HEADER TRANSCRIPTION 11-OCT-11 3U5N
TITLE CRYSTAL STRUCTURE OF THE COMPLEX OF TRIM33 PHD-BROMO AND H3(1-20)
TITLE 2 K9ME3K14AC HISTONE PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE TRIM33;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: THE C-TERMINAL PHD AND BROMO DUAL DOMAINS OF TRIM33, UNP
COMPND 5 RESIDUES 882-1087;
COMPND 6 SYNONYM: ECTODERMIN HOMOLOG, RET-FUSED GENE 7 PROTEIN, PROTEIN RFG7,
COMPND 7 TRANSCRIPTION INTERMEDIARY FACTOR 1-GAMMA, TIF1-GAMMA, TRIPARTITE
COMPND 8 MOTIF-CONTAINING PROTEIN 33;
COMPND 9 EC: 6.3.2.-;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: HISTONE H3.1;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: N-TERMINAL HISTONE H3 PEPTIDE CONTAINING TRIMETHYLATED K9
COMPND 15 AND ACETYLATED K14, UNP RESIDUES 2-21;
COMPND 16 SYNONYM: HISTONE H3;
COMPND 17 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: TRIM33, KIAA1113, RFG7, TIF1G;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSFDUET-1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS
KEYWDS TRIM33, PHD, BROMODOMAIN, TGF-BETA, EPIGENETICS, HISTONE,
KEYWDS 2 METHYLATION, K9ME3, K14AC, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,D.J.PATEL
REVDAT 3 06-DEC-23 3U5N 1 REMARK
REVDAT 2 13-SEP-23 3U5N 1 REMARK SEQADV LINK
REVDAT 1 18-JAN-12 3U5N 0
JRNL AUTH Q.XI,Z.WANG,A.I.ZAROMYTIDOU,X.H.ZHANG,L.F.CHOW-TSANG,
JRNL AUTH 2 J.X.LIU,H.KIM,A.BARLAS,K.MANOVA-TODOROVA,V.KAARTINEN,
JRNL AUTH 3 L.STUDER,W.MARK,D.J.PATEL,J.MASSAGUE
JRNL TITL A POISED CHROMATIN PLATFORM FOR TGF-BETA ACCESS TO MASTER
JRNL TITL 2 REGULATORS
JRNL REF CELL(CAMBRIDGE,MASS.) V. 147 1511 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 22196728
JRNL DOI 10.1016/J.CELL.2011.11.032
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 32513
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1651
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 29.7952 - 4.4522 0.93 2628 132 0.1954 0.2573
REMARK 3 2 4.4522 - 3.5357 0.96 2576 148 0.1804 0.2091
REMARK 3 3 3.5357 - 3.0893 0.97 2591 130 0.1956 0.2532
REMARK 3 4 3.0893 - 2.8071 0.98 2574 163 0.2239 0.2787
REMARK 3 5 2.8071 - 2.6060 0.99 2632 107 0.2076 0.3119
REMARK 3 6 2.6060 - 2.4524 0.99 2582 131 0.2043 0.2637
REMARK 3 7 2.4524 - 2.3296 0.99 2585 148 0.2040 0.2569
REMARK 3 8 2.3296 - 2.2283 0.99 2565 158 0.1934 0.2307
REMARK 3 9 2.2283 - 2.1425 0.99 2597 136 0.2026 0.2220
REMARK 3 10 2.1425 - 2.0686 1.00 2579 140 0.2121 0.2907
REMARK 3 11 2.0686 - 2.0039 0.99 2591 126 0.2461 0.3466
REMARK 3 12 2.0039 - 1.9500 0.91 2362 132 0.2902 0.3564
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.39
REMARK 3 B_SOL : 45.93
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.81890
REMARK 3 B22 (A**2) : 19.41680
REMARK 3 B33 (A**2) : -8.59790
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 3295
REMARK 3 ANGLE : 1.083 4446
REMARK 3 CHIRALITY : 0.082 484
REMARK 3 PLANARITY : 0.005 570
REMARK 3 DIHEDRAL : 18.521 1250
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 883:932)
REMARK 3 ORIGIN FOR THE GROUP (A): 1.6079 -10.5945 4.1595
REMARK 3 T TENSOR
REMARK 3 T11: 0.1375 T22: 0.2143
REMARK 3 T33: 0.1830 T12: 0.0487
REMARK 3 T13: -0.0026 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.0711 L22: 0.0887
REMARK 3 L33: 0.0349 L12: -0.0549
REMARK 3 L13: -0.0191 L23: 0.0219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0043 S12: -0.1327 S13: 0.1125
REMARK 3 S21: -0.0057 S22: -0.0222 S23: -0.1708
REMARK 3 S31: 0.0608 S32: 0.3252 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 933:975)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8088 -3.8908 -2.4676
REMARK 3 T TENSOR
REMARK 3 T11: 0.1549 T22: 0.1967
REMARK 3 T33: 0.1667 T12: 0.0615
REMARK 3 T13: 0.0341 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 0.0318 L22: 0.0637
REMARK 3 L33: 0.0283 L12: 0.0142
REMARK 3 L13: 0.0144 L23: 0.0164
REMARK 3 S TENSOR
REMARK 3 S11: 0.0696 S12: 0.3411 S13: -0.0384
REMARK 3 S21: -0.1478 S22: -0.2030 S23: -0.2204
REMARK 3 S31: 0.1326 S32: 0.2393 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 976:1087)
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2058 -14.4143 8.2142
REMARK 3 T TENSOR
REMARK 3 T11: 0.1454 T22: 0.1277
REMARK 3 T33: 0.1077 T12: 0.0056
REMARK 3 T13: 0.0014 T23: -0.0132
REMARK 3 L TENSOR
REMARK 3 L11: 0.2172 L22: 0.3998
REMARK 3 L33: 0.1856 L12: -0.0157
REMARK 3 L13: -0.0798 L23: 0.0879
REMARK 3 S TENSOR
REMARK 3 S11: 0.0360 S12: 0.0712 S13: -0.0348
REMARK 3 S21: 0.0013 S22: -0.0455 S23: -0.0008
REMARK 3 S31: -0.0186 S32: -0.1172 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'J'
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9984 -18.0518 8.1439
REMARK 3 T TENSOR
REMARK 3 T11: 0.2419 T22: 0.6052
REMARK 3 T33: 0.3486 T12: 0.0725
REMARK 3 T13: -0.0012 T23: 0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 0.0195 L22: 0.0100
REMARK 3 L33: 0.0131 L12: -0.0109
REMARK 3 L13: 0.0076 L23: 0.0127
REMARK 3 S TENSOR
REMARK 3 S11: -0.0170 S12: -0.0247 S13: -0.1044
REMARK 3 S21: 0.0522 S22: 0.0257 S23: 0.0882
REMARK 3 S31: -0.0388 S32: 0.0240 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 883:912)
REMARK 3 ORIGIN FOR THE GROUP (A): -27.4786 -37.2241 -3.6895
REMARK 3 T TENSOR
REMARK 3 T11: 0.2088 T22: 0.3085
REMARK 3 T33: 0.3347 T12: -0.0023
REMARK 3 T13: -0.0437 T23: 0.1118
REMARK 3 L TENSOR
REMARK 3 L11: 0.0206 L22: 0.0269
REMARK 3 L33: 0.0234 L12: 0.0094
REMARK 3 L13: 0.0057 L23: 0.0124
REMARK 3 S TENSOR
REMARK 3 S11: -0.0575 S12: -0.0717 S13: 0.0233
REMARK 3 S21: -0.0149 S22: -0.0177 S23: 0.1198
REMARK 3 S31: -0.2105 S32: -0.2227 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 913:975)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.9934 -47.6926 2.5018
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: -0.4616
REMARK 3 T33: -0.2519 T12: -0.3581
REMARK 3 T13: 0.0992 T23: 0.8691
REMARK 3 L TENSOR
REMARK 3 L11: 0.0235 L22: 0.0016
REMARK 3 L33: 0.0491 L12: -0.0290
REMARK 3 L13: -0.0638 L23: 0.0083
REMARK 3 S TENSOR
REMARK 3 S11: 0.5395 S12: -0.3583 S13: -0.3699
REMARK 3 S21: -0.0793 S22: -0.0488 S23: 0.2221
REMARK 3 S31: 0.2987 S32: -0.3255 S33: -0.0000
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 976:1009)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.3601 -38.7879 -12.3099
REMARK 3 T TENSOR
REMARK 3 T11: 0.2383 T22: 0.2924
REMARK 3 T33: 0.2370 T12: -0.0192
REMARK 3 T13: 0.0140 T23: 0.0235
REMARK 3 L TENSOR
REMARK 3 L11: 0.0210 L22: 0.0190
REMARK 3 L33: 0.0432 L12: 0.0396
REMARK 3 L13: 0.0166 L23: -0.0218
REMARK 3 S TENSOR
REMARK 3 S11: 0.0890 S12: 0.4844 S13: 0.0016
REMARK 3 S21: -0.0257 S22: 0.0752 S23: -0.0411
REMARK 3 S31: -0.1293 S32: 0.0376 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1010:1020)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.1845 -54.5271 -3.3318
REMARK 3 T TENSOR
REMARK 3 T11: 0.3918 T22: 0.1404
REMARK 3 T33: 0.6668 T12: -0.0010
REMARK 3 T13: -0.1144 T23: 0.0507
REMARK 3 L TENSOR
REMARK 3 L11: -0.0052 L22: -0.0024
REMARK 3 L33: 0.0007 L12: -0.0037
REMARK 3 L13: 0.0032 L23: 0.0068
REMARK 3 S TENSOR
REMARK 3 S11: -0.0047 S12: 0.0768 S13: -0.0522
REMARK 3 S21: -0.1740 S22: 0.0637 S23: 0.0344
REMARK 3 S31: 0.1816 S32: -0.0569 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1021:1048)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.5119 -34.5480 -7.4648
REMARK 3 T TENSOR
REMARK 3 T11: 0.1977 T22: 0.1935
REMARK 3 T33: 0.2180 T12: 0.0022
REMARK 3 T13: -0.0030 T23: 0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 0.0499 L22: 0.0050
REMARK 3 L33: 0.0241 L12: 0.0125
REMARK 3 L13: 0.0318 L23: 0.0081
REMARK 3 S TENSOR
REMARK 3 S11: 0.0702 S12: -0.1196 S13: 0.0127
REMARK 3 S21: 0.1500 S22: -0.0358 S23: -0.1358
REMARK 3 S31: -0.1808 S32: 0.0687 S33: 0.0000
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 1049:1087)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6038 -33.9745 2.6791
REMARK 3 T TENSOR
REMARK 3 T11: 0.2698 T22: 0.3245
REMARK 3 T33: 0.2417 T12: -0.0080
REMARK 3 T13: 0.0200 T23: 0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 0.0802 L22: 0.0250
REMARK 3 L33: 0.0333 L12: -0.0251
REMARK 3 L13: -0.0007 L23: 0.0306
REMARK 3 S TENSOR
REMARK 3 S11: 0.0940 S12: -0.2064 S13: 0.0438
REMARK 3 S21: 0.0910 S22: -0.1664 S23: -0.1373
REMARK 3 S31: -0.1271 S32: -0.0755 S33: -0.0000
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'E'
REMARK 3 ORIGIN FOR THE GROUP (A): -27.6394 -30.7281 -12.0473
REMARK 3 T TENSOR
REMARK 3 T11: 0.2620 T22: 0.3489
REMARK 3 T33: 0.2763 T12: -0.0671
REMARK 3 T13: -0.0091 T23: 0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 0.0255 L22: -0.0238
REMARK 3 L33: -0.0209 L12: 0.0117
REMARK 3 L13: 0.0382 L23: -0.0740
REMARK 3 S TENSOR
REMARK 3 S11: 0.0093 S12: -0.1640 S13: -0.2488
REMARK 3 S21: -0.2577 S22: 0.0211 S23: 0.0840
REMARK 3 S31: -0.3677 S32: -0.0973 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 3U5N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 197
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.28215
REMARK 200 MONOCHROMATOR : SI MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32561
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.49500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: 3U5M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM TARTRATE AND 20%
REMARK 280 PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 48.79300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 19.93050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.86850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 19.93050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.79300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.86850
REMARK 290 SMTRY3 4 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: 1260 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -3.0 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 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: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -2.0 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 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 SER A 881
REMARK 465 ASP A 882
REMARK 465 ASN A 945
REMARK 465 LEU A 946
REMARK 465 GLN A 947
REMARK 465 HIS A 948
REMARK 465 SER A 949
REMARK 465 LYS A 950
REMARK 465 LYS A 951
REMARK 465 GLY A 952
REMARK 465 LYS A 953
REMARK 465 THR A 954
REMARK 465 VAL A 1047
REMARK 465 TYR A 1048
REMARK 465 ALA A 1049
REMARK 465 ASP A 1050
REMARK 465 THR A 1051
REMARK 465 GLN A 1052
REMARK 465 GLU A 1053
REMARK 465 ILE A 1054
REMARK 465 ASN A 1055
REMARK 465 LEU A 1056
REMARK 465 THR C 11
REMARK 465 GLY C 12
REMARK 465 GLY C 13
REMARK 465 ALY C 14
REMARK 465 ALA C 15
REMARK 465 PRO C 16
REMARK 465 ARG C 17
REMARK 465 LYS C 18
REMARK 465 GLN C 19
REMARK 465 LEU C 20
REMARK 465 SER B 881
REMARK 465 ASP B 882
REMARK 465 LEU B 946
REMARK 465 GLN B 947
REMARK 465 HIS B 948
REMARK 465 SER B 949
REMARK 465 LYS B 950
REMARK 465 LYS B 951
REMARK 465 GLY B 952
REMARK 465 LYS B 953
REMARK 465 THR B 954
REMARK 465 ALA B 955
REMARK 465 GLN B 956
REMARK 465 ASP B 1050
REMARK 465 THR B 1051
REMARK 465 GLN B 1052
REMARK 465 GLU B 1053
REMARK 465 ILE B 1054
REMARK 465 ASN B 1055
REMARK 465 LEU B 1056
REMARK 465 LYS B 1057
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 944 CG OD1 OD2
REMARK 470 ASN B 945 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OD1 ASP B 1002 O HOH B 174 1.96
REMARK 500 O HOH B 205 O HOH B 206 2.05
REMARK 500 O HOH A 195 O HOH A 198 2.08
REMARK 500 O LYS B 995 NZ LYS B 998 2.10
REMARK 500 O HOH B 176 O HOH B 201 2.12
REMARK 500 O HOH A 140 O HOH A 178 2.13
REMARK 500 OE1 GLN A 1016 N LEU D 20 2.14
REMARK 500 O HOH A 149 O HOH A 189 2.14
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 VAL A 892 -63.51 -91.24
REMARK 500 ASN A 992 -4.17 74.01
REMARK 500 PRO B 885 45.47 -87.30
REMARK 500 VAL B 892 -63.40 -90.78
REMARK 500 LYS B 904 -60.27 -105.21
REMARK 500 CYS B 943 -59.74 -128.50
REMARK 500 ASN B 992 -4.45 74.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 890 SG
REMARK 620 2 CYS A 893 SG 111.8
REMARK 620 3 HIS A 910 ND1 100.9 95.9
REMARK 620 4 CYS A 913 SG 109.3 119.9 117.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 902 SG
REMARK 620 2 CYS A 905 SG 107.1
REMARK 620 3 CYS A 928 SG 115.1 113.0
REMARK 620 4 CYS A 931 SG 109.1 101.2 110.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 890 SG
REMARK 620 2 CYS B 893 SG 108.0
REMARK 620 3 HIS B 910 ND1 106.8 93.6
REMARK 620 4 CYS B 913 SG 111.3 120.0 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 902 SG
REMARK 620 2 CYS B 905 SG 109.2
REMARK 620 3 CYS B 928 SG 103.9 117.8
REMARK 620 4 CYS B 931 SG 104.4 105.6 115.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U5M RELATED DB: PDB
REMARK 900 RELATED ID: 3U5O RELATED DB: PDB
REMARK 900 RELATED ID: 3U5P RELATED DB: PDB
DBREF 3U5N A 882 1087 UNP Q9UPN9 TRI33_HUMAN 882 1087
DBREF 3U5N C 1 20 UNP P68431 H31_HUMAN 2 21
DBREF 3U5N B 882 1087 UNP Q9UPN9 TRI33_HUMAN 882 1087
DBREF 3U5N D 1 20 UNP P68431 H31_HUMAN 2 21
SEQADV 3U5N SER A 881 UNP Q9UPN9 EXPRESSION TAG
SEQADV 3U5N SER B 881 UNP Q9UPN9 EXPRESSION TAG
SEQRES 1 A 207 SER ASP ASP ASP PRO ASN GLU ASP TRP CYS ALA VAL CYS
SEQRES 2 A 207 GLN ASN GLY GLY ASP LEU LEU CYS CYS GLU LYS CYS PRO
SEQRES 3 A 207 LYS VAL PHE HIS LEU THR CYS HIS VAL PRO THR LEU LEU
SEQRES 4 A 207 SER PHE PRO SER GLY ASP TRP ILE CYS THR PHE CYS ARG
SEQRES 5 A 207 ASP ILE GLY LYS PRO GLU VAL GLU TYR ASP CYS ASP ASN
SEQRES 6 A 207 LEU GLN HIS SER LYS LYS GLY LYS THR ALA GLN GLY LEU
SEQRES 7 A 207 SER PRO VAL ASP GLN ARG LYS CYS GLU ARG LEU LEU LEU
SEQRES 8 A 207 TYR LEU TYR CYS HIS GLU LEU SER ILE GLU PHE GLN GLU
SEQRES 9 A 207 PRO VAL PRO ALA SER ILE PRO ASN TYR TYR LYS ILE ILE
SEQRES 10 A 207 LYS LYS PRO MET ASP LEU SER THR VAL LYS LYS LYS LEU
SEQRES 11 A 207 GLN LYS LYS HIS SER GLN HIS TYR GLN ILE PRO ASP ASP
SEQRES 12 A 207 PHE VAL ALA ASP VAL ARG LEU ILE PHE LYS ASN CYS GLU
SEQRES 13 A 207 ARG PHE ASN GLU MET MET LYS VAL VAL GLN VAL TYR ALA
SEQRES 14 A 207 ASP THR GLN GLU ILE ASN LEU LYS ALA ASP SER GLU VAL
SEQRES 15 A 207 ALA GLN ALA GLY LYS ALA VAL ALA LEU TYR PHE GLU ASP
SEQRES 16 A 207 LYS LEU THR GLU ILE TYR SER ASP ARG THR PHE ALA
SEQRES 1 C 20 ALA ARG THR LYS GLN THR ALA ARG M3L SER THR GLY GLY
SEQRES 2 C 20 ALY ALA PRO ARG LYS GLN LEU
SEQRES 1 B 207 SER ASP ASP ASP PRO ASN GLU ASP TRP CYS ALA VAL CYS
SEQRES 2 B 207 GLN ASN GLY GLY ASP LEU LEU CYS CYS GLU LYS CYS PRO
SEQRES 3 B 207 LYS VAL PHE HIS LEU THR CYS HIS VAL PRO THR LEU LEU
SEQRES 4 B 207 SER PHE PRO SER GLY ASP TRP ILE CYS THR PHE CYS ARG
SEQRES 5 B 207 ASP ILE GLY LYS PRO GLU VAL GLU TYR ASP CYS ASP ASN
SEQRES 6 B 207 LEU GLN HIS SER LYS LYS GLY LYS THR ALA GLN GLY LEU
SEQRES 7 B 207 SER PRO VAL ASP GLN ARG LYS CYS GLU ARG LEU LEU LEU
SEQRES 8 B 207 TYR LEU TYR CYS HIS GLU LEU SER ILE GLU PHE GLN GLU
SEQRES 9 B 207 PRO VAL PRO ALA SER ILE PRO ASN TYR TYR LYS ILE ILE
SEQRES 10 B 207 LYS LYS PRO MET ASP LEU SER THR VAL LYS LYS LYS LEU
SEQRES 11 B 207 GLN LYS LYS HIS SER GLN HIS TYR GLN ILE PRO ASP ASP
SEQRES 12 B 207 PHE VAL ALA ASP VAL ARG LEU ILE PHE LYS ASN CYS GLU
SEQRES 13 B 207 ARG PHE ASN GLU MET MET LYS VAL VAL GLN VAL TYR ALA
SEQRES 14 B 207 ASP THR GLN GLU ILE ASN LEU LYS ALA ASP SER GLU VAL
SEQRES 15 B 207 ALA GLN ALA GLY LYS ALA VAL ALA LEU TYR PHE GLU ASP
SEQRES 16 B 207 LYS LEU THR GLU ILE TYR SER ASP ARG THR PHE ALA
SEQRES 1 D 20 ALA ARG THR LYS GLN THR ALA ARG M3L SER THR GLY GLY
SEQRES 2 D 20 ALY ALA PRO ARG LYS GLN LEU
MODRES 3U5N M3L C 9 LYS N-TRIMETHYLLYSINE
MODRES 3U5N M3L D 9 LYS N-TRIMETHYLLYSINE
MODRES 3U5N ALY D 14 LYS N(6)-ACETYLLYSINE
HET M3L C 9 12
HET M3L D 9 12
HET ALY D 14 12
HET ZN A 1 1
HET ZN A 2 1
HET ZN B 1 1
HET ZN B 2 1
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM ZN ZINC ION
FORMUL 2 M3L 2(C9 H21 N2 O2 1+)
FORMUL 4 ALY C8 H16 N2 O3
FORMUL 5 ZN 4(ZN 2+)
FORMUL 9 HOH *212(H2 O)
HELIX 1 1 SER A 959 CYS A 975 1 17
HELIX 2 2 SER A 979 GLN A 983 5 5
HELIX 3 3 ASN A 992 ILE A 997 1 6
HELIX 4 4 ASP A 1002 GLN A 1011 1 10
HELIX 5 5 ILE A 1020 GLN A 1046 1 27
HELIX 6 6 SER A 1060 TYR A 1081 1 22
HELIX 7 7 SER B 959 HIS B 976 1 18
HELIX 8 8 SER B 979 GLN B 983 5 5
HELIX 9 9 ASN B 992 ILE B 997 1 6
HELIX 10 10 ASP B 1002 LEU B 1010 1 9
HELIX 11 11 ILE B 1020 TYR B 1048 1 29
HELIX 12 12 SER B 1060 TYR B 1081 1 22
HELIX 13 13 THR D 11 ALA D 15 5 5
SHEET 1 A 3 VAL A 908 PHE A 909 0
SHEET 2 A 3 GLY A 897 CYS A 901 -1 N LEU A 900 O PHE A 909
SHEET 3 A 3 ARG C 2 THR C 6 -1 O LYS C 4 N LEU A 899
SHEET 1 B 3 VAL B 908 PHE B 909 0
SHEET 2 B 3 GLY B 897 CYS B 901 -1 N LEU B 900 O PHE B 909
SHEET 3 B 3 THR D 3 THR D 6 -1 O LYS D 4 N LEU B 899
LINK C ARG C 8 N M3L C 9 1555 1555 1.33
LINK C M3L C 9 N SER C 10 1555 1555 1.34
LINK C ARG D 8 N M3L D 9 1555 1555 1.33
LINK C M3L D 9 N SER D 10 1555 1555 1.33
LINK C GLY D 13 N ALY D 14 1555 1555 1.33
LINK C ALY D 14 N ALA D 15 1555 1555 1.33
LINK ZN ZN A 1 SG CYS A 890 1555 1555 2.32
LINK ZN ZN A 1 SG CYS A 893 1555 1555 2.33
LINK ZN ZN A 1 ND1 HIS A 910 1555 1555 2.26
LINK ZN ZN A 1 SG CYS A 913 1555 1555 2.29
LINK ZN ZN A 2 SG CYS A 902 1555 1555 2.36
LINK ZN ZN A 2 SG CYS A 905 1555 1555 2.41
LINK ZN ZN A 2 SG CYS A 928 1555 1555 2.40
LINK ZN ZN A 2 SG CYS A 931 1555 1555 2.46
LINK ZN ZN B 1 SG CYS B 890 1555 1555 2.37
LINK ZN ZN B 1 SG CYS B 893 1555 1555 2.52
LINK ZN ZN B 1 ND1 HIS B 910 1555 1555 2.21
LINK ZN ZN B 1 SG CYS B 913 1555 1555 2.25
LINK ZN ZN B 2 SG CYS B 902 1555 1555 2.48
LINK ZN ZN B 2 SG CYS B 905 1555 1555 2.37
LINK ZN ZN B 2 SG CYS B 928 1555 1555 2.48
LINK ZN ZN B 2 SG CYS B 931 1555 1555 2.38
CISPEP 1 VAL A 915 PRO A 916 0 -1.49
CISPEP 2 VAL B 915 PRO B 916 0 2.36
SITE 1 AC1 4 CYS A 890 CYS A 893 HIS A 910 CYS A 913
SITE 1 AC2 4 CYS A 902 CYS A 905 CYS A 928 CYS A 931
SITE 1 AC3 4 CYS B 890 CYS B 893 HIS B 910 CYS B 913
SITE 1 AC4 4 CYS B 902 CYS B 905 CYS B 928 CYS B 931
CRYST1 97.586 113.737 39.861 90.00 90.00 90.00 P 21 21 21 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 0.010247 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008792 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
