Header list of 5gcn.pdb file
Complete list - c 21 2 Bytes
HEADER TRANSFERASE 24-MAR-99 5GCN
TITLE CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN
TITLE 2 COMPLEX WITH COENZYME A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE GCN5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: P55;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: TETRAHYMENA THERMOPHILA;
SOURCE 3 ORGANISM_TAXID: 5911;
SOURCE 4 ORGANELLE: MACRONUCLEUS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET-B
KEYWDS HISTONE ACETYLTRANSFERASE, CHROMATIN REMODELING, TRANSCRIPTION
KEYWDS 2 REGULATION, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR Y.LIN,C.M.FLETCHER,J.ZHOU,C.D.ALLIS,G.WAGNER
REVDAT 5 21-DEC-22 5GCN 1 SEQADV
REVDAT 4 16-MAR-22 5GCN 1 REMARK
REVDAT 3 24-FEB-09 5GCN 1 VERSN
REVDAT 2 20-APR-04 5GCN 1 COMPND SOURCE JRNL HETATM
REVDAT 2 2 1 REMARK
REVDAT 1 19-JUL-99 5GCN 0
JRNL AUTH Y.LIN,C.M.FLETCHER,J.ZHOU,C.D.ALLIS,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF GCN5 HISTONE
JRNL TITL 2 ACETYLTRANSFERASE BOUND TO COENZYME A
JRNL REF NATURE V. 400 86 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10403255
JRNL DOI 10.1038/21922
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5GCN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000717.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 13
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: CLOSE CONTACTS
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 H TYR A 71 O PHE A 76 1.50
REMARK 500 O CYS A 67 H ALA A 80 1.56
REMARK 500 O ASP A 118 H ILE A 122 1.59
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 1 ASN A 12 42.41 -96.03
REMARK 500 1 THR A 15 -80.18 -69.37
REMARK 500 1 HIS A 16 -73.54 176.78
REMARK 500 1 PHE A 29 -74.88 -56.50
REMARK 500 1 ARG A 31 -74.04 -69.77
REMARK 500 1 PRO A 34 80.82 -20.18
REMARK 500 1 LYS A 35 33.29 33.07
REMARK 500 1 ARG A 48 121.87 60.73
REMARK 500 1 HIS A 49 -91.95 44.35
REMARK 500 1 HIS A 50 162.06 58.97
REMARK 500 1 LYS A 57 50.39 -93.65
REMARK 500 1 ASN A 58 24.25 157.08
REMARK 500 1 LYS A 59 -31.52 85.57
REMARK 500 1 ILE A 63 -43.76 -145.16
REMARK 500 1 PHE A 68 -177.97 -171.37
REMARK 500 1 ARG A 69 121.27 -174.16
REMARK 500 1 PHE A 81 152.29 114.71
REMARK 500 1 ALA A 83 135.20 162.96
REMARK 500 1 ALA A 86 -115.48 -28.03
REMARK 500 1 ASN A 87 32.99 -66.56
REMARK 500 1 GLN A 89 -148.57 -67.89
REMARK 500 1 TYR A 93 -56.10 -132.77
REMARK 500 1 TYR A 116 63.08 -112.48
REMARK 500 1 ILE A 122 -72.92 -51.25
REMARK 500 1 PHE A 130 174.55 -49.38
REMARK 500 1 ILE A 145 153.23 85.59
REMARK 500 1 LYS A 146 136.32 59.97
REMARK 500 1 ASP A 147 133.34 61.81
REMARK 500 1 ASP A 149 126.58 63.53
REMARK 500 2 THR A 11 -168.48 -129.29
REMARK 500 2 ASN A 12 46.29 -105.73
REMARK 500 2 THR A 15 -159.48 -113.71
REMARK 500 2 HIS A 16 -65.77 -99.76
REMARK 500 2 PHE A 29 -71.41 -54.19
REMARK 500 2 LEU A 33 76.69 -103.71
REMARK 500 2 ASP A 47 179.93 -53.08
REMARK 500 2 ARG A 48 80.74 -61.10
REMARK 500 2 HIS A 49 108.94 57.84
REMARK 500 2 ASN A 58 23.65 149.78
REMARK 500 2 LYS A 59 -27.48 84.16
REMARK 500 2 GLN A 60 -2.40 -146.39
REMARK 500 2 PHE A 68 -171.90 -176.27
REMARK 500 2 ARG A 69 115.61 -165.93
REMARK 500 2 PRO A 73 47.93 -69.78
REMARK 500 2 GLN A 74 -40.98 -159.49
REMARK 500 2 ARG A 75 11.34 82.67
REMARK 500 2 PHE A 81 146.15 123.43
REMARK 500 2 ALA A 83 -167.47 165.30
REMARK 500 2 ALA A 86 -115.20 -29.88
REMARK 500 2 ASN A 87 32.81 -64.87
REMARK 500
REMARK 500 THIS ENTRY HAS 726 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 201
DBREF 5GCN A 1 166 UNP Q27198 Q27198_TETTH 45 210
SEQADV 5GCN MET A 1 UNP Q27198 ASP 1 CONFLICT
SEQADV 5GCN LYS A 2 UNP Q27198 GLN 2 CONFLICT
SEQADV 5GCN PHE A 46 UNP Q27198 LEU 90 CONFLICT
SEQRES 1 A 166 MET LYS GLY LEU LEU ASP PHE ASP ILE LEU THR ASN ASP
SEQRES 2 A 166 GLY THR HIS ARG ASN MET LYS LEU LEU ILE ASP LEU LYS
SEQRES 3 A 166 ASN ILE PHE SER ARG GLN LEU PRO LYS MET PRO LYS GLU
SEQRES 4 A 166 TYR ILE VAL LYS LEU VAL PHE ASP ARG HIS HIS GLU SER
SEQRES 5 A 166 MET VAL ILE LEU LYS ASN LYS GLN LYS VAL ILE GLY GLY
SEQRES 6 A 166 ILE CYS PHE ARG GLN TYR LYS PRO GLN ARG PHE ALA GLU
SEQRES 7 A 166 VAL ALA PHE LEU ALA VAL THR ALA ASN GLU GLN VAL ARG
SEQRES 8 A 166 GLY TYR GLY THR ARG LEU MET ASN LYS PHE LYS ASP HIS
SEQRES 9 A 166 MET GLN LYS GLN ASN ILE GLU TYR LEU LEU THR TYR ALA
SEQRES 10 A 166 ASP ASN PHE ALA ILE GLY TYR PHE LYS LYS GLN GLY PHE
SEQRES 11 A 166 THR LYS GLU HIS ARG MET PRO GLN GLU LYS TRP LYS GLY
SEQRES 12 A 166 TYR ILE LYS ASP TYR ASP GLY GLY THR LEU MET GLU CYS
SEQRES 13 A 166 TYR ILE HIS PRO TYR VAL ASP TYR GLY ASN
HET COA A 201 80
HETNAM COA COENZYME A
FORMUL 2 COA C21 H36 N7 O16 P3 S
HELIX 1 H1 HIS A 16 LEU A 33 1 18
HELIX 2 H2 LYS A 38 ASP A 47 1 10
HELIX 3 H3 TYR A 93 ILE A 110 1 18
HELIX 4 H4 ASN A 119 GLN A 128 1 10
SHEET 1 S1 7 LEU A 5 THR A 11 0
SHEET 2 S1 7 GLU A 51 ASN A 58 -1 N VAL A 54 O ASP A 8
SHEET 3 S1 7 VAL A 62 LYS A 72 -1 N ILE A 66 O MET A 53
SHEET 4 S1 7 PHE A 76 THR A 85 -1 N ALA A 83 O GLY A 65
SHEET 5 S1 7 TYR A 112 ALA A 117 1 N LEU A 114 O ALA A 77
SHEET 6 S1 7 THR A 152 ILE A 158 -1 N CYS A 156 O LEU A 113
SHEET 7 S1 7 PHE A 130 LYS A 132 -1 N THR A 131 O GLU A 155
SITE 1 AC1 13 GLN A 32 LEU A 33 LEU A 82 ALA A 83
SITE 2 AC1 13 VAL A 84 ASN A 87 GLN A 89 VAL A 90
SITE 3 AC1 13 GLY A 92 PHE A 120 ALA A 121 TYR A 124
SITE 4 AC1 13 PHE A 125
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 - c 21 2 Bytes