Header list of 1g2h.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSCRIPTION 19-OCT-00 1G2H
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE TYRR PROTEIN OF
TITLE 2 HAEMOPHILUS INFLUENZAE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTIONAL REGULATORY PROTEIN TYRR HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN; RESIDUES 258-318;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TYRR; PROTEIN STRUCTURE; NMR; DNA-BINDING DOMAIN; HELIX-TURN-HELIX
KEYWDS 2 MOTIF, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 32
AUTHOR Y.WANG,S.ZHAO,R.L.SOMERVILLE,O.JARDETZKY
REVDAT 4 23-FEB-22 1G2H 1 REMARK
REVDAT 3 24-FEB-09 1G2H 1 VERSN
REVDAT 2 13-JUN-01 1G2H 1 AUTHOR JRNL
REVDAT 1 07-MAR-01 1G2H 0
JRNL AUTH Y.WANG,S.ZHAO,R.L.SOMERVILLE,O.JARDETZKY
JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF THE TYRR
JRNL TITL 2 PROTEIN OF HAEMOPHILUS INFLUENZAE.
JRNL REF PROTEIN SCI. V. 10 592 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11344327
JRNL DOI 10.1110/PS.45301
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.5, X-PLOR 3.85
REMARK 3 AUTHORS : VIARN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G2H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012151.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM TYRR(258-318), 50MM
REMARK 210 PHOSPHATE BUFFER; 2MM TYRR(258-
REMARK 210 318), U-15N, 50MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HMQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.85
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 32
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURES WERE DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D 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 O VAL A 25 H PHE A 29 1.51
REMARK 500 O GLU A 22 H LEU A 26 1.58
REMARK 500 O GLU A 22 H VAL A 25 1.59
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 2 -160.31 -120.93
REMARK 500 1 SER A 5 172.83 172.95
REMARK 500 1 LEU A 14 60.73 38.77
REMARK 500 1 ASP A 15 -36.82 -171.88
REMARK 500 1 ILE A 17 10.22 -152.41
REMARK 500 1 SER A 35 103.25 55.05
REMARK 500 1 SER A 46 40.00 -89.83
REMARK 500 1 HIS A 47 -87.15 43.89
REMARK 500 1 ILE A 59 -140.28 -125.05
REMARK 500 2 ALA A 2 -163.48 -65.52
REMARK 500 2 VAL A 3 -154.75 -62.81
REMARK 500 2 ILE A 4 38.88 28.65
REMARK 500 2 LEU A 6 -82.95 38.40
REMARK 500 2 GLU A 8 50.80 -112.86
REMARK 500 2 LEU A 14 -84.35 59.31
REMARK 500 2 ASP A 15 -31.01 -31.73
REMARK 500 2 ILE A 17 67.81 -156.59
REMARK 500 2 SER A 35 115.66 58.09
REMARK 500 2 SER A 46 41.88 -88.41
REMARK 500 2 HIS A 47 -87.83 47.92
REMARK 500 2 ILE A 59 -139.94 -92.98
REMARK 500 3 ALA A 2 -148.16 -141.66
REMARK 500 3 SER A 5 58.92 178.24
REMARK 500 3 LEU A 6 -67.71 60.91
REMARK 500 3 LEU A 14 -83.40 60.41
REMARK 500 3 ASP A 15 -27.13 -37.77
REMARK 500 3 ILE A 17 14.84 -159.69
REMARK 500 3 TYR A 33 78.43 -108.16
REMARK 500 3 PRO A 34 68.59 -67.81
REMARK 500 3 SER A 35 91.35 164.70
REMARK 500 3 SER A 46 35.34 -90.93
REMARK 500 3 HIS A 47 -86.63 46.19
REMARK 500 3 THR A 48 -36.79 -39.48
REMARK 500 3 ILE A 59 -139.68 -123.17
REMARK 500 4 SER A 5 64.86 179.77
REMARK 500 4 LEU A 6 -77.83 59.85
REMARK 500 4 GLU A 8 45.62 -105.77
REMARK 500 4 LEU A 14 -87.33 57.49
REMARK 500 4 ASP A 15 -31.78 -34.99
REMARK 500 4 GLU A 16 -9.64 -55.08
REMARK 500 4 ILE A 17 19.40 -165.34
REMARK 500 4 SER A 35 106.52 55.51
REMARK 500 4 SER A 46 37.70 -90.26
REMARK 500 4 HIS A 47 -86.30 43.90
REMARK 500 4 THR A 48 -39.74 -38.83
REMARK 500 5 SER A 5 176.35 175.81
REMARK 500 5 LEU A 14 -82.29 66.07
REMARK 500 5 ASP A 15 45.22 -62.24
REMARK 500 5 PRO A 34 67.33 -68.46
REMARK 500 5 SER A 35 102.22 167.80
REMARK 500
REMARK 500 THIS ENTRY HAS 339 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 37 0.32 SIDE CHAIN
REMARK 500 1 ARG A 42 0.24 SIDE CHAIN
REMARK 500 2 ARG A 37 0.32 SIDE CHAIN
REMARK 500 2 ARG A 42 0.18 SIDE CHAIN
REMARK 500 3 ARG A 37 0.20 SIDE CHAIN
REMARK 500 3 ARG A 42 0.32 SIDE CHAIN
REMARK 500 4 ARG A 37 0.24 SIDE CHAIN
REMARK 500 4 ARG A 42 0.31 SIDE CHAIN
REMARK 500 5 ARG A 37 0.23 SIDE CHAIN
REMARK 500 5 ARG A 42 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.23 SIDE CHAIN
REMARK 500 6 ARG A 42 0.28 SIDE CHAIN
REMARK 500 7 ARG A 37 0.31 SIDE CHAIN
REMARK 500 7 ARG A 42 0.32 SIDE CHAIN
REMARK 500 8 ARG A 37 0.26 SIDE CHAIN
REMARK 500 8 ARG A 42 0.29 SIDE CHAIN
REMARK 500 9 ARG A 37 0.25 SIDE CHAIN
REMARK 500 9 ARG A 42 0.30 SIDE CHAIN
REMARK 500 10 ARG A 37 0.30 SIDE CHAIN
REMARK 500 10 ARG A 42 0.28 SIDE CHAIN
REMARK 500 11 ARG A 37 0.26 SIDE CHAIN
REMARK 500 11 ARG A 42 0.32 SIDE CHAIN
REMARK 500 12 ARG A 37 0.32 SIDE CHAIN
REMARK 500 12 ARG A 42 0.24 SIDE CHAIN
REMARK 500 13 ARG A 37 0.32 SIDE CHAIN
REMARK 500 13 ARG A 42 0.26 SIDE CHAIN
REMARK 500 14 ARG A 37 0.32 SIDE CHAIN
REMARK 500 14 ARG A 42 0.24 SIDE CHAIN
REMARK 500 15 ARG A 37 0.17 SIDE CHAIN
REMARK 500 15 ARG A 42 0.21 SIDE CHAIN
REMARK 500 16 ARG A 37 0.28 SIDE CHAIN
REMARK 500 16 ARG A 42 0.31 SIDE CHAIN
REMARK 500 17 ARG A 37 0.30 SIDE CHAIN
REMARK 500 17 ARG A 42 0.23 SIDE CHAIN
REMARK 500 18 ARG A 37 0.23 SIDE CHAIN
REMARK 500 18 ARG A 42 0.30 SIDE CHAIN
REMARK 500 19 ARG A 37 0.29 SIDE CHAIN
REMARK 500 19 ARG A 42 0.30 SIDE CHAIN
REMARK 500 20 ARG A 37 0.31 SIDE CHAIN
REMARK 500 20 ARG A 42 0.31 SIDE CHAIN
REMARK 500 21 ARG A 37 0.13 SIDE CHAIN
REMARK 500 21 ARG A 42 0.23 SIDE CHAIN
REMARK 500 22 ARG A 37 0.31 SIDE CHAIN
REMARK 500 22 ARG A 42 0.29 SIDE CHAIN
REMARK 500 23 ARG A 37 0.32 SIDE CHAIN
REMARK 500 23 ARG A 42 0.14 SIDE CHAIN
REMARK 500 24 ARG A 37 0.23 SIDE CHAIN
REMARK 500 24 ARG A 42 0.19 SIDE CHAIN
REMARK 500 25 ARG A 37 0.09 SIDE CHAIN
REMARK 500 25 ARG A 42 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 64 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4784 RELATED DB: BMRB
DBREF 1G2H A 1 61 UNP P44694 TYRR_HAEIN 258 318
SEQRES 1 A 61 SER ALA VAL ILE SER LEU ASP GLU PHE GLU ASN LYS THR
SEQRES 2 A 61 LEU ASP GLU ILE ILE GLY PHE TYR GLU ALA GLN VAL LEU
SEQRES 3 A 61 LYS LEU PHE TYR ALA GLU TYR PRO SER THR ARG LYS LEU
SEQRES 4 A 61 ALA GLN ARG LEU GLY VAL SER HIS THR ALA ILE ALA ASN
SEQRES 5 A 61 LYS LEU LYS GLN TYR GLY ILE GLY LYS
HELIX 1 1 GLY A 19 TYR A 33 1 15
HELIX 2 2 SER A 35 LEU A 43 1 9
HELIX 3 3 HIS A 47 GLN A 56 1 10
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