HEADER SIGNALING PROTEIN 14-SEP-14 4V0C
TITLE CRYSTAL STRUCTURE OF THE KV7.1 PROXIMAL C-TERMINAL DOMAIN
TITLE 2 IN COMPLEX WITH CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROXIMAL C-TERMINAL DOMAIN, RESIDUES 352-396 AND RESIDUES
COMPND 5 502-539;
COMPND 6 SYNONYM: IKS PRODUCING SLOW VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT
COMPND 7 ALPHA KVLQT1, KQT-LIKE 1, VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT
COMPND 8 KV7.1, KV7.1 CHANNEL;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: CALMODULIN;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: RESIDUES 1-149;
COMPND 15 SYNONYM: CAM, KV7.1 CHANNEL;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET DUET;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET DUET
KEYWDS SIGNALING PROTEIN, VOLTAGE-DEPENDENT POTASSIUM CHANNELS, LONG QT
KEYWDS 2 SYNDROME, CALMODULIN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.SACHYANI,J.A.HIRSCH
REVDAT 2 17-DEC-14 4V0C 1 JRNL
REVDAT 1 05-NOV-14 4V0C 0
JRNL AUTH D.SACHYANI,M.DVIR,R.STRULOVICH,G.TRIA,W.TOBELAIM,A.PERETZ,
JRNL AUTH 2 O.PONGS,D.SVERGUN,B.ATTALI,J.A.HIRSCH
JRNL TITL STRUCTURAL BASIS OF A KV7.1 POTASSIUM CHANNEL GATING
JRNL TITL 2 MODULE: STUDIES OF THE INTRACELLULAR C-TERMINAL DOMAIN IN
JRNL TITL 3 COMPLEX WITH CALMODULIN.
JRNL REF STRUCTURE V. 22 1582 2014
JRNL REFN ISSN 0969-2126
JRNL PMID 25441029
JRNL DOI 10.1016/J.STR.2014.07.016
REMARK 2
REMARK 2 RESOLUTION. 2.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.9_1692)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.784
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.32
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.81
REMARK 3 NUMBER OF REFLECTIONS : 17456
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.2280
REMARK 3 R VALUE (WORKING SET) : 0.2259
REMARK 3 FREE R VALUE : 0.2679
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 883
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 49.7913 - 5.1948 1.00 2862 140 0.2018 0.2694
REMARK 3 2 5.1948 - 4.1239 1.00 2779 139 0.2092 0.2073
REMARK 3 3 4.1239 - 3.6028 1.00 2736 155 0.2299 0.2824
REMARK 3 4 3.6028 - 3.2734 1.00 2759 158 0.2679 0.3089
REMARK 3 5 3.2734 - 3.0388 1.00 2716 151 0.2919 0.3414
REMARK 3 6 3.0388 - 2.8597 0.99 2721 140 0.2887 0.2825
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) : 0.32
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.27
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 3598
REMARK 3 ANGLE : 1.049 4820
REMARK 3 CHIRALITY : 0.035 531
REMARK 3 PLANARITY : 0.004 646
REMARK 3 DIHEDRAL : 16.310 1279
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 19
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 330 THROUGH 354 )
REMARK 3 ORIGIN FOR THE GROUP (A): -61.4027 53.6534 43.2280
REMARK 3 T TENSOR
REMARK 3 T11: 0.8859 T22: 1.4710
REMARK 3 T33: 1.4195 T12: -0.2852
REMARK 3 T13: -0.0808 T23: -0.1213
REMARK 3 L TENSOR
REMARK 3 L11: 0.6321 L22: 1.9233
REMARK 3 L33: -0.0070 L12: -1.2405
REMARK 3 L13: -0.1001 L23: 0.0441
REMARK 3 S TENSOR
REMARK 3 S11: -0.5515 S12: 0.7018 S13: 1.0119
REMARK 3 S21: -0.0681 S22: -0.3984 S23: 0.3398
REMARK 3 S31: 0.4095 S32: -0.0799 S33: 1.5733
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 355 THROUGH 395 )
REMARK 3 ORIGIN FOR THE GROUP (A): -59.4618 14.0227 13.9016
REMARK 3 T TENSOR
REMARK 3 T11: 0.4624 T22: 0.4653
REMARK 3 T33: 0.2742 T12: -0.0833
REMARK 3 T13: -0.0657 T23: 0.1120
REMARK 3 L TENSOR
REMARK 3 L11: 7.4699 L22: 8.2808
REMARK 3 L33: 6.9311 L12: -0.7418
REMARK 3 L13: -1.2285 L23: 0.0816
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: -0.0653 S13: 0.2388
REMARK 3 S21: -0.3630 S22: 0.2254 S23: 1.5352
REMARK 3 S31: 0.6671 S32: -0.4439 S33: -0.1670
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 396 THROUGH 535 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.7635 -19.7160 -11.1132
REMARK 3 T TENSOR
REMARK 3 T11: 0.6754 T22: 0.6084
REMARK 3 T33: 0.3906 T12: 0.2225
REMARK 3 T13: -0.0948 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 1.9717 L22: 3.6810
REMARK 3 L33: 7.2153 L12: -0.6537
REMARK 3 L13: -0.9902 L23: -0.2185
REMARK 3 S TENSOR
REMARK 3 S11: 0.4223 S12: 0.4623 S13: 0.0065
REMARK 3 S21: -0.5095 S22: -0.0138 S23: -0.0182
REMARK 3 S31: -0.3922 S32: 0.0250 S33: -0.1892
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 354 THROUGH 390 )
REMARK 3 ORIGIN FOR THE GROUP (A): -53.1692 -34.0979 -9.9393
REMARK 3 T TENSOR
REMARK 3 T11: 0.6213 T22: 0.6270
REMARK 3 T33: 0.5330 T12: 0.1273
REMARK 3 T13: -0.1697 T23: -0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 5.7103 L22: 2.9802
REMARK 3 L33: 5.5891 L12: 2.0609
REMARK 3 L13: 0.8101 L23: -3.2427
REMARK 3 S TENSOR
REMARK 3 S11: 0.9586 S12: 0.2865 S13: -0.4971
REMARK 3 S21: -0.9792 S22: -0.9228 S23: 0.6065
REMARK 3 S31: -0.1450 S32: -1.0300 S33: -0.0856
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 391 THROUGH 535 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.9721 0.5730 14.4453
REMARK 3 T TENSOR
REMARK 3 T11: 1.0349 T22: 0.4353
REMARK 3 T33: 0.3812 T12: 0.0321
REMARK 3 T13: 0.0020 T23: 0.1264
REMARK 3 L TENSOR
REMARK 3 L11: 3.3424 L22: 8.8537
REMARK 3 L33: 6.5207 L12: -1.6926
REMARK 3 L13: -1.0768 L23: 6.9103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0954 S12: -0.2844 S13: -0.0451
REMARK 3 S21: 0.0631 S22: -0.1079 S23: 0.1038
REMARK 3 S31: 0.0790 S32: 0.3930 S33: 0.0441
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 5 THROUGH 72 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4785 -15.5955 -16.1656
REMARK 3 T TENSOR
REMARK 3 T11: 0.8650 T22: 0.7284
REMARK 3 T33: 0.5037 T12: 0.2396
REMARK 3 T13: 0.0750 T23: 0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 7.3303 L22: 9.7371
REMARK 3 L33: 7.4936 L12: -1.1192
REMARK 3 L13: 1.3506 L23: -2.5211
REMARK 3 S TENSOR
REMARK 3 S11: 0.2229 S12: 0.4372 S13: -0.2444
REMARK 3 S21: -0.7157 S22: -0.0103 S23: -0.9124
REMARK 3 S31: 0.1829 S32: 0.9270 S33: -0.3118
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 73 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -58.4642 -23.0969 -21.1259
REMARK 3 T TENSOR
REMARK 3 T11: 1.3429 T22: 0.9755
REMARK 3 T33: 1.2772 T12: 0.0946
REMARK 3 T13: -0.0490 T23: 0.1306
REMARK 3 L TENSOR
REMARK 3 L11: 5.7105 L22: 6.2280
REMARK 3 L33: 6.0564 L12: -5.8917
REMARK 3 L13: 3.2979 L23: -2.5856
REMARK 3 S TENSOR
REMARK 3 S11: -0.4347 S12: 0.6450 S13: -1.1254
REMARK 3 S21: -0.2333 S22: 0.4034 S23: 2.2337
REMARK 3 S31: 0.9944 S32: 1.2803 S33: -0.3535
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 82 THROUGH 98 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.6759 -37.9565 -12.1793
REMARK 3 T TENSOR
REMARK 3 T11: 0.7493 T22: 1.2889
REMARK 3 T33: 1.5884 T12: -0.2815
REMARK 3 T13: -0.6921 T23: 0.3978
REMARK 3 L TENSOR
REMARK 3 L11: 3.4648 L22: 8.2123
REMARK 3 L33: 9.7935 L12: -2.3987
REMARK 3 L13: 4.0062 L23: 3.1764
REMARK 3 S TENSOR
REMARK 3 S11: -1.0870 S12: -1.1644 S13: -2.2730
REMARK 3 S21: -2.7802 S22: 3.2505 S23: 4.2987
REMARK 3 S31: 0.9823 S32: -5.6300 S33: -1.0362
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 99 THROUGH 125 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.4550 -32.1813 0.4011
REMARK 3 T TENSOR
REMARK 3 T11: 0.6617 T22: 0.4964
REMARK 3 T33: 1.1044 T12: 0.1107
REMARK 3 T13: 0.2080 T23: 0.1191
REMARK 3 L TENSOR
REMARK 3 L11: 9.8997 L22: 8.6401
REMARK 3 L33: 4.1198 L12: 2.2795
REMARK 3 L13: 0.3087 L23: -2.6748
REMARK 3 S TENSOR
REMARK 3 S11: 0.1520 S12: -0.3026 S13: -0.9477
REMARK 3 S21: 1.0552 S22: -0.1451 S23: 1.5146
REMARK 3 S31: -0.1799 S32: -0.4328 S33: -0.0206
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 126 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.4007 -29.7300 -5.2150
REMARK 3 T TENSOR
REMARK 3 T11: 0.7365 T22: 1.2086
REMARK 3 T33: 2.0410 T12: 0.0441
REMARK 3 T13: -0.0023 T23: 0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 3.8132 L22: 8.5752
REMARK 3 L33: 7.3856 L12: -3.1896
REMARK 3 L13: -2.3318 L23: -2.8716
REMARK 3 S TENSOR
REMARK 3 S11: 0.5181 S12: 0.0161 S13: 0.6498
REMARK 3 S21: 0.1893 S22: 1.5322 S23: 3.7299
REMARK 3 S31: -0.1290 S32: -4.1531 S33: -1.2034
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -42.5955 -2.6943 20.4466
REMARK 3 T TENSOR
REMARK 3 T11: 0.7141 T22: 0.5513
REMARK 3 T33: 0.4182 T12: -0.0305
REMARK 3 T13: -0.0591 T23: -0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 9.6554 L22: 7.5858
REMARK 3 L33: 8.4195 L12: 1.2957
REMARK 3 L13: 0.4361 L23: -0.5632
REMARK 3 S TENSOR
REMARK 3 S11: -0.6693 S12: -0.3198 S13: -0.8064
REMARK 3 S21: -1.0929 S22: 0.5918 S23: -0.8701
REMARK 3 S31: 0.8461 S32: 1.1357 S33: -0.1205
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 39 THROUGH 47 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.3964 12.2692 11.4061
REMARK 3 T TENSOR
REMARK 3 T11: 2.0144 T22: -0.0822
REMARK 3 T33: 1.1885 T12: 0.2453
REMARK 3 T13: -0.3091 T23: 0.0708
REMARK 3 L TENSOR
REMARK 3 L11: 1.3998 L22: 1.6112
REMARK 3 L33: 0.0233 L12: -1.4082
REMARK 3 L13: -0.0818 L23: 0.1185
REMARK 3 S TENSOR
REMARK 3 S11: -0.8320 S12: 0.7262 S13: 1.5050
REMARK 3 S21: -0.9935 S22: 0.1801 S23: 0.5124
REMARK 3 S31: -1.6148 S32: 0.9848 S33: 1.0361
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 48 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1904 8.8300 26.9208
REMARK 3 T TENSOR
REMARK 3 T11: 1.2618 T22: 0.8054
REMARK 3 T33: 0.7611 T12: -0.0484
REMARK 3 T13: -0.2429 T23: -0.1924
REMARK 3 L TENSOR
REMARK 3 L11: 3.7639 L22: 6.5701
REMARK 3 L33: 3.0623 L12: -3.0168
REMARK 3 L13: 0.6061 L23: 2.9460
REMARK 3 S TENSOR
REMARK 3 S11: -0.5334 S12: -1.6518 S13: 2.0598
REMARK 3 S21: 1.1648 S22: 0.9453 S23: -0.5656
REMARK 3 S31: -0.6456 S32: 0.9892 S33: -0.4993
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 65 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -48.4110 -0.9821 27.9839
REMARK 3 T TENSOR
REMARK 3 T11: 1.7196 T22: 0.6730
REMARK 3 T33: 0.3963 T12: -0.0570
REMARK 3 T13: -0.1897 T23: 0.2313
REMARK 3 L TENSOR
REMARK 3 L11: 4.2240 L22: 3.1586
REMARK 3 L33: 1.9967 L12: 3.4188
REMARK 3 L13: 4.3617 L23: 5.1854
REMARK 3 S TENSOR
REMARK 3 S11: -0.4036 S12: 0.1348 S13: 1.3177
REMARK 3 S21: 0.6473 S22: 0.0811 S23: 1.2237
REMARK 3 S31: -2.3867 S32: -2.6392 S33: -0.4429
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 74 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4913 4.5005 26.7852
REMARK 3 T TENSOR
REMARK 3 T11: 1.8211 T22: 0.9599
REMARK 3 T33: 0.9170 T12: -0.6954
REMARK 3 T13: -0.1942 T23: 0.6666
REMARK 3 L TENSOR
REMARK 3 L11: -0.0015 L22: 8.5905
REMARK 3 L33: 0.1346 L12: -0.1974
REMARK 3 L13: -0.0421 L23: 1.0156
REMARK 3 S TENSOR
REMARK 3 S11: -1.0296 S12: -0.2417 S13: -0.2147
REMARK 3 S21: -0.2030 S22: 0.8869 S23: 1.7854
REMARK 3 S31: 0.6266 S32: -0.0520 S33: -1.7005
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 82 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): -68.4245 15.7529 19.9755
REMARK 3 T TENSOR
REMARK 3 T11: 0.7780 T22: 0.7804
REMARK 3 T33: 0.7272 T12: -0.1101
REMARK 3 T13: 0.0619 T23: 0.0992
REMARK 3 L TENSOR
REMARK 3 L11: 6.5945 L22: 1.9878
REMARK 3 L33: 5.2258 L12: -3.4943
REMARK 3 L13: 5.7576 L23: -3.0647
REMARK 3 S TENSOR
REMARK 3 S11: -0.3536 S12: -0.9712 S13: -0.7970
REMARK 3 S21: 0.1766 S22: 0.7720 S23: -0.2872
REMARK 3 S31: -1.8016 S32: 0.2656 S33: -0.3850
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 93 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.0777 13.8507 6.6351
REMARK 3 T TENSOR
REMARK 3 T11: 0.7285 T22: 0.6079
REMARK 3 T33: 0.8113 T12: -0.1172
REMARK 3 T13: -0.2208 T23: -0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 9.0807 L22: 6.4171
REMARK 3 L33: 3.7810 L12: -1.4293
REMARK 3 L13: 1.0221 L23: -0.9813
REMARK 3 S TENSOR
REMARK 3 S11: 0.0975 S12: 1.0723 S13: 0.3511
REMARK 3 S21: -0.6025 S22: -0.0961 S23: 0.7725
REMARK 3 S31: 0.4016 S32: -0.5766 S33: -0.0765
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 127 THROUGH 137 )
REMARK 3 ORIGIN FOR THE GROUP (A): -77.3038 10.2956 6.4145
REMARK 3 T TENSOR
REMARK 3 T11: -2.2972 T22: 1.6036
REMARK 3 T33: 1.5636 T12: -1.8309
REMARK 3 T13: 0.1802 T23: -0.1168
REMARK 3 L TENSOR
REMARK 3 L11: 2.1089 L22: 3.6722
REMARK 3 L33: 0.6272 L12: -1.1314
REMARK 3 L13: -0.9097 L23: -0.3670
REMARK 3 S TENSOR
REMARK 3 S11: -0.4158 S12: 0.4634 S13: -0.5538
REMARK 3 S21: -0.9988 S22: 0.1653 S23: 2.2024
REMARK 3 S31: 0.2602 S32: -0.4369 S33: -0.1474
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 138 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): -71.0573 6.1438 16.5149
REMARK 3 T TENSOR
REMARK 3 T11: 1.1019 T22: 0.8730
REMARK 3 T33: 1.3828 T12: -0.2588
REMARK 3 T13: 0.0005 T23: 0.1284
REMARK 3 L TENSOR
REMARK 3 L11: 7.1027 L22: 6.2969
REMARK 3 L33: 7.3081 L12: -5.5489
REMARK 3 L13: 0.2518 L23: -4.1454
REMARK 3 S TENSOR
REMARK 3 S11: 0.9946 S12: 0.7280 S13: -1.4302
REMARK 3 S21: -2.8382 S22: -0.0433 S23: 1.7278
REMARK 3 S31: 1.3603 S32: -0.7877 S33: -1.2114
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 4V0C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-14.
REMARK 100 THE PDBE ID CODE IS EBI-61751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.924
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17341
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.85
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 15.3
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.90
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.47
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.40
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHENIX, SHARP
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.3 M POTASSIUM THIOCYANATE, 0.1 M
REMARK 280 SODIUM ACETATE TRIHYDRATE PH=5.6, 5 MM CACL2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 37.55333
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 18.77667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.16500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 9.38833
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 46.94167
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -150.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 324
REMARK 465 GLY A 325
REMARK 465 SER A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
REMARK 465 HIS A 329
REMARK 465 ASN A 346
REMARK 465 LEU A 347
REMARK 465 TYR A 348
REMARK 465 PHE A 349
REMARK 465 GLN A 350
REMARK 465 GLY A 350A
REMARK 465 TYR A 536
REMARK 465 ASP A 537
REMARK 465 VAL A 538
REMARK 465 ARG A 539
REMARK 465 MET B 324
REMARK 465 GLY B 325
REMARK 465 SER B 326
REMARK 465 HIS B 327
REMARK 465 HIS B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 HIS B 332
REMARK 465 HIS B 333
REMARK 465 HIS B 334
REMARK 465 GLY B 335
REMARK 465 SER B 336
REMARK 465 ASP B 337
REMARK 465 TYR B 338
REMARK 465 ASP B 339
REMARK 465 ASP B 340
REMARK 465 ILE B 341
REMARK 465 PHE B 342
REMARK 465 THR B 343
REMARK 465 THR B 344
REMARK 465 GLU B 345
REMARK 465 ASN B 346
REMARK 465 LEU B 347
REMARK 465 TYR B 348
REMARK 465 PHE B 349
REMARK 465 GLN B 350
REMARK 465 GLY B 350A
REMARK 465 SER B 351
REMARK 465 ALA B 352
REMARK 465 LEU B 353
REMARK 465 TYR B 536
REMARK 465 ASP B 537
REMARK 465 VAL B 538
REMARK 465 ARG B 539
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 LEU C 4
REMARK 465 LYS C 148
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 LYS D 148
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 330 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 331 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 332 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 334 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A 338 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP A 339 CG OD1 OD2
REMARK 470 ILE A 341 CG1 CG2 CD1
REMARK 470 PHE A 342 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLU A 345 CG CD OE1 OE2
REMARK 470 SER A 351 OG
REMARK 470 LEU A 353 CG CD1 CD2
REMARK 470 LYS A 354 CE NZ
REMARK 470 VAL A 355 CG1 CG2
REMARK 470 GLN A 356 CG CD OE1 NE2
REMARK 470 LYS A 358 CG CD CE NZ
REMARK 470 GLN A 359 CG CD OE1 NE2
REMARK 470 ARG A 360 CZ NH1 NH2
REMARK 470 SER A 390 OG
REMARK 470 GLU A 508 CG CD OE1 OE2
REMARK 470 LYS A 534 CG CD CE NZ
REMARK 470 LYS B 354 CG CD CE NZ
REMARK 470 VAL B 355 CG1 CG2
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 GLN B 359 CG CD OE1 NE2
REMARK 470 ARG B 360 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 362 CG CD CE NZ
REMARK 470 LYS B 527 CG CD CE NZ
REMARK 470 LYS B 534 CG CD CE NZ
REMARK 470 GLU C 6 CG CD OE1 OE2
REMARK 470 LYS C 13 CG CD CE NZ
REMARK 470 ASN C 42 CG OD1 ND2
REMARK 470 GLU C 54 CD OE1 OE2
REMARK 470 LYS C 75 CG CD CE NZ
REMARK 470 GLU C 83 CG CD OE1 OE2
REMARK 470 GLU C 84 CG CD OE1 OE2
REMARK 470 ARG C 86 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 94 CG CD CE NZ
REMARK 470 ILE C 100 CG1 CG2 CD1
REMARK 470 GLU C 127 CG CD OE1 OE2
REMARK 470 GLN D 3 CG CD OE1 NE2
REMARK 470 GLU D 6 CG CD OE1 OE2
REMARK 470 GLN D 8 CD OE1 NE2
REMARK 470 LYS D 30 CG CD CE NZ
REMARK 470 LEU D 39 CG CD1 CD2
REMARK 470 GLU D 45 CG CD OE1 OE2
REMARK 470 LYS D 75 CG CD CE NZ
REMARK 470 LYS D 77 CG CD CE NZ
REMARK 470 ASP D 78 CG OD1 OD2
REMARK 470 GLU D 82 CG CD OE1 OE2
REMARK 470 GLU D 83 CG CD OE1 OE2
REMARK 470 LYS D 94 CG CD CE NZ
REMARK 470 ASN D 97 CG OD1 ND2
REMARK 470 ILE D 100 CG1 CG2 CD1
REMARK 470 ILE D 125 CG1 CG2 CD1
REMARK 470 GLU D 127 CG CD OE1 OE2
REMARK 470 ASP D 129 CG OD1 OD2
REMARK 470 ILE D 130 CG1 CG2 CD1
REMARK 470 GLN D 135 CG CD OE1 NE2
REMARK 470 VAL D 136 CG1 CG2
REMARK 470 GLU D 139 CG CD OE1 OE2
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 C 20 O THR C 26 2.03
REMARK 500 OD2 ASP C 22 OE2 GLU C 31 1.84
REMARK 500 OD2 ASP D 22 OE1 GLU D 31 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY D 134 N - CA - C ANGL. DEV. = -20.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 344 178.93 -59.07
REMARK 500 GLN B 356 31.00 -68.14
REMARK 500 SER B 389 100.98 -29.96
REMARK 500 GLU C 7 -58.65 -28.93
REMARK 500 MET C 76 -24.01 -150.66
REMARK 500 ASN C 97 -151.26 -84.26
REMARK 500 LYS C 115 -153.76 54.25
REMARK 500 LEU C 116 143.20 167.51
REMARK 500 ALA C 128 -90.16 -63.38
REMARK 500 ASP C 129 37.05 70.33
REMARK 500 ASP C 131 112.79 -161.59
REMARK 500 ASP C 133 -30.68 -137.85
REMARK 500 ASN D 42 73.43 -119.91
REMARK 500 ALA D 46 -161.49 -73.19
REMARK 500 GLU D 47 -44.61 59.18
REMARK 500 SER D 81 -13.65 159.84
REMARK 500 LYS D 115 87.76 53.51
REMARK 500 GLN D 135 -66.61 -134.73
REMARK 500 VAL D 136 71.69 55.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 26 O
REMARK 620 2 THR C 26 OG1 83.3
REMARK 620 3 GLU C 31 OE2 81.6 127.3
REMARK 620 4 ASP C 20 OD1 50.6 121.0 85.0
REMARK 620 5 ASP C 22 OD2 104.0 167.8 46.1 70.7
REMARK 620 6 ASP C 24 OD1 92.0 77.3 153.0 70.9 111.8
REMARK 620 7 ASP C 24 OD2 143.0 73.8 135.4 119.8 104.2 55.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 20 OD1
REMARK 620 2 ASP D 24 OD1 63.7
REMARK 620 3 ASP D 24 OD2 113.2 54.2
REMARK 620 4 ASP D 22 OD2 90.0 133.8 115.4
REMARK 620 5 THR D 26 O 57.9 83.6 128.7 115.0
REMARK 620 6 THR D 26 OG1 105.7 60.8 64.1 163.3 70.5
REMARK 620 7 GLU D 31 OE1 66.4 128.8 169.9 55.0 60.4 126.0
REMARK 620 8 GLU D 31 OE2 116.9 153.0 129.3 72.0 76.0 95.3 53.6
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 58 OD1
REMARK 620 2 ASP C 56 OD1 75.9
REMARK 620 3 GLU C 67 OE1 82.0 75.1
REMARK 620 4 ASN C 60 OD1 80.4 58.2 132.8
REMARK 620 5 THR C 62 O 131.8 56.0 88.7 71.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 62 O
REMARK 620 2 GLU D 67 OE1 87.5
REMARK 620 3 GLU D 67 OE2 118.3 55.1
REMARK 620 4 HOH D2001 O 65.3 92.7 145.6
REMARK 620 5 ASP D 58 OD2 164.1 102.3 60.4 125.8
REMARK 620 6 ASP D 56 OD1 78.6 98.6 63.9 141.6 87.5
REMARK 620 7 ASN D 60 OD1 76.9 163.2 138.8 75.3 94.3 84.6
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SCN A1536
DBREF 4V0C A 352 396 UNP P51787 KCNQ1_HUMAN 352 396
DBREF 4V0C A 397 539 UNP P51787 KCNQ1_HUMAN 502 539
DBREF 4V0C B 352 396 UNP P51787 KCNQ1_HUMAN 352 396
DBREF 4V0C B 397 539 UNP P51787 KCNQ1_HUMAN 502 539
DBREF 4V0C C 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 4V0C D 0 148 UNP P62158 CALM_HUMAN 1 149
SEQADV 4V0C MET A 324 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY A 325 UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER A 326 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 327 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 328 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 329 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 330 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 331 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 332 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 333 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS A 334 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY A 335 UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER A 336 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP A 337 UNP P51787 EXPRESSION TAG
SEQADV 4V0C TYR A 338 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP A 339 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP A 340 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ILE A 341 UNP P51787 EXPRESSION TAG
SEQADV 4V0C PHE A 342 UNP P51787 EXPRESSION TAG
SEQADV 4V0C THR A 343 UNP P51787 EXPRESSION TAG
SEQADV 4V0C THR A 344 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLU A 345 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASN A 346 UNP P51787 EXPRESSION TAG
SEQADV 4V0C LEU A 347 UNP P51787 EXPRESSION TAG
SEQADV 4V0C TYR A 348 UNP P51787 EXPRESSION TAG
SEQADV 4V0C PHE A 349 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLN A 350 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY A 350A UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER A 351 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLU A 397 UNP P51787 HIS 502 ENGINEERED MUTATION
SEQADV 4V0C PHE A 398 UNP P51787 ILE 503 ENGINEERED MUTATION
SEQADV 4V0C MET B 324 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY B 325 UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER B 326 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 327 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 328 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 329 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 330 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 331 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 332 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 333 UNP P51787 EXPRESSION TAG
SEQADV 4V0C HIS B 334 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY B 335 UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER B 336 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP B 337 UNP P51787 EXPRESSION TAG
SEQADV 4V0C TYR B 338 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP B 339 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASP B 340 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ILE B 341 UNP P51787 EXPRESSION TAG
SEQADV 4V0C PHE B 342 UNP P51787 EXPRESSION TAG
SEQADV 4V0C THR B 343 UNP P51787 EXPRESSION TAG
SEQADV 4V0C THR B 344 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLU B 345 UNP P51787 EXPRESSION TAG
SEQADV 4V0C ASN B 346 UNP P51787 EXPRESSION TAG
SEQADV 4V0C LEU B 347 UNP P51787 EXPRESSION TAG
SEQADV 4V0C TYR B 348 UNP P51787 EXPRESSION TAG
SEQADV 4V0C PHE B 349 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLN B 350 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLY B 350A UNP P51787 EXPRESSION TAG
SEQADV 4V0C SER B 351 UNP P51787 EXPRESSION TAG
SEQADV 4V0C GLU B 397 UNP P51787 HIS 502 ENGINEERED MUTATION
SEQADV 4V0C PHE B 398 UNP P51787 ILE 503 ENGINEERED MUTATION
SEQRES 1 A 112 MET GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 A 112 ASP TYR ASP ASP ILE PHE THR THR GLU ASN LEU TYR PHE
SEQRES 3 A 112 GLN GLY SER ALA LEU LYS VAL GLN GLN LYS GLN ARG GLN
SEQRES 4 A 112 LYS HIS PHE ASN ARG GLN ILE PRO ALA ALA ALA SER LEU
SEQRES 5 A 112 ILE GLN THR ALA TRP ARG CYS TYR ALA ALA GLU ASN PRO
SEQRES 6 A 112 ASP SER SER THR TRP LYS ILE TYR ILE GLU PHE SER GLN
SEQRES 7 A 112 LEU ARG GLU HIS HIS ARG ALA THR ILE LYS VAL ILE ARG
SEQRES 8 A 112 ARG MET GLN TYR PHE VAL ALA LYS LYS LYS PHE GLN GLN
SEQRES 9 A 112 ALA ARG LYS PRO TYR ASP VAL ARG
SEQRES 1 B 112 MET GLY SER HIS HIS HIS HIS HIS HIS HIS HIS GLY SER
SEQRES 2 B 112 ASP TYR ASP ASP ILE PHE THR THR GLU ASN LEU TYR PHE
SEQRES 3 B 112 GLN GLY SER ALA LEU LYS VAL GLN GLN LYS GLN ARG GLN
SEQRES 4 B 112 LYS HIS PHE ASN ARG GLN ILE PRO ALA ALA ALA SER LEU
SEQRES 5 B 112 ILE GLN THR ALA TRP ARG CYS TYR ALA ALA GLU ASN PRO
SEQRES 6 B 112 ASP SER SER THR TRP LYS ILE TYR ILE GLU PHE SER GLN
SEQRES 7 B 112 LEU ARG GLU HIS HIS ARG ALA THR ILE LYS VAL ILE ARG
SEQRES 8 B 112 ARG MET GLN TYR PHE VAL ALA LYS LYS LYS PHE GLN GLN
SEQRES 9 B 112 ALA ARG LYS PRO TYR ASP VAL ARG
SEQRES 1 C 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 C 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 C 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 C 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 C 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 149 GLN MET MET THR ALA LYS
SEQRES 1 D 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MET MET THR ALA LYS
HET CA C 201 1
HET CA C 202 1
HET CA D 201 1
HET CA D 202 1
HET SCN A1536 3
HETNAM CA CALCIUM ION
HETNAM SCN THIOCYANATE ION
FORMUL 5 CA 4(CA 2+)
FORMUL 6 SCN C N S 1-
FORMUL 2 HOH *4(H2 O)
HELIX 1 1 LYS A 358 GLU A 385 1 28
HELIX 2 2 THR A 391 ILE A 394 5 4
HELIX 3 3 TYR A 395 LYS A 534 1 35
HELIX 4 4 GLN B 356 ARG B 366 1 11
HELIX 5 5 ARG B 366 GLU B 385 1 20
HELIX 6 6 THR B 391 ILE B 394 5 4
HELIX 7 7 TYR B 395 LYS B 534 1 35
HELIX 8 8 THR C 5 ASP C 20 1 16
HELIX 9 9 THR C 28 LEU C 39 1 12
HELIX 10 10 THR C 44 ASP C 56 1 13
HELIX 11 11 ASP C 64 ALA C 73 1 10
HELIX 12 12 SER C 81 ASP C 93 1 13
HELIX 13 13 ALA C 102 LEU C 112 1 11
HELIX 14 14 THR C 117 ASP C 129 1 13
HELIX 15 15 TYR C 138 THR C 146 1 9
HELIX 16 16 THR D 5 ASP D 20 1 16
HELIX 17 17 THR D 28 LEU D 39 1 12
HELIX 18 18 GLU D 47 ASP D 56 1 10
HELIX 19 19 ASP D 64 ARG D 74 1 11
HELIX 20 20 SER D 81 VAL D 91 1 11
HELIX 21 21 SER D 101 LEU D 112 1 12
HELIX 22 22 THR D 117 ASP D 129 1 13
HELIX 23 23 ASN D 137 THR D 146 1 10
SHEET 1 CA 2 TYR C 99 SER C 101 0
SHEET 2 CA 2 GLN C 135 ASN C 137 -1 O VAL C 136 N ILE C 100
LINK CA CA C 201 O THR C 26 1555 1555 2.37
LINK CA CA C 201 OG1 THR C 26 1555 1555 2.37
LINK CA CA C 201 OE2 GLU C 31 1555 1555 2.37
LINK CA CA C 201 OD1 ASP C 20 1555 1555 2.37
LINK CA CA C 201 OD2 ASP C 22 1555 1555 2.35
LINK CA CA C 201 OD1 ASP C 24 1555 1555 2.35
LINK CA CA C 201 OD2 ASP C 24 1555 1555 2.38
LINK CA CA C 202 OD1 ASP C 58 1555 1555 2.36
LINK CA CA C 202 O THR C 62 1555 1555 2.37
LINK CA CA C 202 OD1 ASN C 60 1555 1555 2.38
LINK CA CA C 202 OE1 GLU C 67 1555 1555 2.36
LINK CA CA C 202 OD1 ASP C 56 1555 1555 2.37
LINK CA CA D 201 OG1 THR D 26 1555 1555 2.39
LINK CA CA D 201 OE1 GLU D 31 1555 1555 2.38
LINK CA CA D 201 OE2 GLU D 31 1555 1555 2.38
LINK CA CA D 201 O THR D 26 1555 1555 2.38
LINK CA CA D 201 OD2 ASP D 22 1555 1555 2.34
LINK CA CA D 201 OD2 ASP D 24 1555 1555 2.38
LINK CA CA D 201 OD1 ASP D 24 1555 1555 2.37
LINK CA CA D 201 OD1 ASP D 20 1555 1555 2.37
LINK CA CA D 202 OE1 GLU D 67 1555 1555 2.36
LINK CA CA D 202 OE2 GLU D 67 1555 1555 2.36
LINK CA CA D 202 O HOH D2001 1555 1555 3.14
LINK CA CA D 202 OD2 ASP D 58 1555 1555 2.36
LINK CA CA D 202 OD1 ASP D 56 1555 1555 2.36
LINK CA CA D 202 OD1 ASN D 60 1555 1555 2.38
LINK CA CA D 202 O THR D 62 1555 1555 2.37
CISPEP 1 LEU D 39 GLY D 40 0 -3.77
SITE 1 AC1 5 ASP C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC1 5 GLU C 31
SITE 1 AC2 5 ASP C 56 ASP C 58 ASN C 60 THR C 62
SITE 2 AC2 5 GLU C 67
SITE 1 AC3 5 ASP D 20 ASP D 22 ASP D 24 THR D 26
SITE 2 AC3 5 GLU D 31
SITE 1 AC4 5 ASP D 56 ASP D 58 ASN D 60 THR D 62
SITE 2 AC4 5 GLU D 67
SITE 1 AC5 2 GLN B 521 GLN D 41
CRYST1 152.092 152.092 56.330 90.00 90.00 120.00 P 65 12
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 0.006575 0.003796 0.000000 0.00000
SCALE2 0.000000 0.007592 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017753 0.00000
(ATOM LINES ARE NOT SHOWN.)
END