HEADER TRANSCRIPTION 30-MAR-07 2EQR
TITLE SOLUTION STRUCTURE OF THE FIRST SANT DOMAIN FROM HUMAN
TITLE 2 NUCLEAR RECEPTOR COREPRESSOR 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEAR RECEPTOR COREPRESSOR 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SANT DOMAIN;
COMPND 5 SYNONYM: N-COR1, N-COR;
COMPND 6 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: NCOR1;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P061225-49;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS SANT DOMAIN, NUCLEAR RECEPTOR COREPRESSOR 1, N-COR1, N-COR,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.P.ZHANG,F.HAYAHSI,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2EQR 1 VERSN
REVDAT 1 01-APR-08 2EQR 0
JRNL AUTH H.P.ZHANG,F.HAYASHI,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST SANT DOMAIN FROM
JRNL TITL 2 HUMAN NUCLEAR RECEPTOR COREPRESSOR 1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EQR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-07.
REMARK 100 THE RCSB ID CODE IS RCSB026991.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.14MM 13C, 15N-LABELED
REMARK 210 PROTEIN; 20MM D-TRIS-HCL(PH
REMARK 210 7.0); 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY, 3D_
REMARK 210 15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, NMRPIPE 20031121,
REMARK 210 NMRVIEW 5.0.4, KUJIRA 0.9818,
REMARK 210 CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,
REMARK 210 STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, TARGET FUNCTION
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 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 ASN A 13 79.39 -108.32
REMARK 500 1 HIS A 30 77.16 -107.77
REMARK 500 1 LEU A 36 -63.26 -91.10
REMARK 500 1 ILE A 37 -32.66 -39.80
REMARK 500 1 PRO A 47 0.67 -69.79
REMARK 500 1 VAL A 50 -34.25 -39.61
REMARK 500 2 ASP A 8 41.03 -100.40
REMARK 500 2 PHE A 11 160.00 -44.30
REMARK 500 2 MET A 12 157.91 -43.90
REMARK 500 2 TRP A 15 108.03 -47.15
REMARK 500 2 THR A 16 -74.28 -119.33
REMARK 500 2 ASP A 17 -66.31 -126.53
REMARK 500 2 ARG A 43 37.06 -87.91
REMARK 500 3 PHE A 34 -32.19 -38.53
REMARK 500 3 ASN A 59 157.92 -45.79
REMARK 500 4 SER A 6 41.47 35.15
REMARK 500 5 ASN A 13 94.64 -51.06
REMARK 500 5 THR A 16 -75.43 -134.37
REMARK 500 5 ASP A 17 -60.24 -130.42
REMARK 500 5 ASN A 33 113.08 -160.23
REMARK 500 5 ARG A 43 32.93 -88.82
REMARK 500 5 PRO A 47 2.76 -69.74
REMARK 500 6 GLU A 60 94.28 -67.75
REMARK 500 7 SER A 5 101.20 -49.54
REMARK 500 7 PHE A 11 43.02 35.52
REMARK 500 7 MET A 12 46.98 -93.84
REMARK 500 7 ASN A 13 106.21 -174.89
REMARK 500 7 ARG A 43 33.67 -90.34
REMARK 500 7 TYR A 53 -37.42 -39.64
REMARK 500 7 THR A 56 -33.32 -39.10
REMARK 500 8 ARG A 9 170.00 -48.39
REMARK 500 8 ASN A 13 92.44 -66.78
REMARK 500 8 ARG A 43 -67.82 -101.87
REMARK 500 8 LYS A 44 156.63 -38.57
REMARK 500 8 GLU A 60 107.54 -41.02
REMARK 500 9 TRP A 15 100.21 -57.67
REMARK 500 9 LEU A 41 92.94 -67.56
REMARK 500 10 SER A 2 143.19 -34.63
REMARK 500 10 HIS A 18 -72.95 -46.21
REMARK 500 10 LYS A 57 -35.63 -34.61
REMARK 500 10 GLU A 60 44.99 -108.01
REMARK 500 11 ARG A 9 41.38 -99.25
REMARK 500 11 GLN A 10 39.81 37.17
REMARK 500 11 TRP A 15 173.11 -57.72
REMARK 500 11 LEU A 41 -174.64 -56.65
REMARK 500 11 ARG A 43 50.86 75.06
REMARK 500 11 PRO A 47 2.47 -69.74
REMARK 500 11 LYS A 57 119.56 -175.01
REMARK 500 12 SER A 3 173.83 -51.81
REMARK 500 12 THR A 16 -75.44 -111.13
REMARK 500 12 ASP A 17 -53.52 -133.70
REMARK 500 12 PRO A 47 3.20 -69.74
REMARK 500 13 ASP A 8 42.15 -89.92
REMARK 500 13 PHE A 34 -39.07 -37.73
REMARK 500 13 GLU A 42 -76.23 -61.91
REMARK 500 13 LYS A 58 42.13 38.48
REMARK 500 14 SER A 39 -39.20 -39.19
REMARK 500 14 VAL A 50 -39.99 -38.91
REMARK 500 15 ARG A 9 46.06 -96.09
REMARK 500 15 LYS A 24 -70.11 -54.94
REMARK 500 15 GLN A 29 -39.70 -36.47
REMARK 500 15 ARG A 43 45.18 -100.10
REMARK 500 15 THR A 56 -35.34 -37.45
REMARK 500 16 PHE A 27 -39.46 -34.73
REMARK 500 16 HIS A 30 78.69 -108.85
REMARK 500 16 PHE A 34 -33.10 -34.74
REMARK 500 16 LEU A 41 -174.58 -51.79
REMARK 500 16 SER A 45 156.03 -43.75
REMARK 500 17 SER A 2 154.64 -47.57
REMARK 500 17 SER A 3 106.22 -44.12
REMARK 500 17 ARG A 9 -30.80 -36.68
REMARK 500 17 PRO A 47 0.80 -69.80
REMARK 500 17 LYS A 58 38.77 -99.53
REMARK 500 18 PHE A 11 42.00 37.81
REMARK 500 18 HIS A 18 -70.26 -54.93
REMARK 500 19 LYS A 32 37.99 38.64
REMARK 500 19 LEU A 41 -174.82 -54.27
REMARK 500 19 SER A 45 154.27 -40.15
REMARK 500 20 PHE A 11 104.40 -35.49
REMARK 500 20 MET A 12 41.05 -83.18
REMARK 500 20 ASN A 13 128.36 -170.97
REMARK 500 20 GLN A 29 -64.21 -102.60
REMARK 500 20 HIS A 30 78.61 -109.97
REMARK 500 20 GLU A 60 154.75 -44.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSO003013067.1 RELATED DB: TARGETDB
DBREF 2EQR A 8 61 UNP O75376 NCOR1_HUMAN 433 486
SEQADV 2EQR GLY A 1 UNP O75376 EXPRESSION TAG
SEQADV 2EQR SER A 2 UNP O75376 EXPRESSION TAG
SEQADV 2EQR SER A 3 UNP O75376 EXPRESSION TAG
SEQADV 2EQR GLY A 4 UNP O75376 EXPRESSION TAG
SEQADV 2EQR SER A 5 UNP O75376 EXPRESSION TAG
SEQADV 2EQR SER A 6 UNP O75376 EXPRESSION TAG
SEQADV 2EQR GLY A 7 UNP O75376 EXPRESSION TAG
SEQRES 1 A 61 GLY SER SER GLY SER SER GLY ASP ARG GLN PHE MET ASN
SEQRES 2 A 61 VAL TRP THR ASP HIS GLU LYS GLU ILE PHE LYS ASP LYS
SEQRES 3 A 61 PHE ILE GLN HIS PRO LYS ASN PHE GLY LEU ILE ALA SER
SEQRES 4 A 61 TYR LEU GLU ARG LYS SER VAL PRO ASP CYS VAL LEU TYR
SEQRES 5 A 61 TYR TYR LEU THR LYS LYS ASN GLU ASN
HELIX 1 1 THR A 16 HIS A 30 1 15
HELIX 2 2 ASN A 33 LEU A 41 1 9
HELIX 3 3 SER A 45 LYS A 57 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
(ATOM LINES ARE NOT SHOWN.)
END
