
REMARK 465 GLU G 304
REMARK 465 ALA G 305
REMARK 465 ALA G 306
REMARK 465 SER G 307
REMARK 465 GLY G 308
REMARK 465 ARG G 309
REMARK 465 MET H 1
REMARK 465 GLN H 2
REMARK 465 ASN H 3
REMARK 465 GLU H 4
REMARK 465 ARG H 5
REMARK 465 SER H 6
REMARK 465 GLU H 7
REMARK 465 GLN H 8
REMARK 465 SER H 9
REMARK 465 MET H 10
REMARK 465 ALA H 305
REMARK 465 ALA H 306
REMARK 465 SER H 307
REMARK 465 GLY H 308
REMARK 465 ARG H 309
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 35 -31.96 -136.66
REMARK 500 THR A 115 -30.29 -138.07
REMARK 500 SER A 123 -127.73 52.18
REMARK 500 ASP A 147 -40.29 75.52
REMARK 500 ASP A 177 -38.83 73.40
REMARK 500 SER A 258 -112.82 -132.44
REMARK 500 TRP A 285 77.89 -106.49
REMARK 500 ASP B 35 -26.94 -141.49
REMARK 500 SER B 123 -130.74 49.69
REMARK 500 ASP B 147 -38.04 76.53
REMARK 500 ASP B 177 -38.07 74.59
REMARK 500 SER B 258 -111.91 -131.72
REMARK 500 TRP B 285 78.47 -108.18
REMARK 500 ASP C 35 -33.56 -138.16
REMARK 500 SER C 123 -129.09 49.60
REMARK 500 ASP C 147 -36.76 74.32
REMARK 500 ASP C 177 -38.37 73.97
REMARK 500 SER C 258 -113.49 -130.74
REMARK 500 TRP C 285 79.33 -108.77
REMARK 500 SER D 123 -128.02 50.57
REMARK 500 ASP D 147 -39.23 74.85
REMARK 500 ASP D 177 -39.49 73.95
REMARK 500 SER D 258 -111.29 -131.04
REMARK 500 TRP D 285 79.04 -108.40
REMARK 500 THR E 115 -36.09 -130.46
REMARK 500 SER E 123 -127.12 49.92
REMARK 500 ASP E 147 -41.47 74.94
REMARK 500 ASP E 177 -37.97 74.23
REMARK 500 SER E 258 -109.33 -131.63
REMARK 500 LEU F 33 -162.68 -103.67
REMARK 500 THR F 115 -32.86 -146.65
REMARK 500 SER F 123 -128.95 48.78
REMARK 500 ASP F 147 -39.54 72.73
REMARK 500 ASP F 177 -39.45 74.67
REMARK 500 SER F 258 -112.79 -130.31
REMARK 500 TRP F 285 78.79 -109.12
REMARK 500 LEU G 33 -169.82 -107.10
REMARK 500 THR G 115 7.80 -156.10
REMARK 500 SER G 123 -127.24 52.63
REMARK 500 ASP G 147 -37.12 74.92
REMARK 500 ASP G 177 -39.11 74.93
REMARK 500 SER G 258 -111.17 -121.18
REMARK 500 TRP G 285 77.93 -108.12
REMARK 500 PHE G 302 49.39 -97.80
REMARK 500 THR H 115 -37.33 -134.62
REMARK 500 SER H 123 -127.65 49.15
REMARK 500 ASP H 147 -39.13 72.94
REMARK 500 ASP H 177 -38.45 74.02
REMARK 500 SER H 258 -109.29 -133.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7JQX RELATED DB: PDB
REMARK 900 7JQX IS THE WILD-TYPE PROTEIN
DBREF 7JQY A 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY B 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY C 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY D 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY E 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY F 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY G 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
DBREF 7JQY H 1 309 UNP B4EJL9 B4EJL9_BURCJ 1 309
SEQADV 7JQY SER A 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER B 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER C 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER D 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER E 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER F 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER G 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQADV 7JQY SER H 123 UNP B4EJL9 ASP 123 ENGINEERED MUTATION
SEQRES 1 A 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 A 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 A 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 A 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 A 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 A 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 A 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 A 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 A 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 A 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 A 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 A 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 A 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 A 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 A 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 A 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 A 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 A 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 A 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 A 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 A 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 A 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 A 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 A 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 B 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 B 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 B 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 B 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 B 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 B 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 B 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 B 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 B 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 B 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 B 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 B 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 B 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 B 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 B 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 B 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 B 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 B 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 B 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 B 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 B 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 B 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 B 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 B 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 C 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 C 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 C 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 C 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 C 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 C 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 C 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 C 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 C 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 C 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 C 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 C 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 C 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 C 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 C 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 C 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 C 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 C 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 C 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 C 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 C 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 C 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 C 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 C 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 D 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 D 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 D 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 D 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 D 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 D 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 D 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 D 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 D 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 D 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 D 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 D 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 D 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 D 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 D 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 D 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 D 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 D 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 D 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 D 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 D 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 D 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 D 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 D 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 E 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 E 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 E 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 E 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 E 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 E 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 E 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 E 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 E 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 E 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 E 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 E 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 E 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 E 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 E 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 E 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 E 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 E 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 E 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 E 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 E 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 E 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 E 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 E 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 F 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 F 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 F 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 F 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 F 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 F 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 F 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 F 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 F 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 F 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 F 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 F 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 F 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 F 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 F 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 F 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 F 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 F 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 F 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 F 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 F 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 F 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 F 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 F 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 G 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 G 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 G 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 G 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 G 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 G 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 G 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 G 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 G 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 G 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 G 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 G 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 G 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 G 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 G 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 G 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 G 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 G 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 G 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 G 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 G 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 G 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 G 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 G 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
SEQRES 1 H 309 MET GLN ASN GLU ARG SER GLU GLN SER MET PRO GLY MET
SEQRES 2 H 309 PRO ALA PRO GLY LEU PRO ALA GLY PHE GLU ARG ARG PHE
SEQRES 3 H 309 SER ARG ARG TYR ALA GLN LEU ASP ASP VAL ARG LEU HIS
SEQRES 4 H 309 TYR VAL THR GLY GLY PRO ASP ASP GLY GLU MET VAL VAL
SEQRES 5 H 309 LEU LEU HIS GLY TRP PRO GLN THR TRP TYR THR TRP ARG
SEQRES 6 H 309 HIS VAL MET PRO ALA LEU ALA GLU ASP GLY TYR ARG VAL
SEQRES 7 H 309 VAL ALA VAL ASP TYR ARG GLY ALA GLY GLU SER ASP LYS
SEQRES 8 H 309 PRO LEU GLY GLY TYR ASP LYS ALA SER MET ALA GLY ASP
SEQRES 9 H 309 ILE ARG ALA LEU VAL HIS GLN LEU GLY ALA THR ARG ILE
SEQRES 10 H 309 HIS LEU VAL GLY ARG SER ILE GLY VAL MET VAL ALA TYR
SEQRES 11 H 309 ALA TYR ALA ALA GLN TRP PRO THR GLU ILE VAL LYS LEU
SEQRES 12 H 309 ALA MET LEU ASP VAL PRO VAL PRO GLY THR ARG ILE TRP
SEQRES 13 H 309 ASP GLU ALA LYS ALA SER ALA ASP PRO GLN ILE TRP HIS
SEQRES 14 H 309 PHE GLY LEU HIS GLN GLN ARG ASP ILE ALA GLU MET LEU
SEQRES 15 H 309 ILE ALA GLY LYS GLU ARG ALA TYR ILE LEU ASP PHE TYR
SEQRES 16 H 309 LYS LYS ARG THR HIS VAL ALA LEU SER ASN ASP ASP ILE
SEQRES 17 H 309 ALA VAL TYR ALA ASP ALA TYR ALA ALA PRO GLY ALA LEU
SEQRES 18 H 309 ARG ALA GLY PHE GLU LEU TYR ARG ALA PHE PRO GLN ASP
SEQRES 19 H 309 GLU THR ARG PHE LYS ALA PHE MET LYS HIS LYS LEU PRO
SEQRES 20 H 309 MET PRO VAL LEU ALA LEU ALA GLY ASP LYS SER ASN GLY
SEQRES 21 H 309 ALA LYS GLU LEU ASP MET ALA ARG GLU LEU ALA LEU ASP
SEQRES 22 H 309 VAL ARG GLY ALA VAL ALA PRO ASN THR GLY HIS TRP LEU
SEQRES 23 H 309 PRO ASP GLU ASN PRO ALA PHE LEU THR ARG GLN LEU LEU
SEQRES 24 H 309 ASP PHE PHE ARG GLU ALA ALA SER GLY ARG
FORMUL 9 HOH *787(H2 O)
HELIX 1 AA1 GLY A 21 ARG A 25 1 5
HELIX 2 AA2 THR A 60 ARG A 65 5 6
HELIX 3 AA3 VAL A 67 ASP A 74 1 8
HELIX 4 AA4 ASP A 97 LEU A 112 1 16
HELIX 5 AA5 SER A 123 TRP A 136 1 14
HELIX 6 AA6 THR A 153 SER A 162 1 10
HELIX 7 AA7 ASP A 164 ILE A 167 5 4
HELIX 8 AA8 TRP A 168 GLN A 174 1 7
HELIX 9 AA9 ASP A 177 ALA A 184 1 8
HELIX 10 AB1 LYS A 186 THR A 199 1 14
HELIX 11 AB2 SER A 204 ALA A 216 1 13
HELIX 12 AB3 GLY A 219 ALA A 230 1 12
HELIX 13 AB4 ALA A 230 MET A 242 1 13
HELIX 14 AB5 ALA A 261 GLU A 269 1 9
HELIX 15 AB6 TRP A 285 ASN A 290 1 6
HELIX 16 AB7 ASN A 290 ARG A 303 1 14
HELIX 17 AB8 GLY B 21 ARG B 25 1 5
HELIX 18 AB9 THR B 60 ARG B 65 5 6
HELIX 19 AC1 VAL B 67 ASP B 74 1 8
HELIX 20 AC2 ASP B 97 LEU B 112 1 16
HELIX 21 AC3 SER B 123 TRP B 136 1 14
HELIX 22 AC4 THR B 153 SER B 162 1 10
HELIX 23 AC5 ASP B 164 ILE B 167 5 4
HELIX 24 AC6 TRP B 168 GLN B 174 1 7
HELIX 25 AC7 ASP B 177 ALA B 184 1 8
HELIX 26 AC8 LYS B 186 THR B 199 1 14
HELIX 27 AC9 SER B 204 ALA B 216 1 13
HELIX 28 AD1 GLY B 219 ALA B 230 1 12
HELIX 29 AD2 ALA B 230 MET B 242 1 13
HELIX 30 AD3 ALA B 261 GLU B 269 1 9
HELIX 31 AD4 TRP B 285 ASN B 290 1 6
HELIX 32 AD5 ASN B 290 GLU B 304 1 15
HELIX 33 AD6 GLY C 21 ARG C 25 1 5
HELIX 34 AD7 THR C 60 ARG C 65 5 6
HELIX 35 AD8 VAL C 67 ASP C 74 1 8
HELIX 36 AD9 ASP C 97 LEU C 112 1 16
HELIX 37 AE1 SER C 123 TRP C 136 1 14
HELIX 38 AE2 THR C 153 SER C 162 1 10
HELIX 39 AE3 ASP C 164 ILE C 167 5 4
HELIX 40 AE4 TRP C 168 GLN C 174 1 7
HELIX 41 AE5 ASP C 177 ALA C 184 1 8
HELIX 42 AE6 LYS C 186 THR C 199 1 14
HELIX 43 AE7 SER C 204 ALA C 217 1 14
HELIX 44 AE8 GLY C 219 ALA C 230 1 12
HELIX 45 AE9 ALA C 230 MET C 242 1 13
HELIX 46 AF1 ALA C 261 GLU C 269 1 9
HELIX 47 AF2 TRP C 285 ASN C 290 1 6
HELIX 48 AF3 ASN C 290 GLU C 304 1 15
HELIX 49 AF4 GLY D 21 ARG D 25 1 5
HELIX 50 AF5 THR D 60 ARG D 65 5 6
HELIX 51 AF6 VAL D 67 ASP D 74 1 8
HELIX 52 AF7 ASP D 97 LEU D 112 1 16
HELIX 53 AF8 SER D 123 TRP D 136 1 14
HELIX 54 AF9 THR D 153 SER D 162 1 10
HELIX 55 AG1 ASP D 164 ILE D 167 5 4
HELIX 56 AG2 TRP D 168 GLN D 174 1 7
HELIX 57 AG3 ASP D 177 ALA D 184 1 8
HELIX 58 AG4 LYS D 186 THR D 199 1 14
HELIX 59 AG5 SER D 204 ALA D 216 1 13
HELIX 60 AG6 GLY D 219 ALA D 230 1 12
HELIX 61 AG7 ALA D 230 MET D 242 1 13
HELIX 62 AG8 ALA D 261 GLU D 269 1 9
HELIX 63 AG9 TRP D 285 ASN D 290 1 6
HELIX 64 AH1 ASN D 290 GLU D 304 1 15
HELIX 65 AH2 GLY E 21 PHE E 26 1 6
HELIX 66 AH3 THR E 60 ARG E 65 5 6
HELIX 67 AH4 VAL E 67 GLU E 73 1 7
HELIX 68 AH5 ASP E 97 LEU E 112 1 16
HELIX 69 AH6 SER E 123 TRP E 136 1 14
HELIX 70 AH7 THR E 153 SER E 162 1 10
HELIX 71 AH8 ASP E 164 ILE E 167 5 4
HELIX 72 AH9 TRP E 168 GLN E 174 1 7
HELIX 73 AI1 ASP E 177 ALA E 184 1 8
HELIX 74 AI2 LYS E 186 THR E 199 1 14
HELIX 75 AI3 SER E 204 ALA E 217 1 14
HELIX 76 AI4 GLY E 219 ALA E 230 1 12
HELIX 77 AI5 ALA E 230 MET E 242 1 13
HELIX 78 AI6 ALA E 261 GLU E 269 1 9
HELIX 79 AI7 TRP E 285 ASN E 290 1 6
HELIX 80 AI8 ASN E 290 ARG E 303 1 14
HELIX 81 AI9 GLY F 21 ARG F 25 1 5
HELIX 82 AJ1 THR F 60 ARG F 65 5 6
HELIX 83 AJ2 VAL F 67 ASP F 74 1 8
HELIX 84 AJ3 ASP F 97 LEU F 112 1 16
HELIX 85 AJ4 SER F 123 TRP F 136 1 14
HELIX 86 AJ5 THR F 153 SER F 162 1 10
HELIX 87 AJ6 ASP F 164 ILE F 167 5 4
HELIX 88 AJ7 TRP F 168 GLN F 174 1 7
HELIX 89 AJ8 ASP F 177 ALA F 184 1 8
HELIX 90 AJ9 LYS F 186 THR F 199 1 14
HELIX 91 AK1 SER F 204 ALA F 217 1 14
HELIX 92 AK2 GLY F 219 ALA F 230 1 12
HELIX 93 AK3 ALA F 230 MET F 242 1 13
HELIX 94 AK4 ALA F 261 GLU F 269 1 9
HELIX 95 AK5 TRP F 285 ASN F 290 1 6
HELIX 96 AK6 ASN F 290 ARG F 303 1 14
HELIX 97 AK7 GLY G 21 ARG G 25 1 5
HELIX 98 AK8 THR G 60 ARG G 65 5 6
HELIX 99 AK9 VAL G 67 ASP G 74 1 8
HELIX 100 AL1 ASP G 97 LEU G 112 1 16
HELIX 101 AL2 SER G 123 TRP G 136 1 14
HELIX 102 AL3 THR G 153 SER G 162 1 10
HELIX 103 AL4 ASP G 164 ILE G 167 5 4
HELIX 104 AL5 TRP G 168 GLN G 174 1 7
HELIX 105 AL6 ASP G 177 ALA G 184 1 8
HELIX 106 AL7 LYS G 186 THR G 199 1 14
HELIX 107 AL8 SER G 204 ALA G 216 1 13
HELIX 108 AL9 GLY G 219 ALA G 230 1 12
HELIX 109 AM1 ALA G 230 MET G 242 1 13
HELIX 110 AM2 ALA G 261 LEU G 270 1 10
HELIX 111 AM3 TRP G 285 ASN G 290 1 6
HELIX 112 AM4 ASN G 290 PHE G 302 1 13
HELIX 113 AM5 GLY H 21 ARG H 25 1 5
HELIX 114 AM6 THR H 60 ARG H 65 5 6
HELIX 115 AM7 VAL H 67 ASP H 74 1 8
HELIX 116 AM8 ASP H 97 LEU H 112 1 16
HELIX 117 AM9 SER H 123 TRP H 136 1 14
HELIX 118 AN1 THR H 153 SER H 162 1 10
HELIX 119 AN2 ASP H 164 ILE H 167 5 4
HELIX 120 AN3 TRP H 168 GLN H 174 1 7
HELIX 121 AN4 ASP H 177 ALA H 184 1 8
HELIX 122 AN5 LYS H 186 THR H 199 1 14
HELIX 123 AN6 SER H 204 ALA H 216 1 13
HELIX 124 AN7 GLY H 219 ALA H 230 1 12
HELIX 125 AN8 ALA H 230 HIS H 244 1 15
HELIX 126 AN9 ALA H 261 GLU H 269 1 9
HELIX 127 AO1 TRP H 285 ASN H 290 1 6
HELIX 128 AO2 ASN H 290 GLU H 304 1 15
SHEET 1 AA1 8 PHE A 26 GLN A 32 0
SHEET 2 AA1 8 ARG A 37 GLY A 43 -1 O TYR A 40 N ARG A 29
SHEET 3 AA1 8 ARG A 77 ASP A 82 -1 O ALA A 80 N VAL A 41
SHEET 4 AA1 8 MET A 50 LEU A 54 1 N VAL A 51 O ARG A 77
SHEET 5 AA1 8 ILE A 117 ARG A 122 1 O HIS A 118 N VAL A 52
SHEET 6 AA1 8 ILE A 140 LEU A 146 1 O ALA A 144 N LEU A 119
SHEET 7 AA1 8 VAL A 250 GLY A 255 1 O LEU A 251 N MET A 145
SHEET 8 AA1 8 VAL A 274 ALA A 279 1 O ALA A 279 N ALA A 254
SHEET 1 AA2 8 PHE B 26 GLN B 32 0
SHEET 2 AA2 8 ARG B 37 GLY B 43 -1 O TYR B 40 N ARG B 29
SHEET 3 AA2 8 ARG B 77 ASP B 82 -1 O ASP B 82 N HIS B 39
SHEET 4 AA2 8 MET B 50 LEU B 54 1 N VAL B 51 O VAL B 79
SHEET 5 AA2 8 ILE B 117 ARG B 122 1 O HIS B 118 N MET B 50
SHEET 6 AA2 8 ILE B 140 LEU B 146 1 O ALA B 144 N LEU B 119
SHEET 7 AA2 8 VAL B 250 GLY B 255 1 O LEU B 251 N MET B 145
SHEET 8 AA2 8 VAL B 274 ALA B 279 1 O ALA B 279 N ALA B 254
SHEET 1 AA3 8 PHE C 26 GLN C 32 0
SHEET 2 AA3 8 ARG C 37 GLY C 43 -1 O TYR C 40 N ARG C 29
SHEET 3 AA3 8 ARG C 77 VAL C 81 -1 O ALA C 80 N VAL C 41
SHEET 4 AA3 8 MET C 50 LEU C 54 1 N VAL C 51 O VAL C 79
SHEET 5 AA3 8 ILE C 117 ARG C 122 1 O HIS C 118 N VAL C 52
SHEET 6 AA3 8 ILE C 140 LEU C 146 1 O ALA C 144 N LEU C 119
SHEET 7 AA3 8 VAL C 250 GLY C 255 1 O LEU C 251 N MET C 145
SHEET 8 AA3 8 VAL C 274 ALA C 279 1 O ALA C 279 N ALA C 254
SHEET 1 AA4 8 PHE D 26 GLN D 32 0
SHEET 2 AA4 8 ARG D 37 GLY D 43 -1 O LEU D 38 N ALA D 31
SHEET 3 AA4 8 ARG D 77 ASP D 82 -1 O ALA D 80 N VAL D 41
SHEET 4 AA4 8 MET D 50 LEU D 54 1 N VAL D 51 O ARG D 77
SHEET 5 AA4 8 ILE D 117 ARG D 122 1 O HIS D 118 N VAL D 52
SHEET 6 AA4 8 ILE D 140 LEU D 146 1 O ALA D 144 N LEU D 119
SHEET 7 AA4 8 LEU D 246 GLY D 255 1 O LEU D 251 N MET D 145
SHEET 8 AA4 8 ALA D 271 ALA D 279 1 O ASP D 273 N VAL D 250
SHEET 1 AA5 8 SER E 27 GLN E 32 0
SHEET 2 AA5 8 ARG E 37 GLY E 43 -1 O TYR E 40 N ARG E 29
SHEET 3 AA5 8 ARG E 77 ASP E 82 -1 O ALA E 80 N VAL E 41
SHEET 4 AA5 8 MET E 50 LEU E 54 1 N VAL E 51 O ARG E 77
SHEET 5 AA5 8 ILE E 117 ARG E 122 1 O HIS E 118 N VAL E 52
SHEET 6 AA5 8 ILE E 140 LEU E 146 1 O ALA E 144 N LEU E 119
SHEET 7 AA5 8 VAL E 250 GLY E 255 1 O LEU E 251 N MET E 145
SHEET 8 AA5 8 VAL E 274 ALA E 279 1 O ALA E 279 N ALA E 254
SHEET 1 AA6 8 PHE F 26 GLN F 32 0
SHEET 2 AA6 8 ARG F 37 GLY F 43 -1 O THR F 42 N SER F 27
SHEET 3 AA6 8 ARG F 77 ASP F 82 -1 O ALA F 80 N VAL F 41
SHEET 4 AA6 8 MET F 50 LEU F 54 1 N VAL F 51 O VAL F 79
SHEET 5 AA6 8 ILE F 117 ARG F 122 1 O HIS F 118 N VAL F 52
SHEET 6 AA6 8 ILE F 140 LEU F 146 1 O ALA F 144 N LEU F 119
SHEET 7 AA6 8 VAL F 250 GLY F 255 1 O LEU F 251 N MET F 145
SHEET 8 AA6 8 VAL F 274 ALA F 279 1 O ALA F 279 N ALA F 254
SHEET 1 AA7 8 PHE G 26 GLN G 32 0
SHEET 2 AA7 8 ARG G 37 GLY G 43 -1 O THR G 42 N SER G 27
SHEET 3 AA7 8 TYR G 76 ASP G 82 -1 O ALA G 80 N VAL G 41
SHEET 4 AA7 8 GLU G 49 LEU G 54 1 N GLU G 49 O ARG G 77
SHEET 5 AA7 8 ILE G 117 ARG G 122 1 O VAL G 120 N VAL G 52
SHEET 6 AA7 8 ILE G 140 LEU G 146 1 O VAL G 141 N ILE G 117
SHEET 7 AA7 8 LEU G 246 GLY G 255 1 O LEU G 251 N MET G 145
SHEET 8 AA7 8 ALA G 271 ALA G 279 1 O ASP G 273 N VAL G 250
SHEET 1 AA8 8 PHE H 26 GLN H 32 0
SHEET 2 AA8 8 ARG H 37 GLY H 43 -1 O TYR H 40 N ARG H 29
SHEET 3 AA8 8 ARG H 77 ASP H 82 -1 O ALA H 80 N VAL H 41
SHEET 4 AA8 8 MET H 50 LEU H 54 1 N VAL H 51 O VAL H 79
SHEET 5 AA8 8 ILE H 117 ARG H 122 1 O VAL H 120 N LEU H 54
SHEET 6 AA8 8 ILE H 140 LEU H 146 1 O ALA H 144 N LEU H 119
SHEET 7 AA8 8 VAL H 250 GLY H 255 1 O LEU H 251 N MET H 145
SHEET 8 AA8 8 VAL H 274 ALA H 279 1 O ALA H 279 N ALA H 254
CISPEP 1 TRP A 57 PRO A 58 0 -4.69
CISPEP 2 TRP B 57 PRO B 58 0 -3.30
CISPEP 3 TRP C 57 PRO C 58 0 -3.03
CISPEP 4 TRP D 57 PRO D 58 0 -3.60
CISPEP 5 TRP E 57 PRO E 58 0 -3.11
CISPEP 6 TRP F 57 PRO F 58 0 -3.28
CISPEP 7 TRP G 57 PRO G 58 0 -2.25
CISPEP 8 TRP H 57 PRO H 58 0 -2.95
CRYST1 195.000 98.400 170.000 90.00 118.60 90.00 C 1 2 1 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 0.005128 0.000000 0.002796 0.00000
SCALE2 0.000000 0.010163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006700 0.00000
TER 2309 ARG A 303
TER 4627 GLU B 304
TER 6938 GLU C 304
TER 9256 GLU D 304
TER 11574 GLU E 304
TER 13883 ARG F 303
TER 16192 ARG G 303
TER 18510 GLU H 304
MASTER 900 0 0 128 64 0 0 619289 8 0 192
END |