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HEADER TRANSFERASE 27-SEP-18 6MLK
TITLE STRUCTURE OF THIOESTERASE FROM DEBS WITH A THIOESTERASE-SPECIFIC
TITLE 2 ANTIBODY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-DEOXYERYTHRONOLIDE-B SYNTHASE ERYA3, MODULES 5 AND 6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEBS 3,6-DEOXYERYTHRONOLIDE B SYNTHASE III,ERYTHRONOLIDE
COMPND 5 SYNTHASE,ORF C;
COMPND 6 EC: 2.3.1.94;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: LIGHT CHAIN OF FAB 3A6;
COMPND 10 CHAIN: L;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HEAVY CHAIN OF FAB 3A6;
COMPND 14 CHAIN: H;
COMPND 15 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 GENE: ERYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_TAXID: 9606;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS 6-DEOXYERYTHRONOLIDE B SYNTHASE, THIOESTERASE, MONOCLONAL ANTIBODY,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.I.MATHEWS,X.LI,C.KHOSLA
REVDAT 1 17-OCT-18 6MLK 0
JRNL AUTH X.LI,N.SEVILLANO,F.LA GRECA,J.HSU,I.I.MATHEWS,T.MATSUI,
JRNL AUTH 2 C.S.CRAIK,C.KHOSLA
JRNL TITL DISCOVERY AND CHARACTERIZATION OF A THIOESTERASE-SPECIFIC
JRNL TITL 2 MONOCLONAL ANTIBODY THAT RECOGNIZES THE 6-DEOXYERYTHRONOLIDE
JRNL TITL 3 B SYNTHASE.
JRNL REF BIOCHEMISTRY 2018
JRNL REFN ISSN 1520-4995
JRNL PMID 30289692
JRNL DOI 10.1021/ACS.BIOCHEM.8B00886
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.43
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 33432
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1671
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 38.4306 - 5.6038 0.99 2739 144 0.1583 0.2121
REMARK 3 2 5.6038 - 4.4500 0.99 2676 140 0.1350 0.1614
REMARK 3 3 4.4500 - 3.8881 1.00 2642 140 0.1441 0.2238
REMARK 3 4 3.8881 - 3.5329 1.00 2648 139 0.1698 0.2336
REMARK 3 5 3.5329 - 3.2798 1.00 2662 140 0.1928 0.2734
REMARK 3 6 3.2798 - 3.0865 1.00 2632 138 0.2045 0.2653
REMARK 3 7 3.0865 - 2.9320 1.00 2641 139 0.2128 0.3138
REMARK 3 8 2.9320 - 2.8044 1.00 2628 139 0.2343 0.2787
REMARK 3 9 2.8044 - 2.6965 1.00 2609 137 0.2352 0.3148
REMARK 3 10 2.6965 - 2.6035 1.00 2628 139 0.2394 0.3062
REMARK 3 11 2.6035 - 2.5221 1.00 2641 138 0.2593 0.3456
REMARK 3 12 2.5221 - 2.4500 1.00 2615 138 0.3142 0.3855
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 26.280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.61
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.58
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 : 22
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 16 THROUGH 68 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0748 17.7999 -68.0278
REMARK 3 T TENSOR
REMARK 3 T11: 0.9327 T22: 0.4862
REMARK 3 T33: 0.5291 T12: -0.2323
REMARK 3 T13: 0.0247 T23: 0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 0.7135 L22: 0.1186
REMARK 3 L33: 0.3632 L12: -0.2864
REMARK 3 L13: 0.1541 L23: -0.1122
REMARK 3 S TENSOR
REMARK 3 S11: -0.0198 S12: -0.0560 S13: -0.0019
REMARK 3 S21: 0.0162 S22: 0.0118 S23: 0.1269
REMARK 3 S31: 0.4343 S32: -0.4290 S33: -0.1134
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 135 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.4088 13.2386 -54.1232
REMARK 3 T TENSOR
REMARK 3 T11: 1.0200 T22: 0.6024
REMARK 3 T33: 0.5103 T12: -0.1938
REMARK 3 T13: 0.1208 T23: 0.0905
REMARK 3 L TENSOR
REMARK 3 L11: 0.1754 L22: 0.0296
REMARK 3 L33: 0.1590 L12: 0.0581
REMARK 3 L13: 0.1348 L23: 0.0760
REMARK 3 S TENSOR
REMARK 3 S11: -0.2616 S12: -0.3149 S13: -0.2376
REMARK 3 S21: -0.0416 S22: 0.2349 S23: 0.3498
REMARK 3 S31: 0.4195 S32: -0.6617 S33: -0.0127
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 136 THROUGH 230 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.5766 18.6275 -59.0574
REMARK 3 T TENSOR
REMARK 3 T11: 0.9326 T22: 0.4339
REMARK 3 T33: 0.5089 T12: -0.0572
REMARK 3 T13: 0.0158 T23: -0.0151
REMARK 3 L TENSOR
REMARK 3 L11: 0.1359 L22: 0.0397
REMARK 3 L33: 0.4532 L12: -0.0841
REMARK 3 L13: -0.1024 L23: -0.1662
REMARK 3 S TENSOR
REMARK 3 S11: -0.3213 S12: -0.1422 S13: -0.0390
REMARK 3 S21: 0.0366 S22: 0.1530 S23: -0.0991
REMARK 3 S31: 0.2762 S32: 0.0406 S33: -0.0005
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 231 THROUGH 250 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1841 17.9498 -59.5802
REMARK 3 T TENSOR
REMARK 3 T11: 0.8349 T22: 0.5277
REMARK 3 T33: 0.4903 T12: 0.0741
REMARK 3 T13: 0.0337 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 0.0236 L22: 0.0651
REMARK 3 L33: 0.0513 L12: 0.0672
REMARK 3 L13: -0.0271 L23: -0.0486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: -0.3171 S13: 0.0321
REMARK 3 S21: 0.2791 S22: -0.1444 S23: 0.0106
REMARK 3 S31: 0.2711 S32: 0.4953 S33: -0.0003
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 251 THROUGH 279 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.3540 6.6060 -52.5894
REMARK 3 T TENSOR
REMARK 3 T11: 1.4157 T22: 0.5892
REMARK 3 T33: 0.7126 T12: 0.0912
REMARK 3 T13: 0.0288 T23: 0.0582
REMARK 3 L TENSOR
REMARK 3 L11: 0.0749 L22: 0.0178
REMARK 3 L33: 0.0275 L12: 0.0265
REMARK 3 L13: -0.0310 L23: -0.0369
REMARK 3 S TENSOR
REMARK 3 S11: 0.3105 S12: -0.1457 S13: -0.3104
REMARK 3 S21: -0.1723 S22: -0.0444 S23: 0.0932
REMARK 3 S31: 0.1798 S32: 0.1679 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 16 THROUGH 82 )
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3899 11.0863 -88.8997
REMARK 3 T TENSOR
REMARK 3 T11: 1.3236 T22: 0.0470
REMARK 3 T33: 0.6143 T12: -0.1628
REMARK 3 T13: 0.2693 T23: 0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 0.8938 L22: 0.3749
REMARK 3 L33: 0.4825 L12: -0.2938
REMARK 3 L13: -0.3020 L23: 0.1979
REMARK 3 S TENSOR
REMARK 3 S11: -0.9498 S12: 0.2060 S13: -0.2984
REMARK 3 S21: -0.0915 S22: 0.2853 S23: -0.1650
REMARK 3 S31: 1.0024 S32: -0.2772 S33: -0.0800
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 83 THROUGH 111 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.8087 9.6240 -93.5555
REMARK 3 T TENSOR
REMARK 3 T11: 1.4953 T22: -0.0110
REMARK 3 T33: 0.5725 T12: -0.3041
REMARK 3 T13: 0.3551 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.8381 L22: 0.2575
REMARK 3 L33: 0.0104 L12: -0.0869
REMARK 3 L13: -0.0696 L23: 0.0966
REMARK 3 S TENSOR
REMARK 3 S11: -0.9896 S12: 0.1911 S13: -0.3684
REMARK 3 S21: 0.2797 S22: 0.1280 S23: 0.0166
REMARK 3 S31: 1.0115 S32: -0.2568 S33: -0.5948
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 112 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7369 24.5590-104.1165
REMARK 3 T TENSOR
REMARK 3 T11: 0.6762 T22: 0.1936
REMARK 3 T33: 0.4183 T12: -0.0447
REMARK 3 T13: 0.0183 T23: -0.0209
REMARK 3 L TENSOR
REMARK 3 L11: 1.5912 L22: 0.5195
REMARK 3 L33: 0.5798 L12: -0.1833
REMARK 3 L13: -0.6667 L23: -0.2689
REMARK 3 S TENSOR
REMARK 3 S11: -0.2851 S12: 0.4910 S13: 0.0295
REMARK 3 S21: 0.2689 S22: 0.3165 S23: 0.0071
REMARK 3 S31: 0.3116 S32: -0.1876 S33: 0.0729
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 150 THROUGH 171 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.0693 25.0915-115.8441
REMARK 3 T TENSOR
REMARK 3 T11: 0.5407 T22: 0.4468
REMARK 3 T33: 0.5418 T12: -0.0332
REMARK 3 T13: -0.0251 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.0285 L22: 0.0417
REMARK 3 L33: 0.1061 L12: 0.0344
REMARK 3 L13: -0.0226 L23: 0.0646
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: 0.4037 S13: 0.2064
REMARK 3 S21: -0.2208 S22: -0.0092 S23: 0.0666
REMARK 3 S31: 0.5406 S32: 0.0478 S33: 0.0007
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 172 THROUGH 195 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.0166 24.6001-112.1746
REMARK 3 T TENSOR
REMARK 3 T11: 0.6529 T22: 0.5638
REMARK 3 T33: 0.6739 T12: -0.0027
REMARK 3 T13: -0.0402 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 0.0724 L22: 0.2417
REMARK 3 L33: 0.1055 L12: -0.1164
REMARK 3 L13: 0.0111 L23: 0.0631
REMARK 3 S TENSOR
REMARK 3 S11: 0.4551 S12: 0.5339 S13: -0.0882
REMARK 3 S21: 0.2065 S22: -0.3232 S23: -0.2644
REMARK 3 S31: 0.6161 S32: 0.0231 S33: 0.0008
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 196 THROUGH 232 )
REMARK 3 ORIGIN FOR THE GROUP (A): 69.5697 30.5911-121.1316
REMARK 3 T TENSOR
REMARK 3 T11: 0.5510 T22: 0.6338
REMARK 3 T33: 0.6916 T12: -0.0452
REMARK 3 T13: 0.1487 T23: 0.0435
REMARK 3 L TENSOR
REMARK 3 L11: 0.0517 L22: 0.0026
REMARK 3 L33: 0.1579 L12: -0.0025
REMARK 3 L13: -0.0477 L23: -0.0138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0489 S12: 0.2057 S13: 0.0982
REMARK 3 S21: -0.2285 S22: 0.0593 S23: -0.1923
REMARK 3 S31: 0.0805 S32: 0.2028 S33: 0.0000
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 4 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.8323 38.4752 -85.2919
REMARK 3 T TENSOR
REMARK 3 T11: 0.6260 T22: 0.4287
REMARK 3 T33: 0.6898 T12: 0.0452
REMARK 3 T13: -0.0966 T23: 0.0942
REMARK 3 L TENSOR
REMARK 3 L11: 0.7753 L22: 0.0457
REMARK 3 L33: 0.3226 L12: 0.1999
REMARK 3 L13: -0.1517 L23: 0.1095
REMARK 3 S TENSOR
REMARK 3 S11: 0.1984 S12: -0.4805 S13: 0.3402
REMARK 3 S21: 0.4080 S22: 0.2105 S23: 0.1713
REMARK 3 S31: -0.2224 S32: 0.3167 S33: 0.0032
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 20 THROUGH 35 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.8801 32.6993 -80.0384
REMARK 3 T TENSOR
REMARK 3 T11: 0.6481 T22: 0.4797
REMARK 3 T33: 0.6899 T12: -0.0091
REMARK 3 T13: -0.0765 T23: 0.0623
REMARK 3 L TENSOR
REMARK 3 L11: 0.0184 L22: 0.0816
REMARK 3 L33: 0.1017 L12: -0.0468
REMARK 3 L13: -0.0107 L23: 0.0517
REMARK 3 S TENSOR
REMARK 3 S11: -0.1164 S12: 0.1097 S13: 0.4698
REMARK 3 S21: -0.0423 S22: 0.1456 S23: 0.2952
REMARK 3 S31: 0.2190 S32: -0.1053 S33: -0.0001
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 36 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5325 26.0936 -85.3452
REMARK 3 T TENSOR
REMARK 3 T11: 0.7294 T22: 0.3799
REMARK 3 T33: 0.5281 T12: 0.0036
REMARK 3 T13: 0.1248 T23: 0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 0.0348 L22: 0.0053
REMARK 3 L33: 0.0767 L12: 0.0473
REMARK 3 L13: 0.0251 L23: 0.0461
REMARK 3 S TENSOR
REMARK 3 S11: -0.1614 S12: -0.1384 S13: -0.1832
REMARK 3 S21: -0.3868 S22: -0.0265 S23: 0.0530
REMARK 3 S31: 0.2126 S32: 0.0286 S33: 0.0002
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 48 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.4561 27.2477 -73.3593
REMARK 3 T TENSOR
REMARK 3 T11: 0.6573 T22: 0.4250
REMARK 3 T33: 0.4581 T12: 0.0819
REMARK 3 T13: 0.0314 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.0285 L22: 0.0459
REMARK 3 L33: 0.0452 L12: 0.0214
REMARK 3 L13: 0.0147 L23: -0.0368
REMARK 3 S TENSOR
REMARK 3 S11: 0.0846 S12: -0.5680 S13: -0.0445
REMARK 3 S21: 0.2705 S22: -0.2489 S23: 0.1823
REMARK 3 S31: 0.2175 S32: -0.1025 S33: 0.0002
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 62 THROUGH 77 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.0589 32.4659 -73.5847
REMARK 3 T TENSOR
REMARK 3 T11: 0.5984 T22: 0.4387
REMARK 3 T33: 0.6465 T12: 0.0628
REMARK 3 T13: -0.0866 T23: -0.0229
REMARK 3 L TENSOR
REMARK 3 L11: 0.0282 L22: 0.0381
REMARK 3 L33: 0.1701 L12: 0.0369
REMARK 3 L13: -0.0560 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: 0.2018 S12: -0.3343 S13: 0.3244
REMARK 3 S21: 0.2021 S22: -0.1480 S23: 0.4249
REMARK 3 S31: -0.0368 S32: 0.2002 S33: 0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 78 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4045 34.7792 -79.6314
REMARK 3 T TENSOR
REMARK 3 T11: 0.5461 T22: 0.5631
REMARK 3 T33: 0.6012 T12: 0.0750
REMARK 3 T13: 0.0194 T23: -0.1041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0059 L22: 0.0237
REMARK 3 L33: 0.0669 L12: 0.0129
REMARK 3 L13: -0.0030 L23: -0.0354
REMARK 3 S TENSOR
REMARK 3 S11: -0.0724 S12: -0.1060 S13: 0.1144
REMARK 3 S21: -0.1610 S22: -0.0266 S23: 0.2453
REMARK 3 S31: 0.1947 S32: 0.3473 S33: -0.0061
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 93 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6146 23.5282 -83.9525
REMARK 3 T TENSOR
REMARK 3 T11: 0.7502 T22: 0.3102
REMARK 3 T33: 0.5096 T12: -0.0069
REMARK 3 T13: 0.1231 T23: 0.0575
REMARK 3 L TENSOR
REMARK 3 L11: 0.0456 L22: -0.0357
REMARK 3 L33: 0.0714 L12: 0.0475
REMARK 3 L13: 0.0079 L23: 0.0014
REMARK 3 S TENSOR
REMARK 3 S11: -0.1412 S12: 0.1233 S13: -0.2978
REMARK 3 S21: 0.2903 S22: 0.0674 S23: -0.0258
REMARK 3 S31: 0.3848 S32: 0.1039 S33: -0.0001
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 110 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 55.1223 36.3673 -91.5022
REMARK 3 T TENSOR
REMARK 3 T11: 0.5360 T22: 0.4581
REMARK 3 T33: 0.5832 T12: -0.0322
REMARK 3 T13: -0.0906 T23: 0.0323
REMARK 3 L TENSOR
REMARK 3 L11: 0.1258 L22: 0.0322
REMARK 3 L33: 0.1738 L12: -0.0933
REMARK 3 L13: -0.0681 L23: 0.0439
REMARK 3 S TENSOR
REMARK 3 S11: 0.0636 S12: 0.1359 S13: 0.1641
REMARK 3 S21: -0.0521 S22: 0.0622 S23: 0.0155
REMARK 3 S31: 0.3840 S32: -0.0663 S33: 0.0003
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 129 THROUGH 154 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.4757 39.4523-114.6218
REMARK 3 T TENSOR
REMARK 3 T11: 0.3745 T22: 0.4559
REMARK 3 T33: 0.5150 T12: 0.0178
REMARK 3 T13: -0.0434 T23: 0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 0.0826 L22: 0.0747
REMARK 3 L33: 0.0147 L12: -0.1078
REMARK 3 L13: -0.0334 L23: 0.0397
REMARK 3 S TENSOR
REMARK 3 S11: 0.1603 S12: 0.5111 S13: 0.0920
REMARK 3 S21: -0.0498 S22: -0.2094 S23: -0.0813
REMARK 3 S31: -0.0114 S32: 0.1072 S33: -0.0002
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 155 THROUGH 203 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.4676 36.4563-110.4464
REMARK 3 T TENSOR
REMARK 3 T11: 0.4072 T22: 0.5158
REMARK 3 T33: 0.5736 T12: -0.0509
REMARK 3 T13: -0.0448 T23: 0.0907
REMARK 3 L TENSOR
REMARK 3 L11: 0.1409 L22: 0.4042
REMARK 3 L33: 0.2045 L12: -0.0994
REMARK 3 L13: -0.1985 L23: 0.1857
REMARK 3 S TENSOR
REMARK 3 S11: 0.0742 S12: 0.1620 S13: 0.0587
REMARK 3 S21: 0.0248 S22: -0.2676 S23: 0.0920
REMARK 3 S31: 0.0678 S32: -0.2474 S33: -0.0002
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 204 THROUGH 222 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.5923 45.3176-107.0642
REMARK 3 T TENSOR
REMARK 3 T11: 0.3798 T22: 0.4136
REMARK 3 T33: 0.4947 T12: -0.0491
REMARK 3 T13: -0.0038 T23: 0.0920
REMARK 3 L TENSOR
REMARK 3 L11: -0.0017 L22: 0.0372
REMARK 3 L33: 0.0045 L12: 0.0148
REMARK 3 L13: -0.0091 L23: -0.0025
REMARK 3 S TENSOR
REMARK 3 S11: -0.1112 S12: 0.0948 S13: 0.0534
REMARK 3 S21: 0.1886 S22: 0.1031 S23: 0.1670
REMARK 3 S31: -0.1280 S32: -0.1204 S33: -0.0004
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 6MLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-18.
REMARK 100 THE DEPOSITION ID IS D_1000236433.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-16
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 : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97946
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : RH COATED COLLIMATING MIRRORS, K
REMARK 200 -B FOCUSING MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33435
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 38.426
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9.519
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.33
REMARK 200 R MERGE FOR SHELL (I) : 0.85800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB CODES: 1MN6 AND 4LRI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 15% ETHYLENE GLYCOL, 0.2M
REMARK 280 NA2HPO4, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 86.29000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.81955
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 53.01667
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 86.29000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 49.81955
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 53.01667
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 86.29000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 49.81955
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 53.01667
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 86.29000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 49.81955
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 53.01667
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 86.29000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 49.81955
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 53.01667
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 86.29000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 49.81955
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 53.01667
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 99.63911
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 106.03333
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 99.63911
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 106.03333
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 99.63911
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 106.03333
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 99.63911
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 106.03333
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 99.63911
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 106.03333
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 99.63911
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 106.03333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, L, 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 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 H 419 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 ASP A 6
REMARK 465 SER A 7
REMARK 465 GLY A 8
REMARK 465 THR A 9
REMARK 465 PRO A 10
REMARK 465 ALA A 11
REMARK 465 ARG A 12
REMARK 465 GLU A 13
REMARK 465 ALA A 14
REMARK 465 SER A 15
REMARK 465 GLY A 50
REMARK 465 SER A 51
REMARK 465 ASP A 52
REMARK 465 ALA A 62
REMARK 465 ASP A 63
REMARK 465 GLY A 132
REMARK 465 ASP A 133
REMARK 465 GLY A 280
REMARK 465 GLY A 281
REMARK 465 ASN A 282
REMARK 465 SER A 283
REMARK 465 SER A 284
REMARK 465 SER A 285
REMARK 465 VAL A 286
REMARK 465 ASP A 287
REMARK 465 LYS A 288
REMARK 465 LEU A 289
REMARK 465 ALA A 290
REMARK 465 ALA A 291
REMARK 465 ALA A 292
REMARK 465 LEU A 293
REMARK 465 GLU A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 LEU L 1
REMARK 465 PHE L 2
REMARK 465 ALA L 3
REMARK 465 ILE L 4
REMARK 465 PRO L 5
REMARK 465 LEU L 6
REMARK 465 VAL L 7
REMARK 465 VAL L 8
REMARK 465 PRO L 9
REMARK 465 PHE L 10
REMARK 465 TYR L 11
REMARK 465 SER L 12
REMARK 465 HIS L 13
REMARK 465 SER L 14
REMARK 465 ALA L 15
REMARK 465 GLY L 233
REMARK 465 GLU L 234
REMARK 465 CYS L 235
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 GLN H 3
REMARK 465 LYS H 138
REMARK 465 SER H 139
REMARK 465 THR H 140
REMARK 465 SER H 141
REMARK 465 GLY H 142
REMARK 465 GLY H 143
REMARK 465 LYS H 223
REMARK 465 SER H 224
REMARK 465 CYS H 225
REMARK 465 ALA H 226
REMARK 465 ALA H 227
REMARK 465 ALA H 228
REMARK 465 HIS H 229
REMARK 465 HIS H 230
REMARK 465 HIS H 231
REMARK 465 HIS H 232
REMARK 465 HIS H 233
REMARK 465 HIS H 234
REMARK 465 GLY H 235
REMARK 465 ALA H 236
REMARK 465 ALA H 237
REMARK 465 GLU H 238
REMARK 465 GLN H 239
REMARK 465 LYS H 240
REMARK 465 LEU H 241
REMARK 465 ILE H 242
REMARK 465 SER H 243
REMARK 465 GLU H 244
REMARK 465 GLU H 245
REMARK 465 ASP H 246
REMARK 465 LEU H 247
REMARK 465 ASN H 248
REMARK 465 GLY H 249
REMARK 465 ALA H 250
REMARK 465 ALA H 251
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP A 239 OG SER A 241 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 130 27.01 -146.16
REMARK 500 SER A 142 -127.12 59.10
REMARK 500 GLU A 194 94.28 -63.33
REMARK 500 MET A 198 92.44 -69.25
REMARK 500 SER A 241 1.88 -66.39
REMARK 500 GLN A 264 -82.66 -116.09
REMARK 500 SER L 48 -39.45 -36.37
REMARK 500 ASN L 159 70.53 47.48
REMARK 500 SER H 17 -12.28 74.68
REMARK 500 ASP H 153 54.34 72.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL H 301
DBREF 6MLK A 4 283 UNP Q03133 ERYA3_SACER 2893 3172
DBREF 6MLK L 1 235 PDB 6MLK 6MLK 1 235
DBREF 6MLK H 1 251 PDB 6MLK 6MLK 1 251
SEQADV 6MLK MET A 1 UNP Q03133 INITIATING METHIONINE
SEQADV 6MLK ALA A 2 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK SER A 3 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK SER A 284 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK SER A 285 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK VAL A 286 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK ASP A 287 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK LYS A 288 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK LEU A 289 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK ALA A 290 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK ALA A 291 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK ALA A 292 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK LEU A 293 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK GLU A 294 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 295 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 296 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 297 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 298 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 299 UNP Q03133 EXPRESSION TAG
SEQADV 6MLK HIS A 300 UNP Q03133 EXPRESSION TAG
SEQRES 1 A 300 MET ALA SER GLN LEU ASP SER GLY THR PRO ALA ARG GLU
SEQRES 2 A 300 ALA SER SER ALA LEU ARG ASP GLY TYR ARG GLN ALA GLY
SEQRES 3 A 300 VAL SER GLY ARG VAL ARG SER TYR LEU ASP LEU LEU ALA
SEQRES 4 A 300 GLY LEU SER ASP PHE ARG GLU HIS PHE ASP GLY SER ASP
SEQRES 5 A 300 GLY PHE SER LEU ASP LEU VAL ASP MET ALA ASP GLY PRO
SEQRES 6 A 300 GLY GLU VAL THR VAL ILE CYS CYS ALA GLY THR ALA ALA
SEQRES 7 A 300 ILE SER GLY PRO HIS GLU PHE THR ARG LEU ALA GLY ALA
SEQRES 8 A 300 LEU ARG GLY ILE ALA PRO VAL ARG ALA VAL PRO GLN PRO
SEQRES 9 A 300 GLY TYR GLU GLU GLY GLU PRO LEU PRO SER SER MET ALA
SEQRES 10 A 300 ALA VAL ALA ALA VAL GLN ALA ASP ALA VAL ILE ARG THR
SEQRES 11 A 300 GLN GLY ASP LYS PRO PHE VAL VAL ALA GLY HIS SER ALA
SEQRES 12 A 300 GLY ALA LEU MET ALA TYR ALA LEU ALA THR GLU LEU LEU
SEQRES 13 A 300 ASP ARG GLY HIS PRO PRO ARG GLY VAL VAL LEU ILE ASP
SEQRES 14 A 300 VAL TYR PRO PRO GLY HIS GLN ASP ALA MET ASN ALA TRP
SEQRES 15 A 300 LEU GLU GLU LEU THR ALA THR LEU PHE ASP ARG GLU THR
SEQRES 16 A 300 VAL ARG MET ASP ASP THR ARG LEU THR ALA LEU GLY ALA
SEQRES 17 A 300 TYR ASP ARG LEU THR GLY GLN TRP ARG PRO ARG GLU THR
SEQRES 18 A 300 GLY LEU PRO THR LEU LEU VAL SER ALA GLY GLU PRO MET
SEQRES 19 A 300 GLY PRO TRP PRO ASP ASP SER TRP LYS PRO THR TRP PRO
SEQRES 20 A 300 PHE GLU HIS ASP THR VAL ALA VAL PRO GLY ASP HIS PHE
SEQRES 21 A 300 THR MET VAL GLN GLU HIS ALA ASP ALA ILE ALA ARG HIS
SEQRES 22 A 300 ILE ASP ALA TRP LEU GLY GLY GLY ASN SER SER SER VAL
SEQRES 23 A 300 ASP LYS LEU ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS
SEQRES 24 A 300 HIS
SEQRES 1 L 235 LEU PHE ALA ILE PRO LEU VAL VAL PRO PHE TYR SER HIS
SEQRES 2 L 235 SER ALA LEU ASP VAL VAL MET THR GLN SER PRO LEU SER
SEQRES 3 L 235 LEU PRO VAL THR PRO GLY GLU PRO ALA SER ILE SER CYS
SEQRES 4 L 235 ARG SER SER GLN SER LEU LEU HIS SER ASN GLY TYR ASN
SEQRES 5 L 235 TYR LEU ASP TRP TYR LEU GLN LYS PRO GLY GLN SER PRO
SEQRES 6 L 235 GLN LEU LEU ILE TYR LEU GLY SER ASN ARG ALA SER GLY
SEQRES 7 L 235 VAL PRO ASP ARG PHE SER GLY SER GLY SER GLY THR ASP
SEQRES 8 L 235 PHE THR LEU LYS ILE SER ARG VAL GLU ALA GLU ASP VAL
SEQRES 9 L 235 GLY VAL TYR TYR CYS MET GLN GLY THR HIS TRP PRO ARG
SEQRES 10 L 235 THR PHE GLY GLN GLY THR LYS VAL GLU ILE LYS ARG THR
SEQRES 11 L 235 VAL ALA ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP
SEQRES 12 L 235 GLU GLN LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU
SEQRES 13 L 235 LEU ASN ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP
SEQRES 14 L 235 LYS VAL ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU
SEQRES 15 L 235 SER VAL THR GLU GLN ASP SER LYS ASP SER THR TYR SER
SEQRES 16 L 235 LEU SER SER THR LEU THR LEU SER LYS ALA ASP TYR GLU
SEQRES 17 L 235 LYS HIS LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY
SEQRES 18 L 235 LEU SER SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU
SEQRES 19 L 235 CYS
SEQRES 1 H 251 MET ALA GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU
SEQRES 2 H 251 LEU LYS PRO SER GLU THR LEU SER LEU THR CYS ALA VAL
SEQRES 3 H 251 TYR GLY GLY SER PHE SER GLY TYR TYR TRP SER TRP ILE
SEQRES 4 H 251 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU
SEQRES 5 H 251 ILE ASN HIS SER GLY SER THR ASN TYR ASN PRO SER LEU
SEQRES 6 H 251 LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS ASN
SEQRES 7 H 251 GLN PHE SER LEU LYS LEU SER SER VAL THR ALA ALA ASP
SEQRES 8 H 251 THR ALA VAL TYR TYR CYS ALA ARG GLY LEU GLY TYR SER
SEQRES 9 H 251 GLY SER TYR TYR ALA PRO ASN TRP GLY GLN GLY THR LEU
SEQRES 10 H 251 VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL
SEQRES 11 H 251 PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY
SEQRES 12 H 251 THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO
SEQRES 13 H 251 GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR
SEQRES 14 H 251 SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER
SEQRES 15 H 251 GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER
SEQRES 16 H 251 SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN
SEQRES 17 H 251 HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU
SEQRES 18 H 251 PRO LYS SER CYS ALA ALA ALA HIS HIS HIS HIS HIS HIS
SEQRES 19 H 251 GLY ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU
SEQRES 20 H 251 ASN GLY ALA ALA
HET CL H 301 1
HETNAM CL CHLORIDE ION
FORMUL 4 CL CL 1-
FORMUL 5 HOH *65(H2 O)
HELIX 1 AA1 SER A 16 SER A 28 1 13
HELIX 2 AA2 ARG A 30 ASP A 43 1 14
HELIX 3 AA3 GLY A 81 GLU A 84 5 4
HELIX 4 AA4 PHE A 85 ARG A 93 1 9
HELIX 5 AA5 SER A 115 ARG A 129 1 15
HELIX 6 AA6 SER A 142 GLY A 159 1 18
HELIX 7 AA7 GLN A 176 TRP A 182 1 7
HELIX 8 AA8 TRP A 182 ARG A 193 1 12
HELIX 9 AA9 ASP A 199 TRP A 216 1 18
HELIX 10 AB1 ASP A 239 LYS A 243 5 5
HELIX 11 AB2 PHE A 260 GLN A 264 5 5
HELIX 12 AB3 HIS A 266 GLY A 279 1 14
HELIX 13 AB4 GLU L 100 VAL L 104 5 5
HELIX 14 AB5 SER L 142 LYS L 147 1 6
HELIX 15 AB6 LYS L 204 GLU L 208 1 5
HELIX 16 AB7 THR H 75 LYS H 77 5 3
HELIX 17 AB8 THR H 88 THR H 92 5 5
HELIX 18 AB9 SER H 165 ALA H 167 5 3
HELIX 19 AC1 PRO H 194 GLY H 199 5 6
HELIX 20 AC2 LYS H 210 ASN H 213 5 4
SHEET 1 AA1 2 HIS A 47 PHE A 48 0
SHEET 2 AA1 2 LEU A 112 PRO A 113 1 O LEU A 112 N PHE A 48
SHEET 1 AA2 7 VAL A 59 MET A 61 0
SHEET 2 AA2 7 VAL A 98 VAL A 101 -1 O VAL A 98 N MET A 61
SHEET 3 AA2 7 THR A 69 CYS A 73 1 N CYS A 72 O VAL A 101
SHEET 4 AA2 7 PHE A 136 HIS A 141 1 O ALA A 139 N CYS A 73
SHEET 5 AA2 7 VAL A 165 ILE A 168 1 O VAL A 166 N VAL A 138
SHEET 6 AA2 7 THR A 225 ALA A 230 1 O VAL A 228 N LEU A 167
SHEET 7 AA2 7 ASP A 251 VAL A 255 1 O ASP A 251 N LEU A 227
SHEET 1 AA3 4 MET L 20 SER L 23 0
SHEET 2 AA3 4 ALA L 35 SER L 41 -1 O SER L 38 N SER L 23
SHEET 3 AA3 4 ASP L 91 ILE L 96 -1 O LEU L 94 N ILE L 37
SHEET 4 AA3 4 PHE L 83 SER L 88 -1 N SER L 86 O THR L 93
SHEET 1 AA4 6 SER L 26 VAL L 29 0
SHEET 2 AA4 6 THR L 123 ILE L 127 1 O LYS L 124 N LEU L 27
SHEET 3 AA4 6 GLY L 105 GLN L 111 -1 N TYR L 107 O THR L 123
SHEET 4 AA4 6 LEU L 54 GLN L 59 -1 N ASP L 55 O MET L 110
SHEET 5 AA4 6 GLN L 66 TYR L 70 -1 O ILE L 69 N TRP L 56
SHEET 6 AA4 6 ASN L 74 ARG L 75 -1 O ASN L 74 N TYR L 70
SHEET 1 AA5 4 SER L 26 VAL L 29 0
SHEET 2 AA5 4 THR L 123 ILE L 127 1 O LYS L 124 N LEU L 27
SHEET 3 AA5 4 GLY L 105 GLN L 111 -1 N TYR L 107 O THR L 123
SHEET 4 AA5 4 THR L 118 PHE L 119 -1 O THR L 118 N GLN L 111
SHEET 1 AA6 4 SER L 135 PHE L 139 0
SHEET 2 AA6 4 THR L 150 PHE L 160 -1 O LEU L 156 N PHE L 137
SHEET 3 AA6 4 TYR L 194 SER L 203 -1 O LEU L 196 N LEU L 157
SHEET 4 AA6 4 SER L 180 VAL L 184 -1 N SER L 183 O SER L 197
SHEET 1 AA7 4 ALA L 174 LEU L 175 0
SHEET 2 AA7 4 ALA L 165 VAL L 171 -1 N VAL L 171 O ALA L 174
SHEET 3 AA7 4 VAL L 212 HIS L 219 -1 O ALA L 214 N LYS L 170
SHEET 4 AA7 4 VAL L 226 ASN L 231 -1 O VAL L 226 N VAL L 217
SHEET 1 AA8 4 GLN H 5 GLY H 10 0
SHEET 2 AA8 4 LEU H 20 TYR H 27 -1 O TYR H 27 N GLN H 5
SHEET 3 AA8 4 GLN H 79 LEU H 84 -1 O PHE H 80 N CYS H 24
SHEET 4 AA8 4 VAL H 69 ASP H 74 -1 N ASP H 74 O GLN H 79
SHEET 1 AA9 6 LEU H 13 LEU H 14 0
SHEET 2 AA9 6 THR H 116 VAL H 120 1 O THR H 119 N LEU H 14
SHEET 3 AA9 6 ALA H 93 ARG H 99 -1 N ALA H 93 O VAL H 118
SHEET 4 AA9 6 TRP H 36 GLN H 41 -1 N ILE H 39 O TYR H 96
SHEET 5 AA9 6 GLU H 48 ILE H 53 -1 O ILE H 53 N TRP H 36
SHEET 6 AA9 6 THR H 59 TYR H 61 -1 O ASN H 60 N GLU H 52
SHEET 1 AB1 4 SER H 129 LEU H 133 0
SHEET 2 AB1 4 ALA H 145 TYR H 154 -1 O LEU H 150 N PHE H 131
SHEET 3 AB1 4 TYR H 185 VAL H 193 -1 O VAL H 193 N ALA H 145
SHEET 4 AB1 4 VAL H 172 THR H 174 -1 N HIS H 173 O VAL H 190
SHEET 1 AB2 4 SER H 129 LEU H 133 0
SHEET 2 AB2 4 ALA H 145 TYR H 154 -1 O LEU H 150 N PHE H 131
SHEET 3 AB2 4 TYR H 185 VAL H 193 -1 O VAL H 193 N ALA H 145
SHEET 4 AB2 4 VAL H 178 LEU H 179 -1 N VAL H 178 O SER H 186
SHEET 1 AB3 3 THR H 160 TRP H 163 0
SHEET 2 AB3 3 TYR H 203 HIS H 209 -1 O ASN H 206 N SER H 162
SHEET 3 AB3 3 THR H 214 VAL H 220 -1 O VAL H 216 N VAL H 207
SSBOND 1 CYS L 155 CYS L 215 1555 1555 2.07
SSBOND 2 CYS H 24 CYS H 97 1555 1555 2.12
SSBOND 3 CYS H 149 CYS H 205 1555 1555 2.05
CISPEP 1 SER L 23 PRO L 24 0 -7.20
CISPEP 2 TRP L 115 PRO L 116 0 -8.03
CISPEP 3 TYR L 161 PRO L 162 0 1.37
CISPEP 4 PHE H 155 PRO H 156 0 -12.40
CISPEP 5 GLU H 157 PRO H 158 0 3.91
SITE 1 AC1 3 TYR H 107 TYR H 108 SER L 77
CRYST1 172.580 172.580 159.050 90.00 90.00 120.00 H 3 2 18
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 0.005794 0.003345 0.000000 0.00000
SCALE2 0.000000 0.006691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006287 0.00000
TER 1961 GLY A 279
TER 3638 ARG L 232
TER 5234 PRO H 222
MASTER 746 0 1 20 52 0 1 6 5291 3 6 63
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