Header list of 1uzc.pdb file
Complete list - n 24 2 Bytes
HEADER NUCLEAR PROTEIN 09-MAR-04 1UZC
TITLE THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN FLJ21157;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FF DOMAIN, RESIDUES 250-319;
COMPND 5 SYNONYM: HUNTINGTIN-INTERACTING PROTEIN HYPA/FBP11;
COMPND 6 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 BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSET-GROEL
KEYWDS NUCLEAR PROTEIN, TRANSCRIPTION, PHOSPHOPEPTIDE RECOGNITION, RNA
KEYWDS 2 POLYMERASE II CARBOXYL-TERMINAL DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 23
AUTHOR M.D.ALLEN,P.JEMTH,A.FRIEDLER,O.SCHON,M.BYCROFT
REVDAT 5 24-JAN-18 1UZC 1 SOURCE
REVDAT 4 17-JAN-18 1UZC 1 JRNL
REVDAT 3 24-FEB-09 1UZC 1 VERSN
REVDAT 2 20-DEC-06 1UZC 1 JRNL
REVDAT 1 05-APR-04 1UZC 0
SPRSDE 05-APR-04 1UZC 1H40
JRNL AUTH M.D.ALLEN,A.FRIEDLER,O.SCHON,M.BYCROFT
JRNL TITL THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11.
JRNL REF J.MOL.BIOL. V. 323 411 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12381297
JRNL DOI 10.1016/S0022-2836(02)00968-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1UZC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-MAR-04.
REMARK 100 THE DEPOSITION ID IS D_1290014766.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : STANDARD 13C; 15N; 1H
REMARK 210 EXPERIMENTS
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : ANSIG 3.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 23
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO DISTANCE VIOLATION 0.25A AND
REMARK 210 NO ANGLE VIOLATIONS > 5 DEGREES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED FF DOMAIN)
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 400
REMARK 400 COMPOUND
REMARK 400 THE FF DOMAIN MAY BE INVOLVED IN PROTEIN-PROTEIN INTERACTION
REMARK 400 AND OFTEN OCCURS IN CONJUNCTION WITH WW DOMAINS
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 MODELS 1-23
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 SER A 2
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 H LYS A 54 OE2 GLU A 57 1.55
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 ALA A 5 -165.04 174.34
REMARK 500 1 ASN A 12 -34.71 -130.26
REMARK 500 1 GLU A 70 -167.95 -107.11
REMARK 500 2 PRO A 4 -167.82 -75.50
REMARK 500 2 ALA A 5 21.71 49.99
REMARK 500 2 GLU A 70 -167.22 43.25
REMARK 500 3 ALA A 5 -173.92 67.37
REMARK 500 3 GLU A 70 58.85 -90.00
REMARK 500 4 LYS A 6 30.52 -93.32
REMARK 500 5 LYS A 6 141.78 62.25
REMARK 500 6 ALA A 5 -45.56 -173.97
REMARK 500 7 PRO A 4 -165.29 -72.82
REMARK 500 7 ALA A 5 17.18 54.34
REMARK 500 7 LYS A 6 -166.21 42.17
REMARK 500 8 PRO A 4 -160.16 -73.03
REMARK 500 8 ALA A 5 -144.78 -145.13
REMARK 500 8 LYS A 6 -33.76 -137.66
REMARK 500 9 LYS A 6 99.56 52.00
REMARK 500 9 GLU A 70 -139.12 40.09
REMARK 500 10 LYS A 6 -135.20 44.91
REMARK 500 10 GLU A 70 -141.01 -117.78
REMARK 500 11 ALA A 5 -158.17 60.18
REMARK 500 11 GLU A 70 156.11 -45.60
REMARK 500 12 LYS A 6 64.25 -116.98
REMARK 500 12 GLU A 70 -88.76 51.16
REMARK 500 13 LYS A 6 -169.91 60.75
REMARK 500 13 GLU A 70 -93.11 43.60
REMARK 500 14 LYS A 6 89.53 -160.49
REMARK 500 14 GLU A 70 -154.97 -108.92
REMARK 500 15 ALA A 5 -82.50 60.47
REMARK 500 15 GLU A 70 -94.55 41.68
REMARK 500 16 ALA A 5 -163.83 52.34
REMARK 500 16 LYS A 6 -70.50 68.43
REMARK 500 16 GLU A 70 -157.34 -115.88
REMARK 500 17 LYS A 6 -157.58 -83.67
REMARK 500 17 GLU A 70 -74.76 -55.49
REMARK 500 18 ALA A 5 70.29 -116.19
REMARK 500 18 GLU A 70 -91.67 50.12
REMARK 500 19 ALA A 5 -61.18 -164.68
REMARK 500 19 LYS A 6 -143.39 62.90
REMARK 500 20 ARG A 29 39.88 39.77
REMARK 500 21 LYS A 6 -99.94 41.65
REMARK 500 21 GLU A 70 -162.39 50.64
REMARK 500 22 GLU A 70 29.47 -146.38
REMARK 500 23 LYS A 6 57.05 -94.74
REMARK 500 23 GLU A 70 90.06 -51.45
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 ARG A 29 0.30 SIDE CHAIN
REMARK 500 1 ARG A 48 0.12 SIDE CHAIN
REMARK 500 2 ARG A 29 0.22 SIDE CHAIN
REMARK 500 2 ARG A 48 0.19 SIDE CHAIN
REMARK 500 3 ARG A 29 0.27 SIDE CHAIN
REMARK 500 3 ARG A 48 0.17 SIDE CHAIN
REMARK 500 4 ARG A 29 0.26 SIDE CHAIN
REMARK 500 4 ARG A 48 0.26 SIDE CHAIN
REMARK 500 5 ARG A 29 0.21 SIDE CHAIN
REMARK 500 5 ARG A 48 0.18 SIDE CHAIN
REMARK 500 6 ARG A 29 0.31 SIDE CHAIN
REMARK 500 6 ARG A 48 0.27 SIDE CHAIN
REMARK 500 7 ARG A 29 0.32 SIDE CHAIN
REMARK 500 7 ARG A 48 0.22 SIDE CHAIN
REMARK 500 8 ARG A 29 0.31 SIDE CHAIN
REMARK 500 8 ARG A 48 0.19 SIDE CHAIN
REMARK 500 9 ARG A 29 0.32 SIDE CHAIN
REMARK 500 9 ARG A 48 0.09 SIDE CHAIN
REMARK 500 10 ARG A 29 0.32 SIDE CHAIN
REMARK 500 10 ARG A 48 0.13 SIDE CHAIN
REMARK 500 11 ARG A 29 0.16 SIDE CHAIN
REMARK 500 11 ARG A 48 0.23 SIDE CHAIN
REMARK 500 12 ARG A 29 0.27 SIDE CHAIN
REMARK 500 12 ARG A 48 0.20 SIDE CHAIN
REMARK 500 13 ARG A 29 0.32 SIDE CHAIN
REMARK 500 13 ARG A 48 0.20 SIDE CHAIN
REMARK 500 14 ARG A 29 0.31 SIDE CHAIN
REMARK 500 14 ARG A 48 0.24 SIDE CHAIN
REMARK 500 15 ARG A 29 0.21 SIDE CHAIN
REMARK 500 15 ARG A 48 0.26 SIDE CHAIN
REMARK 500 16 ARG A 29 0.28 SIDE CHAIN
REMARK 500 16 ARG A 48 0.23 SIDE CHAIN
REMARK 500 17 ARG A 29 0.30 SIDE CHAIN
REMARK 500 17 ARG A 48 0.23 SIDE CHAIN
REMARK 500 18 ARG A 29 0.32 SIDE CHAIN
REMARK 500 18 ARG A 48 0.22 SIDE CHAIN
REMARK 500 19 ARG A 29 0.30 SIDE CHAIN
REMARK 500 20 ARG A 48 0.19 SIDE CHAIN
REMARK 500 21 ARG A 29 0.28 SIDE CHAIN
REMARK 500 21 ARG A 48 0.12 SIDE CHAIN
REMARK 500 22 ARG A 29 0.26 SIDE CHAIN
REMARK 500 22 ARG A 48 0.17 SIDE CHAIN
REMARK 500 23 ARG A 29 0.26 SIDE CHAIN
REMARK 500 23 ARG A 48 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS ENTRY ALSO MATCHES FRAGMENTS OF
REMARK 999 FORMIN BINDING PROTEIN 11 (SWISS-PROT ACCESSION Q9R1C7)
REMARK 999 AND HUNTINGTIN-INTERACTING PROTEIN HYPA/FBP11
REMARK 999 (SWISS-PROT ACCESSION O75404, 98% IDENTITY)
DBREF 1UZC A 1 1 PDB 1UZC 1UZC 1 1
DBREF 1UZC A 2 71 UNP Q9H782 Q9H782 250 319
SEQRES 1 A 71 GLY SER GLN PRO ALA LYS LYS THR TYR THR TRP ASN THR
SEQRES 2 A 71 LYS GLU GLU ALA LYS GLN ALA PHE LYS GLU LEU LEU LYS
SEQRES 3 A 71 GLU LYS ARG VAL PRO SER ASN ALA SER TRP GLU GLN ALA
SEQRES 4 A 71 MET LYS MET ILE ILE ASN ASP PRO ARG TYR SER ALA LEU
SEQRES 5 A 71 ALA LYS LEU SER GLU LYS LYS GLN ALA PHE ASN ALA TYR
SEQRES 6 A 71 LYS VAL GLN THR GLU LYS
HELIX 1 1 THR A 13 LYS A 28 1 16
HELIX 2 2 SER A 35 ASN A 45 1 11
HELIX 3 3 ASP A 46 LEU A 52 5 7
HELIX 4 4 LYS A 54 THR A 69 1 16
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 - n 24 2 Bytes