Header list of 1eq1.pdb file
Complete list - b 16 2 Bytes
HEADER LIPID BINDING PROTEIN 31-MAR-00 1EQ1
TITLE NMR STRUCTURE OF AN EXCHANGEABLE APOLIPOPROTEIN-MANDUCA SEXTA
TITLE 2 APOLIPOPHORIN-III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPHORIN-III;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: APOLP-III;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: INTACT EXCHANGEABLE APOLIPOPROTEIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MANDUCA SEXTA;
SOURCE 3 ORGANISM_COMMON: TOBACCO HORNWORM;
SOURCE 4 ORGANISM_TAXID: 7130;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET22B
KEYWDS FIVE HELIX-BUNDLE, "HELIX-SHORT HELIX-HELIX" RECOGNITION MOTIF, LIPID
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR J.WANG,B.D.SYKES,R.O.RYAN
REVDAT 3 16-FEB-22 1EQ1 1 REMARK
REVDAT 2 24-FEB-09 1EQ1 1 VERSN
REVDAT 1 13-FEB-02 1EQ1 0
JRNL AUTH J.WANG,B.D.SYKES,R.O.RYAN
JRNL TITL STRUCTURAL BASIS FOR THE CONFORMATIONAL ADAPTABILITY OF
JRNL TITL 2 APOLIPOPHORIN III, A HELIX-BUNDLE EXCHANGEABLE
JRNL TITL 3 APOLIPOPROTEIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 99 1188 2002
JRNL REFN ISSN 0027-8424
JRNL PMID 11818551
JRNL DOI 10.1073/PNAS.032565999
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.WANG,S.M.GAGNE,B.D.SYKES,R.O.RYAN
REMARK 1 TITL INSIGHT INTO LIPID SURFACE RECOGNITION AND REVERSIBLE
REMARK 1 TITL 2 CONFORMATIONAL ADAPTATION OF AN EXCHANGEABLE APOLIPOPROTEIN
REMARK 1 TITL 3 BY MULTIDIMENSIONAL HETERONUCLEAR NMR TECHNIQUES
REMARK 1 REF J.BIOL.CHEM. V. 272 17912 1997
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.272.29.17912
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, X-PLOR 3.1
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2365 RESTRAINTS, INCLUDING
REMARK 3 2257 NOE-DIREVIED DISTANCE RESTRAINTS AND 108 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1EQ1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010805.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8-1.2 MM U-15N, 13C DOUBLE
REMARK 210 LABELD L-APOLP-III; 200 MM
REMARK 210 PHOSPHATE BUFFER, 0.5 MM NAN3,
REMARK 210 DSS
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA;
REMARK 210 4D_13C-SEPARATED_NOESY; 4D_13C/
REMARK 210 15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
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 GLN A 26 H SER A 29 1.49
REMARK 500 O PHE A 57 H SER A 60 1.52
REMARK 500 O GLN A 62 H SER A 66 1.53
REMARK 500 O GLN A 78 H ASN A 82 1.54
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 ALA A 2 -52.92 164.30
REMARK 500 1 PRO A 3 45.94 -79.01
REMARK 500 1 ALA A 4 -42.50 -156.68
REMARK 500 1 ALA A 8 142.98 63.24
REMARK 500 1 SER A 33 -168.42 -117.28
REMARK 500 1 ASN A 35 73.38 -160.48
REMARK 500 1 THR A 36 34.22 -142.56
REMARK 500 1 ASP A 38 29.03 -146.07
REMARK 500 1 ASP A 67 41.90 -167.23
REMARK 500 1 LYS A 71 35.36 -90.64
REMARK 500 1 ALA A 93 -166.68 -106.05
REMARK 500 1 HIS A 94 -53.16 164.69
REMARK 500 1 ASN A 102 -75.03 -84.91
REMARK 500 1 THR A 133 -29.16 178.46
REMARK 500 1 LYS A 165 -148.87 39.48
REMARK 500 2 ALA A 2 90.29 -179.55
REMARK 500 2 PRO A 3 46.01 -78.74
REMARK 500 2 ALA A 4 -78.64 -161.09
REMARK 500 2 ASN A 7 -86.42 -91.33
REMARK 500 2 ALA A 8 115.28 67.45
REMARK 500 2 PHE A 9 -155.93 -165.78
REMARK 500 2 VAL A 31 68.40 -65.59
REMARK 500 2 ASN A 35 66.60 -160.65
REMARK 500 2 GLN A 37 17.66 57.09
REMARK 500 2 ASP A 38 26.91 -140.57
REMARK 500 2 ASP A 67 -45.96 -150.82
REMARK 500 2 ALA A 68 -157.01 59.68
REMARK 500 2 ASN A 69 -42.01 -151.92
REMARK 500 2 ALA A 93 135.13 175.60
REMARK 500 2 HIS A 94 59.96 -140.52
REMARK 500 2 ALA A 101 23.83 48.38
REMARK 500 2 ALA A 103 46.39 164.88
REMARK 500 2 ASN A 129 -70.82 65.49
REMARK 500 2 MET A 130 -59.53 69.37
REMARK 500 2 GLU A 132 16.26 -148.51
REMARK 500 2 THR A 133 34.08 -179.72
REMARK 500 2 PRO A 139 47.42 -77.41
REMARK 500 2 LYS A 140 -35.53 -163.21
REMARK 500 2 THR A 164 16.21 -145.29
REMARK 500 2 LYS A 165 91.58 44.07
REMARK 500 3 ALA A 2 89.46 66.58
REMARK 500 3 ALA A 4 -40.07 -169.41
REMARK 500 3 ALA A 8 155.99 62.96
REMARK 500 3 ASN A 32 26.45 -166.83
REMARK 500 3 SER A 33 -62.06 -142.76
REMARK 500 3 LYS A 34 -91.26 -97.48
REMARK 500 3 ASN A 35 82.58 39.21
REMARK 500 3 THR A 36 38.63 -153.00
REMARK 500 3 ASP A 38 15.19 -140.23
REMARK 500 3 PHE A 39 12.69 -143.79
REMARK 500
REMARK 500 THIS ENTRY HAS 422 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 91 0.19 SIDE CHAIN
REMARK 500 2 ARG A 80 0.14 SIDE CHAIN
REMARK 500 2 ARG A 91 0.25 SIDE CHAIN
REMARK 500 3 ARG A 80 0.20 SIDE CHAIN
REMARK 500 3 ARG A 91 0.20 SIDE CHAIN
REMARK 500 4 ARG A 80 0.30 SIDE CHAIN
REMARK 500 4 ARG A 91 0.32 SIDE CHAIN
REMARK 500 5 ARG A 80 0.19 SIDE CHAIN
REMARK 500 5 ARG A 91 0.32 SIDE CHAIN
REMARK 500 6 ARG A 80 0.10 SIDE CHAIN
REMARK 500 6 ARG A 91 0.31 SIDE CHAIN
REMARK 500 7 ARG A 80 0.28 SIDE CHAIN
REMARK 500 7 ARG A 91 0.32 SIDE CHAIN
REMARK 500 8 ARG A 80 0.31 SIDE CHAIN
REMARK 500 8 ARG A 91 0.32 SIDE CHAIN
REMARK 500 9 ARG A 80 0.13 SIDE CHAIN
REMARK 500 9 ARG A 91 0.32 SIDE CHAIN
REMARK 500 10 ARG A 80 0.13 SIDE CHAIN
REMARK 500 10 ARG A 91 0.25 SIDE CHAIN
REMARK 500 11 ARG A 80 0.31 SIDE CHAIN
REMARK 500 11 ARG A 91 0.32 SIDE CHAIN
REMARK 500 12 ARG A 80 0.08 SIDE CHAIN
REMARK 500 12 ARG A 91 0.31 SIDE CHAIN
REMARK 500 13 ARG A 80 0.26 SIDE CHAIN
REMARK 500 13 ARG A 91 0.32 SIDE CHAIN
REMARK 500 14 ARG A 80 0.20 SIDE CHAIN
REMARK 500 14 ARG A 91 0.21 SIDE CHAIN
REMARK 500 15 ARG A 80 0.09 SIDE CHAIN
REMARK 500 15 ARG A 91 0.16 SIDE CHAIN
REMARK 500 16 ARG A 80 0.26 SIDE CHAIN
REMARK 500 16 ARG A 91 0.21 SIDE CHAIN
REMARK 500 17 ARG A 80 0.32 SIDE CHAIN
REMARK 500 17 ARG A 91 0.28 SIDE CHAIN
REMARK 500 18 ARG A 80 0.23 SIDE CHAIN
REMARK 500 18 ARG A 91 0.28 SIDE CHAIN
REMARK 500 19 ARG A 80 0.31 SIDE CHAIN
REMARK 500 19 ARG A 91 0.22 SIDE CHAIN
REMARK 500 20 ARG A 80 0.23 SIDE CHAIN
REMARK 500 20 ARG A 91 0.16 SIDE CHAIN
REMARK 500 21 ARG A 80 0.30 SIDE CHAIN
REMARK 500 21 ARG A 91 0.32 SIDE CHAIN
REMARK 500 22 ARG A 80 0.18 SIDE CHAIN
REMARK 500 22 ARG A 91 0.31 SIDE CHAIN
REMARK 500 23 ARG A 80 0.31 SIDE CHAIN
REMARK 500 23 ARG A 91 0.31 SIDE CHAIN
REMARK 500 24 ARG A 80 0.28 SIDE CHAIN
REMARK 500 24 ARG A 91 0.09 SIDE CHAIN
REMARK 500 25 ARG A 80 0.20 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1AEP RELATED DB: PDB
REMARK 900 LOCUSTA MIGRATORIA APOLIPOPHORIN-III
REMARK 900 RELATED ID: 1LPE RELATED DB: PDB
REMARK 900 APOLIPOPROTEIN-E N-TERMINAL DOMAIN
DBREF 1EQ1 A 1 166 UNP P13276 APL3_MANSE 24 189
SEQRES 1 A 166 ASP ALA PRO ALA GLY GLY ASN ALA PHE GLU GLU MET GLU
SEQRES 2 A 166 LYS HIS ALA LYS GLU PHE GLN LYS THR PHE SER GLU GLN
SEQRES 3 A 166 PHE ASN SER LEU VAL ASN SER LYS ASN THR GLN ASP PHE
SEQRES 4 A 166 ASN LYS ALA LEU LYS ASP GLY SER ASP SER VAL LEU GLN
SEQRES 5 A 166 GLN LEU SER ALA PHE SER SER SER LEU GLN GLY ALA ILE
SEQRES 6 A 166 SER ASP ALA ASN GLY LYS ALA LYS GLU ALA LEU GLU GLN
SEQRES 7 A 166 ALA ARG GLN ASN VAL GLU LYS THR ALA GLU GLU LEU ARG
SEQRES 8 A 166 LYS ALA HIS PRO ASP VAL GLU LYS GLU ALA ASN ALA PHE
SEQRES 9 A 166 LYS ASP LYS LEU GLN ALA ALA VAL GLN THR THR VAL GLN
SEQRES 10 A 166 GLU SER GLN LYS LEU ALA LYS GLU VAL ALA SER ASN MET
SEQRES 11 A 166 GLU GLU THR ASN LYS LYS LEU ALA PRO LYS ILE LYS GLN
SEQRES 12 A 166 ALA TYR ASP ASP PHE VAL LYS HIS ALA GLU GLU VAL GLN
SEQRES 13 A 166 LYS LYS LEU HIS GLU ALA ALA THR LYS GLN
HELIX 1 1 GLU A 10 VAL A 31 1 22
HELIX 2 2 ASN A 40 SER A 66 1 27
HELIX 3 3 LYS A 71 GLU A 89 1 19
HELIX 4 4 LEU A 90 ALA A 93 5 4
HELIX 5 5 HIS A 94 GLU A 100 1 7
HELIX 6 6 PHE A 104 SER A 128 1 25
HELIX 7 7 ASN A 134 LYS A 136 5 3
HELIX 8 8 LEU A 137 ALA A 163 1 27
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 16 2 Bytes