Header list of 1wyo.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN 15-FEB-05 1WYO
TITLE SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN MICROTUBULE-ASSOCIATED
TITLE 2 PROTEIN RP/EB FAMILY MEMBER 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CH DOMAIN;
COMPND 5 SYNONYM: PROTEIN EB3;
COMPND 6 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: MAPRE3;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040621-06;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS RP/EB FAMILY, CH DOMAIN, MICROTUBULE-BINDING, STRUCTURAL GENOMICS,
KEYWDS 2 NPPSFA, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI,
KEYWDS 3 STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN STRUCTURAL
AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1WYO 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1WYO 1 VERSN
REVDAT 1 15-AUG-05 1WYO 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE CH DOMAIN OF HUMAN
JRNL TITL 2 MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000024159.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.28MM CH DOMAIN U-15N,13C; 20MM
REMARK 210 D-TRIS-HCL(PH 7.0); 100MM NACL;
REMARK 210 1MM D-DTT; 0.02% NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9295, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION,STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY,STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
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: 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 5 27.30 42.51
REMARK 500 1 ASN A 11 154.41 -36.83
REMARK 500 1 TYR A 13 -71.58 -103.35
REMARK 500 1 HIS A 25 -70.89 -48.31
REMARK 500 1 ALA A 49 -36.56 -34.89
REMARK 500 1 PRO A 99 82.70 -69.68
REMARK 500 1 GLN A 109 -71.68 -89.91
REMARK 500 1 PHE A 114 -70.88 -43.84
REMARK 500 1 ASP A 141 -34.58 -38.24
REMARK 500 1 ALA A 143 147.62 -35.89
REMARK 500 1 PRO A 148 4.46 -69.83
REMARK 500 2 SER A 3 101.55 -51.88
REMARK 500 2 SER A 5 104.86 -34.56
REMARK 500 2 ASN A 11 123.03 -35.34
REMARK 500 2 LEU A 22 176.19 -49.74
REMARK 500 2 GLN A 71 40.55 -82.76
REMARK 500 2 ASP A 95 38.59 -82.71
REMARK 500 2 PRO A 99 83.20 -69.75
REMARK 500 2 PHE A 108 -37.47 -34.59
REMARK 500 2 GLN A 109 -71.00 -74.58
REMARK 500 2 PHE A 114 -70.66 -63.04
REMARK 500 2 ASP A 127 77.28 -114.43
REMARK 500 2 PRO A 148 81.64 -69.77
REMARK 500 2 ASP A 150 36.97 71.09
REMARK 500 3 ASN A 11 142.46 -34.03
REMARK 500 3 SER A 16 33.90 -89.02
REMARK 500 3 ARG A 24 -37.21 -34.58
REMARK 500 3 HIS A 25 -72.54 -64.38
REMARK 500 3 GLN A 71 33.51 -89.53
REMARK 500 3 LYS A 91 -36.51 -34.35
REMARK 500 3 ASP A 95 37.57 -83.36
REMARK 500 3 PRO A 99 83.60 -69.71
REMARK 500 3 LYS A 107 106.85 -45.68
REMARK 500 3 GLN A 109 -71.92 -67.41
REMARK 500 3 PHE A 114 -70.89 -59.49
REMARK 500 3 ASN A 147 131.93 -39.72
REMARK 500 3 ASP A 150 35.57 -88.72
REMARK 500 3 PRO A 156 95.39 -69.77
REMARK 500 4 ASN A 11 127.31 -34.40
REMARK 500 4 SER A 16 162.64 -46.22
REMARK 500 4 THR A 18 -44.16 -134.51
REMARK 500 4 ASN A 21 149.60 -174.58
REMARK 500 4 LEU A 22 -179.63 -57.65
REMARK 500 4 ARG A 24 -35.64 -34.89
REMARK 500 4 SER A 34 -75.05 -47.56
REMARK 500 4 GLN A 71 33.57 -95.63
REMARK 500 4 LYS A 83 -71.02 -52.54
REMARK 500 4 LYS A 91 -35.10 -34.15
REMARK 500 4 PRO A 99 81.11 -69.76
REMARK 500 4 LYS A 107 121.25 -34.18
REMARK 500
REMARK 500 THIS ENTRY HAS 281 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSS001000902.1 RELATED DB: TARGETDB
DBREF 1WYO A 8 153 UNP Q9UPY8 MARE3_HUMAN 1 146
SEQADV 1WYO GLY A 1 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 2 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 3 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO GLY A 4 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 5 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 6 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO GLY A 7 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 154 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO GLY A 155 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO PRO A 156 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 157 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO SER A 158 UNP Q9UPY8 CLONING ARTIFACT
SEQADV 1WYO GLY A 159 UNP Q9UPY8 CLONING ARTIFACT
SEQRES 1 A 159 GLY SER SER GLY SER SER GLY MET ALA VAL ASN VAL TYR
SEQRES 2 A 159 SER THR SER VAL THR SER GLU ASN LEU SER ARG HIS ASP
SEQRES 3 A 159 MET LEU ALA TRP VAL ASN ASP SER LEU HIS LEU ASN TYR
SEQRES 4 A 159 THR LYS ILE GLU GLN LEU CYS SER GLY ALA ALA TYR CYS
SEQRES 5 A 159 GLN PHE MET ASP MET LEU PHE PRO GLY CYS VAL HIS LEU
SEQRES 6 A 159 ARG LYS VAL LYS PHE GLN ALA LYS LEU GLU HIS GLU TYR
SEQRES 7 A 159 ILE HIS ASN PHE LYS VAL LEU GLN ALA ALA PHE LYS LYS
SEQRES 8 A 159 MET GLY VAL ASP LYS ILE ILE PRO VAL GLU LYS LEU VAL
SEQRES 9 A 159 LYS GLY LYS PHE GLN ASP ASN PHE GLU PHE ILE GLN TRP
SEQRES 10 A 159 PHE LYS LYS PHE PHE ASP ALA ASN TYR ASP GLY LYS ASP
SEQRES 11 A 159 TYR ASN PRO LEU LEU ALA ARG GLN GLY GLN ASP VAL ALA
SEQRES 12 A 159 PRO PRO PRO ASN PRO GLY ASP GLN ILE PHE SER GLY PRO
SEQRES 13 A 159 SER SER GLY
HELIX 1 1 SER A 23 LEU A 35 1 13
HELIX 2 2 LYS A 41 SER A 47 5 7
HELIX 3 3 GLY A 48 PHE A 59 1 12
HELIX 4 4 GLU A 75 GLY A 93 1 19
HELIX 5 5 PRO A 99 VAL A 104 1 6
HELIX 6 6 PHE A 108 ALA A 124 1 17
HELIX 7 7 LEU A 134 GLN A 138 5 5
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