HEADER LIGASE 22-AUG-18 6M93
TITLE MONOPHOSPHORYLATED PSER33 B-CATENIN PEPTIDE, B-TRCP/SKP1, NRX-1933
TITLE 2 TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-BOX/WD REPEAT-CONTAINING PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: E3RSIKAPPAB,EPIDIDYMIS TISSUE PROTEIN LI 2A,F-BOX AND WD
COMPND 5 REPEATS PROTEIN BETA-TRCP,PIKAPPABALPHA-E3 RECEPTOR SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: S-PHASE KINASE-ASSOCIATED PROTEIN 1;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CYCLIN-A/CDK2-ASSOCIATED PROTEIN P19,P19A,ORGAN OF CORTI
COMPND 11 PROTEIN 2,OCP-2,ORGAN OF CORTI PROTEIN II,OCP-II,RNA POLYMERASE II
COMPND 12 ELONGATION FACTOR-LIKE PROTEIN,SIII,TRANSCRIPTION ELONGATION FACTOR B
COMPND 13 POLYPEPTIDE 1-LIKE,P19SKP1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: CATENIN BETA-1;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: BETA-CATENIN;
COMPND 19 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: BTRC, BTRCP, FBW1A, FBXW1A;
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: SKP1, EMC19, OCP2, SKP1A, TCEB1L;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606
KEYWDS UBIQUITIN MOLECULAR GLUE ENHANCER, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.SIMONETTA,M.C.CLIFTON,R.L.WALTER,G.M.RANIERI,S.J.LEE
REVDAT 2 10-APR-19 6M93 1 JRNL
REVDAT 1 03-APR-19 6M93 0
JRNL AUTH K.R.SIMONETTA,J.TAYGERLY,K.BOYLE,S.E.BASHAM,C.PADOVANI,
JRNL AUTH 2 Y.LOU,T.J.CUMMINS,S.L.YUNG,S.K.VON SOLY,F.KAYSER,J.KURIYAN,
JRNL AUTH 3 M.RAPE,M.CARDOZO,M.A.GALLOP,N.F.BENCE,P.A.BARSANTI,A.SAHA
JRNL TITL PROSPECTIVE DISCOVERY OF SMALL MOLECULE ENHANCERS OF AN E3
JRNL TITL 2 LIGASE-SUBSTRATE INTERACTION.
JRNL REF NAT COMMUN V. 10 1402 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30926793
JRNL DOI 10.1038/S41467-019-09358-9
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.27
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.980
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 29129
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.910
REMARK 3 FREE R VALUE TEST SET COUNT : 2013
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 41.2706 - 6.0198 0.95 1852 138 0.1995 0.1970
REMARK 3 2 6.0198 - 4.7804 0.99 1915 152 0.1914 0.2045
REMARK 3 3 4.7804 - 4.1768 0.99 1950 133 0.1653 0.1689
REMARK 3 4 4.1768 - 3.7952 0.99 1949 149 0.2011 0.2219
REMARK 3 5 3.7952 - 3.5233 1.00 1937 144 0.2138 0.2368
REMARK 3 6 3.5233 - 3.3157 1.00 1928 135 0.2301 0.2588
REMARK 3 7 3.3157 - 3.1497 1.00 1957 154 0.2512 0.2843
REMARK 3 8 3.1497 - 3.0126 1.00 1955 148 0.2587 0.2835
REMARK 3 9 3.0126 - 2.8967 1.00 1954 142 0.2680 0.3115
REMARK 3 10 2.8967 - 2.7968 1.00 1966 144 0.2801 0.3263
REMARK 3 11 2.7968 - 2.7093 1.00 1914 142 0.2859 0.3084
REMARK 3 12 2.7093 - 2.6319 1.00 1966 154 0.2919 0.3353
REMARK 3 13 2.6319 - 2.5626 1.00 1934 138 0.2904 0.3115
REMARK 3 14 2.5626 - 2.5001 1.00 1939 140 0.3158 0.3464
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.77
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 90.18
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 8 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.9045 -73.7519 -9.3383
REMARK 3 T TENSOR
REMARK 3 T11: 1.3722 T22: 1.6259
REMARK 3 T33: 1.1138 T12: -0.3838
REMARK 3 T13: 0.5326 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 0.0323 L22: 0.0314
REMARK 3 L33: 0.0421 L12: -0.0233
REMARK 3 L13: -0.0136 L23: 0.0453
REMARK 3 S TENSOR
REMARK 3 S11: 0.0724 S12: -0.1369 S13: 0.0240
REMARK 3 S21: -0.0584 S22: 0.0998 S23: 0.1171
REMARK 3 S31: 0.3695 S32: 0.0889 S33: 0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 9 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1319 -75.7508 -6.3631
REMARK 3 T TENSOR
REMARK 3 T11: 1.1043 T22: 1.6038
REMARK 3 T33: 0.8145 T12: 0.0286
REMARK 3 T13: 0.3042 T23: 0.1048
REMARK 3 L TENSOR
REMARK 3 L11: 0.0445 L22: 0.0198
REMARK 3 L33: 0.0025 L12: 0.0156
REMARK 3 L13: -0.0074 L23: -0.0101
REMARK 3 S TENSOR
REMARK 3 S11: 0.2445 S12: -0.2798 S13: -0.2067
REMARK 3 S21: 0.6800 S22: -0.2632 S23: -0.4150
REMARK 3 S31: -0.0899 S32: -0.2935 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 24 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.1545 -62.3158 -8.3512
REMARK 3 T TENSOR
REMARK 3 T11: 1.1587 T22: 1.7964
REMARK 3 T33: 1.2437 T12: 0.4659
REMARK 3 T13: 0.1660 T23: -0.2951
REMARK 3 L TENSOR
REMARK 3 L11: 0.0467 L22: 0.0142
REMARK 3 L33: 0.0153 L12: 0.0245
REMARK 3 L13: -0.0038 L23: -0.0096
REMARK 3 S TENSOR
REMARK 3 S11: 0.1072 S12: 0.0711 S13: 0.0183
REMARK 3 S21: -0.1352 S22: -0.3801 S23: 0.3026
REMARK 3 S31: -0.1431 S32: 0.0956 S33: 0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 32 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6697 -64.7422 -16.5233
REMARK 3 T TENSOR
REMARK 3 T11: 0.8086 T22: 1.6805
REMARK 3 T33: 1.2689 T12: 0.3001
REMARK 3 T13: 0.2659 T23: 0.1768
REMARK 3 L TENSOR
REMARK 3 L11: 0.0147 L22: 0.0280
REMARK 3 L33: 0.0388 L12: -0.0042
REMARK 3 L13: -0.0077 L23: -0.0148
REMARK 3 S TENSOR
REMARK 3 S11: -0.3482 S12: 0.0547 S13: 0.0429
REMARK 3 S21: -0.1861 S22: 0.4170 S23: 0.5253
REMARK 3 S31: -0.0127 S32: -0.1984 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 33 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.2850 -70.9967 -18.9775
REMARK 3 T TENSOR
REMARK 3 T11: 1.1032 T22: 2.3719
REMARK 3 T33: 1.2644 T12: 0.1654
REMARK 3 T13: 0.2886 T23: 0.1162
REMARK 3 L TENSOR
REMARK 3 L11: 0.0320 L22: 0.0505
REMARK 3 L33: 0.1086 L12: 0.0352
REMARK 3 L13: 0.0567 L23: 0.0688
REMARK 3 S TENSOR
REMARK 3 S11: -0.8626 S12: -0.3827 S13: 0.1820
REMARK 3 S21: 0.0342 S22: -0.2917 S23: 0.2314
REMARK 3 S31: -0.2306 S32: -0.2635 S33: -0.0064
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 39 THROUGH 45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5934 -73.1369 -12.4196
REMARK 3 T TENSOR
REMARK 3 T11: 0.9542 T22: 1.3395
REMARK 3 T33: 0.9530 T12: 0.0688
REMARK 3 T13: 0.3828 T23: 0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 0.0737 L22: 0.2174
REMARK 3 L33: 0.0688 L12: -0.1319
REMARK 3 L13: 0.0676 L23: -0.1227
REMARK 3 S TENSOR
REMARK 3 S11: -0.4253 S12: 0.1910 S13: -0.1073
REMARK 3 S21: 0.5238 S22: -0.4234 S23: -0.6325
REMARK 3 S31: -0.2210 S32: -0.4692 S33: 0.0002
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 46 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9095 -66.1704 -0.9685
REMARK 3 T TENSOR
REMARK 3 T11: 1.3017 T22: 1.4383
REMARK 3 T33: 0.9736 T12: 0.1216
REMARK 3 T13: 0.6095 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 1.0621 L22: 0.4457
REMARK 3 L33: 0.3138 L12: -0.4817
REMARK 3 L13: 0.5707 L23: -0.1694
REMARK 3 S TENSOR
REMARK 3 S11: -0.2490 S12: -1.0092 S13: 0.6281
REMARK 3 S21: 0.4006 S22: -0.5381 S23: -0.2242
REMARK 3 S31: -0.5779 S32: -0.5956 S33: -0.0766
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6302 -59.6652 4.9669
REMARK 3 T TENSOR
REMARK 3 T11: 1.3942 T22: 1.6664
REMARK 3 T33: 0.8228 T12: 0.1634
REMARK 3 T13: 0.2777 T23: -0.1819
REMARK 3 L TENSOR
REMARK 3 L11: 0.2459 L22: 3.3032
REMARK 3 L33: 0.7081 L12: 0.8422
REMARK 3 L13: -0.3644 L23: -1.5072
REMARK 3 S TENSOR
REMARK 3 S11: -0.4499 S12: -0.6602 S13: -0.2394
REMARK 3 S21: 0.5987 S22: -1.4013 S23: -0.1395
REMARK 3 S31: -0.2668 S32: -0.2625 S33: -0.3058
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 94 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4563 -64.5247 -7.9146
REMARK 3 T TENSOR
REMARK 3 T11: 1.1624 T22: 1.2131
REMARK 3 T33: 0.8487 T12: 0.3238
REMARK 3 T13: 0.2307 T23: 0.0687
REMARK 3 L TENSOR
REMARK 3 L11: 0.1641 L22: 0.1771
REMARK 3 L33: 0.0297 L12: 0.1902
REMARK 3 L13: -0.0134 L23: -0.0293
REMARK 3 S TENSOR
REMARK 3 S11: 0.3115 S12: 0.0111 S13: -0.5566
REMARK 3 S21: 1.3742 S22: -0.1470 S23: 0.6355
REMARK 3 S31: 0.4986 S32: -0.3916 S33: 0.0006
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 95 THROUGH 109 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0109 -55.3601 -3.4367
REMARK 3 T TENSOR
REMARK 3 T11: 1.3059 T22: 1.1411
REMARK 3 T33: 0.7955 T12: 0.4843
REMARK 3 T13: 0.2738 T23: -0.1048
REMARK 3 L TENSOR
REMARK 3 L11: 1.3291 L22: 0.7677
REMARK 3 L33: 0.9382 L12: -0.9851
REMARK 3 L13: 1.0355 L23: -0.8258
REMARK 3 S TENSOR
REMARK 3 S11: -0.3071 S12: 0.0787 S13: 0.2896
REMARK 3 S21: 0.9273 S22: -0.1751 S23: 0.4426
REMARK 3 S31: -0.5525 S32: -0.2169 S33: -0.1322
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 110 THROUGH 128 )
REMARK 3 ORIGIN FOR THE GROUP (A): 42.6849 -57.4814 -2.6423
REMARK 3 T TENSOR
REMARK 3 T11: 1.4101 T22: 0.7917
REMARK 3 T33: 0.7494 T12: 0.4612
REMARK 3 T13: -0.0792 T23: -0.1901
REMARK 3 L TENSOR
REMARK 3 L11: 1.6929 L22: 1.7777
REMARK 3 L33: 0.0279 L12: 1.2296
REMARK 3 L13: -0.0913 L23: -0.1924
REMARK 3 S TENSOR
REMARK 3 S11: 0.1676 S12: -1.0641 S13: -0.4583
REMARK 3 S21: 1.0566 S22: -0.4007 S23: -0.5570
REMARK 3 S31: 0.2677 S32: 0.5007 S33: -0.0775
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 129 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.8056 -48.7889 -10.1095
REMARK 3 T TENSOR
REMARK 3 T11: 0.9806 T22: 1.0541
REMARK 3 T33: 1.5731 T12: 0.2432
REMARK 3 T13: -0.1645 T23: 0.2768
REMARK 3 L TENSOR
REMARK 3 L11: 0.0510 L22: 0.0080
REMARK 3 L33: 0.0228 L12: 0.0195
REMARK 3 L13: -0.0415 L23: -0.0139
REMARK 3 S TENSOR
REMARK 3 S11: -0.6743 S12: 0.1917 S13: -0.0112
REMARK 3 S21: 0.0392 S22: 0.4799 S23: 0.3116
REMARK 3 S31: 0.1156 S32: -0.4099 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 30 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0739 -0.6324 5.7470
REMARK 3 T TENSOR
REMARK 3 T11: 0.8749 T22: 0.5826
REMARK 3 T33: 0.7157 T12: 0.0619
REMARK 3 T13: 0.0657 T23: -0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 0.0239 L22: 0.0374
REMARK 3 L33: 0.0490 L12: 0.0179
REMARK 3 L13: -0.0055 L23: 0.0615
REMARK 3 S TENSOR
REMARK 3 S11: 0.4903 S12: -0.2848 S13: 0.4348
REMARK 3 S21: 0.4458 S22: -0.0988 S23: -0.1291
REMARK 3 S31: 0.3256 S32: -0.0774 S33: 0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6870 -43.6490 -11.4505
REMARK 3 T TENSOR
REMARK 3 T11: 1.0058 T22: 0.6642
REMARK 3 T33: 0.9171 T12: 0.3337
REMARK 3 T13: 0.0701 T23: -0.0633
REMARK 3 L TENSOR
REMARK 3 L11: 1.0197 L22: 0.8509
REMARK 3 L33: 0.2892 L12: -0.2683
REMARK 3 L13: 0.3016 L23: 0.5285
REMARK 3 S TENSOR
REMARK 3 S11: 0.0115 S12: -0.0743 S13: 0.4641
REMARK 3 S21: -0.0711 S22: -0.0811 S23: -0.2577
REMARK 3 S31: 0.2009 S32: 0.1101 S33: 0.0118
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 547 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4286 -13.1670 -1.5616
REMARK 3 T TENSOR
REMARK 3 T11: 0.7688 T22: 0.4175
REMARK 3 T33: 0.6475 T12: 0.1370
REMARK 3 T13: -0.0701 T23: -0.0315
REMARK 3 L TENSOR
REMARK 3 L11: 2.8972 L22: 1.9711
REMARK 3 L33: 2.4874 L12: -0.2947
REMARK 3 L13: -0.3378 L23: -0.3127
REMARK 3 S TENSOR
REMARK 3 S11: 0.1646 S12: 0.0856 S13: -0.1186
REMARK 3 S21: -0.0004 S22: 0.0106 S23: -0.2834
REMARK 3 S31: 0.1610 S32: -0.1397 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6M93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1000236369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JAN-14
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29168
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.265
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.115
REMARK 200 R MERGE (I) : 0.11500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.9100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.44
REMARK 200 R MERGE FOR SHELL (I) : 1.94000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000 0.1M BTP PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.08667
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 74.17333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 ASN A 219
REMARK 465 LYS A 220
REMARK 465 PRO A 221
REMARK 465 PRO A 222
REMARK 465 ASP A 223
REMARK 465 GLY A 224
REMARK 465 ASN A 225
REMARK 465 ALA A 226
REMARK 465 ASN A 548
REMARK 465 ASP A 549
REMARK 465 PRO A 550
REMARK 465 ALA A 551
REMARK 465 ALA A 552
REMARK 465 GLN A 553
REMARK 465 ALA A 554
REMARK 465 GLU A 555
REMARK 465 PRO A 556
REMARK 465 PRO A 557
REMARK 465 ARG A 558
REMARK 465 SER A 559
REMARK 465 PRO A 560
REMARK 465 SER A 561
REMARK 465 ARG A 562
REMARK 465 THR A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 TYR A 566
REMARK 465 ILE A 567
REMARK 465 SER A 568
REMARK 465 ARG A 569
REMARK 465 PRO B 2
REMARK 465 LYS B 60
REMARK 465 ASP B 61
REMARK 465 ASP B 62
REMARK 465 PRO B 63
REMARK 465 PRO B 64
REMARK 465 ASP B 65
REMARK 465 ASP B 66
REMARK 465 ILE B 67
REMARK 465 GLN B 140
REMARK 465 TRP B 141
REMARK 465 CYS B 142
REMARK 465 GLU B 143
REMARK 465 GLU B 144
REMARK 465 LYS B 145
REMARK 465 CYS C 16
REMARK 465 ASP C 17
REMARK 465 ARG C 18
REMARK 465 LYS C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 VAL C 22
REMARK 465 SER C 23
REMARK 465 HIS C 24
REMARK 465 TRP C 25
REMARK 465 GLN C 26
REMARK 465 GLN C 27
REMARK 465 GLN C 28
REMARK 465 SER C 29
REMARK 465 THR C 41
REMARK 465 THR C 42
REMARK 465 ALA C 43
REMARK 465 PRO C 44
REMARK 465 SER C 45
REMARK 465 LEU C 46
REMARK 465 SER C 47
REMARK 465 GLY C 48
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 SER A 138 OG
REMARK 470 LEU A 140 CG CD1 CD2
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 ARG A 198 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 204 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 208 CG CD OE1 OE2
REMARK 470 ARG A 209 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 LYS A 218 CG CD CE NZ
REMARK 470 GLN A 241 CG CD OE1 NE2
REMARK 470 GLU A 244 CG CD OE1 OE2
REMARK 470 GLU A 247 CG CD OE1 OE2
REMARK 470 ARG A 251 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 265 CG CD OE1 OE2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 ARG A 301 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 317 CG CD OE1 OE2
REMARK 470 ARG A 318 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 338 CG CD OE1 OE2
REMARK 470 ASN A 357 CG OD1 ND2
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 ARG A 439 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 470 CG CD OE1 OE2
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 ASN A 480 CG OD1 ND2
REMARK 470 ARG A 504 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 GLU B 12 CG CD OE1 OE2
REMARK 470 GLU B 15 CG CD OE1 OE2
REMARK 470 ASP B 17 CG OD1 OD2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 ILE B 20 CG1 CG2 CD1
REMARK 470 LYS B 22 CG CD CE NZ
REMARK 470 LYS B 28 CG CD CE NZ
REMARK 470 GLU B 32 CG CD OE1 OE2
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 ASP B 71 CG OD1 OD2
REMARK 470 GLU B 73 CG CD OE1 OE2
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 ASP B 78 CG OD1 OD2
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 LYS B 110 CG CD CE NZ
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 GLU B 130 CG CD OE1 OE2
REMARK 470 GLN B 134 CG CD OE1 NE2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 GLU B 138 CG CD OE1 OE2
REMARK 470 TYR C 30 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR C 40 OG1 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 OG SER B 24 O LEU B 92 2.09
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 266 -79.29 -118.62
REMARK 500 ASN A 287 4.14 87.96
REMARK 500 ASP A 316 -159.37 -130.31
REMARK 500 SER A 327 6.76 80.01
REMARK 500 HIS A 345 -53.19 -145.14
REMARK 500 ASN A 356 139.74 -178.53
REMARK 500 ARG A 367 7.29 83.33
REMARK 500 ASP A 440 -113.06 59.96
REMARK 500 ARG A 464 136.81 -172.05
REMARK 500 ASP A 479 -148.95 -123.32
REMARK 500 SER C 37 -164.78 -104.69
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 J8Y A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602
DBREF 6M93 A 139 569 UNP Q9Y297 FBW1A_HUMAN 175 605
DBREF 6M93 B 2 145 UNP P63208 SKP1_HUMAN 2 163
DBREF 6M93 C 17 48 UNP P35222 CTNB1_HUMAN 17 48
SEQADV 6M93 SER A 138 UNP Q9Y297 EXPRESSION TAG
SEQADV 6M93 B UNP P63208 ASP 37 DELETION
SEQADV 6M93 B UNP P63208 ASP 38 DELETION
SEQADV 6M93 B UNP P63208 GLU 39 DELETION
SEQADV 6M93 B UNP P63208 GLY 40 DELETION
SEQADV 6M93 B UNP P63208 ASP 41 DELETION
SEQADV 6M93 B UNP P63208 ASP 42 DELETION
SEQADV 6M93 B UNP P63208 PRO 71 DELETION
SEQADV 6M93 B UNP P63208 PRO 72 DELETION
SEQADV 6M93 B UNP P63208 GLU 73 DELETION
SEQADV 6M93 B UNP P63208 ASP 74 DELETION
SEQADV 6M93 B UNP P63208 ASP 75 DELETION
SEQADV 6M93 B UNP P63208 GLU 76 DELETION
SEQADV 6M93 B UNP P63208 ASN 77 DELETION
SEQADV 6M93 B UNP P63208 LYS 78 DELETION
SEQADV 6M93 B UNP P63208 GLU 79 DELETION
SEQADV 6M93 B UNP P63208 LYS 80 DELETION
SEQADV 6M93 B UNP P63208 ARG 81 DELETION
SEQADV 6M93 B UNP P63208 THR 82 DELETION
SEQADV 6M93 CYS C 16 UNP P35222 EXPRESSION TAG
SEQRES 1 A 432 SER MET LEU GLN ARG ASP PHE ILE THR ALA LEU PRO ALA
SEQRES 2 A 432 ARG GLY LEU ASP HIS ILE ALA GLU ASN ILE LEU SER TYR
SEQRES 3 A 432 LEU ASP ALA LYS SER LEU CYS ALA ALA GLU LEU VAL CYS
SEQRES 4 A 432 LYS GLU TRP TYR ARG VAL THR SER ASP GLY MET LEU TRP
SEQRES 5 A 432 LYS LYS LEU ILE GLU ARG MET VAL ARG THR ASP SER LEU
SEQRES 6 A 432 TRP ARG GLY LEU ALA GLU ARG ARG GLY TRP GLY GLN TYR
SEQRES 7 A 432 LEU PHE LYS ASN LYS PRO PRO ASP GLY ASN ALA PRO PRO
SEQRES 8 A 432 ASN SER PHE TYR ARG ALA LEU TYR PRO LYS ILE ILE GLN
SEQRES 9 A 432 ASP ILE GLU THR ILE GLU SER ASN TRP ARG CYS GLY ARG
SEQRES 10 A 432 HIS SER LEU GLN ARG ILE HIS CYS ARG SER GLU THR SER
SEQRES 11 A 432 LYS GLY VAL TYR CYS LEU GLN TYR ASP ASP GLN LYS ILE
SEQRES 12 A 432 VAL SER GLY LEU ARG ASP ASN THR ILE LYS ILE TRP ASP
SEQRES 13 A 432 LYS ASN THR LEU GLU CYS LYS ARG ILE LEU THR GLY HIS
SEQRES 14 A 432 THR GLY SER VAL LEU CYS LEU GLN TYR ASP GLU ARG VAL
SEQRES 15 A 432 ILE ILE THR GLY SER SER ASP SER THR VAL ARG VAL TRP
SEQRES 16 A 432 ASP VAL ASN THR GLY GLU MET LEU ASN THR LEU ILE HIS
SEQRES 17 A 432 HIS CYS GLU ALA VAL LEU HIS LEU ARG PHE ASN ASN GLY
SEQRES 18 A 432 MET MET VAL THR CYS SER LYS ASP ARG SER ILE ALA VAL
SEQRES 19 A 432 TRP ASP MET ALA SER PRO THR ASP ILE THR LEU ARG ARG
SEQRES 20 A 432 VAL LEU VAL GLY HIS ARG ALA ALA VAL ASN VAL VAL ASP
SEQRES 21 A 432 PHE ASP ASP LYS TYR ILE VAL SER ALA SER GLY ASP ARG
SEQRES 22 A 432 THR ILE LYS VAL TRP ASN THR SER THR CYS GLU PHE VAL
SEQRES 23 A 432 ARG THR LEU ASN GLY HIS LYS ARG GLY ILE ALA CYS LEU
SEQRES 24 A 432 GLN TYR ARG ASP ARG LEU VAL VAL SER GLY SER SER ASP
SEQRES 25 A 432 ASN THR ILE ARG LEU TRP ASP ILE GLU CYS GLY ALA CYS
SEQRES 26 A 432 LEU ARG VAL LEU GLU GLY HIS GLU GLU LEU VAL ARG CYS
SEQRES 27 A 432 ILE ARG PHE ASP ASN LYS ARG ILE VAL SER GLY ALA TYR
SEQRES 28 A 432 ASP GLY LYS ILE LYS VAL TRP ASP LEU VAL ALA ALA LEU
SEQRES 29 A 432 ASP PRO ARG ALA PRO ALA GLY THR LEU CYS LEU ARG THR
SEQRES 30 A 432 LEU VAL GLU HIS SER GLY ARG VAL PHE ARG LEU GLN PHE
SEQRES 31 A 432 ASP GLU PHE GLN ILE VAL SER SER SER HIS ASP ASP THR
SEQRES 32 A 432 ILE LEU ILE TRP ASP PHE LEU ASN ASP PRO ALA ALA GLN
SEQRES 33 A 432 ALA GLU PRO PRO ARG SER PRO SER ARG THR TYR THR TYR
SEQRES 34 A 432 ILE SER ARG
SEQRES 1 B 144 PRO SER ILE LYS LEU GLN SER SER ASP GLY GLU ILE PHE
SEQRES 2 B 144 GLU VAL ASP VAL GLU ILE ALA LYS GLN SER VAL THR ILE
SEQRES 3 B 144 LYS THR MET LEU GLU ASP LEU GLY MET ASP PRO VAL PRO
SEQRES 4 B 144 LEU PRO ASN VAL ASN ALA ALA ILE LEU LYS LYS VAL ILE
SEQRES 5 B 144 GLN TRP CYS THR HIS HIS LYS ASP ASP PRO PRO ASP ASP
SEQRES 6 B 144 ILE PRO VAL TRP ASP GLN GLU PHE LEU LYS VAL ASP GLN
SEQRES 7 B 144 GLY THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU
SEQRES 8 B 144 ASP ILE LYS GLY LEU LEU ASP VAL THR CYS LYS THR VAL
SEQRES 9 B 144 ALA ASN MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG
SEQRES 10 B 144 LYS THR PHE ASN ILE LYS ASN ASP PHE THR GLU GLU GLU
SEQRES 11 B 144 GLU ALA GLN VAL ARG LYS GLU ASN GLN TRP CYS GLU GLU
SEQRES 12 B 144 LYS
SEQRES 1 C 33 CYS ASP ARG LYS ALA ALA VAL SER HIS TRP GLN GLN GLN
SEQRES 2 C 33 SER TYR LEU ASP SEP GLY ILE HIS SER GLY ALA THR THR
SEQRES 3 C 33 THR ALA PRO SER LEU SER GLY
MODRES 6M93 SEP C 33 SER MODIFIED RESIDUE
HET SEP C 33 10
HET J8Y A 601 25
HET PO4 A 602 5
HETNAM SEP PHOSPHOSERINE
HETNAM J8Y 2-OXO-N-[3-(1H-TETRAZOL-5-YL)PHENYL]-6-
HETNAM 2 J8Y (TRIFLUOROMETHYL)-1,2-DIHYDROPYRIDINE-3-CARBOXAMIDE
HETNAM PO4 PHOSPHATE ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 3 SEP C3 H8 N O6 P
FORMUL 4 J8Y C14 H9 F3 N6 O2
FORMUL 5 PO4 O4 P 3-
FORMUL 6 HOH *14(H2 O)
HELIX 1 AA1 ASP A 143 ARG A 151 1 9
HELIX 2 AA2 LEU A 153 SER A 162 1 10
HELIX 3 AA3 ASP A 165 LEU A 174 1 10
HELIX 4 AA4 CYS A 176 GLY A 186 1 11
HELIX 5 AA5 MET A 187 ASP A 200 1 14
HELIX 6 AA6 ASP A 200 GLY A 211 1 12
HELIX 7 AA7 TRP A 212 LEU A 216 5 5
HELIX 8 AA8 PRO A 228 GLY A 253 1 26
HELIX 9 AA9 LEU A 497 ASP A 502 1 6
HELIX 10 AB1 PRO A 506 THR A 509 5 4
HELIX 11 AB2 ASP B 17 LYS B 22 1 6
HELIX 12 AB3 SER B 24 ASP B 33 1 10
HELIX 13 AB4 ASN B 45 HIS B 59 1 15
HELIX 14 AB5 VAL B 69 LEU B 75 1 7
HELIX 15 AB6 ASP B 78 ASP B 93 1 16
HELIX 16 AB7 ILE B 94 LYS B 110 1 17
HELIX 17 AB8 THR B 113 ASN B 122 1 10
HELIX 18 AB9 THR B 128 GLU B 138 1 11
SHEET 1 AA1 4 SER A 256 HIS A 261 0
SHEET 2 AA1 4 THR A 540 ASP A 545 -1 O ASP A 545 N SER A 256
SHEET 3 AA1 4 GLN A 531 SER A 536 -1 N ILE A 532 O TRP A 544
SHEET 4 AA1 4 VAL A 522 PHE A 527 -1 N GLN A 526 O VAL A 533
SHEET 1 AA2 4 VAL A 270 TYR A 275 0
SHEET 2 AA2 4 LYS A 279 LEU A 284 -1 O VAL A 281 N GLN A 274
SHEET 3 AA2 4 ILE A 289 ASP A 293 -1 O TRP A 292 N ILE A 280
SHEET 4 AA2 4 CYS A 299 LEU A 303 -1 O LYS A 300 N ILE A 291
SHEET 1 AA3 4 VAL A 310 TYR A 315 0
SHEET 2 AA3 4 VAL A 319 SER A 324 -1 O ILE A 321 N GLN A 314
SHEET 3 AA3 4 THR A 328 ASP A 333 -1 O TRP A 332 N ILE A 320
SHEET 4 AA3 4 MET A 339 ILE A 344 -1 O LEU A 340 N VAL A 331
SHEET 1 AA4 4 VAL A 350 ASN A 356 0
SHEET 2 AA4 4 MET A 359 SER A 364 -1 O VAL A 361 N ARG A 354
SHEET 3 AA4 4 SER A 368 SER A 376 -1 O TRP A 372 N MET A 360
SHEET 4 AA4 4 ASP A 379 VAL A 387 -1 O LEU A 386 N ILE A 369
SHEET 1 AA5 4 VAL A 393 PHE A 398 0
SHEET 2 AA5 4 TYR A 402 SER A 407 -1 O VAL A 404 N ASP A 397
SHEET 3 AA5 4 ILE A 412 ASN A 416 -1 O TRP A 415 N ILE A 403
SHEET 4 AA5 4 PHE A 422 LEU A 426 -1 O LEU A 426 N ILE A 412
SHEET 1 AA6 4 ILE A 433 ARG A 439 0
SHEET 2 AA6 4 LEU A 442 SER A 447 -1 O VAL A 444 N GLN A 437
SHEET 3 AA6 4 ILE A 452 ASP A 456 -1 O TRP A 455 N VAL A 443
SHEET 4 AA6 4 CYS A 462 LEU A 466 -1 O LEU A 466 N ILE A 452
SHEET 1 AA7 4 VAL A 473 PHE A 478 0
SHEET 2 AA7 4 ARG A 482 ALA A 487 -1 O VAL A 484 N ARG A 477
SHEET 3 AA7 4 LYS A 491 ASP A 496 -1 O TRP A 495 N ILE A 483
SHEET 4 AA7 4 CYS A 511 VAL A 516 -1 O LEU A 515 N ILE A 492
SHEET 1 AA8 3 ILE B 13 VAL B 16 0
SHEET 2 AA8 3 ILE B 4 SER B 8 -1 N ILE B 4 O VAL B 16
SHEET 3 AA8 3 VAL B 39 LEU B 41 1 O LEU B 41 N GLN B 7
LINK C ASP C 32 N SEP C 33 1555 1555 1.33
LINK C SEP C 33 N GLY C 34 1555 1555 1.33
CISPEP 1 ASP B 37 PRO B 38 0 -6.17
SITE 1 AC1 14 ARG A 330 LEU A 340 ASN A 341 THR A 342
SITE 2 AC1 14 ASN A 394 GLY A 408 ARG A 431 GLY A 432
SITE 3 AC1 14 ILE A 433 ALA A 434 SER A 448 ILE C 35
SITE 4 AC1 14 HIS C 36 SER C 37
SITE 1 AC2 5 ARG A 477 PHE A 478 GLN A 526 PHE A 527
SITE 2 AC2 5 HOH A 707
CRYST1 82.530 82.530 111.260 90.00 90.00 120.00 P 31 3
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 0.012117 0.006996 0.000000 0.00000
SCALE2 0.000000 0.013991 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008988 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
