Header list of 2hoa.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN 04-APR-92 2HOA
TITLE STRUCTURE DETERMINATION OF THE ANTP(C39->S) HOMEODOMAIN FROM NUCLEAR
TITLE 2 MAGNETIC RESONANCE DATA IN SOLUTION USING A NOVEL STRATEGY FOR THE
TITLE 3 STRUCTURE CALCULATION WITH THE PROGRAMS DIANA, CALIBA, HABAS AND
TITLE 4 GLOMSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTENNAPEDIA PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.GUNTERT,Y.-Q.QIAN,G.OTTING,M.MULLER,W.J.GEHRING,K.WUTHRICH
REVDAT 4 09-MAR-22 2HOA 1 KEYWDS REMARK SEQADV
REVDAT 3 24-FEB-09 2HOA 1 VERSN
REVDAT 2 01-APR-03 2HOA 1 JRNL
REVDAT 1 31-OCT-93 2HOA 0
JRNL AUTH P.GUNTERT,Y.Q.QIAN,G.OTTING,M.MULLER,W.GEHRING,K.WUTHRICH
JRNL TITL STRUCTURE DETERMINATION OF THE ANTP (C39----S) HOMEODOMAIN
JRNL TITL 2 FROM NUCLEAR MAGNETIC RESONANCE DATA IN SOLUTION USING A
JRNL TITL 3 NOVEL STRATEGY FOR THE STRUCTURE CALCULATION WITH THE
JRNL TITL 4 PROGRAMS DIANA, CALIBA, HABAS AND GLOMSA.
JRNL REF J.MOL.BIOL. V. 217 531 1991
JRNL REFN ISSN 0022-2836
JRNL PMID 1671604
JRNL DOI 10.1016/0022-2836(91)90755-U
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.-Q.QIAN,M.BILLETER,G.OTTING,M.MUELLER,W.J.GEHRING,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL THE STRUCTURE OF THE ANTENNAPEDIA HOMEODOMAIN DETERMINED BY
REMARK 1 TITL 2 NMR SPECTROSCOPY IN SOLUTION: COMPARISON WITH PROKARYOTIC
REMARK 1 TITL 3 REPRESSORS
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 59 573 1989
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.BILLETER,Y.-Q.QIAN,G.OTTING,M.MUELLER,W.J.GEHRING,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF THE
REMARK 1 TITL 2 ANTENNAPEDIA HOMEODOMAIN FROM DROSOPHILA IN SOLUTION BY 1H
REMARK 1 TITL 3 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
REMARK 1 REF J.MOL.BIOL. V. 214 183 1990
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 3
REMARK 1 AUTH G.OTTING,Y.-Q.QIAN,M.MUELLER,M.AFFOLTER,W.J.GEHRING,
REMARK 1 AUTH 2 K.WUTHRICH
REMARK 1 TITL SECONDARY STRUCTURE DETERMINATION FOR THE ANTENNAPEDIA
REMARK 1 TITL 2 HOMEODOMAIN BY NUCLEAR MAGNETIC RESONANCE AND EVIDENCE FOR A
REMARK 1 TITL 3 HELIX-TURN-HELIX MOTIF
REMARK 1 REF EMBO J. V. 7 4305 1988
REMARK 1 REFN ISSN 0261-4189
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DIANA, AMBER
REMARK 3 AUTHORS : GUNTERT,BRAUN,WUTHRICH (DIANA),
REMARK 3 PEARLMAN,CASE,CALDWELL,SIEBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HOA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178213.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 7 TYR A 25 CB - CG - CD2 ANGL. DEV. = -11.8 DEGREES
REMARK 500 7 TYR A 25 CB - CG - CD1 ANGL. DEV. = 11.4 DEGREES
REMARK 500 8 ARG A 53 C - N - CA ANGL. DEV. = 18.0 DEGREES
REMARK 500 10 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 13 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 14 TYR A 25 CB - CG - CD2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 15 TYR A 25 CB - CG - CD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 15 TYR A 25 CB - CG - CD1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 18 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 19 TYR A 25 CB - CG - CD2 ANGL. DEV. = -3.8 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 ARG A 1 -96.47 -163.28
REMARK 500 1 LYS A 2 74.41 50.04
REMARK 500 1 SER A 39 72.33 70.81
REMARK 500 1 THR A 62 -44.96 -141.36
REMARK 500 2 LYS A 2 85.45 -154.56
REMARK 500 2 ARG A 3 -89.07 -97.11
REMARK 500 2 ARG A 5 92.51 78.33
REMARK 500 2 PHE A 22 -75.42 -82.57
REMARK 500 2 SER A 39 60.16 117.16
REMARK 500 2 LYS A 58 38.90 -81.28
REMARK 500 2 ASN A 60 12.52 57.60
REMARK 500 2 LYS A 61 62.98 -155.25
REMARK 500 3 ARG A 1 -99.14 46.17
REMARK 500 3 ARG A 3 -155.19 45.91
REMARK 500 3 GLN A 6 -165.87 56.32
REMARK 500 3 LEU A 38 -85.16 -94.65
REMARK 500 3 SER A 39 52.50 158.43
REMARK 500 3 ASN A 60 62.58 -116.42
REMARK 500 3 GLU A 65 73.20 -152.85
REMARK 500 4 LYS A 2 31.72 -145.59
REMARK 500 4 ARG A 5 87.74 -153.83
REMARK 500 4 PHE A 22 -76.75 -80.78
REMARK 500 4 SER A 39 63.52 80.81
REMARK 500 4 LYS A 61 67.05 -157.57
REMARK 500 4 THR A 62 103.06 71.32
REMARK 500 4 PRO A 66 37.21 -76.24
REMARK 500 5 ARG A 1 92.36 68.24
REMARK 500 5 SER A 39 79.41 70.39
REMARK 500 5 ASN A 60 92.36 -170.47
REMARK 500 5 LYS A 61 -58.28 -135.27
REMARK 500 5 THR A 62 -32.78 -174.59
REMARK 500 6 ARG A 1 -91.30 44.98
REMARK 500 6 ARG A 3 -158.84 58.62
REMARK 500 6 GLN A 6 113.22 77.66
REMARK 500 6 SER A 39 58.30 78.22
REMARK 500 6 ASN A 60 93.84 -164.00
REMARK 500 6 LYS A 63 -156.47 54.15
REMARK 500 6 GLU A 65 79.40 -107.76
REMARK 500 7 ARG A 1 -47.37 -177.84
REMARK 500 7 ARG A 3 -173.13 58.90
REMARK 500 7 ARG A 5 114.30 67.62
REMARK 500 7 THR A 7 32.82 -81.73
REMARK 500 7 LEU A 38 -80.37 -84.34
REMARK 500 7 SER A 39 57.42 150.05
REMARK 500 7 THR A 62 -60.41 -99.85
REMARK 500 8 ARG A 1 138.30 -170.18
REMARK 500 8 ARG A 5 72.64 66.60
REMARK 500 8 GLN A 6 179.31 70.05
REMARK 500 8 SER A 39 60.84 73.59
REMARK 500 8 ASN A 51 -73.05 -51.28
REMARK 500
REMARK 500 THIS ENTRY HAS 142 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 ASN A 51 ARG A 52 8 -120.63
REMARK 500 ARG A 52 ARG A 53 8 -98.61
REMARK 500 ARG A 53 MET A 54 8 128.39
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 25 0.06 SIDE CHAIN
REMARK 500 1 ARG A 30 0.08 SIDE CHAIN
REMARK 500 2 ARG A 29 0.08 SIDE CHAIN
REMARK 500 2 ARG A 31 0.13 SIDE CHAIN
REMARK 500 3 TYR A 8 0.09 SIDE CHAIN
REMARK 500 3 TYR A 11 0.10 SIDE CHAIN
REMARK 500 3 TYR A 25 0.07 SIDE CHAIN
REMARK 500 3 ARG A 31 0.08 SIDE CHAIN
REMARK 500 4 PHE A 22 0.11 SIDE CHAIN
REMARK 500 4 ARG A 30 0.08 SIDE CHAIN
REMARK 500 6 TYR A 11 0.08 SIDE CHAIN
REMARK 500 6 TYR A 25 0.15 SIDE CHAIN
REMARK 500 6 ARG A 30 0.11 SIDE CHAIN
REMARK 500 7 PHE A 20 0.08 SIDE CHAIN
REMARK 500 7 ARG A 31 0.11 SIDE CHAIN
REMARK 500 8 TYR A 25 0.07 SIDE CHAIN
REMARK 500 10 TYR A 8 0.09 SIDE CHAIN
REMARK 500 10 TYR A 25 0.15 SIDE CHAIN
REMARK 500 11 TYR A 8 0.12 SIDE CHAIN
REMARK 500 11 ARG A 24 0.11 SIDE CHAIN
REMARK 500 12 PHE A 22 0.06 SIDE CHAIN
REMARK 500 12 ARG A 52 0.12 SIDE CHAIN
REMARK 500 13 TYR A 11 0.12 SIDE CHAIN
REMARK 500 13 ARG A 52 0.08 SIDE CHAIN
REMARK 500 14 TYR A 8 0.09 SIDE CHAIN
REMARK 500 14 ARG A 24 0.09 SIDE CHAIN
REMARK 500 14 ARG A 52 0.10 SIDE CHAIN
REMARK 500 14 ARG A 53 0.08 SIDE CHAIN
REMARK 500 15 PHE A 22 0.06 SIDE CHAIN
REMARK 500 15 ARG A 31 0.09 SIDE CHAIN
REMARK 500 16 TYR A 25 0.10 SIDE CHAIN
REMARK 500 16 PHE A 49 0.08 SIDE CHAIN
REMARK 500 16 ARG A 52 0.11 SIDE CHAIN
REMARK 500 18 TYR A 25 0.09 SIDE CHAIN
REMARK 500 18 ARG A 53 0.08 SIDE CHAIN
REMARK 500 19 PHE A 22 0.08 SIDE CHAIN
REMARK 500 19 ARG A 31 0.08 SIDE CHAIN
REMARK 500 19 ARG A 52 0.09 SIDE CHAIN
REMARK 500 20 TYR A 8 0.07 SIDE CHAIN
REMARK 500 20 ARG A 24 0.11 SIDE CHAIN
REMARK 500 20 ARG A 52 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 8 ASN A 51 10.45
REMARK 500 8 ARG A 53 -10.04
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HOA A 1 67 UNP P02833 ANTP_DROME 297 363
SEQADV 2HOA SER A 39 UNP P02833 CYS 335 CONFLICT
SEQRES 1 A 68 MET ARG LYS ARG GLY ARG GLN THR TYR THR ARG TYR GLN
SEQRES 2 A 68 THR LEU GLU LEU GLU LYS GLU PHE HIS PHE ASN ARG TYR
SEQRES 3 A 68 LEU THR ARG ARG ARG ARG ILE GLU ILE ALA HIS ALA LEU
SEQRES 4 A 68 SER LEU THR GLU ARG GLN ILE LYS ILE TRP PHE GLN ASN
SEQRES 5 A 68 ARG ARG MET LYS TRP LYS LYS GLU ASN LYS THR LYS GLY
SEQRES 6 A 68 GLU PRO GLY
HELIX 1 H1 ARG A 10 HIS A 21 1ALPHA HELIX 12
HELIX 2 H2 ARG A 28 LEU A 38 1ALPHA HELIX 11
HELIX 3 H3 GLU A 42 ARG A 52 1ALPHA HELIX 11
HELIX 4 H4 ARG A 53 GLU A 59 1DISORDERED HELIX 7
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