Header list of 1pls.pdb file
Complete list - v 29 2 Bytes
HEADER PHOSPHORYLATION 03-MAY-94 1PLS
TITLE SOLUTION STRUCTURE OF A PLECKSTRIN HOMOLOGY DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PLECKSTRIN HOMOLOGY DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDNA;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS PHOSPHORYLATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.S.YOON,P.J.HAJDUK,A.M.PETROS,E.T.OLEJNICZAK,R.P.MEADOWS,S.W.FESIK
REVDAT 4 29-NOV-17 1PLS 1 REMARK HELIX
REVDAT 3 24-FEB-09 1PLS 1 VERSN
REVDAT 2 01-APR-03 1PLS 1 JRNL
REVDAT 1 03-JUN-95 1PLS 0
JRNL AUTH H.S.YOON,P.J.HAJDUK,A.M.PETROS,E.T.OLEJNICZAK,R.P.MEADOWS,
JRNL AUTH 2 S.W.FESIK
JRNL TITL SOLUTION STRUCTURE OF A PLECKSTRIN-HOMOLOGY DOMAIN.
JRNL REF NATURE V. 369 672 1994
JRNL REFN ISSN 0028-0836
JRNL PMID 8208296
JRNL DOI 10.1038/369672A0
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.E.HARLAN,P.J.HAJDUK,H.S.YOON,S.W.FESIK
REMARK 1 TITL PLECKSTRIN HOMOLOGY DOMAINS BIND TO
REMARK 1 TITL 2 PHOSPHATIDYLINOSITOL-4,5-BIPHOSPHATE
REMARK 1 REF NATURE V. 371 168 1994
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1PLS 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_1000175730.
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 : 25
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: 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 SER A 16 -41.11 161.85
REMARK 500 1 VAL A 17 -144.22 -100.92
REMARK 500 1 ASN A 19 88.54 44.16
REMARK 500 1 TYR A 36 -145.41 -124.13
REMARK 500 1 SER A 40 73.47 -157.12
REMARK 500 1 ASN A 42 -18.32 91.16
REMARK 500 1 LEU A 50 37.98 -85.49
REMARK 500 1 LYS A 51 99.36 -172.71
REMARK 500 1 PRO A 58 -172.85 -62.15
REMARK 500 1 CYS A 59 -146.78 -98.14
REMARK 500 1 GLN A 60 -149.95 -102.72
REMARK 500 1 LYS A 64 29.86 42.79
REMARK 500 1 ARG A 65 -99.97 -93.78
REMARK 500 1 MET A 66 -99.58 -68.49
REMARK 500 1 ALA A 83 -146.69 -89.64
REMARK 500 1 LEU A 106 62.67 -116.65
REMARK 500 1 HIS A 108 -157.54 -117.43
REMARK 500 1 HIS A 109 87.34 55.72
REMARK 500 2 PRO A 3 -95.01 -71.54
REMARK 500 2 LYS A 4 93.12 56.16
REMARK 500 2 ILE A 6 -71.10 -66.81
REMARK 500 2 LEU A 11 -143.03 -105.86
REMARK 500 2 SER A 16 -31.73 177.03
REMARK 500 2 VAL A 17 -39.83 -143.06
REMARK 500 2 PHE A 18 61.59 -168.29
REMARK 500 2 TYR A 36 -153.32 -132.77
REMARK 500 2 SER A 40 -50.27 -148.53
REMARK 500 2 ASN A 42 23.12 42.61
REMARK 500 2 SER A 43 108.19 -169.84
REMARK 500 2 LEU A 50 38.70 -85.82
REMARK 500 2 LYS A 51 -70.75 -91.53
REMARK 500 2 PRO A 58 -163.02 -72.41
REMARK 500 2 CYS A 59 -158.84 -106.15
REMARK 500 2 GLN A 60 -149.57 -71.33
REMARK 500 2 ARG A 65 -31.31 179.73
REMARK 500 2 MET A 66 -155.95 -141.03
REMARK 500 2 THR A 73 162.16 -45.70
REMARK 500 2 ALA A 83 -155.40 -89.93
REMARK 500 2 ALA A 84 -91.69 -75.73
REMARK 500 2 LEU A 106 60.69 -110.50
REMARK 500 2 HIS A 109 35.76 -98.37
REMARK 500 2 HIS A 111 -154.75 179.17
REMARK 500 2 HIS A 112 -86.80 67.42
REMARK 500 3 GLU A 2 162.04 60.33
REMARK 500 3 ARG A 5 136.44 69.38
REMARK 500 3 VAL A 17 98.79 -50.46
REMARK 500 3 PHE A 18 159.62 61.11
REMARK 500 3 TYR A 36 -154.72 -133.44
REMARK 500 3 SER A 40 -52.13 -150.99
REMARK 500 3 ASP A 41 11.37 59.95
REMARK 500
REMARK 500 THIS ENTRY HAS 548 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 5 0.19 SIDE CHAIN
REMARK 500 1 ARG A 7 0.08 SIDE CHAIN
REMARK 500 1 ARG A 65 0.32 SIDE CHAIN
REMARK 500 1 ARG A 89 0.08 SIDE CHAIN
REMARK 500 1 ARG A 94 0.30 SIDE CHAIN
REMARK 500 2 ARG A 5 0.14 SIDE CHAIN
REMARK 500 2 ARG A 7 0.31 SIDE CHAIN
REMARK 500 2 ARG A 65 0.30 SIDE CHAIN
REMARK 500 2 ARG A 89 0.16 SIDE CHAIN
REMARK 500 2 ARG A 94 0.28 SIDE CHAIN
REMARK 500 3 ARG A 5 0.28 SIDE CHAIN
REMARK 500 3 ARG A 7 0.32 SIDE CHAIN
REMARK 500 3 ARG A 65 0.27 SIDE CHAIN
REMARK 500 3 ARG A 89 0.32 SIDE CHAIN
REMARK 500 3 ARG A 94 0.17 SIDE CHAIN
REMARK 500 4 ARG A 5 0.30 SIDE CHAIN
REMARK 500 4 ARG A 7 0.25 SIDE CHAIN
REMARK 500 4 ARG A 65 0.22 SIDE CHAIN
REMARK 500 4 ARG A 89 0.20 SIDE CHAIN
REMARK 500 4 ARG A 94 0.24 SIDE CHAIN
REMARK 500 5 ARG A 5 0.32 SIDE CHAIN
REMARK 500 5 ARG A 7 0.27 SIDE CHAIN
REMARK 500 5 ARG A 65 0.32 SIDE CHAIN
REMARK 500 5 ARG A 89 0.32 SIDE CHAIN
REMARK 500 5 ARG A 94 0.24 SIDE CHAIN
REMARK 500 6 ARG A 5 0.24 SIDE CHAIN
REMARK 500 6 ARG A 7 0.30 SIDE CHAIN
REMARK 500 6 ARG A 65 0.30 SIDE CHAIN
REMARK 500 6 ARG A 89 0.30 SIDE CHAIN
REMARK 500 6 ARG A 94 0.23 SIDE CHAIN
REMARK 500 7 ARG A 5 0.30 SIDE CHAIN
REMARK 500 7 ARG A 7 0.09 SIDE CHAIN
REMARK 500 7 ARG A 65 0.08 SIDE CHAIN
REMARK 500 7 ARG A 89 0.31 SIDE CHAIN
REMARK 500 7 ARG A 94 0.26 SIDE CHAIN
REMARK 500 8 ARG A 5 0.25 SIDE CHAIN
REMARK 500 8 ARG A 7 0.12 SIDE CHAIN
REMARK 500 8 ARG A 65 0.32 SIDE CHAIN
REMARK 500 8 ARG A 89 0.32 SIDE CHAIN
REMARK 500 8 ARG A 94 0.13 SIDE CHAIN
REMARK 500 9 ARG A 5 0.31 SIDE CHAIN
REMARK 500 9 ARG A 7 0.26 SIDE CHAIN
REMARK 500 9 ARG A 65 0.32 SIDE CHAIN
REMARK 500 9 ARG A 89 0.25 SIDE CHAIN
REMARK 500 9 ARG A 94 0.20 SIDE CHAIN
REMARK 500 10 ARG A 5 0.21 SIDE CHAIN
REMARK 500 10 ARG A 7 0.28 SIDE CHAIN
REMARK 500 10 ARG A 65 0.08 SIDE CHAIN
REMARK 500 10 ARG A 94 0.32 SIDE CHAIN
REMARK 500 11 ARG A 5 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 116 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1PLS A 1 105 UNP P08567 PLEK_HUMAN 1 105
SEQRES 1 A 113 MET GLU PRO LYS ARG ILE ARG GLU GLY TYR LEU VAL LYS
SEQRES 2 A 113 LYS GLY SER VAL PHE ASN THR TRP LYS PRO MET TRP VAL
SEQRES 3 A 113 VAL LEU LEU GLU ASP GLY ILE GLU PHE TYR LYS LYS LYS
SEQRES 4 A 113 SER ASP ASN SER PRO LYS GLY MET ILE PRO LEU LYS GLY
SEQRES 5 A 113 SER THR LEU THR SER PRO CYS GLN ASP PHE GLY LYS ARG
SEQRES 6 A 113 MET PHE VAL PHE LYS ILE THR THR THR LYS GLN GLN ASP
SEQRES 7 A 113 HIS PHE PHE GLN ALA ALA PHE LEU GLU GLU ARG ASP ALA
SEQRES 8 A 113 TRP VAL ARG ASP ILE ASN LYS ALA ILE LYS CYS ILE GLU
SEQRES 9 A 113 GLY LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 H1 GLU A 87 ILE A 103 1AMPHIPATHIC 17
SHEET 1 B1 7 SER A 53 SER A 57 0
SHEET 2 B1 7 PHE A 67 THR A 73 -1 O THR A 72 N THR A 54
SHEET 3 B1 7 GLN A 77 ALA A 83 -1 N GLN A 82 O PHE A 67
SHEET 4 B1 7 ARG A 7 LYS A 14 -1 N LYS A 14 O PHE A 80
SHEET 5 B1 7 TRP A 21 LEU A 29 -1 O LYS A 22 N LYS A 13
SHEET 6 B1 7 GLY A 32 TYR A 36 -1 N GLY A 32 O LEU A 29
SHEET 7 B1 7 GLY A 46 ILE A 48 -1 O GLY A 46 N PHE A 35
CISPEP 1 SER A 57 PRO A 58 1 -1.08
CISPEP 2 SER A 57 PRO A 58 2 0.17
CISPEP 3 SER A 57 PRO A 58 3 0.00
CISPEP 4 SER A 57 PRO A 58 4 -0.05
CISPEP 5 SER A 57 PRO A 58 5 -0.79
CISPEP 6 SER A 57 PRO A 58 6 -0.76
CISPEP 7 SER A 57 PRO A 58 7 0.37
CISPEP 8 SER A 57 PRO A 58 8 -1.21
CISPEP 9 SER A 57 PRO A 58 9 -0.11
CISPEP 10 SER A 57 PRO A 58 10 -0.05
CISPEP 11 SER A 57 PRO A 58 11 -0.01
CISPEP 12 SER A 57 PRO A 58 12 0.07
CISPEP 13 SER A 57 PRO A 58 13 -0.40
CISPEP 14 SER A 57 PRO A 58 14 -0.26
CISPEP 15 SER A 57 PRO A 58 15 -0.12
CISPEP 16 SER A 57 PRO A 58 16 -0.23
CISPEP 17 SER A 57 PRO A 58 17 -0.39
CISPEP 18 SER A 57 PRO A 58 18 -0.07
CISPEP 19 SER A 57 PRO A 58 19 -0.05
CISPEP 20 SER A 57 PRO A 58 20 -0.10
CISPEP 21 SER A 57 PRO A 58 21 -0.52
CISPEP 22 SER A 57 PRO A 58 22 -0.45
CISPEP 23 SER A 57 PRO A 58 23 -0.56
CISPEP 24 SER A 57 PRO A 58 24 0.21
CISPEP 25 SER A 57 PRO A 58 25 -0.62
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 29 2 Bytes