Header list of 1x0o.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSCRIPTION 25-MAR-05 1X0O
TITLE HUMAN ARNT C-TERMINAL PAS DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYL HYDROCARBON RECEPTOR NUCLEAR TRANSLOCATOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL PAS DOMAIN;
COMPND 5 SYNONYM: ARNT PROTEIN, DIOXIN RECEPTOR, NUCLEAR TRANSLOCATOR,
COMPND 6 HYPOXIA-INDUCIBLE FACTOR 1 BETA, HIF-1 BETA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PAS, MIXED ALPHA-BETA FOLD, HYPOXIA, ARYL HYDROCARBON RECEPTOR
KEYWDS 2 NUCLEAR TRANSLOCATOR, ARNT, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR P.B.CARD,P.J.ERBEL,K.H.GARDNER
REVDAT 3 02-MAR-22 1X0O 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X0O 1 VERSN
REVDAT 1 25-OCT-05 1X0O 0
JRNL AUTH P.B.CARD,P.J.ERBEL,K.H.GARDNER
JRNL TITL STRUCTURAL BASIS OF ARNT PAS-B DIMERIZATION: USE OF A COMMON
JRNL TITL 2 BETA-SHEET INTERFACE FOR HETERO- AND HOMODIMERIZATION.
JRNL REF J.MOL.BIOL. V. 353 664 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 16181639
JRNL DOI 10.1016/J.JMB.2005.08.043
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X0O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000024231.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 310
REMARK 210 PH : 6.5; 6.6
REMARK 210 IONIC STRENGTH : 17MM NACL; 17MM NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM HARNT C-TERM PAS DOMAIN U
REMARK 210 -15N,13C; 50MM TRIS BUFFER; 17MM
REMARK 210 NACL, 5MM DTT; 0.478MM HARNT C-
REMARK 210 TERM PAS DOMAIN U-15N; 50MM TRIS
REMARK 210 BUFFER; 17MM NACL, 5MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N_13C-SEPERATED NOESY;
REMARK 210 3D_15N-SEPARATED_NOESY; HNHA; 3D
REMARK 210 HNCACB; 3D CBCA(CO)NH; 3D HNCO;
REMARK 210 3D_15N-SEPERATED TOCSY; 3D HCCH-
REMARK 210 TOCSY; HBCBCGCDHD; IPAP_HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRVIEW 5.2.2, ARIA 1.2, CNS 1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
REMARK 210
REMARK 210 REMARK: USED STANDARD 2D AND 3D HOMONUCLEAR AND HETERONUCLEAR
REMARK 210 -EDITED 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 HD1 HIS A 50 OD2 ASP A 53 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 65.40 60.08
REMARK 500 1 VAL A 6 122.98 74.37
REMARK 500 1 LYS A 68 98.46 61.93
REMARK 500 1 PRO A 98 32.19 -69.71
REMARK 500 1 VAL A 113 -90.33 -101.75
REMARK 500 1 SER A 116 43.59 -145.67
REMARK 500 1 SER A 117 -43.66 -164.16
REMARK 500 2 MET A 3 -32.95 175.71
REMARK 500 2 LYS A 68 96.37 62.12
REMARK 500 2 SER A 100 -21.34 -146.35
REMARK 500 2 VAL A 113 -92.47 -98.88
REMARK 500 2 SER A 117 131.60 -178.04
REMARK 500 3 VAL A 6 132.84 -170.26
REMARK 500 3 THR A 10 31.43 -87.34
REMARK 500 3 LYS A 68 93.48 57.48
REMARK 500 3 SER A 100 -16.31 -145.06
REMARK 500 3 VAL A 113 -97.96 -95.08
REMARK 500 3 ASN A 115 -148.40 53.30
REMARK 500 4 ASN A 5 93.81 -171.24
REMARK 500 4 CYS A 7 77.47 57.77
REMARK 500 4 LYS A 68 80.54 49.08
REMARK 500 4 PRO A 98 -9.91 -59.55
REMARK 500 4 VAL A 113 -91.09 -92.92
REMARK 500 5 VAL A 6 144.28 -175.99
REMARK 500 5 PRO A 9 153.29 -48.12
REMARK 500 5 LYS A 68 109.72 -29.58
REMARK 500 5 SER A 80 -178.53 -63.79
REMARK 500 5 ASP A 101 -19.30 73.24
REMARK 500 5 TYR A 105 -174.59 -179.03
REMARK 500 5 VAL A 113 -140.81 -92.57
REMARK 500 5 LYS A 114 -154.54 -129.33
REMARK 500 5 ASN A 115 -48.64 74.83
REMARK 500 6 MET A 3 -66.05 69.47
REMARK 500 6 ASN A 5 -75.59 69.30
REMARK 500 6 VAL A 6 -172.35 -179.02
REMARK 500 6 CYS A 7 91.54 -61.65
REMARK 500 6 LYS A 68 92.33 58.66
REMARK 500 6 SER A 100 -24.47 -145.96
REMARK 500 6 ASP A 101 -7.40 69.75
REMARK 500 6 SER A 116 -71.56 73.29
REMARK 500 6 GLN A 118 91.09 77.76
REMARK 500 7 MET A 3 -156.98 64.53
REMARK 500 7 THR A 10 32.86 -89.13
REMARK 500 7 LYS A 68 99.36 62.36
REMARK 500 7 PRO A 98 9.40 -68.25
REMARK 500 7 VAL A 113 -113.60 -88.90
REMARK 500 7 ASN A 115 45.97 73.02
REMARK 500 7 SER A 116 44.49 -154.90
REMARK 500 8 ALA A 2 -64.86 -134.68
REMARK 500 8 MET A 3 117.62 67.75
REMARK 500
REMARK 500 THIS ENTRY HAS 154 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 12 ARG A 79 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1X0O A 5 119 UNP P27540 ARNT_HUMAN 356 470
SEQADV 1X0O GLY A 1 UNP P27540 CLONING ARTIFACT
SEQADV 1X0O ALA A 2 UNP P27540 CLONING ARTIFACT
SEQADV 1X0O MET A 3 UNP P27540 CLONING ARTIFACT
SEQADV 1X0O ASP A 4 UNP P27540 CLONING ARTIFACT
SEQRES 1 A 119 GLY ALA MET ASP ASN VAL CYS GLN PRO THR GLU PHE ILE
SEQRES 2 A 119 SER ARG HIS ASN ILE GLU GLY ILE PHE THR PHE VAL ASP
SEQRES 3 A 119 HIS ARG CYS VAL ALA THR VAL GLY TYR GLN PRO GLN GLU
SEQRES 4 A 119 LEU LEU GLY LYS ASN ILE VAL GLU PHE CYS HIS PRO GLU
SEQRES 5 A 119 ASP GLN GLN LEU LEU ARG ASP SER PHE GLN GLN VAL VAL
SEQRES 6 A 119 LYS LEU LYS GLY GLN VAL LEU SER VAL MET PHE ARG PHE
SEQRES 7 A 119 ARG SER LYS ASN GLN GLU TRP LEU TRP MET ARG THR SER
SEQRES 8 A 119 SER PHE THR PHE GLN ASN PRO TYR SER ASP GLU ILE GLU
SEQRES 9 A 119 TYR ILE ILE CYS THR ASN THR ASN VAL LYS ASN SER SER
SEQRES 10 A 119 GLN GLU
HELIX 1 1 ARG A 28 GLY A 34 1 7
HELIX 2 2 GLN A 36 LEU A 41 1 6
HELIX 3 3 ASP A 53 LYS A 68 1 16
SHEET 1 A 5 PHE A 22 VAL A 25 0
SHEET 2 A 5 GLU A 11 HIS A 16 -1 N ARG A 15 O PHE A 24
SHEET 3 A 5 ILE A 103 ASN A 112 -1 O CYS A 108 N SER A 14
SHEET 4 A 5 TRP A 85 GLN A 96 -1 N ARG A 89 O THR A 111
SHEET 5 A 5 LEU A 72 ARG A 79 -1 N VAL A 74 O THR A 90
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 2 2 Bytes