Header list of 1e91.pdb file
Complete list - n 17 2 Bytes
HEADER EUKARYOTIC TRANSCRIPTIONAL REGULATION 04-OCT-00 1E91
TITLE STRUCTURE OF THE COMPLEX OF THE MAD1-SIN3B INTERACTION DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PAIRED AMPHIPATHIC HELIX PROTEIN SIN3B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PAH2 DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: MAD PROTEIN (MAX DIMERIZER);
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: SIN INTERACTION DOMAIN;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: SIN3B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX2T;
SOURCE 11 EXPRESSION_SYSTEM_GENE: SIN3B;
SOURCE 12 MOL_ID: 2;
SOURCE 13 SYNTHETIC: YES;
SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 15 ORGANISM_COMMON: HUMAN;
SOURCE 16 ORGANISM_TAXID: 9606
KEYWDS EUKARYOTIC TRANSCRIPTIONAL REGULATION, SIN3, PAH DOMAINS, MAD1,
KEYWDS 2 PROTEIN-PROTEIN INTERACTIONS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.A.E.M.SPRONK,M.TESSARI,A.M.KAAN,J.F.A.JANSEN,M.VERMEULEN,
AUTHOR 2 H.G.STUNNENBERG,G.W.VUISTER
REVDAT 4 17-JAN-18 1E91 1 SOURCE JRNL
REVDAT 3 24-FEB-09 1E91 1 VERSN
REVDAT 2 07-DEC-00 1E91 1 JRNL
REVDAT 1 20-NOV-00 1E91 0
JRNL AUTH C.A.E.M.SPRONK,M.TESSARI,A.M.KAAN,J.F.A.JANSEN,M.VERMEULEN,
JRNL AUTH 2 H.G.STUNNENBERG,G.W.VUISTER
JRNL TITL THE MAD1-SIN3B INTERACTION INVOLVES A NOVEL HELICAL FOLD
JRNL REF NAT.STRUCT.BIOL. V. 7 1100 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11101889
JRNL DOI 10.1038/81944
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER, A.T. ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE REFINED USING THE
REMARK 3 PROGRAM ARIA 1.0 (NILGES ET AL) FOR ITERATIVE NOE ASSIGNMENT.
REMARK 4
REMARK 4 1E91 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1290005397.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C-NOESY-HSQC; 15N-NOESY-HSQC;
REMARK 210 15N-HMQC-NOESY-HSQC; (13C-
REMARK 210 FILTERED)-NOESY- (13C-EDITED)-
REMARK 210 HSQC; HNCA; HNCO; HN(CO)CA;
REMARK 210 CBCA(CO)NNH; HNCACB; (H)CCH-
REMARK 210 TOCSY; (13C/15N-FILTERED)-NOESY;
REMARK 210 (13C/15N-FILTERED)-TOCSY; HNHA;
REMARK 210 HBHA(CBCACO)NNH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DRX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ARIA ARIA
REMARK 210 METHOD USED : SIMULATED ANNEALING, ITERATIVE
REMARK 210 NOE-ASSIGNMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 30 STRUCTURES WITH NO RESTRAINT
REMARK 210 VIOLATIONS, 20 LOWEST ENERGY
REMARK 210 STRUCTURES FINALLY SELECTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ASP A 3 46.66 -167.60
REMARK 500 1 PHE A 21 40.16 -93.29
REMARK 500 1 HIS A 24 78.53 -105.56
REMARK 500 1 GLU A 41 47.71 -80.36
REMARK 500 1 GLN A 42 -47.08 -142.31
REMARK 500 1 LEU A 43 -145.10 -70.67
REMARK 500 1 HIS A 44 45.57 70.86
REMARK 500 1 THR A 45 -133.22 51.37
REMARK 500 1 PHE A 50 51.63 -179.13
REMARK 500 1 SER A 54 -149.89 -158.75
REMARK 500 1 PHE A 66 42.23 -75.47
REMARK 500 1 GLU A 70 1.70 -63.46
REMARK 500 1 ALA A 83 -145.00 -75.99
REMARK 500 2 SER A 2 -52.20 -161.93
REMARK 500 2 PHE A 21 41.54 -93.70
REMARK 500 2 HIS A 24 78.56 -106.71
REMARK 500 2 HIS A 44 120.96 81.41
REMARK 500 2 THR A 45 -140.68 -66.48
REMARK 500 2 ARG A 51 59.29 -147.99
REMARK 500 2 SER A 54 -154.59 -161.10
REMARK 500 2 PHE A 66 42.25 -75.28
REMARK 500 2 GLN A 69 49.78 -84.15
REMARK 500 2 GLU A 70 6.32 -65.19
REMARK 500 2 LYS A 84 -60.56 -163.02
REMARK 500 3 PHE A 21 43.44 -95.52
REMARK 500 3 HIS A 24 77.51 -107.17
REMARK 500 3 GLU A 41 43.10 -80.17
REMARK 500 3 GLN A 42 -52.11 -152.23
REMARK 500 3 THR A 45 130.27 66.71
REMARK 500 3 LYS A 46 117.42 -177.29
REMARK 500 3 ARG A 51 43.19 -74.66
REMARK 500 3 SER A 54 -144.47 -169.31
REMARK 500 3 PHE A 66 41.19 -74.20
REMARK 500 3 GLU A 70 -5.54 -59.97
REMARK 500 3 ALA A 83 -50.44 -160.86
REMARK 500 3 LYS A 84 -150.71 -72.08
REMARK 500 4 SER A 2 130.23 57.76
REMARK 500 4 ASP A 3 -133.47 -70.86
REMARK 500 4 PHE A 21 38.89 -90.94
REMARK 500 4 HIS A 24 78.69 -105.42
REMARK 500 4 LEU A 43 -147.72 -63.84
REMARK 500 4 HIS A 44 142.11 -178.30
REMARK 500 4 PRO A 49 -160.89 -63.14
REMARK 500 4 PHE A 50 134.02 -173.21
REMARK 500 4 ARG A 51 36.90 -81.31
REMARK 500 4 SER A 54 -145.64 -162.05
REMARK 500 4 PHE A 66 37.47 -73.11
REMARK 500 4 GLN A 69 48.76 -78.04
REMARK 500 4 GLU A 82 -55.16 178.79
REMARK 500 4 LYS A 84 46.39 -175.37
REMARK 500
REMARK 500 THIS ENTRY HAS 246 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5457 RELATED DB: BMRB
DBREF 1E91 A 1 85 UNP Q62141 Q62141 148 232
DBREF 1E91 B 1 13 UNP Q05195 MAD_HUMAN 8 20
SEQADV 1E91 ALA A 83 UNP Q62141 GLY 230 CONFLICT
SEQRES 1 A 85 GLU SER ASP SER VAL GLU PHE ASN ASN ALA ILE SER TYR
SEQRES 2 A 85 VAL ASN LYS ILE LYS THR ARG PHE LEU ASP HIS PRO GLU
SEQRES 3 A 85 ILE TYR ARG SER PHE LEU GLU ILE LEU HIS THR TYR GLN
SEQRES 4 A 85 LYS GLU GLN LEU HIS THR LYS GLY ARG PRO PHE ARG GLY
SEQRES 5 A 85 MET SER GLU GLU GLU VAL PHE THR GLU VAL ALA ASN LEU
SEQRES 6 A 85 PHE ARG GLY GLN GLU ASP LEU LEU SER GLU PHE GLY GLN
SEQRES 7 A 85 PHE LEU PRO GLU ALA LYS ARG
SEQRES 1 B 13 ASN ILE GLN MET LEU LEU GLU ALA ALA ASP TYR LEU GLU
HELIX 1 1 SER A 4 PHE A 21 1 18
HELIX 2 2 HIS A 24 GLU A 41 1 18
HELIX 3 3 SER A 54 PHE A 66 1 13
HELIX 4 4 GLN A 69 LEU A 80 1 12
HELIX 5 5 ASN B 1 GLU B 13 1 13
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 - n 17 2 Bytes