Header list of 1fex.pdb file
Complete list - b 23 2 Bytes
HEADER STRUCTURAL PROTEIN 24-JUL-00 1FEX
TITLE SOLUTION STRUCTURE OF MYB-DOMAIN OF HUMAN RAP1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRF2-INTERACTING TELOMERIC RAP1 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MYB-DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PEPTIDE OCCURS NATURALLY IN HUMANS (HOMO SAPIENS).
KEYWDS HELIX TURN HELIX, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE,
KEYWDS 2 RSGI, STRUCTURAL GENOMICS, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR S.HANAOKA,Y.NISHIMURA,RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE
AUTHOR 2 (RSGI)
REVDAT 3 23-FEB-22 1FEX 1 REMARK
REVDAT 2 24-FEB-09 1FEX 1 VERSN
REVDAT 1 19-SEP-01 1FEX 0
JRNL AUTH S.HANAOKA,A.NAGADOI,S.YOSHIMURA,S.AIMOTO,B.LI,T.DE LANGE,
JRNL AUTH 2 Y.NISHIMURA
JRNL TITL NMR STRUCTURE OF THE HRAP1 MYB MOTIF REVEALS A CANONICAL
JRNL TITL 2 THREE-HELIX BUNDLE LACKING THE POSITIVE SURFACE CHARGE
JRNL TITL 3 TYPICAL OF MYB DNA-BINDING DOMAINS.
JRNL REF J.MOL.BIOL. V. 312 167 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11545594
JRNL DOI 10.1006/JMBI.2001.4924
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 4.2.5, X-PLOR 3.851
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU,G.,
REMARK 3 PFEIFER, J. AND BAX,A. (NMRPIPE), BRNGER,A.T. (X-
REMARK 3 PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 884 RESTRAINTS, 838 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 39
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 7 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1FEX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011526.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0MM PROTEIN CONCENTRATION IN
REMARK 210 100MM POTASSIUM PHOSPHATE BUFFER
REMARK 210 PH5.5, 1MM NAN3 ; 90%H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
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 : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE 25 STRUCTURE WITH THE LOWEST
REMARK 210 ENERGY IN THOSE WITH THE FEWEST
REMARK 210 NUMBER OF CONSTRAINT VIOLATIONS.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR 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: 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 ARG A 2 64.14 -103.32
REMARK 500 1 ILE A 3 -169.86 46.31
REMARK 500 1 THR A 6 -165.20 -112.87
REMARK 500 1 ASN A 20 -60.79 -98.27
REMARK 500 1 ALA A 21 92.71 -60.51
REMARK 500 1 ARG A 22 28.76 -141.46
REMARK 500 1 SER A 25 -57.61 -158.95
REMARK 500 1 ALA A 31 -63.73 -90.40
REMARK 500 1 THR A 42 -166.54 -108.94
REMARK 500 1 HIS A 56 46.65 -169.87
REMARK 500 1 LEU A 57 -69.31 -129.91
REMARK 500 2 ARG A 2 -157.44 -157.93
REMARK 500 2 ILE A 3 -172.15 38.58
REMARK 500 2 ALA A 4 89.77 47.06
REMARK 500 2 THR A 6 -176.28 -67.37
REMARK 500 2 ARG A 22 -43.11 -166.63
REMARK 500 2 SER A 25 -43.14 -165.92
REMARK 500 2 SER A 39 -72.38 -66.40
REMARK 500 2 THR A 42 -81.21 -88.44
REMARK 500 2 GLN A 43 65.07 -164.60
REMARK 500 2 HIS A 56 49.43 -168.69
REMARK 500 2 LEU A 57 -47.96 -131.88
REMARK 500 3 ALA A 21 76.09 -67.83
REMARK 500 3 SER A 25 -56.78 -162.77
REMARK 500 3 THR A 28 29.11 -156.39
REMARK 500 3 SER A 39 72.86 -161.63
REMARK 500 3 GLN A 43 86.41 59.82
REMARK 500 3 HIS A 56 49.69 -163.63
REMARK 500 3 LEU A 57 -65.11 -124.55
REMARK 500 3 ARG A 58 105.46 -58.69
REMARK 500 4 ALA A 4 -166.94 53.14
REMARK 500 4 ARG A 22 27.42 -153.36
REMARK 500 4 SER A 25 -38.61 -168.19
REMARK 500 4 SER A 39 -73.36 -123.98
REMARK 500 4 LEU A 41 -137.70 -140.52
REMARK 500 4 THR A 42 -62.33 -144.83
REMARK 500 4 GLN A 43 71.22 -173.22
REMARK 500 4 HIS A 56 44.41 -169.08
REMARK 500 4 LEU A 57 -70.08 -127.25
REMARK 500 5 PHE A 5 73.64 -115.09
REMARK 500 5 ALA A 21 99.91 -45.84
REMARK 500 5 ARG A 22 28.97 -144.90
REMARK 500 5 SER A 25 -42.70 -165.16
REMARK 500 5 THR A 28 15.93 -147.93
REMARK 500 5 ASN A 30 27.07 49.48
REMARK 500 5 THR A 42 -171.55 -56.44
REMARK 500 5 HIS A 56 20.24 -150.00
REMARK 500 5 LEU A 57 -64.84 -93.14
REMARK 500 6 ALA A 21 -86.67 -49.58
REMARK 500 6 SER A 25 -49.66 -152.44
REMARK 500
REMARK 500 THIS ENTRY HAS 225 RAMACHANDRAN OUTLIERS.
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 2 0.30 SIDE CHAIN
REMARK 500 1 ARG A 22 0.26 SIDE CHAIN
REMARK 500 1 ARG A 52 0.23 SIDE CHAIN
REMARK 500 1 ARG A 58 0.29 SIDE CHAIN
REMARK 500 2 ARG A 2 0.25 SIDE CHAIN
REMARK 500 2 ARG A 22 0.28 SIDE CHAIN
REMARK 500 2 ARG A 52 0.27 SIDE CHAIN
REMARK 500 2 ARG A 58 0.30 SIDE CHAIN
REMARK 500 3 ARG A 2 0.28 SIDE CHAIN
REMARK 500 3 ARG A 22 0.29 SIDE CHAIN
REMARK 500 3 ARG A 52 0.19 SIDE CHAIN
REMARK 500 3 ARG A 58 0.30 SIDE CHAIN
REMARK 500 4 ARG A 2 0.22 SIDE CHAIN
REMARK 500 4 ARG A 22 0.29 SIDE CHAIN
REMARK 500 4 ARG A 52 0.21 SIDE CHAIN
REMARK 500 4 ARG A 58 0.32 SIDE CHAIN
REMARK 500 5 ARG A 2 0.28 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 5 ARG A 52 0.25 SIDE CHAIN
REMARK 500 5 ARG A 58 0.32 SIDE CHAIN
REMARK 500 6 ARG A 2 0.31 SIDE CHAIN
REMARK 500 6 ARG A 22 0.28 SIDE CHAIN
REMARK 500 6 ARG A 52 0.27 SIDE CHAIN
REMARK 500 6 ARG A 58 0.21 SIDE CHAIN
REMARK 500 7 ARG A 2 0.23 SIDE CHAIN
REMARK 500 7 ARG A 22 0.27 SIDE CHAIN
REMARK 500 7 ARG A 52 0.31 SIDE CHAIN
REMARK 500 7 ARG A 58 0.32 SIDE CHAIN
REMARK 500 8 ARG A 2 0.21 SIDE CHAIN
REMARK 500 8 ARG A 22 0.23 SIDE CHAIN
REMARK 500 8 ARG A 52 0.32 SIDE CHAIN
REMARK 500 8 ARG A 58 0.26 SIDE CHAIN
REMARK 500 9 ARG A 2 0.23 SIDE CHAIN
REMARK 500 9 ARG A 22 0.29 SIDE CHAIN
REMARK 500 9 ARG A 52 0.23 SIDE CHAIN
REMARK 500 9 ARG A 58 0.28 SIDE CHAIN
REMARK 500 10 ARG A 2 0.30 SIDE CHAIN
REMARK 500 10 ARG A 22 0.29 SIDE CHAIN
REMARK 500 10 ARG A 52 0.29 SIDE CHAIN
REMARK 500 10 ARG A 58 0.31 SIDE CHAIN
REMARK 500 11 ARG A 2 0.22 SIDE CHAIN
REMARK 500 11 ARG A 22 0.26 SIDE CHAIN
REMARK 500 11 ARG A 52 0.29 SIDE CHAIN
REMARK 500 11 ARG A 58 0.32 SIDE CHAIN
REMARK 500 12 ARG A 2 0.29 SIDE CHAIN
REMARK 500 12 ARG A 22 0.30 SIDE CHAIN
REMARK 500 12 ARG A 52 0.31 SIDE CHAIN
REMARK 500 12 ARG A 58 0.22 SIDE CHAIN
REMARK 500 13 ARG A 2 0.28 SIDE CHAIN
REMARK 500 13 ARG A 22 0.29 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 100 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: TRT001000207.1 RELATED DB: TARGETDB
DBREF 1FEX A 1 59 UNP Q9NYB0 TE2IP_HUMAN 132 190
SEQRES 1 A 59 GLY ARG ILE ALA PHE THR ASP ALA ASP ASP VAL ALA ILE
SEQRES 2 A 59 LEU THR TYR VAL LYS GLU ASN ALA ARG SER PRO SER SER
SEQRES 3 A 59 VAL THR GLY ASN ALA LEU TRP LYS ALA MET GLU LYS SER
SEQRES 4 A 59 SER LEU THR GLN HIS SER TRP GLN SER LEU LYS ASP ARG
SEQRES 5 A 59 TYR LEU LYS HIS LEU ARG GLY
HELIX 1 1 THR A 6 ASN A 20 1 15
HELIX 2 2 ARG A 22 VAL A 27 1 6
HELIX 3 3 ASN A 30 LYS A 38 1 9
HELIX 4 4 SER A 45 LEU A 57 1 13
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