Header list of 1n72.pdb file
Complete list - 23 20 Bytes
HEADER TRANSFERASE 12-NOV-02 1N72
TITLE STRUCTURE AND LIGAND OF A HISTONE ACETYLTRANSFERASE BROMODOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN;
COMPND 5 SYNONYM: P300/CBP-ASSOCIATED FACTOR, P/CAF, HISTONE ACETYLASE PCAF;
COMPND 6 EC: 2.3.1.48;
COMPND 7 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: PCAF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS HISTONE ACETYLTRANSFERASE BROMODOMAIN, 4-HELICAL BUNDLE, TRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR C.DHALLUIN,J.E.CARLSON,L.ZENG,C.HE,A.K.AGGARWAL,M.-M.ZHOU
REVDAT 3 23-FEB-22 1N72 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1N72 1 VERSN
REVDAT 1 11-DEC-02 1N72 0
SPRSDE 11-DEC-02 1N72 1B91
JRNL AUTH C.DHALLUIN,J.E.CARLSON,L.ZENG,C.HE,A.K.AGGARWAL,M.-M.ZHOU
JRNL TITL STRUCTURE AND LIGAND OF A HISTONE ACETYLTRANSFERASE
JRNL TITL 2 BROMODOMAIN
JRNL REF NATURE V. 399 491 1999
JRNL REFN ISSN 0028-0836
JRNL PMID 10365964
JRNL DOI 10.1038/20974
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, ARIA
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N72 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017599.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 200
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM BROMODOMAIN, 100MM SODIUM
REMARK 210 PHOSPHATE, 5MM DTT-D10, 0.5MM
REMARK 210 EDTA, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR, XWINNMR
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 MATRIX RELAXATION TORSION ANGLE
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 715
REMARK 465 SER A 716
REMARK 465 HIS A 717
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 GLU A 721 70.50 -162.51
REMARK 500 ARG A 723 51.99 -160.22
REMARK 500 VAL A 752 173.67 -53.22
REMARK 500 LYS A 753 -169.96 -117.11
REMARK 500 MET A 768 70.70 58.41
REMARK 500 ASP A 769 -162.26 -59.32
REMARK 500 ASN A 779 -88.78 -124.85
REMARK 500 VAL A 783 64.13 -168.32
REMARK 500 SER A 784 49.51 -159.07
REMARK 500 LYS A 785 -85.81 56.43
REMARK 500 PRO A 804 -178.08 -60.07
REMARK 500 PRO A 805 62.49 -67.36
REMARK 500 GLU A 806 -85.47 -57.12
REMARK 500 SER A 807 -49.03 -179.20
REMARK 500 ASP A 831 172.34 -50.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS BELIEVE PRO IS AT BOTH
REMARK 999 POSITIONS 804 AND 805 IN THE WILD PROTEIN
REMARK 999 SEQUENCE.
DBREF 1N72 A 719 832 UNP Q92831 PCAF_HUMAN 719 832
SEQADV 1N72 GLY A 715 UNP Q92831 CLONING ARTIFACT
SEQADV 1N72 SER A 716 UNP Q92831 CLONING ARTIFACT
SEQADV 1N72 HIS A 717 UNP Q92831 CLONING ARTIFACT
SEQADV 1N72 MET A 718 UNP Q92831 CLONING ARTIFACT
SEQADV 1N72 PRO A 804 UNP Q92831 ALA 804 SEE REMARK 999
SEQADV 1N72 PRO A 805 UNP Q92831 ALA 805 SEE REMARK 999
SEQRES 1 A 118 GLY SER HIS MET SER LYS GLU PRO ARG ASP PRO ASP GLN
SEQRES 2 A 118 LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN VAL LYS
SEQRES 3 A 118 SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO VAL LYS
SEQRES 4 A 118 ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE ARG PHE
SEQRES 5 A 118 PRO MET ASP LEU LYS THR MET SER GLU ARG LEU LYS ASN
SEQRES 6 A 118 ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA ASP LEU
SEQRES 7 A 118 GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN PRO PRO
SEQRES 8 A 118 GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU GLU LYS
SEQRES 9 A 118 PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU ILE ASP
SEQRES 10 A 118 LYS
HELIX 1 1 ASP A 724 HIS A 742 1 19
HELIX 2 2 ALA A 745 MET A 749 5 5
HELIX 3 3 GLY A 759 ILE A 764 1 6
HELIX 4 4 LYS A 771 LYS A 778 1 8
HELIX 5 5 LYS A 785 TYR A 802 1 18
HELIX 6 6 GLU A 808 GLY A 828 1 21
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
Complete list - 23 20 Bytes