Header list of 1n3j.pdb file
Complete list - 23 20 Bytes
HEADER TRANSFERASE 28-OCT-02 1N3J
TITLE STRUCTURE AND SUBSTRATE OF A HISTONE H3 LYSINE METHYLTRANSFERASE FROM
TITLE 2 PARAMECIUM BURSARIA CHLORELLA VIRUS 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE H3 LYSINE METHYLTRANSFERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: A612L;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PARAMECIUM BURSARIA CHLORELLA VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 10506;
SOURCE 4 GENE: A612L;
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: PET22B
KEYWDS BETA BARREL, HOMODIMER, TRANSFERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR K.L.MANZUR,A.FAROOQ,L.ZENG,O.PLOTNIKOVA,SACHCHIDANAND,A.W.KOCH,M.-
AUTHOR 2 M.ZHOU
REVDAT 4 23-FEB-22 1N3J 1 REMARK
REVDAT 3 24-FEB-09 1N3J 1 VERSN
REVDAT 2 01-MAR-05 1N3J 1 JRNL
REVDAT 1 28-JAN-03 1N3J 0
JRNL AUTH K.L.MANZUR,A.FAROOQ,L.ZENG,O.PLOTNIKOVA,A.W.KOCH,
JRNL AUTH 2 SACHCHIDANAND,M.-M.ZHOU
JRNL TITL A DIMERIC VIRAL SET DOMAIN METHYLTRANSFERASE SPECIFIC TO
JRNL TITL 2 LYS27 OF HISTONE H3.
JRNL REF NAT.STRUCT.BIOL. V. 10 187 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 12567185
JRNL DOI 10.1038/NSB898
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 3.1, X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1N3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-02.
REMARK 100 THE DEPOSITION ID IS D_1000017473.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 1M
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM PROTEIN, 50MM SODIUM
REMARK 210 PHOSPHATE, 700MM NACL, 300MM
REMARK 210 UREA, 0.1MM EDTA, 5MM DTT-D10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-FILTERED_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1, XWINNMR 3.1, ARIA
REMARK 210 1.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MIMIZED AVERAGE STRUCTURE
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: 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 LEU A 13 33.21 -175.23
REMARK 500 ARG A 21 70.21 -111.24
REMARK 500 LYS A 22 89.70 -173.39
REMARK 500 LYS A 26 106.27 -53.48
REMARK 500 GLU A 32 -161.92 -165.56
REMARK 500 CYS A 33 57.20 -174.82
REMARK 500 LEU A 34 51.69 -150.85
REMARK 500 GLU A 48 92.56 -44.19
REMARK 500 ASP A 49 -107.79 -149.50
REMARK 500 TYR A 50 65.98 -104.29
REMARK 500 LYS A 55 -76.73 60.37
REMARK 500 ALA A 61 -163.31 -129.67
REMARK 500 LEU A 62 61.75 -172.52
REMARK 500 HIS A 70 81.38 -63.54
REMARK 500 PRO A 74 96.21 -67.52
REMARK 500 GLU A 79 88.47 -150.80
REMARK 500 LYS A 85 -127.15 60.91
REMARK 500 ARG A 86 -151.78 -175.58
REMARK 500 ILE A 97 34.78 39.48
REMARK 500 THR A 102 -145.48 -137.92
REMARK 500 SER A 104 107.92 56.58
REMARK 500 TYR A 105 67.86 -160.99
REMARK 500 ASP A 107 -65.33 -148.79
REMARK 500 TYR A 109 107.80 -59.13
REMARK 500 SER A 112 31.52 -174.30
REMARK 500 ARG A 113 85.28 53.44
REMARK 500 THR A 117 87.82 -58.52
REMARK 500 GLN A 118 -83.57 57.64
REMARK 500 LEU B 13 33.18 -175.40
REMARK 500 ARG B 21 70.21 -111.26
REMARK 500 LYS B 22 89.71 -173.44
REMARK 500 LYS B 26 106.21 -53.37
REMARK 500 GLU B 32 -161.90 -165.56
REMARK 500 CYS B 33 57.20 -174.83
REMARK 500 LEU B 34 51.70 -150.88
REMARK 500 GLU B 48 92.47 -44.13
REMARK 500 ASP B 49 -107.72 -149.39
REMARK 500 TYR B 50 65.75 -104.33
REMARK 500 LYS B 55 -76.80 60.37
REMARK 500 ALA B 61 -163.27 -129.77
REMARK 500 LEU B 62 61.74 -172.54
REMARK 500 HIS B 70 81.38 -63.59
REMARK 500 PRO B 74 96.23 -67.53
REMARK 500 GLU B 79 88.53 -151.07
REMARK 500 LYS B 85 -127.25 60.78
REMARK 500 ARG B 86 -151.75 -175.48
REMARK 500 ILE B 97 34.71 39.49
REMARK 500 THR B 102 -145.36 -137.99
REMARK 500 SER B 104 107.95 56.55
REMARK 500 TYR B 105 67.90 -161.01
REMARK 500
REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1N3J A 1 119 UNP O41094 O41094_CHVP1 1 119
DBREF 1N3J B 1 119 UNP O41094 O41094_CHVP1 1 119
SEQRES 1 A 119 MET PHE ASN ASP ARG VAL ILE VAL LYS LYS SER PRO LEU
SEQRES 2 A 119 GLY GLY TYR GLY VAL PHE ALA ARG LYS SER PHE GLU LYS
SEQRES 3 A 119 GLY GLU LEU VAL GLU GLU CYS LEU CYS ILE VAL ARG HIS
SEQRES 4 A 119 ASN ASP ASP TRP GLY THR ALA LEU GLU ASP TYR LEU PHE
SEQRES 5 A 119 SER ARG LYS ASN MET SER ALA MET ALA LEU GLY PHE GLY
SEQRES 6 A 119 ALA ILE PHE ASN HIS SER LYS ASP PRO ASN ALA ARG HIS
SEQRES 7 A 119 GLU LEU THR ALA GLY LEU LYS ARG MET ARG ILE PHE THR
SEQRES 8 A 119 ILE LYS PRO ILE ALA ILE GLY GLU GLU ILE THR ILE SER
SEQRES 9 A 119 TYR GLY ASP ASP TYR TRP LEU SER ARG PRO ARG LEU THR
SEQRES 10 A 119 GLN ASN
SEQRES 1 B 119 MET PHE ASN ASP ARG VAL ILE VAL LYS LYS SER PRO LEU
SEQRES 2 B 119 GLY GLY TYR GLY VAL PHE ALA ARG LYS SER PHE GLU LYS
SEQRES 3 B 119 GLY GLU LEU VAL GLU GLU CYS LEU CYS ILE VAL ARG HIS
SEQRES 4 B 119 ASN ASP ASP TRP GLY THR ALA LEU GLU ASP TYR LEU PHE
SEQRES 5 B 119 SER ARG LYS ASN MET SER ALA MET ALA LEU GLY PHE GLY
SEQRES 6 B 119 ALA ILE PHE ASN HIS SER LYS ASP PRO ASN ALA ARG HIS
SEQRES 7 B 119 GLU LEU THR ALA GLY LEU LYS ARG MET ARG ILE PHE THR
SEQRES 8 B 119 ILE LYS PRO ILE ALA ILE GLY GLU GLU ILE THR ILE SER
SEQRES 9 B 119 TYR GLY ASP ASP TYR TRP LEU SER ARG PRO ARG LEU THR
SEQRES 10 B 119 GLN ASN
HELIX 1 1 ASN A 40 LEU A 47 1 8
HELIX 2 2 PHE A 64 HIS A 70 1 7
HELIX 3 3 ASN B 40 LEU B 47 1 8
HELIX 4 4 PHE B 64 HIS B 70 1 7
SHEET 1 A 3 VAL A 6 LYS A 9 0
SHEET 2 A 3 GLY A 17 ALA A 20 -1 O GLY A 17 N LYS A 9
SHEET 3 A 3 GLU A 99 ILE A 101 -1 O GLU A 99 N ALA A 20
SHEET 1 B 3 GLU A 28 VAL A 30 0
SHEET 2 B 3 MET A 87 THR A 91 -1 O THR A 91 N GLU A 28
SHEET 3 B 3 ARG A 77 LEU A 80 -1 N GLU A 79 O ARG A 88
SHEET 1 C 3 ILE A 36 ARG A 38 0
SHEET 2 C 3 MET A 57 ALA A 61 -1 O SER A 58 N ARG A 38
SHEET 3 C 3 TYR A 50 ARG A 54 -1 N PHE A 52 O ALA A 59
SHEET 1 D 3 VAL B 6 LYS B 9 0
SHEET 2 D 3 GLY B 17 ALA B 20 -1 O GLY B 17 N LYS B 9
SHEET 3 D 3 GLU B 99 ILE B 101 -1 O GLU B 99 N ALA B 20
SHEET 1 E 3 GLU B 28 VAL B 30 0
SHEET 2 E 3 MET B 87 THR B 91 -1 O THR B 91 N GLU B 28
SHEET 3 E 3 ARG B 77 LEU B 80 -1 N GLU B 79 O ARG B 88
SHEET 1 F 3 ILE B 36 ARG B 38 0
SHEET 2 F 3 MET B 57 ALA B 61 -1 O SER B 58 N ARG B 38
SHEET 3 F 3 TYR B 50 ARG B 54 -1 N PHE B 52 O ALA B 59
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