Header list of 1ztr.pdb file
Complete list - v 10 2 Bytes
HEADER TRANSCRIPTION 27-MAY-05 1ZTR
TITLE SOLUTION STRUCTURE OF ENGRAILED HOMEODOMAIN L16A MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEGMENTATION POLARITY HOMEOBOX PROTEIN ENGRAILED;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ENGRAILED HOMEODOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: EN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: C41;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSET
KEYWDS ENGRAILED HOMEODOMAIN, DENATURED STATE, PROTEIN FOLDING, FOLDING
KEYWDS 2 INTERMEDIATE, MUTANT, TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR T.L.RELIGA,J.S.MARKSON,U.MAYOR,S.M.V.FREUND,A.R.FERSHT
REVDAT 3 10-NOV-21 1ZTR 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZTR 1 VERSN
REVDAT 1 18-OCT-05 1ZTR 0
JRNL AUTH T.L.RELIGA,J.S.MARKSON,U.MAYOR,S.M.FREUND,A.R.FERSHT
JRNL TITL SOLUTION STRUCTURE OF A PROTEIN DENATURED STATE AND FOLDING
JRNL TITL 2 INTERMEDIATE.
JRNL REF NATURE V. 437 1053 2005
JRNL REFN ISSN 0028-0836
JRNL PMID 16222301
JRNL DOI 10.1038/NATURE04054
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2004-04-12, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO ET AL (NMRPIPE), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 861 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS , INCLUDING 91 LONG RANGE NOES.
REMARK 4
REMARK 4 1ZTR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033107.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 150MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : U-15N, 50MM D-ACETATE, 100MM
REMARK 210 NACL, 7% D2O; U-15N, 100%D, 50MM
REMARK 210 D-ACETATE, 100MM NACL, 7% D2O; U-
REMARK 210 15N, 100%D, PHE, TYR-
REMARK 210 BACKPROTONATED, 50MM D-ACETATE,
REMARK 210 100MM NACL, 7% D2O; U-15N, 13C,
REMARK 210 50MM D-ACETATE, 100MM NACL, 7%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HSQC-NOESY-
REMARK 210 HSQC, 600MS MIXING TIME; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.106, CNS 1.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 TYR A 25 H GLU A 28 1.56
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 LYS A 2 66.18 -177.09
REMARK 500 1 PRO A 4 -165.62 -69.37
REMARK 500 1 ARG A 5 48.96 -140.09
REMARK 500 1 THR A 6 -77.90 -135.70
REMARK 500 1 PHE A 8 112.99 172.29
REMARK 500 1 SER A 9 36.76 -90.84
REMARK 500 1 SER A 10 -30.58 90.35
REMARK 500 1 ASN A 23 33.97 -161.22
REMARK 500 1 ILE A 56 68.94 79.41
REMARK 500 1 ARG A 57 -41.88 -153.14
REMARK 500 1 ARG A 58 53.77 36.03
REMARK 500 2 GLU A 1 51.30 -159.39
REMARK 500 2 LYS A 2 51.47 -146.93
REMARK 500 2 ARG A 5 52.41 -144.96
REMARK 500 2 THR A 6 -77.84 -129.98
REMARK 500 2 PHE A 8 109.15 179.11
REMARK 500 2 SER A 9 38.57 -98.29
REMARK 500 2 SER A 10 -29.85 94.95
REMARK 500 2 LEU A 40 -164.91 -101.25
REMARK 500 2 ALA A 54 -56.76 -162.12
REMARK 500 2 ILE A 56 68.55 78.56
REMARK 500 2 ARG A 57 -46.18 -147.69
REMARK 500 3 LYS A 2 57.65 -158.35
REMARK 500 3 PRO A 4 -165.60 -70.60
REMARK 500 3 THR A 6 -77.07 -107.71
REMARK 500 3 PHE A 8 114.31 172.11
REMARK 500 3 SER A 9 35.14 -89.30
REMARK 500 3 SER A 10 -30.68 90.16
REMARK 500 3 LEU A 40 -151.45 -156.66
REMARK 500 3 ASN A 41 -89.49 -136.55
REMARK 500 3 GLU A 42 -46.46 -136.97
REMARK 500 3 ALA A 54 -60.38 -90.73
REMARK 500 3 ILE A 56 68.76 78.94
REMARK 500 3 ARG A 57 -49.20 -149.11
REMARK 500 3 ARG A 58 85.19 59.99
REMARK 500 4 ASP A 0 108.11 -168.69
REMARK 500 4 LYS A 2 47.97 -170.30
REMARK 500 4 PRO A 4 -161.52 -54.80
REMARK 500 4 THR A 6 -76.59 -109.78
REMARK 500 4 PHE A 8 113.23 170.94
REMARK 500 4 SER A 9 38.58 -95.28
REMARK 500 4 SER A 10 -31.00 93.27
REMARK 500 4 ARG A 18 -43.37 -145.76
REMARK 500 4 ARG A 24 -55.95 -133.28
REMARK 500 4 TYR A 25 -34.37 -37.78
REMARK 500 4 SER A 35 -33.04 -39.13
REMARK 500 4 ASN A 41 -88.76 -118.69
REMARK 500 4 GLU A 42 -46.14 -141.04
REMARK 500 4 ARG A 57 -41.40 -174.10
REMARK 500 5 GLU A 1 57.36 -169.26
REMARK 500
REMARK 500 THIS ENTRY HAS 304 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ENH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ENGRAILED HOMEODOMAIN WT
DBREF 1ZTR A 0 59 UNP P02836 HMEN_DROME 453 512
SEQADV 1ZTR GLY A -1 UNP P02836 CLONING ARTIFACT
SEQADV 1ZTR ALA A 16 UNP P02836 LEU 469 ENGINEERED MUTATION
SEQADV 1ZTR ARG A 57 UNP P02836 LYS 510 CONFLICT
SEQADV 1ZTR ARG A 58 UNP P02836 LYS 511 CONFLICT
SEQRES 1 A 61 GLY ASP GLU LYS ARG PRO ARG THR ALA PHE SER SER GLU
SEQRES 2 A 61 GLN LEU ALA ARG ALA LYS ARG GLU PHE ASN GLU ASN ARG
SEQRES 3 A 61 TYR LEU THR GLU ARG ARG ARG GLN GLN LEU SER SER GLU
SEQRES 4 A 61 LEU GLY LEU ASN GLU ALA GLN ILE LYS ILE TRP PHE GLN
SEQRES 5 A 61 ASN LYS ARG ALA LYS ILE ARG ARG SER
HELIX 1 1 SER A 10 GLU A 22 1 13
HELIX 2 2 TYR A 25 ARG A 30 1 6
HELIX 3 3 ARG A 30 GLY A 39 1 10
HELIX 4 4 ASN A 41 ARG A 53 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 - v 10 2 Bytes