HEADER TRANSCRIPTION/DNA 03-OCT-11 3U2B
TITLE STRUCTURE OF THE SOX4 HMG DOMAIN BOUND TO DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*GP*TP*CP*TP*CP*TP*AP*TP*TP*GP*TP*CP*CP*TP*GP*G)-
COMPND 3 3');
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SEQUENCE DERIVED FROM THE LAMA1 GENE;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(*CP*CP*AP*GP*GP*AP*CP*AP*AP*TP*AP*GP*AP*GP*AP*C)-
COMPND 9 3');
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES;
COMPND 12 OTHER_DETAILS: SEQUENCE DERIVED FROM THE LAMA1 GENE;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: TRANSCRIPTION FACTOR SOX-4;
COMPND 15 CHAIN: C;
COMPND 16 FRAGMENT: UNP RESIDUES 57-135;
COMPND 17 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHETIC DNA;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 OTHER_DETAILS: SYNTHETIC DNA;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 9 ORGANISM_COMMON: MOUSE;
SOURCE 10 ORGANISM_TAXID: 10090;
SOURCE 11 GENE: SOX4, SOX-4;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS HMG DOMAIN, TRANSCRIPTIONAL REGULATION, TRANSCRIPTION-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.JAUCH,C.K.L.NG,P.R.KOLATKAR
REVDAT 3 20-MAR-24 3U2B 1 REMARK
REVDAT 2 12-MAR-14 3U2B 1 JRNL
REVDAT 1 28-DEC-11 3U2B 0
JRNL AUTH R.JAUCH,C.K.L.NG,K.NARASIMHAN,P.R.KOLATKAR
JRNL TITL THE CRYSTAL STRUCTURE OF THE SOX4 HMG DOMAIN-DNA COMPLEX
JRNL TITL 2 SUGGESTS A MECHANISM FOR POSITIONAL INTERDEPENDENCE IN DNA
JRNL TITL 3 RECOGNITION
JRNL REF BIOCHEM.J. V. 443 39 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22181698
JRNL DOI 10.1042/BJ20111768
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.220
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 6855
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.490
REMARK 3 FREE R VALUE TEST SET COUNT : 376
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 43.7388 - 3.4642 0.94 2227 127 0.1908 0.2385
REMARK 3 2 3.4642 - 2.7498 0.97 2192 127 0.2791 0.2992
REMARK 3 3 2.7498 - 2.4022 0.92 2060 122 0.3591 0.4502
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 : 0.26
REMARK 3 B_SOL : 29.21
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.57
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.89
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.00610
REMARK 3 B22 (A**2) : 2.00610
REMARK 3 B33 (A**2) : -4.01220
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 : 0.003 1399
REMARK 3 ANGLE : 0.698 2014
REMARK 3 CHIRALITY : 0.037 212
REMARK 3 PLANARITY : 0.003 146
REMARK 3 DIHEDRAL : 24.890 587
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 11
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 1:10)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.5302 -7.5161 -8.4456
REMARK 3 T TENSOR
REMARK 3 T11: 0.6340 T22: 0.4538
REMARK 3 T33: 0.2204 T12: 0.2218
REMARK 3 T13: 0.1990 T23: 0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 7.6374 L22: 1.5972
REMARK 3 L33: 7.4450 L12: -1.2494
REMARK 3 L13: -5.6314 L23: 0.9629
REMARK 3 S TENSOR
REMARK 3 S11: -0.8943 S12: -0.2544 S13: -0.2371
REMARK 3 S21: 0.1673 S22: 0.3079 S23: -0.4225
REMARK 3 S31: 2.8629 S32: 1.2355 S33: 0.5651
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 11:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8510 -19.5895 8.9273
REMARK 3 T TENSOR
REMARK 3 T11: 0.9253 T22: 0.5692
REMARK 3 T33: 0.3341 T12: -0.2281
REMARK 3 T13: -0.2215 T23: 0.1895
REMARK 3 L TENSOR
REMARK 3 L11: 2.8597 L22: 1.1632
REMARK 3 L33: 6.6135 L12: 0.8426
REMARK 3 L13: -2.1481 L23: 1.5653
REMARK 3 S TENSOR
REMARK 3 S11: 0.5902 S12: -0.6225 S13: -1.0452
REMARK 3 S21: 0.2513 S22: 0.0523 S23: 0.7233
REMARK 3 S31: 1.5990 S32: 0.3340 S33: -0.2603
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 1:11)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.0406 -11.4428 2.3563
REMARK 3 T TENSOR
REMARK 3 T11: 0.5272 T22: 0.5327
REMARK 3 T33: 0.2119 T12: -0.2526
REMARK 3 T13: -0.0103 T23: 0.1182
REMARK 3 L TENSOR
REMARK 3 L11: 2.6121 L22: 2.9649
REMARK 3 L33: 1.2445 L12: -0.9410
REMARK 3 L13: 0.7600 L23: 1.4230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0847 S12: 0.7993 S13: -0.2328
REMARK 3 S21: 0.2106 S22: -0.1775 S23: 0.0518
REMARK 3 S31: 0.6691 S32: 0.4062 S33: 0.1627
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 12:16)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.6440 -4.8566 -16.7356
REMARK 3 T TENSOR
REMARK 3 T11: 0.6263 T22: 0.6622
REMARK 3 T33: 0.5988 T12: 0.0048
REMARK 3 T13: 0.4617 T23: -0.1776
REMARK 3 L TENSOR
REMARK 3 L11: 6.0928 L22: 3.7013
REMARK 3 L33: 2.7565 L12: -2.0125
REMARK 3 L13: -0.3851 L23: 1.2465
REMARK 3 S TENSOR
REMARK 3 S11: -1.2034 S12: 0.7565 S13: 0.0544
REMARK 3 S21: 0.2181 S22: 0.5447 S23: -0.2486
REMARK 3 S31: 0.7093 S32: -0.3444 S33: 0.2063
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN C AND RESID 1:7)
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1041 -14.6357 -5.6810
REMARK 3 T TENSOR
REMARK 3 T11: 0.4437 T22: 0.9623
REMARK 3 T33: 0.2836 T12: -0.5075
REMARK 3 T13: -0.3428 T23: 0.2268
REMARK 3 L TENSOR
REMARK 3 L11: 9.6933 L22: 3.8631
REMARK 3 L33: 4.1938 L12: -2.9901
REMARK 3 L13: 5.0092 L23: -2.5760
REMARK 3 S TENSOR
REMARK 3 S11: -0.0264 S12: -0.1858 S13: -0.4912
REMARK 3 S21: 1.1903 S22: -0.3155 S23: -0.0117
REMARK 3 S31: -0.5069 S32: -0.8782 S33: 0.6314
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN C AND RESID 8:13)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.6968 -1.2435 -0.1227
REMARK 3 T TENSOR
REMARK 3 T11: 0.0463 T22: 0.8696
REMARK 3 T33: 0.1220 T12: -0.0530
REMARK 3 T13: -0.0449 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.8325 L22: 3.7934
REMARK 3 L33: 5.1385 L12: 2.7483
REMARK 3 L13: -1.8277 L23: -0.4493
REMARK 3 S TENSOR
REMARK 3 S11: 0.4217 S12: 0.4815 S13: 0.2950
REMARK 3 S21: 0.4255 S22: -0.6231 S23: 0.7407
REMARK 3 S31: 0.2253 S32: -1.5636 S33: 0.1027
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN C AND RESID 14:25)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5422 6.2999 -9.3945
REMARK 3 T TENSOR
REMARK 3 T11: 0.2092 T22: 0.8143
REMARK 3 T33: 0.2387 T12: 0.0845
REMARK 3 T13: 0.0578 T23: 0.1743
REMARK 3 L TENSOR
REMARK 3 L11: 0.5174 L22: 2.1135
REMARK 3 L33: 6.3302 L12: 0.6392
REMARK 3 L13: -1.4106 L23: -2.4776
REMARK 3 S TENSOR
REMARK 3 S11: 0.1308 S12: 1.0269 S13: 0.0636
REMARK 3 S21: 0.1178 S22: 0.7733 S23: 0.3393
REMARK 3 S31: 0.1043 S32: -2.4853 S33: -0.7255
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN C AND RESID 26:30)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.1498 5.5569 -12.6161
REMARK 3 T TENSOR
REMARK 3 T11: 0.5927 T22: 0.7689
REMARK 3 T33: 0.5795 T12: -0.0314
REMARK 3 T13: 0.1466 T23: 0.1935
REMARK 3 L TENSOR
REMARK 3 L11: 7.8883 L22: 9.3547
REMARK 3 L33: 1.1835 L12: -5.8112
REMARK 3 L13: 1.5636 L23: -3.2327
REMARK 3 S TENSOR
REMARK 3 S11: 1.1757 S12: 1.4909 S13: 0.7496
REMARK 3 S21: -0.8439 S22: -0.9111 S23: -0.3870
REMARK 3 S31: 0.3114 S32: -0.0050 S33: 0.1848
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 31:54)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.4696 4.7899 3.1427
REMARK 3 T TENSOR
REMARK 3 T11: -0.0992 T22: 0.2222
REMARK 3 T33: -0.5290 T12: 0.1589
REMARK 3 T13: -0.2474 T23: 0.4858
REMARK 3 L TENSOR
REMARK 3 L11: 0.3476 L22: 3.3255
REMARK 3 L33: 2.1810 L12: -0.7507
REMARK 3 L13: 1.4596 L23: -1.0877
REMARK 3 S TENSOR
REMARK 3 S11: 0.1477 S12: 0.0320 S13: 0.7666
REMARK 3 S21: 1.3762 S22: -1.1691 S23: 2.1082
REMARK 3 S31: -1.3788 S32: -4.3178 S33: -0.8130
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 55:65)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2748 -11.3080 0.0428
REMARK 3 T TENSOR
REMARK 3 T11: 0.4583 T22: 1.9028
REMARK 3 T33: 0.1521 T12: -0.7068
REMARK 3 T13: -0.0614 T23: 0.1109
REMARK 3 L TENSOR
REMARK 3 L11: 0.9268 L22: 5.4698
REMARK 3 L33: 3.8632 L12: -1.5190
REMARK 3 L13: -1.0066 L23: 0.0452
REMARK 3 S TENSOR
REMARK 3 S11: -0.3030 S12: -0.1664 S13: 0.0360
REMARK 3 S21: -1.5723 S22: 1.1893 S23: -0.6565
REMARK 3 S31: 0.7749 S32: -2.7487 S33: -0.9329
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 66:76)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2937 -21.4458 -2.2962
REMARK 3 T TENSOR
REMARK 3 T11: 2.2215 T22: 0.5172
REMARK 3 T33: 0.3913 T12: -0.2727
REMARK 3 T13: -0.1977 T23: -0.1352
REMARK 3 L TENSOR
REMARK 3 L11: 8.4039 L22: 0.8012
REMARK 3 L33: 5.7957 L12: -0.9141
REMARK 3 L13: -6.9038 L23: 0.6608
REMARK 3 S TENSOR
REMARK 3 S11: -1.5004 S12: 0.8187 S13: -0.7454
REMARK 3 S21: 1.3108 S22: 0.7501 S23: 0.0039
REMARK 3 S31: 2.2174 S32: -1.1047 S33: 0.8168
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 3U2B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-11.
REMARK 100 THE DEPOSITION ID IS D_1000068216.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK DOUBLE CRYSTAL
REMARK 200 SAGITTAL FOCUSING MONOCHROMATOR
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 : 7040
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.2, 20% PEG 3350 PH
REMARK 280 7.2, 50MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-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 42.13667
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 21.06833
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 21.06833
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.13667
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: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 LYS C 77
REMARK 465 VAL C 78
REMARK 465 LYS C 79
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC B 1 C3' - C2' - C1' ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR C 72 82.08 -69.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F27 RELATED DB: PDB
REMARK 900 RELATED ID: 1GT0 RELATED DB: PDB
DBREF 3U2B A 1 16 PDB 3U2B 3U2B 1 16
DBREF 3U2B B 1 16 PDB 3U2B 3U2B 1 16
DBREF 3U2B C 1 79 UNP Q06831 SOX4_MOUSE 57 135
SEQRES 1 A 16 DG DT DC DT DC DT DA DT DT DG DT DC DC
SEQRES 2 A 16 DT DG DG
SEQRES 1 B 16 DC DC DA DG DG DA DC DA DA DT DA DG DA
SEQRES 2 B 16 DG DA DC
SEQRES 1 C 79 GLY HIS ILE LYS ARG PRO MET ASN ALA PHE MET VAL TRP
SEQRES 2 C 79 SER GLN ILE GLU ARG ARG LYS ILE MET GLU GLN SER PRO
SEQRES 3 C 79 ASP MET HIS ASN ALA GLU ILE SER LYS ARG LEU GLY LYS
SEQRES 4 C 79 ARG TRP LYS LEU LEU LYS ASP SER ASP LYS ILE PRO PHE
SEQRES 5 C 79 ILE GLN GLU ALA GLU ARG LEU ARG LEU LYS HIS MET ALA
SEQRES 6 C 79 ASP TYR PRO ASP TYR LYS TYR ARG PRO ARG LYS LYS VAL
SEQRES 7 C 79 LYS
FORMUL 4 HOH *8(H2 O)
HELIX 1 1 ASN C 8 GLU C 23 1 16
HELIX 2 2 HIS C 29 LEU C 44 1 16
HELIX 3 3 LYS C 45 TYR C 67 1 23
CRYST1 69.941 69.941 63.205 90.00 90.00 120.00 P 32 2 1 6
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 0.014298 0.008255 0.000000 0.00000
SCALE2 0.000000 0.016510 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015822 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
