Header list of 1hz3.pdb file
Complete list - 23 20 Bytes
HEADER SUGAR BINDING PROTEIN 23-JAN-01 1HZ3
TITLE ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: A-BETA AMYLOID;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 10-35;
COMPND 5 SYNONYM: BETA-AMYLOID A4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE IS TAKEN FROM THE A-BETA PEPTIDE, WHICH
SOURCE 4 OCCURS NATURALLY IN HOMO SAPIENS (HUMAN). THE PEPTIDE WAS
SOURCE 5 SYNTHESIZED BY MERRIFIELD SOLID-PHASE METHODOLOGY.
KEYWDS COLLAPSED COIL, HYDROPHOBIC CLUSTER, HYDROPHOBIC PATCH, SUGAR BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR S.ZHANG,K.IWATA,M.J.LACHENMANN,J.W.PENG,S.LI,E.R.STIMSON,Y.LU,
AUTHOR 2 A.M.FELIX,J.E.MAGGIO,J.P.LEE
REVDAT 4 23-FEB-22 1HZ3 1 REMARK
REVDAT 3 24-FEB-09 1HZ3 1 VERSN
REVDAT 2 01-APR-03 1HZ3 1 JRNL
REVDAT 1 31-JAN-01 1HZ3 0
JRNL AUTH S.ZHANG,K.IWATA,M.J.LACHENMANN,J.W.PENG,S.LI,E.R.STIMSON,
JRNL AUTH 2 Y.LU,A.M.FELIX,J.E.MAGGIO,J.P.LEE
JRNL TITL THE ALZHEIMER'S PEPTIDE A BETA ADOPTS A COLLAPSED COIL
JRNL TITL 2 STRUCTURE IN WATER.
JRNL REF J.STRUCT.BIOL. V. 130 130 2000
JRNL REFN ISSN 1047-8477
JRNL PMID 10940221
JRNL DOI 10.1006/JSBI.2000.4288
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.P.LEE,E.R.STIMSON,J.R.GHILARDI,P.W.MANTYH,Y.A.LU,
REMARK 1 AUTH 2 A.M.FELIX,W.LLANOS,A.BEHBIN,M.CUMMINGS,M.VAN CRIEKINGE,
REMARK 1 AUTH 3 W.TIMMS,J.E.MAGGIO
REMARK 1 TITL 1H NMR OF A-BETA AMYLOID PEPTIDE CONGENERS IN WATER
REMARK 1 TITL 2 SOLUTION. CONFORMATIONAL CHANGES CORRELATE WITH PLAQUE
REMARK 1 TITL 3 COMPETENCE.
REMARK 1 REF BIOCHEMISTRY V. 34 5191 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 2
REMARK 1 AUTH F.MASSI,J.W.PENG,J.P.LEE,J.E.STRAUB
REMARK 1 TITL SIMULATION STUDY OF THE STRUCTURE AND DYNAMICS OF THE
REMARK 1 TITL 2 ALZHEIMER'S AMYLOID PEPTIDE CONGENER IN SOLUTION.
REMARK 1 REF BIOPHYS.J. V. 80 31 2001
REMARK 1 REFN ISSN 0006-3495
REMARK 1 REFERENCE 3
REMARK 1 AUTH F.MASSI,J.E.STRAUB
REMARK 1 TITL ENERGY LANDSCAPE THEORY FOR ALZHEIMER'S AMYLOID BETA-PEPTIDE
REMARK 1 TITL 2 FIBRIL ELONGATION
REMARK 1 REF PROTEINS V. 42 217 2001
REMARK 1 REFN ISSN 0887-3585
REMARK 1 DOI 10.1002/1097-0134(20010201)42:2<217::AID-PROT90>3.0.CO;2-N
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3B, DISCOVER 3.0
REMARK 3 AUTHORS : VARIAN ASSOCIATES (VNMR), MSI, INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 84 SEQUENTIAL, 66 MEDIUM- (I TO I+2 OR I+3) AND 32 LONG-RANGE
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS.
REMARK 4
REMARK 4 1HZ3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1000012702.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : <1MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 300UM A-BETA(10-35); 90% H2O,
REMARK 210 10% D2O; 300UM A-BETA(1-40) U-
REMARK 210 15N; 90% H2O, 10% D2O; 300 UM A-
REMARK 210 BETA(10-35) 2H-VAL12, -LEU17, -
REMARK 210 VAL18, -PHE19, -ILE32 AND -LEU34;
REMARK 210 15N-PHE19, -VAL24, -GLY25 AND -
REMARK 210 GLY29; 13C-VAL24; 13C-ALA21 BETA
REMARK 210 METHYL; 13C-ALA30 BETA METHYL;
REMARK 210 13C-MET35 DELTA METHYL; 300 UM A-
REMARK 210 BETA(10-35) 2H-VAL12, -LEU17, -
REMARK 210 PHE19, -VAL24, -ILE31 AND -LEU34;
REMARK 210 15N-VAL 18, -PHE20, -GLY25, -
REMARK 210 GLY29 AND -GLY33; 13C-VAL24; 13C-
REMARK 210 ALA21 BETA METHYL; 13C-ALA30
REMARK 210 BETA METHYL; 13C-MET35 DELTA
REMARK 210 METHYL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 15N EDITED
REMARK 210 NOESY-HMQC; 13C EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DGII
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, AND RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1, 9
REMARK 210
REMARK 210 REMARK: MANY OBSERVED INTRA-RESIDUE NOE-BASED DISTANCE CONSTRAINTS
REMARK 210 WERE NOT INCLUDED IN THE STRUCTURE CALCULATIONS.
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 GLY A 20 HXT MET A 26 1.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 MET A 26 C MET A 26 OXT 0.145
REMARK 500 2 HIS A 4 CG HIS A 4 CD2 0.061
REMARK 500 2 HIS A 5 CG HIS A 5 CD2 0.064
REMARK 500 2 MET A 26 C MET A 26 OXT 0.144
REMARK 500 3 HIS A 4 CG HIS A 4 CD2 0.058
REMARK 500 3 MET A 26 C MET A 26 OXT 0.143
REMARK 500 4 MET A 26 C MET A 26 OXT 0.144
REMARK 500 5 HIS A 4 CG HIS A 4 CD2 0.060
REMARK 500 5 HIS A 5 CG HIS A 5 CD2 0.058
REMARK 500 5 MET A 26 C MET A 26 OXT 0.145
REMARK 500 6 HIS A 4 CG HIS A 4 CD2 0.054
REMARK 500 6 MET A 26 C MET A 26 OXT 0.143
REMARK 500 7 HIS A 4 CG HIS A 4 CD2 0.055
REMARK 500 7 MET A 26 C MET A 26 OXT 0.144
REMARK 500 8 HIS A 4 CG HIS A 4 CD2 0.059
REMARK 500 8 MET A 26 C MET A 26 OXT 0.143
REMARK 500 9 HIS A 4 CG HIS A 4 CD2 0.061
REMARK 500 9 MET A 26 C MET A 26 OXT 0.142
REMARK 500 10 HIS A 4 CG HIS A 4 CD2 0.062
REMARK 500 10 MET A 26 C MET A 26 OXT 0.143
REMARK 500 11 MET A 26 C MET A 26 OXT 0.140
REMARK 500 12 HIS A 4 CG HIS A 4 CD2 0.057
REMARK 500 12 HIS A 5 CG HIS A 5 CD2 0.055
REMARK 500 12 MET A 26 C MET A 26 OXT 0.144
REMARK 500 13 HIS A 4 CG HIS A 4 CD2 0.056
REMARK 500 13 HIS A 5 CG HIS A 5 CD2 0.054
REMARK 500 13 MET A 26 C MET A 26 OXT 0.145
REMARK 500 14 HIS A 4 CG HIS A 4 CD2 0.056
REMARK 500 14 MET A 26 C MET A 26 OXT 0.142
REMARK 500 15 MET A 26 C MET A 26 OXT 0.145
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ALA A 12 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 1 ALA A 21 N - CA - CB ANGL. DEV. = -9.4 DEGREES
REMARK 500 2 ALA A 12 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 2 ALA A 21 N - CA - CB ANGL. DEV. = -10.7 DEGREES
REMARK 500 3 ALA A 21 N - CA - CB ANGL. DEV. = -9.3 DEGREES
REMARK 500 4 ALA A 12 N - CA - CB ANGL. DEV. = -10.5 DEGREES
REMARK 500 4 ALA A 21 N - CA - CB ANGL. DEV. = -9.6 DEGREES
REMARK 500 7 ALA A 12 N - CA - CB ANGL. DEV. = -10.6 DEGREES
REMARK 500 7 ALA A 21 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 8 ALA A 12 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 8 ALA A 21 N - CA - CB ANGL. DEV. = -8.8 DEGREES
REMARK 500 12 ALA A 21 N - CA - CB ANGL. DEV. = -9.6 DEGREES
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 VAL A 3 -51.99 69.42
REMARK 500 1 HIS A 4 -34.19 71.53
REMARK 500 1 HIS A 5 162.46 64.43
REMARK 500 1 LYS A 7 -64.68 -138.08
REMARK 500 1 LEU A 8 0.91 -152.57
REMARK 500 1 VAL A 9 99.06 -68.27
REMARK 500 1 ALA A 12 -90.30 -149.27
REMARK 500 1 ASP A 14 31.93 -86.51
REMARK 500 1 VAL A 15 -27.88 158.16
REMARK 500 1 ASN A 18 70.77 -174.44
REMARK 500 1 ALA A 21 -37.28 -147.49
REMARK 500 1 ILE A 23 90.85 68.63
REMARK 500 2 GLU A 2 -79.38 -93.09
REMARK 500 2 HIS A 5 115.49 -5.21
REMARK 500 2 GLN A 6 -92.94 -141.64
REMARK 500 2 LYS A 7 -39.62 -165.74
REMARK 500 2 ALA A 12 -102.27 -141.95
REMARK 500 2 ASP A 14 44.86 -91.41
REMARK 500 2 VAL A 15 -33.17 150.68
REMARK 500 2 ASN A 18 63.27 -169.59
REMARK 500 2 ALA A 21 -52.53 -142.51
REMARK 500 2 ILE A 23 81.58 64.90
REMARK 500 3 VAL A 3 106.57 -58.05
REMARK 500 3 HIS A 5 133.17 -29.53
REMARK 500 3 GLN A 6 -85.31 -158.43
REMARK 500 3 LYS A 7 -20.59 -169.45
REMARK 500 3 ALA A 12 -95.32 -98.54
REMARK 500 3 VAL A 15 -27.81 168.05
REMARK 500 3 ASN A 18 78.62 -173.78
REMARK 500 3 LYS A 19 70.43 -104.65
REMARK 500 3 ALA A 21 -50.96 -152.80
REMARK 500 3 ILE A 23 71.73 62.84
REMARK 500 3 LEU A 25 -87.30 -106.30
REMARK 500 4 GLU A 2 -56.83 -150.50
REMARK 500 4 HIS A 5 170.22 91.46
REMARK 500 4 GLN A 6 -73.82 122.52
REMARK 500 4 LYS A 7 -46.68 -153.99
REMARK 500 4 ALA A 12 -82.91 -139.72
REMARK 500 4 ASP A 14 25.98 -78.21
REMARK 500 4 VAL A 15 -27.27 164.91
REMARK 500 4 ASN A 18 72.34 -171.39
REMARK 500 4 ALA A 21 -39.54 -147.51
REMARK 500 4 ILE A 23 81.89 69.72
REMARK 500 5 HIS A 5 132.64 1.07
REMARK 500 5 GLN A 6 68.41 67.82
REMARK 500 5 LYS A 7 -53.43 -124.01
REMARK 500 5 LEU A 8 -47.13 -173.36
REMARK 500 5 VAL A 9 101.64 -16.25
REMARK 500 5 ALA A 12 -86.36 -145.94
REMARK 500 5 VAL A 15 -20.20 176.51
REMARK 500
REMARK 500 THIS ENTRY HAS 155 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 PHE A 10 0.08 SIDE CHAIN
REMARK 500 4 PHE A 10 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE PEPTIDE RESIDUES ARE NUMBERED 1-26 AS THEY WERE
REMARK 999 DESIGNATED IN THE DISTANCE-GEOMETRY CALCULATION.
REMARK 999 THIS CORRESPONDS TO RESIDUES 10-35 OF THE "HUMAN
REMARK 999 AMYLOID PEPTIDE ABETA." ABETA IS A 40-43 RESIDUE
REMARK 999 PEPTIDE DERIVED FROM THE HUMAN AMYLOID PRECURSOR
REMARK 999 PROTEIN (APP) (ACCESSION QRHUA4).
REMARK 999 RESIDUE #10 IN ABETA CORRESPONDS TO RESIDUE #681
REMARK 999 IN APP, AND RESIDUE #35 IN ABETA CORRESPONDS TO
REMARK 999 RESIDUE #706 IN APP.
DBREF 1HZ3 A 1 26 UNP P05067 A4_HUMAN 681 706
SEQRES 1 A 26 TYR GLU VAL HIS HIS GLN LYS LEU VAL PHE PHE ALA GLU
SEQRES 2 A 26 ASP VAL GLY SER ASN LYS GLY ALA ILE ILE GLY LEU MET
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 - 23 20 Bytes