Header list of 1jm4.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSFERASE 17-JUL-01 1JM4
TITLE NMR STRUCTURE OF P/CAF BROMODOMAIN IN COMPLEX WITH HIV-1 TAT PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HIV-1 TAT PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: P300/CBP-ASSOCIATED FACTOR;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: BROMODOMAIN;
COMPND 9 SYNONYM: P/CAF;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED.;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 6 ORGANISM_COMMON: HUMAN;
SOURCE 7 ORGANISM_TAXID: 9606;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PET14B
KEYWDS BROMODOMAIN, PROTEIN-PEPTIDE COMPLEX, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR S.MUJTABA,Y.HE,L.ZENG,A.FAROOQ,J.E.CARLSON,M.OTT,E.VERDIN,M.-M.ZHOU
REVDAT 4 23-FEB-22 1JM4 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1JM4 1 VERSN
REVDAT 2 17-MAY-05 1JM4 1 JRNL
REVDAT 1 17-JUL-02 1JM4 0
JRNL AUTH S.MUJTABA,Y.HE,L.ZENG,A.FAROOQ,J.E.CARLSON,M.OTT,E.VERDIN,
JRNL AUTH 2 M.-M.ZHOU
JRNL TITL STRUCTURAL BASIS OF LYSINE-ACETYLATED HIV-1 TAT RECOGNITION
JRNL TITL 2 BY PCAF BROMODOMAIN
JRNL REF MOL.CELL V. 9 575 2002
JRNL REFN ISSN 1097-2765
JRNL PMID 11931765
JRNL DOI 10.1016/S1097-2765(02)00483-5
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.DHALLUIN,J.E.CARLSON,L.ZENG,C.HE,A.K.AGGARWAL,M.-M.ZHOU
REMARK 1 TITL STRUCTURE AND LIGAND OF A HISTONE ACETYLTRANSFERASE
REMARK 1 TITL 2 BROMODOMAIN
REMARK 1 REF NATURE V. 399 491 1999
REMARK 1 REFN ISSN 0028-0836
REMARK 1 DOI 10.1038/20974
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 3, X-PLOR 3.851
REMARK 3 AUTHORS : FRANK DELAGLIO (NMRPIPE), BRUNGER (X-PLOR 3.851)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE ARIA/X-PLOR PLATFORM HAS BEEN USED
REMARK 3 FOR THE NOE ASSIGNMENT
REMARK 4
REMARK 4 1JM4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013928.
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 : 100 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM BROMODOMAIN (U-15N)/TAT
REMARK 210 PEPTIDE; 100 MM PHOSPHATE BUFFER
REMARK 210 OF PH 6.5, 5 MM PERDEUTERATED
REMARK 210 DTT AND 0.5 MM EDTA; 0.5 MM
REMARK 210 BROMODOMAIN (U-13C,15N)/TAT
REMARK 210 PEPTIDE; 100 MM PHOSPHATE BUFFER
REMARK 210 OF PH 6.5, 5 MM PERDEUTERATED
REMARK 210 DTT AND 0.5 MM EDTA; 0.5 MM
REMARK 210 BROMODOMAIN (U-13C,15N, 75%-2H)/
REMARK 210 TAT PEPTIDE; 100 MM PHOSPHATE
REMARK 210 BUFFER OF PH 6.5, 5 MM
REMARK 210 PERDEUTERATED DTT AND 0.5 MM EDTA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 FILTERED_NOESY; 3D_13C/15N-
REMARK 210 FILTERED_NOESY; 2D_ROESY
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 : NMRVIEW 3.5, X-PLOR/ARIA 2
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM,
REMARK 210 STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 O ASP B 769 H MET B 773 1.55
REMARK 500 O LEU B 736 H LYS B 740 1.56
REMARK 500 O ILE B 824 H LEU B 829 1.58
REMARK 500 O LYS A 51 HZ2 LYS B 753 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 TYR A 47 -172.33 52.77
REMARK 500 1 ARG A 49 -62.98 -140.43
REMARK 500 1 LYS A 51 -156.33 -131.92
REMARK 500 1 HIS B 717 -43.98 -143.00
REMARK 500 1 MET B 718 72.43 53.23
REMARK 500 1 SER B 719 -73.38 -75.96
REMARK 500 1 ARG B 723 -86.07 57.37
REMARK 500 1 VAL B 752 -144.99 -76.60
REMARK 500 1 THR B 755 -39.91 -163.50
REMARK 500 1 TYR B 760 178.39 -52.84
REMARK 500 1 GLU B 762 -54.70 -164.58
REMARK 500 1 ILE B 764 76.28 -106.24
REMARK 500 1 MET B 768 168.40 54.88
REMARK 500 1 ASP B 769 145.65 -178.84
REMARK 500 1 VAL B 783 46.13 -102.79
REMARK 500 1 LYS B 785 -113.30 -63.93
REMARK 500 1 ASN B 803 159.03 -48.09
REMARK 500 1 GLU B 806 59.44 175.62
REMARK 500 1 SER B 807 -61.64 -120.97
REMARK 500 1 GLU B 808 -44.80 -137.61
REMARK 500 1 ASP B 831 30.29 38.52
REMARK 500 2 ARG A 53 -172.08 53.16
REMARK 500 2 ARG A 55 -170.33 51.67
REMARK 500 2 SER B 716 30.11 -148.17
REMARK 500 2 MET B 718 -173.69 -65.39
REMARK 500 2 ARG B 723 -86.91 55.84
REMARK 500 2 VAL B 752 -90.16 -51.08
REMARK 500 2 LYS B 753 -35.60 -179.86
REMARK 500 2 THR B 755 -31.66 178.34
REMARK 500 2 ALA B 757 95.17 -37.91
REMARK 500 2 TYR B 760 94.00 -59.54
REMARK 500 2 TYR B 761 -42.58 178.09
REMARK 500 2 PRO B 767 102.05 -43.65
REMARK 500 2 ASP B 769 143.69 -177.74
REMARK 500 2 ARG B 780 18.20 56.45
REMARK 500 2 VAL B 783 54.07 -147.65
REMARK 500 2 ALA B 790 -73.08 -65.15
REMARK 500 2 ASN B 803 172.76 -50.27
REMARK 500 2 PRO B 805 82.28 -61.98
REMARK 500 2 SER B 807 -60.89 -102.37
REMARK 500 2 GLU B 808 -41.76 -154.89
REMARK 500 2 ASP B 831 24.53 47.66
REMARK 500 3 TYR A 47 -177.95 53.14
REMARK 500 3 ARG A 49 93.71 -173.13
REMARK 500 3 ALY A 50 43.80 -91.56
REMARK 500 3 PRO B 751 33.71 -92.33
REMARK 500 3 VAL B 752 -166.29 47.35
REMARK 500 3 THR B 755 -40.40 -177.02
REMARK 500 3 ALA B 757 103.45 -47.27
REMARK 500 3 TYR B 760 88.27 -58.22
REMARK 500
REMARK 500 THIS ENTRY HAS 531 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1B91 RELATED DB: PDB
REMARK 900 FREE FORM P/CAF BROMODOMAIN STRUCTURE
DBREF 1JM4 B 719 832 UNP Q92831 PCAF_HUMAN 448 561
DBREF 1JM4 A 46 56 PDB 1JM4 1JM4 46 56
SEQADV 1JM4 GLY B 715 UNP Q92831 CLONING ARTIFACT
SEQADV 1JM4 SER B 716 UNP Q92831 CLONING ARTIFACT
SEQADV 1JM4 HIS B 717 UNP Q92831 CLONING ARTIFACT
SEQADV 1JM4 MET B 718 UNP Q92831 CLONING ARTIFACT
SEQRES 1 A 11 SER TYR GLY ARG ALY LYS ARG ARG GLN ARG CYS
SEQRES 1 B 118 GLY SER HIS MET SER LYS GLU PRO ARG ASP PRO ASP GLN
SEQRES 2 B 118 LEU TYR SER THR LEU LYS SER ILE LEU GLN GLN VAL LYS
SEQRES 3 B 118 SER HIS GLN SER ALA TRP PRO PHE MET GLU PRO VAL LYS
SEQRES 4 B 118 ARG THR GLU ALA PRO GLY TYR TYR GLU VAL ILE ARG PHE
SEQRES 5 B 118 PRO MET ASP LEU LYS THR MET SER GLU ARG LEU LYS ASN
SEQRES 6 B 118 ARG TYR TYR VAL SER LYS LYS LEU PHE MET ALA ASP LEU
SEQRES 7 B 118 GLN ARG VAL PHE THR ASN CYS LYS GLU TYR ASN PRO PRO
SEQRES 8 B 118 GLU SER GLU TYR TYR LYS CYS ALA ASN ILE LEU GLU LYS
SEQRES 9 B 118 PHE PHE PHE SER LYS ILE LYS GLU ALA GLY LEU ILE ASP
SEQRES 10 B 118 LYS
MODRES 1JM4 ALY A 50 LYS N(6)-ACETYLLYSINE
HET ALY A 50 26
HETNAM ALY N(6)-ACETYLLYSINE
FORMUL 1 ALY C8 H16 N2 O3
HELIX 1 1 ASP B 724 SER B 741 1 18
HELIX 2 2 TRP B 746 GLU B 750 5 5
HELIX 3 3 ASP B 769 ASN B 779 1 11
HELIX 4 4 SER B 784 ASN B 803 1 20
HELIX 5 5 GLU B 808 GLY B 828 1 21
LINK C ARG A 49 N ALY A 50 1555 1555 1.31
LINK C ALY A 50 N LYS A 51 1555 1555 1.31
CISPEP 1 PRO B 804 PRO B 805 24 6.87
CISPEP 2 PRO B 804 PRO B 805 25 6.87
CRYST1 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 - b 23 2 Bytes