Header list of 1s5r.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 21-JAN-04 1S5R
TITLE SOLUTION STRUCTURE OF HBP1 SID-MSIN3A PAH2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIGH MOBILITY GROUP BOX TRANSCRIPTION FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SIN3 INTERACTION DOMAIN, RESIDUES 6 TO 21;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SIN3A PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: PAIRED AMPHIPATHIC HELIX 2, (PAH2 REPEAT), RESIDUES 295 TO
COMPND 10 383;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE SEQUENCE WAS SYNTHESIZED USING AUTOMATED
SOURCE 4 METHODS. THE SEQUENCE IS NATURALLY FOUND IN MUS MUSCULUS (MOUSE).;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 7 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 8 ORGANISM_TAXID: 10090;
SOURCE 9 GENE: SIN3A;
SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 12 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PET24
KEYWDS PROTEIN-PEPTIDE COMPLEX, AMPHIPATHIC HELIX MOTIF, FOUR-HELIX BUNDLE,
KEYWDS 2 REPRESSOR-COREPRESSOR COMPLEX, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.A.SWANSON,P.S.KNOEPFLER,K.HUANG,R.S.KANG,S.M.COWLEY,C.D.LAHERTY,
AUTHOR 2 R.N.EISENMAN,I.RADHAKRISHNAN
REVDAT 4 02-MAR-22 1S5R 1 REMARK
REVDAT 3 24-FEB-09 1S5R 1 VERSN
REVDAT 2 03-AUG-04 1S5R 1 JRNL
REVDAT 1 06-JUL-04 1S5R 0
JRNL AUTH K.A.SWANSON,P.S.KNOEPFLER,K.HUANG,R.S.KANG,S.M.COWLEY,
JRNL AUTH 2 C.D.LAHERTY,R.N.EISENMAN,I.RADHAKRISHNAN
JRNL TITL HBP1 AND MAD1 REPRESSORS BIND THE SIN3 COREPRESSOR PAH2
JRNL TITL 2 DOMAIN WITH OPPOSITE HELICAL ORIENTATIONS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 738 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15235594
JRNL DOI 10.1038/NSMB798
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, ARIA 1.2, CNS 1.1
REMARK 3 AUTHORS : VARIAN NMR INC (VNMR), LINGE, NILGES (ARIA),
REMARK 3 BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1S5R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000021401.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 20 MM SODIUM PHOSPHATE, PH 6,
REMARK 210 0.2% NAN3
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.1 MM 1:1 SID UNLABELED, PAH2 U
REMARK 210 -15N; 1.4 MM 1:1 SID UNLABELED,
REMARK 210 PAH2 U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D_DOUBLE_HALF-
REMARK 210 FILTERED_NOESY; 3D_13C-FILTERED,
REMARK 210 13C-EDITED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMERS ARE THE
REMARK 210 20 STRUCTURES WITH THE LOWEST
REMARK 210 RESTRAINT ENERGIES, RESTRAINT
REMARK 210 VIOLATIONS, AND RMS DEVIATIONS
REMARK 210 FROM IDEAL COVALENT GEOMETRY.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 1 PRO A 361 -170.34 -62.18
REMARK 500 1 SER A 364 -83.89 -128.38
REMARK 500 1 SER A 365 19.28 -161.10
REMARK 500 1 ASN B 298 -20.11 -145.07
REMARK 500 1 GLN B 300 72.90 57.25
REMARK 500 1 PHE B 304 -77.08 -60.22
REMARK 500 1 PHE B 318 35.66 -91.24
REMARK 500 1 LYS B 367 -73.83 -123.36
REMARK 500 2 PRO A 361 -164.51 -72.78
REMARK 500 2 ASP A 363 -53.06 -167.79
REMARK 500 2 SER A 364 6.39 177.14
REMARK 500 2 GLN A 376 -85.38 -54.42
REMARK 500 2 ARG A 377 -158.66 50.94
REMARK 500 2 ALA A 379 -87.50 60.42
REMARK 500 2 GLN B 297 9.82 -162.48
REMARK 500 2 ASN B 299 102.27 60.21
REMARK 500 2 PHE B 318 31.59 -81.62
REMARK 500 2 THR B 354 -164.18 -113.06
REMARK 500 2 LYS B 367 -80.37 -133.89
REMARK 500 3 MET A 362 -71.52 -59.56
REMARK 500 3 ASP A 363 -40.65 -174.42
REMARK 500 3 SER A 365 92.05 -175.03
REMARK 500 3 GLN A 376 -82.51 -57.05
REMARK 500 3 ALA A 379 -30.06 -147.14
REMARK 500 3 GLN B 297 -36.65 -130.86
REMARK 500 3 ASN B 299 97.29 61.45
REMARK 500 3 PRO B 301 93.75 -65.05
REMARK 500 3 PHE B 318 33.08 -84.38
REMARK 500 3 ASN B 348 13.93 59.81
REMARK 500 3 LYS B 367 -78.16 -129.25
REMARK 500 3 PRO B 381 108.71 -48.79
REMARK 500 4 PRO A 361 -162.24 -69.17
REMARK 500 4 ASP A 363 -71.50 -171.13
REMARK 500 4 SER A 364 20.55 -174.96
REMARK 500 4 LEU B 296 100.73 60.70
REMARK 500 4 GLN B 297 -42.95 -163.61
REMARK 500 4 PHE B 318 42.80 -86.71
REMARK 500 4 PRO B 351 170.67 -56.36
REMARK 500 4 ALA B 352 -69.44 -98.41
REMARK 500 4 LYS B 367 -82.87 -137.40
REMARK 500 4 GLN B 369 58.14 -98.32
REMARK 500 5 PRO A 361 -172.29 -62.16
REMARK 500 5 ASP A 363 -72.08 -170.70
REMARK 500 5 SER A 364 9.62 -160.58
REMARK 500 5 GLN A 376 -82.97 -59.94
REMARK 500 5 ARG A 377 -168.24 53.49
REMARK 500 5 ASN B 299 -71.68 -137.76
REMARK 500 5 PHE B 304 -76.94 -58.05
REMARK 500 5 HIS B 306 -74.63 -59.24
REMARK 500 5 THR B 354 -166.06 -111.25
REMARK 500
REMARK 500 THIS ENTRY HAS 208 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1S5Q RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF MAD1 SID-MSIN3A PAH2 COMPLEX
DBREF 1S5R A 358 380 UNP Q8BUS3 Q8BUS3_MOUSE 358 380
DBREF 1S5R B 295 383 UNP Q60520 SIN3A_MOUSE 295 383
SEQRES 1 A 23 ASP PHE THR PRO MET ASP SER SER ALA VAL TYR VAL LEU
SEQRES 2 A 23 SER SER MET ALA ARG GLN ARG ARG ALA SER
SEQRES 1 B 89 SER LEU GLN ASN ASN GLN PRO VAL GLU PHE ASN HIS ALA
SEQRES 2 B 89 ILE ASN TYR VAL ASN LYS ILE LYS ASN ARG PHE GLN GLY
SEQRES 3 B 89 GLN PRO ASP ILE TYR LYS ALA PHE LEU GLU ILE LEU HIS
SEQRES 4 B 89 THR TYR GLN LYS GLU GLN ARG ASN ALA LYS GLU ALA GLY
SEQRES 5 B 89 GLY ASN TYR THR PRO ALA LEU THR GLU GLN GLU VAL TYR
SEQRES 6 B 89 ALA GLN VAL ALA ARG LEU PHE LYS ASN GLN GLU ASP LEU
SEQRES 7 B 89 LEU SER GLU PHE GLY GLN PHE LEU PRO ASP ALA
HELIX 1 1 SER A 365 ARG A 375 1 11
HELIX 2 2 VAL B 302 ARG B 317 1 16
HELIX 3 3 PRO B 322 ALA B 345 1 24
HELIX 4 4 GLU B 355 LEU B 365 1 11
HELIX 5 5 ASP B 371 PHE B 379 1 9
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - r 2 2 Bytes