Header list of 2f3i.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSFERASE 21-NOV-05 2F3I
TITLE SOLUTION STRUCTURE OF A SUBUNIT OF RNA POLYMERASE II
CAVEAT 2F3I CHIRALITAY ERROR AT CA CENTER AT ILE A 4 IN MODEL 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 17.1 KDA
COMPND 3 POLYPEPTIDE;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: RNA POLYMERASE II SUBUNIT, RPB17, RPB8, RPABC3;
COMPND 6 EC: 2.7.7.6;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET24A
KEYWDS RNA POLYMERASE II, TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR X.KANG,C.JIN
REVDAT 4 09-MAR-22 2F3I 1 REMARK
REVDAT 3 24-FEB-09 2F3I 1 VERSN
REVDAT 2 26-SEP-06 2F3I 1 JRNL
REVDAT 1 02-MAY-06 2F3I 0
JRNL AUTH X.KANG,Y.HU,Y.LI,X.GUO,X.JIANG,L.LAI,B.XIA,C.JIN
JRNL TITL STRUCTURAL, BIOCHEMICAL, AND DYNAMIC CHARACTERIZATIONS OF
JRNL TITL 2 THE HRPB8 SUBUNIT OF HUMAN RNA POLYMERASES
JRNL REF J.BIOL.CHEM. V. 281 18216 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16632472
JRNL DOI 10.1074/JBC.M513241200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID CASE (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F3I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035406.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5MM RNA POLYMERASE II SUBUNIT
REMARK 210 U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D_15N-EDITED_
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 15 ARG A 57 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 18 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 19 TYR A 118 CB - CG - CD2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 20 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
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 ILE A 4 -157.19 67.46
REMARK 500 1 LEU A 5 15.59 -149.33
REMARK 500 1 PRO A 17 30.88 -67.48
REMARK 500 1 PHE A 35 -134.08 -126.01
REMARK 500 1 LYS A 36 13.54 -143.61
REMARK 500 1 VAL A 50 -143.77 -152.67
REMARK 500 1 THR A 63 -89.67 -94.47
REMARK 500 1 LEU A 64 -37.87 -153.45
REMARK 500 1 ASP A 67 -78.51 -120.20
REMARK 500 1 LEU A 70 -42.54 -132.69
REMARK 500 1 GLU A 74 -143.87 -95.72
REMARK 500 1 TYR A 75 -7.42 62.84
REMARK 500 1 PRO A 77 -157.43 -87.29
REMARK 500 1 THR A 78 1.62 -30.54
REMARK 500 1 ASP A 80 -142.59 -143.89
REMARK 500 1 ARG A 81 -109.42 53.19
REMARK 500 1 ALA A 85 80.01 -55.88
REMARK 500 1 ASP A 86 -41.80 -154.69
REMARK 500 1 PHE A 88 73.22 -167.39
REMARK 500 1 GLU A 89 -33.23 -39.03
REMARK 500 1 GLU A 103 15.25 -143.43
REMARK 500 1 SER A 105 -36.58 117.77
REMARK 500 1 THR A 106 -29.55 -151.10
REMARK 500 1 ALA A 109 103.05 -1.28
REMARK 500 2 ARG A 24 2.17 -68.64
REMARK 500 2 PHE A 35 -102.16 -124.20
REMARK 500 2 LYS A 36 10.80 -168.19
REMARK 500 2 ASN A 44 90.71 -68.48
REMARK 500 2 ILE A 45 3.88 -69.65
REMARK 500 2 SER A 62 51.85 -145.05
REMARK 500 2 THR A 63 105.29 -43.87
REMARK 500 2 GLU A 74 40.96 -80.60
REMARK 500 2 PRO A 82 58.07 23.36
REMARK 500 2 SER A 83 22.49 -65.77
REMARK 500 2 ASP A 86 -32.55 -159.45
REMARK 500 2 TYR A 97 58.59 -143.34
REMARK 500 2 ASP A 102 -97.77 -147.49
REMARK 500 2 GLU A 103 74.60 -167.85
REMARK 500 2 THR A 104 -159.79 -150.15
REMARK 500 2 THR A 106 38.41 109.77
REMARK 500 3 LYS A 20 25.97 -73.03
REMARK 500 3 LYS A 21 -59.84 68.02
REMARK 500 3 ASP A 54 -64.06 -141.77
REMARK 500 3 ALA A 61 175.43 57.55
REMARK 500 3 THR A 63 -179.18 62.66
REMARK 500 3 ASP A 80 -49.05 -152.25
REMARK 500 3 ALA A 85 24.11 -75.05
REMARK 500 3 ASP A 86 35.26 -82.32
REMARK 500 3 PHE A 88 38.27 -75.35
REMARK 500 3 SER A 105 -15.41 121.46
REMARK 500
REMARK 500 THIS ENTRY HAS 332 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ASP A 51 LEU A 52 1 -147.93
REMARK 500 THR A 63 LEU A 64 1 110.77
REMARK 500 LEU A 64 TYR A 65 1 -71.99
REMARK 500 GLU A 66 ASP A 67 1 -149.15
REMARK 500 ARG A 84 ALA A 85 1 131.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 TYR A 65 0.09 SIDE CHAIN
REMARK 500 1 TYR A 75 0.08 SIDE CHAIN
REMARK 500 1 ARG A 98 0.12 SIDE CHAIN
REMARK 500 5 TYR A 118 0.07 SIDE CHAIN
REMARK 500 7 TYR A 65 0.07 SIDE CHAIN
REMARK 500 10 ARG A 140 0.11 SIDE CHAIN
REMARK 500 13 ARG A 124 0.10 SIDE CHAIN
REMARK 500 16 ARG A 140 0.10 SIDE CHAIN
REMARK 500 19 ARG A 98 0.11 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2F3I A 1 150 UNP P52434 RPB8_HUMAN 1 150
SEQRES 1 A 150 MET ALA GLY ILE LEU PHE GLU ASP ILE PHE ASP VAL LYS
SEQRES 2 A 150 ASP ILE ASP PRO GLU GLY LYS LYS PHE ASP ARG VAL SER
SEQRES 3 A 150 ARG LEU HIS CYS GLU SER GLU SER PHE LYS MET ASP LEU
SEQRES 4 A 150 ILE LEU ASP VAL ASN ILE GLN ILE TYR PRO VAL ASP LEU
SEQRES 5 A 150 GLY ASP LYS PHE ARG LEU VAL ILE ALA SER THR LEU TYR
SEQRES 6 A 150 GLU ASP GLY THR LEU ASP ASP GLY GLU TYR ASN PRO THR
SEQRES 7 A 150 ASP ASP ARG PRO SER ARG ALA ASP GLN PHE GLU TYR VAL
SEQRES 8 A 150 MET TYR GLY LYS VAL TYR ARG ILE GLU GLY ASP GLU THR
SEQRES 9 A 150 SER THR GLU ALA ALA THR ARG LEU SER ALA TYR VAL SER
SEQRES 10 A 150 TYR GLY GLY LEU LEU MET ARG LEU GLN GLY ASP ALA ASN
SEQRES 11 A 150 ASN LEU HIS GLY PHE GLU VAL ASP SER ARG VAL TYR LEU
SEQRES 12 A 150 LEU MET LYS LYS LEU ALA PHE
HELIX 1 1 ASP A 128 HIS A 133 1 6
SHEET 1 A 9 TYR A 90 MET A 92 0
SHEET 2 A 9 LEU A 143 LYS A 147 -1 O MET A 145 N TYR A 90
SHEET 3 A 9 PHE A 56 VAL A 59 -1 N ARG A 57 O LYS A 146
SHEET 4 A 9 GLU A 7 ASP A 16 -1 N ASP A 8 O LEU A 58
SHEET 5 A 9 VAL A 25 SER A 32 -1 O HIS A 29 N LYS A 13
SHEET 6 A 9 ASP A 38 ASN A 44 -1 O LEU A 39 N CYS A 30
SHEET 7 A 9 LEU A 121 GLY A 127 -1 O LEU A 122 N ASP A 42
SHEET 8 A 9 LEU A 112 TYR A 118 -1 N ALA A 114 O LEU A 125
SHEET 9 A 9 GLY A 94 TYR A 97 -1 N LYS A 95 O SER A 117
CISPEP 1 ILE A 4 LEU A 5 1 19.61
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 - r 9 2 Bytes