HEADER PROTEIN BINDING 28-JUL-15 5CX3
TITLE CRYSTAL STRUCTURE OF FYCO1 LIR IN COMPLEX WITH LC3A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROTUBULE-ASSOCIATED PROTEINS 1A/1B LIGHT CHAIN 3A;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: AUTOPHAGY-RELATED PROTEIN LC3 A,AUTOPHAGY-RELATED UBIQUITIN-
COMPND 5 LIKE MODIFIER LC3 A,MAP1 LIGHT CHAIN 3-LIKE PROTEIN 1,MAP1A/MAP1B
COMPND 6 LIGHT CHAIN 3 A,MAP1A/MAP1B LC3 A,MICROTUBULE-ASSOCIATED PROTEIN 1
COMPND 7 LIGHT CHAIN 3 ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: FYVE AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1;
COMPND 11 CHAIN: E, F, G, H;
COMPND 12 SYNONYM: ZINC FINGER FYVE DOMAIN-CONTAINING PROTEIN 7;
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: MAP1LC3A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: FYCO1, ZFYVE7;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS AUTOPHAGY ADAPTOR, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR X.CHENG,L.PAN
REVDAT 5 06-MAR-24 5CX3 1 REMARK
REVDAT 4 08-JAN-20 5CX3 1 REMARK
REVDAT 3 17-AUG-16 5CX3 1 JRNL
REVDAT 2 10-AUG-16 5CX3 1 AUTHOR JRNL
REVDAT 1 03-AUG-16 5CX3 0
JRNL AUTH X.CHENG,Y.WANG,Y.GONG,F.LI,Y.GUO,S.HU,J.LIU,L.PAN
JRNL TITL STRUCTURAL BASIS OF FYCO1 AND MAP1LC3A INTERACTION REVEALS A
JRNL TITL 2 NOVEL BINDING MODE FOR ATG8-FAMILY PROTEINS.
JRNL REF AUTOPHAGY V. 12 1330 2016
JRNL REFN ESSN 1554-8635
JRNL PMID 27246247
JRNL DOI 10.1080/15548627.2016.1185590
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.2_1309
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.62
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 24033
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1235
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 34.6186 - 4.7805 0.99 2728 143 0.1520 0.1914
REMARK 3 2 4.7805 - 3.7960 0.99 2679 142 0.1351 0.1833
REMARK 3 3 3.7960 - 3.3166 1.00 2688 148 0.1688 0.2367
REMARK 3 4 3.3166 - 3.0135 0.99 2676 149 0.1967 0.3004
REMARK 3 5 3.0135 - 2.7976 0.99 2676 144 0.2066 0.2997
REMARK 3 6 2.7976 - 2.6328 0.99 2649 153 0.2248 0.3223
REMARK 3 7 2.6328 - 2.5010 0.98 2623 151 0.2147 0.2720
REMARK 3 8 2.5010 - 2.3921 0.87 2338 110 0.2308 0.3096
REMARK 3 9 2.3921 - 2.3000 0.64 1741 95 0.2252 0.3257
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.020
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 4703
REMARK 3 ANGLE : 1.161 6353
REMARK 3 CHIRALITY : 0.053 698
REMARK 3 PLANARITY : 0.006 841
REMARK 3 DIHEDRAL : 16.347 1841
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 26
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6115 -30.1926 62.5532
REMARK 3 T TENSOR
REMARK 3 T11: 0.3953 T22: 0.4293
REMARK 3 T33: 0.2325 T12: 0.0423
REMARK 3 T13: -0.0040 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 5.3278 L22: 4.3070
REMARK 3 L33: 5.6709 L12: 4.5936
REMARK 3 L13: -4.2716 L23: -2.7563
REMARK 3 S TENSOR
REMARK 3 S11: -0.3012 S12: 0.0696 S13: 0.0572
REMARK 3 S21: -0.3282 S22: 0.1437 S23: -0.0410
REMARK 3 S31: 0.5315 S32: 0.6591 S33: 0.1734
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3536 -23.0950 78.0553
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: 0.2307
REMARK 3 T33: 0.1704 T12: 0.0268
REMARK 3 T13: 0.0319 T23: 0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 5.6202 L22: 3.9899
REMARK 3 L33: 3.1744 L12: 1.0069
REMARK 3 L13: 1.2808 L23: 1.1711
REMARK 3 S TENSOR
REMARK 3 S11: 0.0775 S12: 0.0139 S13: 0.0159
REMARK 3 S21: 0.3019 S22: -0.0109 S23: -0.0844
REMARK 3 S31: -0.1563 S32: 0.0356 S33: -0.0798
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.9632 -29.0221 50.6025
REMARK 3 T TENSOR
REMARK 3 T11: 0.4101 T22: 0.5016
REMARK 3 T33: 0.3053 T12: 0.0315
REMARK 3 T13: 0.0277 T23: 0.0804
REMARK 3 L TENSOR
REMARK 3 L11: 5.3337 L22: 3.2663
REMARK 3 L33: 8.9745 L12: -4.0608
REMARK 3 L13: -5.6141 L23: 3.4185
REMARK 3 S TENSOR
REMARK 3 S11: -0.4508 S12: 0.1789 S13: -0.2798
REMARK 3 S21: 0.1892 S22: 0.1976 S23: 0.1691
REMARK 3 S31: 0.6101 S32: -0.2219 S33: 0.2225
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 27 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.5940 -23.2648 35.5804
REMARK 3 T TENSOR
REMARK 3 T11: 0.2503 T22: 0.3685
REMARK 3 T33: 0.2223 T12: -0.0448
REMARK 3 T13: -0.0218 T23: -0.0363
REMARK 3 L TENSOR
REMARK 3 L11: 2.4448 L22: 3.8457
REMARK 3 L33: 3.6246 L12: -2.0825
REMARK 3 L13: -0.0370 L23: -0.3836
REMARK 3 S TENSOR
REMARK 3 S11: 0.0808 S12: 0.1254 S13: -0.3478
REMARK 3 S21: -0.3105 S22: -0.0762 S23: 0.1933
REMARK 3 S31: 0.0980 S32: -0.1584 S33: -0.0717
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 71 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.1089 -14.9971 33.0781
REMARK 3 T TENSOR
REMARK 3 T11: 0.2792 T22: 0.4319
REMARK 3 T33: 0.3237 T12: 0.0180
REMARK 3 T13: -0.0789 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 2.4471 L22: 7.6753
REMARK 3 L33: 5.4829 L12: 4.0569
REMARK 3 L13: 0.8895 L23: 3.2065
REMARK 3 S TENSOR
REMARK 3 S11: -0.1546 S12: 0.2647 S13: -0.1668
REMARK 3 S21: -0.4555 S22: 0.0231 S23: 0.8258
REMARK 3 S31: -0.3915 S32: -0.4946 S33: 0.0458
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 95 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8681 -16.0671 41.6181
REMARK 3 T TENSOR
REMARK 3 T11: 0.2492 T22: 0.3213
REMARK 3 T33: 0.1780 T12: -0.0179
REMARK 3 T13: 0.0402 T23: -0.1106
REMARK 3 L TENSOR
REMARK 3 L11: 4.7939 L22: 6.4714
REMARK 3 L33: 4.6008 L12: -1.3670
REMARK 3 L13: -0.9761 L23: -1.4393
REMARK 3 S TENSOR
REMARK 3 S11: -0.0742 S12: -0.3952 S13: 0.0760
REMARK 3 S21: -0.0122 S22: 0.1233 S23: -0.1393
REMARK 3 S31: -0.4980 S32: 0.3218 S33: 0.0083
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.0762 11.3615 69.7107
REMARK 3 T TENSOR
REMARK 3 T11: 0.3297 T22: 0.3346
REMARK 3 T33: 0.4364 T12: 0.0110
REMARK 3 T13: 0.0700 T23: -0.0318
REMARK 3 L TENSOR
REMARK 3 L11: 1.2665 L22: 6.3575
REMARK 3 L33: 4.1466 L12: 1.1708
REMARK 3 L13: 1.3617 L23: -1.8738
REMARK 3 S TENSOR
REMARK 3 S11: 0.5199 S12: -0.0643 S13: 0.0919
REMARK 3 S21: -0.2143 S22: -0.1670 S23: 0.4861
REMARK 3 S31: 0.1925 S32: -0.3508 S33: -0.3541
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 27 THROUGH 71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8878 4.3742 82.5066
REMARK 3 T TENSOR
REMARK 3 T11: 0.4654 T22: 0.2344
REMARK 3 T33: 0.5576 T12: 0.0043
REMARK 3 T13: 0.0059 T23: 0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 1.7272 L22: 8.5850
REMARK 3 L33: 7.3132 L12: 0.8895
REMARK 3 L13: -1.2304 L23: -0.2985
REMARK 3 S TENSOR
REMARK 3 S11: 0.0572 S12: -0.0464 S13: -0.0166
REMARK 3 S21: 1.1103 S22: -0.1798 S23: 0.1866
REMARK 3 S31: -0.1863 S32: -0.0784 S33: 0.1146
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 72 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.4303 -4.2124 84.4869
REMARK 3 T TENSOR
REMARK 3 T11: 0.6386 T22: 0.2630
REMARK 3 T33: 0.4393 T12: -0.0361
REMARK 3 T13: 0.1818 T23: 0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 3.0434 L22: 2.0666
REMARK 3 L33: 5.9803 L12: -0.5935
REMARK 3 L13: -2.2643 L23: 2.5017
REMARK 3 S TENSOR
REMARK 3 S11: -0.1235 S12: -0.0589 S13: 0.3573
REMARK 3 S21: 0.6291 S22: 0.0035 S23: 0.3642
REMARK 3 S31: 0.3813 S32: 0.4091 S33: 0.0349
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 95 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0810 -2.2691 76.0038
REMARK 3 T TENSOR
REMARK 3 T11: 0.4132 T22: 0.2559
REMARK 3 T33: 0.4653 T12: -0.0045
REMARK 3 T13: 0.0903 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 2.7913 L22: 4.2042
REMARK 3 L33: 5.2676 L12: 1.4031
REMARK 3 L13: 0.0238 L23: -4.3274
REMARK 3 S TENSOR
REMARK 3 S11: -0.1297 S12: 0.2086 S13: 0.0863
REMARK 3 S21: 0.0644 S22: -0.0173 S23: -0.1006
REMARK 3 S31: 0.1730 S32: 0.2411 S33: 0.0188
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 5 THROUGH 12 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.1669 10.7273 48.5470
REMARK 3 T TENSOR
REMARK 3 T11: 0.4761 T22: 0.5579
REMARK 3 T33: 0.7571 T12: 0.0356
REMARK 3 T13: 0.2066 T23: -0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 4.1413 L22: 9.4994
REMARK 3 L33: 5.0907 L12: -6.2307
REMARK 3 L13: -4.5733 L23: 6.9492
REMARK 3 S TENSOR
REMARK 3 S11: 0.1086 S12: -0.3060 S13: 0.9709
REMARK 3 S21: -0.9247 S22: 0.4104 S23: -2.2625
REMARK 3 S31: -0.2613 S32: 1.1670 S33: -0.5161
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 13 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.2127 13.5704 55.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.4923 T22: 0.5013
REMARK 3 T33: 0.3621 T12: 0.0720
REMARK 3 T13: 0.0075 T23: -0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 3.9954 L22: 7.9278
REMARK 3 L33: 8.5652 L12: 3.9952
REMARK 3 L13: 4.1215 L23: 0.9948
REMARK 3 S TENSOR
REMARK 3 S11: -0.6270 S12: -1.3018 S13: 0.6344
REMARK 3 S21: -0.1206 S22: -0.1651 S23: 0.0175
REMARK 3 S31: -0.5067 S32: -0.1741 S33: 0.7196
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 27 THROUGH 59 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7138 8.8418 40.3135
REMARK 3 T TENSOR
REMARK 3 T11: 0.6958 T22: 0.3284
REMARK 3 T33: 0.4169 T12: 0.0741
REMARK 3 T13: 0.0113 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 2.4715 L22: 7.4688
REMARK 3 L33: 7.3952 L12: -1.6549
REMARK 3 L13: -2.6688 L23: 3.5944
REMARK 3 S TENSOR
REMARK 3 S11: 0.3684 S12: 0.3201 S13: 0.1771
REMARK 3 S21: -1.3503 S22: -0.0435 S23: -0.2616
REMARK 3 S31: -1.3809 S32: -0.4029 S33: -0.2402
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 60 THROUGH 70 )
REMARK 3 ORIGIN FOR THE GROUP (A): 20.6877 7.6193 33.6048
REMARK 3 T TENSOR
REMARK 3 T11: 1.2300 T22: 0.5314
REMARK 3 T33: 0.5963 T12: 0.4278
REMARK 3 T13: -0.1231 T23: -0.1139
REMARK 3 L TENSOR
REMARK 3 L11: 3.6076 L22: 5.4503
REMARK 3 L33: 6.3171 L12: 3.7421
REMARK 3 L13: -2.2210 L23: 0.3491
REMARK 3 S TENSOR
REMARK 3 S11: 0.6867 S12: 0.4776 S13: 0.3526
REMARK 3 S21: -2.0415 S22: -0.6642 S23: 1.0198
REMARK 3 S31: -0.1081 S32: -0.6475 S33: -0.1190
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 71 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 25.6458 0.6154 34.6930
REMARK 3 T TENSOR
REMARK 3 T11: 0.7005 T22: 0.3745
REMARK 3 T33: 0.4386 T12: 0.2152
REMARK 3 T13: 0.0310 T23: -0.0855
REMARK 3 L TENSOR
REMARK 3 L11: 2.9435 L22: 2.3537
REMARK 3 L33: 8.4757 L12: 0.4966
REMARK 3 L13: -0.5600 L23: -2.4547
REMARK 3 S TENSOR
REMARK 3 S11: 0.3035 S12: 0.2997 S13: 0.1640
REMARK 3 S21: -0.5306 S22: -0.3625 S23: -0.0058
REMARK 3 S31: -0.2214 S32: -0.5365 S33: 0.3269
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 95 THROUGH 102 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4024 0.0702 49.1503
REMARK 3 T TENSOR
REMARK 3 T11: 0.5850 T22: 0.6423
REMARK 3 T33: 0.5314 T12: 0.0853
REMARK 3 T13: 0.1892 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 3.8655 L22: 9.4635
REMARK 3 L33: 4.6902 L12: 3.4242
REMARK 3 L13: 4.1153 L23: 5.0403
REMARK 3 S TENSOR
REMARK 3 S11: 0.1915 S12: -0.8686 S13: -0.9128
REMARK 3 S21: 0.3940 S22: -1.1609 S23: 0.9812
REMARK 3 S31: 0.8292 S32: -1.5007 S33: 1.0824
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 103 THROUGH 121 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5439 0.5570 40.7541
REMARK 3 T TENSOR
REMARK 3 T11: 0.5009 T22: 0.2794
REMARK 3 T33: 0.3359 T12: 0.0571
REMARK 3 T13: 0.0911 T23: 0.0667
REMARK 3 L TENSOR
REMARK 3 L11: 3.1793 L22: 5.5761
REMARK 3 L33: 7.7009 L12: -0.8914
REMARK 3 L13: -1.6470 L23: 6.2035
REMARK 3 S TENSOR
REMARK 3 S11: 0.0330 S12: -0.0525 S13: -0.0353
REMARK 3 S21: -0.3159 S22: 0.1780 S23: -0.0159
REMARK 3 S31: -0.1948 S32: 0.0785 S33: -0.2659
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1273 THROUGH 1284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0162 -35.5009 74.2536
REMARK 3 T TENSOR
REMARK 3 T11: 0.3533 T22: 0.5330
REMARK 3 T33: 0.5613 T12: 0.1313
REMARK 3 T13: -0.0291 T23: 0.0312
REMARK 3 L TENSOR
REMARK 3 L11: 2.1629 L22: 3.1504
REMARK 3 L33: 7.0441 L12: -0.9464
REMARK 3 L13: -1.1383 L23: 1.5466
REMARK 3 S TENSOR
REMARK 3 S11: 0.1439 S12: 0.7417 S13: -0.4697
REMARK 3 S21: 0.2594 S22: -0.1639 S23: -0.9954
REMARK 3 S31: 0.5362 S32: 0.5380 S33: -0.0182
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1285 THROUGH 1292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9323 -33.2423 89.7296
REMARK 3 T TENSOR
REMARK 3 T11: 0.6990 T22: 0.9383
REMARK 3 T33: 0.4611 T12: -0.2003
REMARK 3 T13: 0.1294 T23: -0.1118
REMARK 3 L TENSOR
REMARK 3 L11: 4.6944 L22: 4.8781
REMARK 3 L33: 2.9492 L12: -1.6479
REMARK 3 L13: 3.2611 L23: -2.8594
REMARK 3 S TENSOR
REMARK 3 S11: 0.3737 S12: -2.2006 S13: 1.0808
REMARK 3 S21: 2.0230 S22: -1.3276 S23: 0.0020
REMARK 3 S31: -0.6050 S32: -0.7552 S33: 0.8053
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1276 THROUGH 1284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 31.6671 -32.4158 38.5197
REMARK 3 T TENSOR
REMARK 3 T11: 0.4147 T22: 0.3870
REMARK 3 T33: 0.5354 T12: 0.0050
REMARK 3 T13: 0.0608 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 4.9443 L22: 5.4839
REMARK 3 L33: 5.6949 L12: 5.0869
REMARK 3 L13: -5.2583 L23: -5.5559
REMARK 3 S TENSOR
REMARK 3 S11: -0.3637 S12: 0.5001 S13: -0.7169
REMARK 3 S21: -0.7775 S22: -0.0088 S23: 0.8795
REMARK 3 S31: 1.1399 S32: -0.4186 S33: 0.5384
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1285 THROUGH 1292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 38.2773 -26.8165 24.6023
REMARK 3 T TENSOR
REMARK 3 T11: 0.5508 T22: 0.5522
REMARK 3 T33: 0.4945 T12: 0.0071
REMARK 3 T13: 0.0401 T23: -0.0951
REMARK 3 L TENSOR
REMARK 3 L11: 2.8924 L22: 3.6777
REMARK 3 L33: 3.8347 L12: 0.1790
REMARK 3 L13: -1.7157 L23: -3.3104
REMARK 3 S TENSOR
REMARK 3 S11: -1.1088 S12: 1.0953 S13: -1.4806
REMARK 3 S21: -0.4437 S22: 0.0272 S23: -0.4134
REMARK 3 S31: 0.9412 S32: 0.2550 S33: 0.9079
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1293 THROUGH 1300 )
REMARK 3 ORIGIN FOR THE GROUP (A): 43.3434 -13.9350 18.6926
REMARK 3 T TENSOR
REMARK 3 T11: 0.6347 T22: 0.5404
REMARK 3 T33: 0.3777 T12: -0.1441
REMARK 3 T13: 0.0241 T23: -0.0705
REMARK 3 L TENSOR
REMARK 3 L11: 9.8316 L22: 5.2661
REMARK 3 L33: 4.1104 L12: 6.9758
REMARK 3 L13: -6.3000 L23: -4.3157
REMARK 3 S TENSOR
REMARK 3 S11: 1.3568 S12: -0.9288 S13: 0.5957
REMARK 3 S21: 2.4953 S22: -1.1134 S23: 0.6003
REMARK 3 S31: -0.1862 S32: 0.5166 S33: -0.1159
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1276 THROUGH 1284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.3551 14.4413 80.0789
REMARK 3 T TENSOR
REMARK 3 T11: 0.4752 T22: 0.4743
REMARK 3 T33: 0.5277 T12: 0.0155
REMARK 3 T13: -0.1057 T23: -0.0198
REMARK 3 L TENSOR
REMARK 3 L11: 7.3531 L22: 6.3409
REMARK 3 L33: 6.6674 L12: -6.8140
REMARK 3 L13: 6.9968 L23: -6.5008
REMARK 3 S TENSOR
REMARK 3 S11: -0.2786 S12: -1.3789 S13: 0.7886
REMARK 3 S21: 1.2561 S22: 0.2944 S23: -0.4625
REMARK 3 S31: -0.4029 S32: -0.9464 S33: 0.2270
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1285 THROUGH 1294 )
REMARK 3 ORIGIN FOR THE GROUP (A): 39.2888 6.6748 90.4560
REMARK 3 T TENSOR
REMARK 3 T11: 0.7761 T22: 0.7527
REMARK 3 T33: 0.7098 T12: -0.0420
REMARK 3 T13: -0.0873 T23: 0.1240
REMARK 3 L TENSOR
REMARK 3 L11: 8.8357 L22: 4.2421
REMARK 3 L33: 3.2153 L12: -4.2616
REMARK 3 L13: 3.0319 L23: -3.6153
REMARK 3 S TENSOR
REMARK 3 S11: -0.6931 S12: -0.1341 S13: 0.1323
REMARK 3 S21: 0.8222 S22: -0.6716 S23: -1.1348
REMARK 3 S31: -0.1901 S32: 0.0494 S33: 1.7350
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1277 THROUGH 1284 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5928 17.5166 43.2194
REMARK 3 T TENSOR
REMARK 3 T11: 1.7684 T22: 1.0323
REMARK 3 T33: 1.1262 T12: 0.5986
REMARK 3 T13: -0.1970 T23: 0.3185
REMARK 3 L TENSOR
REMARK 3 L11: 9.6579 L22: 3.8029
REMARK 3 L33: 0.9458 L12: 4.4548
REMARK 3 L13: -0.6346 L23: 0.8351
REMARK 3 S TENSOR
REMARK 3 S11: -0.3361 S12: -0.9575 S13: -0.6203
REMARK 3 S21: -1.1682 S22: 0.1581 S23: -0.1053
REMARK 3 S31: 0.6022 S32: -0.0538 S33: 0.0051
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1285 THROUGH 1292 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8937 13.6860 32.7900
REMARK 3 T TENSOR
REMARK 3 T11: 1.0493 T22: 1.1580
REMARK 3 T33: 0.8481 T12: 0.2452
REMARK 3 T13: -0.0489 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 4.1207 L22: 2.5935
REMARK 3 L33: 4.1602 L12: 2.6649
REMARK 3 L13: 3.9209 L23: 1.9152
REMARK 3 S TENSOR
REMARK 3 S11: 0.8613 S12: -0.3827 S13: -0.8909
REMARK 3 S21: -0.3623 S22: 0.1381 S23: 0.2708
REMARK 3 S31: -1.0651 S32: -0.7099 S33: -0.9007
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 5CX3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000212299.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9-8.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97945
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25680
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: REFMAC 5.7.0029
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM CITRATE TRIBASIC
REMARK 280 DIHYDRATE, 0.1 M HEPES SODIUM, PH 7.3, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 57.62850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 4940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 4770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, 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 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 PRO A 2
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 SER B 3
REMARK 465 MET C 1
REMARK 465 PRO C 2
REMARK 465 MET D 1
REMARK 465 PRO D 2
REMARK 465 SER D 3
REMARK 465 ASP D 4
REMARK 465 GLU E 1293
REMARK 465 SER E 1294
REMARK 465 GLY E 1295
REMARK 465 SER E 1296
REMARK 465 SER E 1297
REMARK 465 LEU E 1298
REMARK 465 VAL E 1299
REMARK 465 PRO E 1300
REMARK 465 ARG E 1301
REMARK 465 GLY E 1302
REMARK 465 SER E 1303
REMARK 465 ARG F 1273
REMARK 465 PRO F 1274
REMARK 465 PRO F 1275
REMARK 465 ARG F 1301
REMARK 465 GLY F 1302
REMARK 465 SER F 1303
REMARK 465 ARG G 1273
REMARK 465 PRO G 1274
REMARK 465 PRO G 1275
REMARK 465 GLY G 1295
REMARK 465 SER G 1296
REMARK 465 SER G 1297
REMARK 465 LEU G 1298
REMARK 465 VAL G 1299
REMARK 465 PRO G 1300
REMARK 465 ARG G 1301
REMARK 465 GLY G 1302
REMARK 465 SER G 1303
REMARK 465 ARG H 1273
REMARK 465 PRO H 1274
REMARK 465 PRO H 1275
REMARK 465 ASP H 1276
REMARK 465 GLU H 1293
REMARK 465 SER H 1294
REMARK 465 GLY H 1295
REMARK 465 SER H 1296
REMARK 465 SER H 1297
REMARK 465 LEU H 1298
REMARK 465 VAL H 1299
REMARK 465 PRO H 1300
REMARK 465 ARG H 1301
REMARK 465 GLY H 1302
REMARK 465 SER H 1303
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 A 4 CG OD1 OD2
REMARK 470 GLU A 105 CG CD OE1 OE2
REMARK 470 GLN B 26 CG CD OE1 NE2
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ILE D 23 CD1
REMARK 470 VAL H1279 CG1 CG2
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 NH2 ARG B 68 O GLN B 77 2.06
REMARK 500 NH1 ARG B 10 OD2 ASP F 1277 2.09
REMARK 500 NH2 ARG D 70 OE2 GLU H 1287 2.13
REMARK 500 OE1 GLN B 43 O HOH B 201 2.18
REMARK 500 OE2 GLU C 19 NZ LYS C 51 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 ASN A 84 -124.08 61.01
REMARK 500 HIS A 86 26.92 -155.82
REMARK 500 ASN B 84 -125.78 61.75
REMARK 500 HIS B 86 22.54 -159.87
REMARK 500 ASP C 4 13.25 100.24
REMARK 500 ASN C 84 -129.35 60.80
REMARK 500 HIS C 86 22.07 -159.54
REMARK 500 ASN D 84 -129.16 61.15
REMARK 500 HIS D 86 21.58 -159.40
REMARK 500 GLU F1293 -117.66 59.31
REMARK 500 CYS H1289 49.04 -70.87
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 GOL A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 201
DBREF 5CX3 A 1 121 UNP Q9H492 MLP3A_HUMAN 1 121
DBREF 5CX3 B 1 121 UNP Q9H492 MLP3A_HUMAN 1 121
DBREF 5CX3 C 1 121 UNP Q9H492 MLP3A_HUMAN 1 121
DBREF 5CX3 D 1 121 UNP Q9H492 MLP3A_HUMAN 1 121
DBREF 5CX3 E 1273 1298 UNP Q9BQS8 FYCO1_HUMAN 1273 1298
DBREF 5CX3 F 1273 1298 UNP Q9BQS8 FYCO1_HUMAN 1273 1298
DBREF 5CX3 G 1273 1298 UNP Q9BQS8 FYCO1_HUMAN 1273 1298
DBREF 5CX3 H 1273 1298 UNP Q9BQS8 FYCO1_HUMAN 1273 1298
SEQADV 5CX3 VAL E 1299 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 PRO E 1300 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 ARG E 1301 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 GLY E 1302 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 SER E 1303 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 VAL F 1299 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 PRO F 1300 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 ARG F 1301 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 GLY F 1302 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 SER F 1303 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 VAL G 1299 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 PRO G 1300 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 ARG G 1301 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 GLY G 1302 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 SER G 1303 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 VAL H 1299 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 PRO H 1300 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 ARG H 1301 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 GLY H 1302 UNP Q9BQS8 EXPRESSION TAG
SEQADV 5CX3 SER H 1303 UNP Q9BQS8 EXPRESSION TAG
SEQRES 1 A 121 MET PRO SER ASP ARG PRO PHE LYS GLN ARG ARG SER PHE
SEQRES 2 A 121 ALA ASP ARG CYS LYS GLU VAL GLN GLN ILE ARG ASP GLN
SEQRES 3 A 121 HIS PRO SER LYS ILE PRO VAL ILE ILE GLU ARG TYR LYS
SEQRES 4 A 121 GLY GLU LYS GLN LEU PRO VAL LEU ASP LYS THR LYS PHE
SEQRES 5 A 121 LEU VAL PRO ASP HIS VAL ASN MET SER GLU LEU VAL LYS
SEQRES 6 A 121 ILE ILE ARG ARG ARG LEU GLN LEU ASN PRO THR GLN ALA
SEQRES 7 A 121 PHE PHE LEU LEU VAL ASN GLN HIS SER MET VAL SER VAL
SEQRES 8 A 121 SER THR PRO ILE ALA ASP ILE TYR GLU GLN GLU LYS ASP
SEQRES 9 A 121 GLU ASP GLY PHE LEU TYR MET VAL TYR ALA SER GLN GLU
SEQRES 10 A 121 THR PHE GLY PHE
SEQRES 1 B 121 MET PRO SER ASP ARG PRO PHE LYS GLN ARG ARG SER PHE
SEQRES 2 B 121 ALA ASP ARG CYS LYS GLU VAL GLN GLN ILE ARG ASP GLN
SEQRES 3 B 121 HIS PRO SER LYS ILE PRO VAL ILE ILE GLU ARG TYR LYS
SEQRES 4 B 121 GLY GLU LYS GLN LEU PRO VAL LEU ASP LYS THR LYS PHE
SEQRES 5 B 121 LEU VAL PRO ASP HIS VAL ASN MET SER GLU LEU VAL LYS
SEQRES 6 B 121 ILE ILE ARG ARG ARG LEU GLN LEU ASN PRO THR GLN ALA
SEQRES 7 B 121 PHE PHE LEU LEU VAL ASN GLN HIS SER MET VAL SER VAL
SEQRES 8 B 121 SER THR PRO ILE ALA ASP ILE TYR GLU GLN GLU LYS ASP
SEQRES 9 B 121 GLU ASP GLY PHE LEU TYR MET VAL TYR ALA SER GLN GLU
SEQRES 10 B 121 THR PHE GLY PHE
SEQRES 1 C 121 MET PRO SER ASP ARG PRO PHE LYS GLN ARG ARG SER PHE
SEQRES 2 C 121 ALA ASP ARG CYS LYS GLU VAL GLN GLN ILE ARG ASP GLN
SEQRES 3 C 121 HIS PRO SER LYS ILE PRO VAL ILE ILE GLU ARG TYR LYS
SEQRES 4 C 121 GLY GLU LYS GLN LEU PRO VAL LEU ASP LYS THR LYS PHE
SEQRES 5 C 121 LEU VAL PRO ASP HIS VAL ASN MET SER GLU LEU VAL LYS
SEQRES 6 C 121 ILE ILE ARG ARG ARG LEU GLN LEU ASN PRO THR GLN ALA
SEQRES 7 C 121 PHE PHE LEU LEU VAL ASN GLN HIS SER MET VAL SER VAL
SEQRES 8 C 121 SER THR PRO ILE ALA ASP ILE TYR GLU GLN GLU LYS ASP
SEQRES 9 C 121 GLU ASP GLY PHE LEU TYR MET VAL TYR ALA SER GLN GLU
SEQRES 10 C 121 THR PHE GLY PHE
SEQRES 1 D 121 MET PRO SER ASP ARG PRO PHE LYS GLN ARG ARG SER PHE
SEQRES 2 D 121 ALA ASP ARG CYS LYS GLU VAL GLN GLN ILE ARG ASP GLN
SEQRES 3 D 121 HIS PRO SER LYS ILE PRO VAL ILE ILE GLU ARG TYR LYS
SEQRES 4 D 121 GLY GLU LYS GLN LEU PRO VAL LEU ASP LYS THR LYS PHE
SEQRES 5 D 121 LEU VAL PRO ASP HIS VAL ASN MET SER GLU LEU VAL LYS
SEQRES 6 D 121 ILE ILE ARG ARG ARG LEU GLN LEU ASN PRO THR GLN ALA
SEQRES 7 D 121 PHE PHE LEU LEU VAL ASN GLN HIS SER MET VAL SER VAL
SEQRES 8 D 121 SER THR PRO ILE ALA ASP ILE TYR GLU GLN GLU LYS ASP
SEQRES 9 D 121 GLU ASP GLY PHE LEU TYR MET VAL TYR ALA SER GLN GLU
SEQRES 10 D 121 THR PHE GLY PHE
SEQRES 1 E 31 ARG PRO PRO ASP ASP ALA VAL PHE ASP ILE ILE THR ASP
SEQRES 2 E 31 GLU GLU LEU CYS GLN ILE GLN GLU SER GLY SER SER LEU
SEQRES 3 E 31 VAL PRO ARG GLY SER
SEQRES 1 F 31 ARG PRO PRO ASP ASP ALA VAL PHE ASP ILE ILE THR ASP
SEQRES 2 F 31 GLU GLU LEU CYS GLN ILE GLN GLU SER GLY SER SER LEU
SEQRES 3 F 31 VAL PRO ARG GLY SER
SEQRES 1 G 31 ARG PRO PRO ASP ASP ALA VAL PHE ASP ILE ILE THR ASP
SEQRES 2 G 31 GLU GLU LEU CYS GLN ILE GLN GLU SER GLY SER SER LEU
SEQRES 3 G 31 VAL PRO ARG GLY SER
SEQRES 1 H 31 ARG PRO PRO ASP ASP ALA VAL PHE ASP ILE ILE THR ASP
SEQRES 2 H 31 GLU GLU LEU CYS GLN ILE GLN GLU SER GLY SER SER LEU
SEQRES 3 H 31 VAL PRO ARG GLY SER
HET GOL A 201 6
HET GOL D 201 14
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GOL 2(C3 H8 O3)
FORMUL 11 HOH *95(H2 O)
HELIX 1 AA1 PRO A 6 ARG A 11 1 6
HELIX 2 AA2 SER A 12 HIS A 27 1 16
HELIX 3 AA3 ASN A 59 GLN A 72 1 14
HELIX 4 AA4 PRO A 94 LYS A 103 1 10
HELIX 5 AA5 GLU A 117 GLY A 120 5 4
HELIX 6 AA6 PRO B 6 ARG B 11 1 6
HELIX 7 AA7 SER B 12 HIS B 27 1 16
HELIX 8 AA8 ASN B 59 LEU B 71 1 13
HELIX 9 AA9 PRO B 94 LYS B 103 1 10
HELIX 10 AB1 GLU B 117 GLY B 120 5 4
HELIX 11 AB2 PRO C 6 ARG C 11 1 6
HELIX 12 AB3 SER C 12 HIS C 27 1 16
HELIX 13 AB4 ASN C 59 GLN C 72 1 14
HELIX 14 AB5 PRO C 94 LYS C 103 1 10
HELIX 15 AB6 GLU C 117 GLY C 120 5 4
HELIX 16 AB7 PRO D 6 ARG D 11 1 6
HELIX 17 AB8 SER D 12 HIS D 27 1 16
HELIX 18 AB9 ASN D 59 LEU D 71 1 13
HELIX 19 AC1 PRO D 94 LYS D 103 1 10
HELIX 20 AC2 GLU D 117 GLY D 120 5 4
HELIX 21 AC3 THR E 1284 GLN E 1290 1 7
HELIX 22 AC4 THR F 1284 ILE F 1291 1 8
HELIX 23 AC5 THR G 1284 CYS G 1289 1 6
HELIX 24 AC6 THR H 1284 CYS H 1289 1 6
SHEET 1 AA1 5 PHE A 79 VAL A 83 0
SHEET 2 AA1 5 LEU A 109 SER A 115 -1 O ALA A 114 N PHE A 80
SHEET 3 AA1 5 LYS A 30 ARG A 37 1 N ILE A 34 O LEU A 109
SHEET 4 AA1 5 LYS A 49 PRO A 55 -1 O VAL A 54 N ILE A 31
SHEET 5 AA1 5 ASP E1276 ILE E1282 1 O ASP E1281 N LYS A 51
SHEET 1 AA2 5 PHE B 79 VAL B 83 0
SHEET 2 AA2 5 LEU B 109 SER B 115 -1 O ALA B 114 N PHE B 80
SHEET 3 AA2 5 LYS B 30 ARG B 37 1 N ILE B 34 O LEU B 109
SHEET 4 AA2 5 LYS B 51 PRO B 55 -1 O VAL B 54 N ILE B 31
SHEET 5 AA2 5 ASP F1281 ILE F1282 1 O ASP F1281 N LYS B 51
SHEET 1 AA3 5 PHE C 79 VAL C 83 0
SHEET 2 AA3 5 LEU C 109 SER C 115 -1 O VAL C 112 N LEU C 82
SHEET 3 AA3 5 LYS C 30 ARG C 37 1 N ILE C 34 O MET C 111
SHEET 4 AA3 5 LYS C 51 PRO C 55 -1 O VAL C 54 N ILE C 31
SHEET 5 AA3 5 ASP G1281 ILE G1282 1 O ASP G1281 N LYS C 51
SHEET 1 AA4 5 PHE D 79 VAL D 83 0
SHEET 2 AA4 5 LEU D 109 SER D 115 -1 O VAL D 112 N LEU D 82
SHEET 3 AA4 5 LYS D 30 ARG D 37 1 N ILE D 34 O MET D 111
SHEET 4 AA4 5 LYS D 51 PRO D 55 -1 O VAL D 54 N ILE D 31
SHEET 5 AA4 5 ASP H1281 ILE H1282 1 O ASP H1281 N LYS D 51
CISPEP 1 SER A 3 ASP A 4 0 2.64
CISPEP 2 GLN E 1290 ILE E 1291 0 3.26
SITE 1 AC1 6 CYS A 17 VAL A 20 GLU A 105 ASP A 106
SITE 2 AC1 6 GLY A 107 HOH A 328
SITE 1 AC2 7 HIS B 86 VAL D 83 ASN D 84 GLN D 85
SITE 2 AC2 7 HIS D 86 SER D 87 GLU D 102
CRYST1 35.426 115.257 73.517 90.00 102.29 90.00 P 1 21 1 8
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 0.028228 0.000000 0.006147 0.00000
SCALE2 0.000000 0.008676 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013921 0.00000
(ATOM LINES ARE NOT SHOWN.)
END