HEADER SIGNALING PROTEIN 24-MAR-17 5NIN
TITLE CRYSTAL STRUCTURE OF AKAP79 CALMODULIN BINDING DOMAIN PEPTIDE IN
TITLE 2 COMPLEX WITH CA2+/CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: B, A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: A-KINASE ANCHOR PROTEIN 5;
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: UNP RESIDUES 77-92;
COMPND 10 SYNONYM: AKAP-5,A-KINASE ANCHOR PROTEIN 79 KDA,AKAP 79,H21,CAMP-
COMPND 11 DEPENDENT PROTEIN KINASE REGULATORY SUBUNIT II HIGH AFFINITY-BINDING
COMPND 12 PROTEIN;
COMPND 13 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS CALMODULIN, CALCIUM, AKAP79, AKAP150, AKAP5, AKAP, EF HAND, CA2+,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.GOLD,N.PATEL
REVDAT 2 17-JAN-24 5NIN 1 LINK
REVDAT 1 06-DEC-17 5NIN 0
JRNL AUTH N.PATEL,F.STENGEL,R.AEBERSOLD,M.G.GOLD
JRNL TITL MOLECULAR BASIS OF AKAP79 REGULATION BY CALMODULIN.
JRNL REF NAT COMMUN V. 8 1681 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29162807
JRNL DOI 10.1038/S41467-017-01715-W
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155)
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 42303
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 3860
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 54.0927 - 5.1608 0.95 2578 146 0.2343 0.2326
REMARK 3 2 5.1608 - 4.0967 0.96 2615 145 0.1610 0.1766
REMARK 3 3 4.0967 - 3.5790 0.97 2642 137 0.1386 0.1580
REMARK 3 4 3.5790 - 3.2518 0.97 2682 125 0.1464 0.1859
REMARK 3 5 3.2518 - 3.0187 0.97 2642 136 0.1530 0.1880
REMARK 3 6 3.0187 - 2.8408 0.96 2598 148 0.1572 0.2113
REMARK 3 7 2.8408 - 2.6985 0.97 2659 154 0.1432 0.1826
REMARK 3 8 2.6985 - 2.5810 0.97 2640 136 0.1366 0.1753
REMARK 3 9 2.5810 - 2.4817 0.97 2678 117 0.1373 0.1468
REMARK 3 10 2.4817 - 2.3960 0.96 2586 180 0.1396 0.2078
REMARK 3 11 2.3960 - 2.3211 0.97 2648 147 0.1371 0.1597
REMARK 3 12 2.3211 - 2.2548 0.97 2666 103 0.1334 0.1898
REMARK 3 13 2.2548 - 2.1954 0.97 2636 150 0.1399 0.1617
REMARK 3 14 2.1954 - 2.1419 0.97 2638 128 0.1425 0.1533
REMARK 3 15 2.1419 - 2.0932 0.98 2661 162 0.1464 0.1938
REMARK 3 16 2.0932 - 2.0486 0.98 2675 154 0.1579 0.1866
REMARK 3 17 2.0486 - 2.0076 0.97 2615 148 0.1587 0.1787
REMARK 3 18 2.0076 - 1.9697 0.98 2647 151 0.1630 0.1970
REMARK 3 19 1.9697 - 1.9346 0.98 2703 123 0.1795 0.1995
REMARK 3 20 1.9346 - 1.9018 0.98 2680 130 0.1883 0.2587
REMARK 3 21 1.9018 - 1.8711 0.98 2690 134 0.2054 0.2338
REMARK 3 22 1.8711 - 1.8423 0.98 2691 116 0.1949 0.2425
REMARK 3 23 1.8423 - 1.8152 0.98 2639 151 0.2026 0.2105
REMARK 3 24 1.8152 - 1.7896 0.98 2734 113 0.2180 0.2827
REMARK 3 25 1.7896 - 1.7655 0.98 2715 132 0.2185 0.2299
REMARK 3 26 1.7655 - 1.7425 0.99 2670 124 0.2307 0.2686
REMARK 3 27 1.7425 - 1.7207 0.98 2660 159 0.2255 0.2630
REMARK 3 28 1.7207 - 1.7000 0.98 2659 111 0.2387 0.2585
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.930
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 : 0.009 2465
REMARK 3 ANGLE : 0.904 3319
REMARK 3 CHIRALITY : 0.052 370
REMARK 3 PLANARITY : 0.005 438
REMARK 3 DIHEDRAL : 10.668 1501
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.8674 -26.9563 -27.8416
REMARK 3 T TENSOR
REMARK 3 T11: 0.0529 T22: 0.0659
REMARK 3 T33: 0.0511 T12: 0.0189
REMARK 3 T13: 0.0115 T23: 0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 0.0162 L22: 0.0607
REMARK 3 L33: 0.0069 L12: -0.0135
REMARK 3 L13: -0.0004 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: -0.0740 S13: -0.0168
REMARK 3 S21: -0.0394 S22: -0.0096 S23: 0.0544
REMARK 3 S31: 0.0099 S32: -0.0019 S33: -0.0009
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 20 THROUGH 25 )
REMARK 3 ORIGIN FOR THE GROUP (A): 1.1044 -21.5112 -41.0999
REMARK 3 T TENSOR
REMARK 3 T11: 0.1144 T22: 0.0720
REMARK 3 T33: 0.0737 T12: 0.0153
REMARK 3 T13: -0.0010 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.0182 L22: 0.0014
REMARK 3 L33: 0.0042 L12: -0.0026
REMARK 3 L13: -0.0029 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: 0.0131 S13: 0.0057
REMARK 3 S21: -0.0094 S22: 0.0035 S23: -0.0010
REMARK 3 S31: -0.0123 S32: 0.0014 S33: -0.0001
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 26 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 2.5112 -14.5323 -27.5451
REMARK 3 T TENSOR
REMARK 3 T11: 0.0306 T22: 0.0263
REMARK 3 T33: 0.0564 T12: -0.0053
REMARK 3 T13: 0.0138 T23: -0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.0143 L22: 0.0522
REMARK 3 L33: 0.0199 L12: -0.0148
REMARK 3 L13: -0.0060 L23: 0.0122
REMARK 3 S TENSOR
REMARK 3 S11: 0.0445 S12: 0.0051 S13: 0.0160
REMARK 3 S21: 0.0194 S22: -0.0064 S23: -0.0188
REMARK 3 S31: -0.0780 S32: -0.0095 S33: 0.0017
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 45 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.0588 -7.4539 -28.2829
REMARK 3 T TENSOR
REMARK 3 T11: 0.2004 T22: -0.0233
REMARK 3 T33: 0.1264 T12: -0.1083
REMARK 3 T13: -0.0160 T23: -0.0294
REMARK 3 L TENSOR
REMARK 3 L11: 0.0031 L22: 0.0060
REMARK 3 L33: 0.0113 L12: 0.0081
REMARK 3 L13: -0.0055 L23: -0.0046
REMARK 3 S TENSOR
REMARK 3 S11: -0.0107 S12: -0.0264 S13: -0.0011
REMARK 3 S21: -0.1050 S22: 0.0601 S23: -0.0192
REMARK 3 S31: -0.0089 S32: 0.0090 S33: 0.0163
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 62 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2748 -18.5870 -28.3505
REMARK 3 T TENSOR
REMARK 3 T11: 0.0805 T22: 0.0635
REMARK 3 T33: 0.0718 T12: -0.0014
REMARK 3 T13: 0.0086 T23: -0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 0.0184 L22: 0.0050
REMARK 3 L33: 0.0049 L12: -0.0070
REMARK 3 L13: -0.0020 L23: 0.0043
REMARK 3 S TENSOR
REMARK 3 S11: -0.0068 S12: -0.0912 S13: 0.0518
REMARK 3 S21: 0.0011 S22: 0.0159 S23: 0.0136
REMARK 3 S31: -0.1050 S32: 0.0232 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1828 -17.0062 -11.6369
REMARK 3 T TENSOR
REMARK 3 T11: 0.0390 T22: 0.0498
REMARK 3 T33: 0.0414 T12: 0.0042
REMARK 3 T13: -0.0022 T23: -0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 0.0079 L22: 0.0141
REMARK 3 L33: 0.0407 L12: 0.0032
REMARK 3 L13: -0.0086 L23: -0.0114
REMARK 3 S TENSOR
REMARK 3 S11: -0.0293 S12: -0.0214 S13: 0.0118
REMARK 3 S21: 0.0358 S22: 0.0143 S23: -0.0117
REMARK 3 S31: -0.1320 S32: 0.0380 S33: -0.0046
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2255 -26.4649 -21.2529
REMARK 3 T TENSOR
REMARK 3 T11: 0.0423 T22: 0.0504
REMARK 3 T33: 0.0353 T12: -0.0153
REMARK 3 T13: 0.0086 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 0.0020 L22: 0.0045
REMARK 3 L33: 0.0109 L12: -0.0001
REMARK 3 L13: 0.0017 L23: -0.0103
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.0043 S13: 0.0079
REMARK 3 S21: -0.0119 S22: -0.0073 S23: -0.0151
REMARK 3 S31: 0.0393 S32: -0.0411 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 118 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6879 -32.9721 -12.7818
REMARK 3 T TENSOR
REMARK 3 T11: -0.0129 T22: -0.0893
REMARK 3 T33: -0.1327 T12: -0.1758
REMARK 3 T13: -0.1277 T23: -0.1970
REMARK 3 L TENSOR
REMARK 3 L11: 0.0361 L22: 0.0409
REMARK 3 L33: 0.0291 L12: 0.0342
REMARK 3 L13: 0.0167 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0199 S12: 0.0017 S13: -0.0339
REMARK 3 S21: -0.0202 S22: -0.0806 S23: 0.0656
REMARK 3 S31: 0.0590 S32: -0.0318 S33: -0.0389
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5762 -25.2121 -5.2899
REMARK 3 T TENSOR
REMARK 3 T11: 0.0336 T22: 0.0819
REMARK 3 T33: 0.0149 T12: -0.0052
REMARK 3 T13: -0.0041 T23: 0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.1659 L22: 0.1339
REMARK 3 L33: 0.0165 L12: -0.0209
REMARK 3 L13: -0.0343 L23: -0.0127
REMARK 3 S TENSOR
REMARK 3 S11: 0.0557 S12: -0.0234 S13: -0.0183
REMARK 3 S21: -0.0303 S22: 0.0367 S23: 0.0302
REMARK 3 S31: 0.0758 S32: -0.0261 S33: 0.0276
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 19 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9528 -31.5816 -38.1399
REMARK 3 T TENSOR
REMARK 3 T11: 0.0062 T22: -0.0339
REMARK 3 T33: -0.0379 T12: 0.0811
REMARK 3 T13: 0.0830 T23: -0.0800
REMARK 3 L TENSOR
REMARK 3 L11: 0.0348 L22: 0.0311
REMARK 3 L33: 0.0317 L12: 0.0039
REMARK 3 L13: -0.0091 L23: 0.0100
REMARK 3 S TENSOR
REMARK 3 S11: -0.0521 S12: -0.0344 S13: -0.0772
REMARK 3 S21: -0.0211 S22: -0.0387 S23: 0.0083
REMARK 3 S31: -0.0062 S32: -0.0153 S33: -0.0528
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 20 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0075 -35.8160 -34.8701
REMARK 3 T TENSOR
REMARK 3 T11: 0.0218 T22: 0.0341
REMARK 3 T33: 0.0551 T12: 0.0244
REMARK 3 T13: 0.0083 T23: -0.0097
REMARK 3 L TENSOR
REMARK 3 L11: 0.0242 L22: 0.0509
REMARK 3 L33: 0.0671 L12: 0.0157
REMARK 3 L13: 0.0347 L23: 0.0555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0398 S12: -0.0414 S13: -0.0147
REMARK 3 S21: 0.0265 S22: 0.1079 S23: -0.0692
REMARK 3 S31: -0.0375 S32: 0.0458 S33: 0.0398
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 45 THROUGH 61 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.1052 -28.3397 -34.9807
REMARK 3 T TENSOR
REMARK 3 T11: 0.0411 T22: 0.0592
REMARK 3 T33: 0.0986 T12: -0.0120
REMARK 3 T13: 0.0060 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 0.0493 L22: 0.0214
REMARK 3 L33: 0.0157 L12: 0.0317
REMARK 3 L13: 0.0028 L23: -0.0076
REMARK 3 S TENSOR
REMARK 3 S11: 0.1778 S12: 0.0310 S13: 0.0156
REMARK 3 S21: -0.0222 S22: 0.0202 S23: 0.0110
REMARK 3 S31: -0.0248 S32: 0.0475 S33: 0.0181
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 62 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.1764 -25.2711 -37.5392
REMARK 3 T TENSOR
REMARK 3 T11: 0.0607 T22: 0.0561
REMARK 3 T33: 0.0573 T12: -0.0091
REMARK 3 T13: 0.0188 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 0.0091 L22: 0.0130
REMARK 3 L33: 0.0032 L12: 0.0136
REMARK 3 L13: 0.0073 L23: -0.0012
REMARK 3 S TENSOR
REMARK 3 S11: -0.0228 S12: 0.0852 S13: 0.0398
REMARK 3 S21: -0.1019 S22: 0.0202 S23: -0.0548
REMARK 3 S31: -0.0173 S32: 0.0407 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7435 -33.6442 -52.8623
REMARK 3 T TENSOR
REMARK 3 T11: 0.0593 T22: 0.0535
REMARK 3 T33: 0.0437 T12: -0.0143
REMARK 3 T13: 0.0008 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.0012 L22: 0.0051
REMARK 3 L33: 0.0076 L12: 0.0012
REMARK 3 L13: -0.0004 L23: 0.0070
REMARK 3 S TENSOR
REMARK 3 S11: 0.0241 S12: -0.0128 S13: 0.0116
REMARK 3 S21: -0.0643 S22: 0.0225 S23: -0.0259
REMARK 3 S31: -0.0103 S32: 0.1208 S33: 0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 101 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.1084 -47.4618 -53.2197
REMARK 3 T TENSOR
REMARK 3 T11: 0.0820 T22: 0.0508
REMARK 3 T33: 0.0642 T12: 0.0202
REMARK 3 T13: -0.0100 T23: 0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 0.0014 L22: 0.0044
REMARK 3 L33: 0.0007 L12: -0.0008
REMARK 3 L13: -0.0001 L23: -0.0009
REMARK 3 S TENSOR
REMARK 3 S11: 0.0730 S12: 0.0099 S13: -0.0014
REMARK 3 S21: -0.0118 S22: 0.0172 S23: -0.0459
REMARK 3 S31: 0.0272 S32: 0.0379 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 102 THROUGH 117 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6815 -46.1606 -44.2871
REMARK 3 T TENSOR
REMARK 3 T11: 0.0726 T22: 0.0781
REMARK 3 T33: 0.0880 T12: -0.0198
REMARK 3 T13: -0.0064 T23: 0.0107
REMARK 3 L TENSOR
REMARK 3 L11: 0.0004 L22: 0.0006
REMARK 3 L33: 0.0093 L12: 0.0006
REMARK 3 L13: 0.0041 L23: 0.0016
REMARK 3 S TENSOR
REMARK 3 S11: 0.0787 S12: -0.0986 S13: -0.0319
REMARK 3 S21: 0.0344 S22: -0.0590 S23: 0.0372
REMARK 3 S31: 0.0948 S32: -0.0337 S33: -0.0000
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 118 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1860 -48.5065 -53.0537
REMARK 3 T TENSOR
REMARK 3 T11: 0.0801 T22: 0.0856
REMARK 3 T33: 0.0622 T12: -0.0258
REMARK 3 T13: -0.0104 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 0.0048 L22: 0.0041
REMARK 3 L33: 0.0045 L12: 0.0023
REMARK 3 L13: -0.0054 L23: -0.0048
REMARK 3 S TENSOR
REMARK 3 S11: 0.0165 S12: -0.0856 S13: -0.0496
REMARK 3 S21: -0.0142 S22: -0.0082 S23: 0.0334
REMARK 3 S31: 0.0337 S32: -0.0822 S33: -0.0023
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5895 -41.6861 -60.2842
REMARK 3 T TENSOR
REMARK 3 T11: 0.0760 T22: -0.0131
REMARK 3 T33: -0.0957 T12: 0.0010
REMARK 3 T13: -0.0524 T23: -0.0761
REMARK 3 L TENSOR
REMARK 3 L11: 0.1449 L22: 0.0215
REMARK 3 L33: 0.1522 L12: -0.0310
REMARK 3 L13: -0.0584 L23: 0.0495
REMARK 3 S TENSOR
REMARK 3 S11: 0.1650 S12: -0.0298 S13: -0.0726
REMARK 3 S21: -0.0539 S22: 0.1263 S23: -0.0065
REMARK 3 S31: 0.1621 S32: -0.0607 S33: 0.1968
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 78 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1349 -34.2167 -50.0995
REMARK 3 T TENSOR
REMARK 3 T11: 0.0604 T22: 0.0613
REMARK 3 T33: 0.0594 T12: 0.0001
REMARK 3 T13: 0.0111 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.0305 L22: 0.0293
REMARK 3 L33: 0.0453 L12: 0.0040
REMARK 3 L13: -0.0079 L23: 0.0021
REMARK 3 S TENSOR
REMARK 3 S11: -0.0495 S12: 0.0562 S13: 0.0136
REMARK 3 S21: 0.0046 S22: -0.0991 S23: 0.0483
REMARK 3 S31: -0.0385 S32: -0.0338 S33: -0.0138
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 88 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2638 -28.4329 -15.8878
REMARK 3 T TENSOR
REMARK 3 T11: 0.0518 T22: 0.0064
REMARK 3 T33: 0.0810 T12: -0.0174
REMARK 3 T13: 0.0297 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 0.1111 L22: 0.0058
REMARK 3 L33: 0.0864 L12: -0.0031
REMARK 3 L13: 0.0130 L23: -0.0181
REMARK 3 S TENSOR
REMARK 3 S11: -0.0631 S12: 0.0305 S13: -0.0285
REMARK 3 S21: 0.0072 S22: -0.0698 S23: -0.0890
REMARK 3 S31: 0.0286 S32: -0.0186 S33: -0.0091
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 5NIN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004194.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9685
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42359
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 65.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 7.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 1IWQ (85-148)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.4 M AMMONIUM SULPHATE, 50 MM CITRATE
REMARK 280 PH 5.4, 0.3 M NDSB-195, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 287K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 38.23000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 38.23000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 64.49500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 38.23000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 38.23000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 64.49500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 38.23000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.23000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 64.49500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 38.23000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.23000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 64.49500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 56
REMARK 465 ALA B 57
REMARK 465 ASP B 58
REMARK 465 GLY B 59
REMARK 465 ASN B 60
REMARK 465 LYS B 148
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 ASP A 56
REMARK 465 ALA A 57
REMARK 465 ASP A 58
REMARK 465 GLY A 59
REMARK 465 LYS A 148
REMARK 465 GLY C 77
REMARK 465 ARG C 89
REMARK 465 LYS C 90
REMARK 465 ARG C 91
REMARK 465 SER C 92
REMARK 465 GLY D 77
REMARK 465 ARG D 89
REMARK 465 LYS D 90
REMARK 465 ARG D 91
REMARK 465 SER D 92
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 ASP B 2 CG OD1 OD2
REMARK 470 ARG B 74 NE CZ NH1 NH2
REMARK 470 LYS B 94 CD CE NZ
REMARK 470 ASP A 2 CG OD1 OD2
REMARK 470 ASN A 60 CG OD1 ND2
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 ARG C 88 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 88 CG CD NE CZ NH1 NH2
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 HE21 GLN A 135 O HOH A 303 1.52
REMARK 500 O HOH A 433 O HOH A 496 1.72
REMARK 500 O HOH B 437 O HOH B 486 1.97
REMARK 500 O HOH B 481 O HOH B 540 2.01
REMARK 500 O HOH C 108 O HOH C 115 2.02
REMARK 500 O HOH D 206 O HOH D 219 2.03
REMARK 500 O HOH A 458 O HOH A 492 2.06
REMARK 500 O HOH B 439 O HOH B 484 2.07
REMARK 500 O HOH A 442 O HOH A 481 2.08
REMARK 500 O HOH B 310 O HOH B 477 2.11
REMARK 500 OD2 ASP B 64 O HOH B 301 2.16
REMARK 500 O HOH B 339 O HOH B 506 2.18
REMARK 500 O HOH A 364 O HOH A 473 2.19
REMARK 500 O HOH B 435 O HOH B 477 2.19
REMARK 500 NH2 ARG A 86 O HOH A 301 2.19
REMARK 500 O HOH B 520 O HOH B 542 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 302 O HOH A 429 5554 1.83
REMARK 500 O HOH B 502 O HOH A 470 5554 1.99
REMARK 500 O HOH B 423 O HOH A 439 6444 2.11
REMARK 500 O HOH B 363 O HOH A 407 6444 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 543 DISTANCE = 5.88 ANGSTROMS
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 B 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 81.8
REMARK 620 3 ASN B 97 OD1 86.6 77.7
REMARK 620 4 TYR B 99 O 85.2 155.4 80.6
REMARK 620 5 GLU B 104 OE1 104.0 126.3 154.4 77.2
REMARK 620 6 GLU B 104 OE2 102.0 74.5 149.3 128.9 51.9
REMARK 620 7 HOH B 450 O 165.7 85.6 84.1 103.8 89.0 81.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 131 OD1 78.4
REMARK 620 3 ASP B 133 OD1 84.7 79.8
REMARK 620 4 GLN B 135 O 89.7 156.1 78.5
REMARK 620 5 GLU B 140 OE1 111.1 124.8 152.2 78.9
REMARK 620 6 GLU B 140 OE2 86.9 75.6 155.2 124.9 52.0
REMARK 620 7 HOH B 360 O 160.6 86.8 80.3 99.3 87.6 101.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 85.1
REMARK 620 3 ASN A 97 OD1 89.3 76.6
REMARK 620 4 TYR A 99 O 84.2 155.6 81.3
REMARK 620 5 GLU A 104 OE1 101.2 125.1 156.2 78.6
REMARK 620 6 GLU A 104 OE2 97.9 73.8 148.8 129.5 51.3
REMARK 620 7 HOH A 354 O 166.2 81.5 84.6 106.9 89.1 81.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 78.3
REMARK 620 3 ASP A 133 OD1 83.5 77.5
REMARK 620 4 GLN A 135 O 87.0 151.8 77.0
REMARK 620 5 GLU A 140 OE1 111.9 127.1 152.2 80.7
REMARK 620 6 GLU A 140 OE2 91.6 76.0 153.5 128.9 52.8
REMARK 620 7 HOH A 347 O 159.8 86.2 80.6 101.3 87.8 97.1
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 B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 102
DBREF 5NIN B 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 5NIN A 0 148 UNP P62158 CALM_HUMAN 1 149
DBREF 5NIN C 77 92 UNP P24588 AKAP5_HUMAN 77 92
DBREF 5NIN D 77 92 UNP P24588 AKAP5_HUMAN 77 92
SEQRES 1 B 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 GLN MET MET THR ALA LYS
SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MET MET THR ALA LYS
SEQRES 1 C 16 GLY ALA TRP ALA SER LEU LYS ARG LEU VAL THR ARG ARG
SEQRES 2 C 16 LYS ARG SER
SEQRES 1 D 16 GLY ALA TRP ALA SER LEU LYS ARG LEU VAL THR ARG ARG
SEQRES 2 D 16 LYS ARG SER
HET CA B 201 1
HET CA B 202 1
HET SO4 B 203 5
HET SO4 B 204 5
HET SO4 B 205 5
HET CA A 201 1
HET CA A 202 1
HET SO4 D 101 5
HET SO4 D 102 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 5 CA 4(CA 2+)
FORMUL 7 SO4 5(O4 S 2-)
FORMUL 14 HOH *499(H2 O)
HELIX 1 AA1 THR B 5 LEU B 18 1 14
HELIX 2 AA2 GLU B 31 LEU B 39 1 9
HELIX 3 AA3 THR B 44 GLU B 54 1 11
HELIX 4 AA4 PHE B 65 THR B 79 1 15
HELIX 5 AA5 ASP B 80 ASP B 93 1 14
HELIX 6 AA6 SER B 101 GLY B 113 1 13
HELIX 7 AA7 THR B 117 ASP B 129 1 13
HELIX 8 AA8 TYR B 138 ALA B 147 1 10
HELIX 9 AA9 THR A 5 LEU A 18 1 14
HELIX 10 AB1 THR A 29 LEU A 39 1 11
HELIX 11 AB2 THR A 44 VAL A 55 1 12
HELIX 12 AB3 PHE A 65 THR A 79 1 15
HELIX 13 AB4 ASP A 80 ASP A 93 1 14
HELIX 14 AB5 SER A 101 LEU A 112 1 12
HELIX 15 AB6 THR A 117 ASP A 129 1 13
HELIX 16 AB7 TYR A 138 THR A 146 1 9
HELIX 17 AB8 TRP C 79 ARG C 84 1 6
HELIX 18 AB9 TRP D 79 ARG D 84 1 6
SHEET 1 AA1 2 THR B 26 THR B 28 0
SHEET 2 AA1 2 THR B 62 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 AA2 2 TYR B 99 ILE B 100 0
SHEET 2 AA2 2 VAL B 136 ASN B 137 -1 O VAL B 136 N ILE B 100
SHEET 1 AA3 2 THR A 26 THR A 28 0
SHEET 2 AA3 2 THR A 62 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 AA4 2 TYR A 99 ILE A 100 0
SHEET 2 AA4 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP B 93 CA CA B 201 1555 1555 2.30
LINK OD1 ASP B 95 CA CA B 201 1555 1555 2.39
LINK OD1 ASN B 97 CA CA B 201 1555 1555 2.47
LINK O TYR B 99 CA CA B 201 1555 1555 2.25
LINK OE1 GLU B 104 CA CA B 201 1555 1555 2.46
LINK OE2 GLU B 104 CA CA B 201 1555 1555 2.55
LINK OD1 ASP B 129 CA CA B 202 1555 1555 2.23
LINK OD1 ASP B 131 CA CA B 202 1555 1555 2.32
LINK OD1 ASP B 133 CA CA B 202 1555 1555 2.36
LINK O GLN B 135 CA CA B 202 1555 1555 2.34
LINK OE1 GLU B 140 CA CA B 202 1555 1555 2.42
LINK OE2 GLU B 140 CA CA B 202 1555 1555 2.55
LINK CA CA B 201 O HOH B 450 1555 1555 2.34
LINK CA CA B 202 O HOH B 360 1555 1555 2.39
LINK OD1 ASP A 93 CA CA A 201 1555 1555 2.31
LINK OD1 ASP A 95 CA CA A 201 1555 1555 2.37
LINK OD1 ASN A 97 CA CA A 201 1555 1555 2.40
LINK O TYR A 99 CA CA A 201 1555 1555 2.24
LINK OE1 GLU A 104 CA CA A 201 1555 1555 2.47
LINK OE2 GLU A 104 CA CA A 201 1555 1555 2.58
LINK OD1 ASP A 129 CA CA A 202 1555 1555 2.21
LINK OD1 ASP A 131 CA CA A 202 1555 1555 2.34
LINK OD1 ASP A 133 CA CA A 202 1555 1555 2.35
LINK O GLN A 135 CA CA A 202 1555 1555 2.33
LINK OE1 GLU A 140 CA CA A 202 1555 1555 2.41
LINK OE2 GLU A 140 CA CA A 202 1555 1555 2.53
LINK CA CA A 201 O HOH A 354 1555 1555 2.40
LINK CA CA A 202 O HOH A 347 1555 1555 2.21
SITE 1 AC1 6 ASP B 93 ASP B 95 ASN B 97 TYR B 99
SITE 2 AC1 6 GLU B 104 HOH B 450
SITE 1 AC2 6 ASP B 129 ASP B 131 ASP B 133 GLN B 135
SITE 2 AC2 6 GLU B 140 HOH B 360
SITE 1 AC3 3 ARG B 106 HOH B 310 HOH B 435
SITE 1 AC4 6 ARG A 74 HIS B 107 ASN B 111 HOH B 396
SITE 2 AC4 6 HOH B 440 HOH B 468
SITE 1 AC5 5 ASN B 42 ARG B 90 HOH B 387 HOH B 423
SITE 2 AC5 5 HOH B 426
SITE 1 AC6 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC6 6 GLU A 104 HOH A 354
SITE 1 AC7 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC7 6 GLU A 140 HOH A 347
SITE 1 AC8 6 ALA D 78 TRP D 79 ALA D 80 LYS D 83
SITE 2 AC8 6 HOH D 202 HOH D 208
SITE 1 AC9 5 THR D 87 ARG D 88 HOH D 203 HOH D 205
SITE 2 AC9 5 HOH D 207
CRYST1 76.460 76.460 128.990 90.00 90.00 90.00 P 42 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013079 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013079 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007753 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
