Header list of 1pfj.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 27-MAY-03 1PFJ
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL PH/PTB DOMAIN OF THE TFIIH P62
TITLE 2 SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TFIIH BASAL TRANSCRIPTION FACTOR COMPLEX P62 SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL PH/PTB DOMAIN;
COMPND 5 SYNONYM: BASIC TRANSCRIPTION FACTOR 62 KDA SUBUNIT, BTF2-P62, GENERAL
COMPND 6 TRANSCRIPTION FACTOR IIH POLYPEPTIDE 1;
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: GTF2H1 OR BTF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS PH/PTB DOMAIN, STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL
KEYWDS 2 GENOMICS, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR V.GERVAIS,V.LAMOUR,A.JAWHARI,F.FRINDEL,E.WASIELEWSKI,J.C.THIERRY,
AUTHOR 2 B.KIEFFER,A.POTERSZMAN,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 23-FEB-22 1PFJ 1 REMARK
REVDAT 3 24-FEB-09 1PFJ 1 VERSN
REVDAT 2 06-JUL-04 1PFJ 1 JRNL
REVDAT 1 08-JUN-04 1PFJ 0
JRNL AUTH V.GERVAIS,V.LAMOUR,A.JAWHARI,F.FRINDEL,E.WASIELEWSKI,
JRNL AUTH 2 S.DUBAELE,J.M.EGLY,J.C.THIERRY,B.KIEFFER,A.POTERSZMAN
JRNL TITL TFIIH CONTAINS A PH DOMAIN INVOLVED IN DNA NUCLEOTIDE
JRNL TITL 2 EXCISION REPAIR.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 616 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 15195146
JRNL DOI 10.1038/NSMB782
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: TOTAL NOE RESTRAINTS: 1944
REMARK 3 DIHEDRAL ANGLE RESTRAINTS: 148
REMARK 3 HYDROGEN BONDS: 35
REMARK 3 RESIDUAL DIPOLAR COUPLING: 76
REMARK 4
REMARK 4 1PFJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019294.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293; 293; 298; 293
REMARK 210 PH : 7.4; 7.4; 7.4; 7.4
REMARK 210 IONIC STRENGTH : 20MM; 20MM; 20MM; 20MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM P62 U-15N,13C; 20MM
REMARK 210 DEUTERATED TRIS; 90% H2O, 10%
REMARK 210 D2O; 1.2MM P62 U-15N; 20MM
REMARK 210 DEUTERATED TRIS; 90% H2O, 10%
REMARK 210 D2O; 0.9MM P62 U-15N; 20MM
REMARK 210 DEUTERATED TRIS + 26UG C12E6/
REMARK 210 HEXANOL; 90% H2O, 10% D2O; 1.5MM
REMARK 210 P62; 20MM DEUTERATED TRIS; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; IPAP-[1H-
REMARK 210 15N] HSQC
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 : CNS 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 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 LEU A 99 H LYS A 102 1.40
REMARK 500 H VAL A 12 O LEU A 24 1.46
REMARK 500 HZ2 LYS A 93 OE1 GLN A 97 1.47
REMARK 500 H ARG A 16 O HIS A 78 1.48
REMARK 500 O LEU A 95 H GLN A 98 1.53
REMARK 500 O TYR A 25 H ALA A 32 1.54
REMARK 500 O LEU A 10 H LEU A 26 1.57
REMARK 500 O VAL A 15 H GLY A 22 1.58
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 PRO A 35 C - N - CD ANGL. DEV. = -17.2 DEGREES
REMARK 500 1 PRO A 57 C - N - CD ANGL. DEV. = -20.4 DEGREES
REMARK 500 2 PRO A 35 C - N - CD ANGL. DEV. = -14.6 DEGREES
REMARK 500 2 PRO A 57 C - N - CD ANGL. DEV. = -26.5 DEGREES
REMARK 500 3 PRO A 35 C - N - CD ANGL. DEV. = -16.8 DEGREES
REMARK 500 4 PRO A 35 C - N - CD ANGL. DEV. = -14.0 DEGREES
REMARK 500 7 PRO A 35 C - N - CD ANGL. DEV. = -16.3 DEGREES
REMARK 500 8 PRO A 35 C - N - CD ANGL. DEV. = -15.2 DEGREES
REMARK 500 10 PRO A 35 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 10 PRO A 57 C - N - CD ANGL. DEV. = -24.2 DEGREES
REMARK 500 12 PRO A 35 C - N - CD ANGL. DEV. = -14.5 DEGREES
REMARK 500 15 PRO A 35 C - N - CD ANGL. DEV. = -16.0 DEGREES
REMARK 500 18 PRO A 35 C - N - CD ANGL. DEV. = -15.7 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 SER A 4 -92.75 -150.22
REMARK 500 1 LYS A 18 -23.69 -36.47
REMARK 500 1 GLU A 36 96.64 -48.04
REMARK 500 1 LYS A 38 -100.08 -109.22
REMARK 500 1 ARG A 40 -159.67 -111.55
REMARK 500 1 SER A 44 119.90 -166.68
REMARK 500 1 CYS A 52 132.01 172.61
REMARK 500 1 PRO A 57 63.60 -119.61
REMARK 500 1 ALA A 61 -72.65 -30.43
REMARK 500 1 LYS A 62 42.88 -168.59
REMARK 500 1 ILE A 63 81.60 89.19
REMARK 500 1 ALA A 71 -153.71 -73.38
REMARK 500 1 SER A 80 143.48 -177.25
REMARK 500 1 SER A 83 21.71 -151.23
REMARK 500 1 VAL A 86 -140.37 -152.26
REMARK 500 1 GLU A 88 -74.22 -38.58
REMARK 500 2 SER A 5 -160.99 -106.04
REMARK 500 2 LYS A 18 -21.03 -36.44
REMARK 500 2 PRO A 35 -158.38 -106.16
REMARK 500 2 LYS A 38 40.98 -89.28
REMARK 500 2 ARG A 40 -99.82 -119.25
REMARK 500 2 PHE A 41 93.94 -41.52
REMARK 500 2 SER A 44 102.52 -168.69
REMARK 500 2 CYS A 52 132.00 173.17
REMARK 500 2 LYS A 60 -168.18 -116.68
REMARK 500 2 ALA A 61 -72.94 -38.19
REMARK 500 2 LYS A 62 46.39 -167.40
REMARK 500 2 ILE A 63 83.31 79.46
REMARK 500 2 ALA A 71 -154.42 -78.77
REMARK 500 2 SER A 80 142.03 -177.22
REMARK 500 2 SER A 83 17.90 -150.28
REMARK 500 2 VAL A 86 -141.63 -153.09
REMARK 500 2 GLU A 88 -72.63 -45.28
REMARK 500 2 ARG A 105 -49.54 -160.25
REMARK 500 2 LYS A 106 -79.69 -111.58
REMARK 500 2 ALA A 107 33.14 -156.03
REMARK 500 3 THR A 3 -171.14 -62.03
REMARK 500 3 SER A 5 -149.01 -113.42
REMARK 500 3 LYS A 18 -23.67 -36.72
REMARK 500 3 PRO A 35 -152.40 -115.80
REMARK 500 3 GLU A 36 39.78 -89.26
REMARK 500 3 LYS A 38 51.16 -152.18
REMARK 500 3 ASP A 39 -121.95 -160.93
REMARK 500 3 ARG A 40 -50.99 -138.74
REMARK 500 3 SER A 44 101.48 -164.18
REMARK 500 3 CYS A 52 134.41 173.08
REMARK 500 3 PRO A 57 55.48 -68.56
REMARK 500 3 ALA A 61 -70.16 -45.11
REMARK 500 3 LYS A 62 54.21 -171.08
REMARK 500 3 ILE A 63 71.48 83.65
REMARK 500
REMARK 500 THIS ENTRY HAS 360 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4901 RELATED DB: BMRB
REMARK 900 1H, 15N, 13C ASSIGNMENTS OF THE N-TERMINAL DOMAIN OF THE HUMAN
REMARK 900 TFIIH P62 SUBUNIT
REMARK 900 RELATED ID: IGBMC-0024-000 RELATED DB: TARGETDB
DBREF 1PFJ A 1 108 UNP P32780 TF2H1_HUMAN 1 108
SEQRES 1 A 108 MET ALA THR SER SER GLU GLU VAL LEU LEU ILE VAL LYS
SEQRES 2 A 108 LYS VAL ARG GLN LYS LYS GLN ASP GLY ALA LEU TYR LEU
SEQRES 3 A 108 MET ALA GLU ARG ILE ALA TRP ALA PRO GLU GLY LYS ASP
SEQRES 4 A 108 ARG PHE THR ILE SER HIS MET TYR ALA ASP ILE LYS CYS
SEQRES 5 A 108 GLN LYS ILE SER PRO GLU GLY LYS ALA LYS ILE GLN LEU
SEQRES 6 A 108 GLN LEU VAL LEU HIS ALA GLY ASP THR THR ASN PHE HIS
SEQRES 7 A 108 PHE SER ASN GLU SER THR ALA VAL LYS GLU ARG ASP ALA
SEQRES 8 A 108 VAL LYS ASP LEU LEU GLN GLN LEU LEU PRO LYS PHE LYS
SEQRES 9 A 108 ARG LYS ALA ASN
HELIX 1 1 VAL A 86 LYS A 104 1 19
SHEET 1 A 4 VAL A 8 VAL A 12 0
SHEET 2 A 4 ALA A 23 MET A 27 -1 O LEU A 24 N VAL A 12
SHEET 3 A 4 ARG A 30 ALA A 34 -1 O ALA A 32 N TYR A 25
SHEET 4 A 4 ILE A 43 MET A 46 -1 O HIS A 45 N ILE A 31
SHEET 1 B 3 GLN A 53 ILE A 55 0
SHEET 2 B 3 GLN A 64 VAL A 68 -1 O GLN A 66 N LYS A 54
SHEET 3 B 3 THR A 74 HIS A 78 -1 O THR A 75 N LEU A 67
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 - b 23 2 Bytes