Header list of 1owt.pdb file
Complete list - b 23 2 Bytes
HEADER APOPTOSIS 30-MAR-03 1OWT
TITLE STRUCTURE OF THE ALZHEIMER'S DISEASE AMYLOID PRECURSOR PROTEIN COPPER
TITLE 2 BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AMYLOID BETA A4 PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: COPPER BINDING DOMAIN;
COMPND 5 SYNONYM: AMYLOID PRECURSOR PROTEIN;
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: APP;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: GS115;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PIC9
KEYWDS BETA-ALPHA-BETA-BETA, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR K.J.BARNHAM,W.J.MCKINSTRY,G.MULTHAUP,D.GALATIS,C.J.MORTON,
AUTHOR 2 C.C.CURTAIN,N.A.WILLIAMSON,A.R.WHITE,M.G.HINDS,R.S.NORTON,
AUTHOR 3 K.BEYREUTHER,C.L.MASTERS,M.W.PARKER,R.CAPPAI
REVDAT 3 23-FEB-22 1OWT 1 REMARK
REVDAT 2 24-FEB-09 1OWT 1 VERSN
REVDAT 1 13-MAY-03 1OWT 0
JRNL AUTH K.J.BARNHAM,W.J.MCKINSTRY,G.MULTHAUP,D.GALATIS,C.J.MORTON,
JRNL AUTH 2 C.C.CURTAIN,N.A.WILLIAMSON,A.R.WHITE,M.G.HINDS,R.S.NORTON,
JRNL AUTH 3 K.BEYREUTHER,C.L.MASTERS,M.W.PARKER,R.CAPPAI
JRNL TITL STRUCTURE OF THE ALZHEIMER'S DISEASE AMYLOID PRECURSOR
JRNL TITL 2 PROTEIN COPPER BINDING DOMAIN. A REGULATOR OF NEURONAL
JRNL TITL 3 COPPER HOMEOSTASIS.
JRNL REF J.BIOL.CHEM. V. 278 17401 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12611883
JRNL DOI 10.1074/JBC.M300629200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0, CNS 1.0
REMARK 3 AUTHORS : BRUNGER (CNS),
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: 1233 NOE RESTRAINTS, 111 ANGLE
REMARK 3 RESTRAINTS
REMARK 4
REMARK 4 1OWT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018750.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 0.3
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.5MM CUBD U-15N,13C; 20MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DPX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
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: 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
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 PRO A 130 -94.06 -86.57
REMARK 500 1 ASP A 131 -101.57 -85.13
REMARK 500 1 LEU A 136 74.84 -116.83
REMARK 500 1 MET A 141 34.67 -74.61
REMARK 500 1 LYS A 161 -137.53 -96.12
REMARK 500 1 SER A 162 51.75 -119.98
REMARK 500 1 LEU A 171 -162.80 -113.38
REMARK 500 1 LEU A 172 66.56 39.42
REMARK 500 2 PRO A 130 -157.43 -76.25
REMARK 500 2 MET A 141 32.60 -74.25
REMARK 500 2 LYS A 161 -138.33 -104.15
REMARK 500 2 LEU A 171 -165.72 -121.03
REMARK 500 3 LEU A 128 -152.06 -139.19
REMARK 500 3 PRO A 130 -92.91 -83.77
REMARK 500 3 ASP A 131 -101.20 -85.59
REMARK 500 3 MET A 141 33.27 -74.35
REMARK 500 3 LYS A 161 -137.49 -94.59
REMARK 500 3 SER A 162 52.32 -118.81
REMARK 500 3 LEU A 171 -167.47 -109.80
REMARK 500 3 LEU A 172 73.52 37.40
REMARK 500 4 LEU A 128 -154.30 -128.94
REMARK 500 4 PRO A 130 -98.75 -82.25
REMARK 500 4 ASP A 131 -101.40 -85.45
REMARK 500 4 MET A 141 35.89 -73.91
REMARK 500 4 LYS A 161 -136.86 -98.51
REMARK 500 4 LEU A 171 -159.96 -116.51
REMARK 500 5 LEU A 128 -147.83 -132.64
REMARK 500 5 PRO A 130 -92.63 -81.53
REMARK 500 5 ASP A 131 -102.68 -85.69
REMARK 500 5 MET A 141 36.76 -74.57
REMARK 500 5 LYS A 161 -137.05 -94.37
REMARK 500 5 SER A 162 51.13 -118.60
REMARK 500 5 LEU A 171 -165.41 -111.94
REMARK 500 6 ASP A 125 -151.35 -98.83
REMARK 500 6 LEU A 128 -148.97 -135.27
REMARK 500 6 PRO A 130 -89.31 -86.65
REMARK 500 6 ASP A 131 -101.46 -85.09
REMARK 500 6 LEU A 136 79.43 -120.00
REMARK 500 6 MET A 141 28.56 -71.16
REMARK 500 6 LYS A 161 -137.91 -94.84
REMARK 500 6 SER A 162 50.29 -117.93
REMARK 500 6 LEU A 171 -161.17 -110.34
REMARK 500 7 LEU A 128 -151.15 -139.54
REMARK 500 7 PRO A 130 -88.24 -86.47
REMARK 500 7 ASP A 131 -101.04 -85.00
REMARK 500 7 MET A 141 32.53 -74.22
REMARK 500 7 LYS A 161 -138.68 -106.89
REMARK 500 8 LEU A 128 -148.52 -134.11
REMARK 500 8 PRO A 130 -88.47 -85.27
REMARK 500 8 ASP A 131 -101.44 -85.29
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1OWT A 124 189 UNP P05067 A4_HUMAN 124 189
SEQRES 1 A 66 SER ASP ALA LEU LEU VAL PRO ASP LYS CYS LYS PHE LEU
SEQRES 2 A 66 HIS GLN GLU ARG MET ASP VAL CYS GLU THR HIS LEU HIS
SEQRES 3 A 66 TRP HIS THR VAL ALA LYS GLU THR CYS SER GLU LYS SER
SEQRES 4 A 66 THR ASN LEU HIS ASP TYR GLY MET LEU LEU PRO CYS GLY
SEQRES 5 A 66 ILE ASP LYS PHE ARG GLY VAL GLU PHE VAL CYS CYS PRO
SEQRES 6 A 66 LEU
HELIX 1 1 HIS A 147 GLU A 160 1 14
SHEET 1 A 3 LYS A 134 GLU A 139 0
SHEET 2 A 3 GLY A 181 PRO A 188 -1 O CYS A 186 N LYS A 134
SHEET 3 A 3 THR A 163 ASP A 167 -1 N ASN A 164 O CYS A 187
SHEET 1 B 2 GLU A 145 THR A 146 0
SHEET 2 B 2 LYS A 178 PHE A 179 -1 O PHE A 179 N GLU A 145
SSBOND 1 CYS A 133 CYS A 187 1555 1555 2.03
SSBOND 2 CYS A 144 CYS A 174 1555 1555 2.03
SSBOND 3 CYS A 158 CYS A 186 1555 1555 2.03
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 - b 23 2 Bytes