Header list of 1apc.pdb file
Complete list - 29 20 Bytes
HEADER ELECTRON TRANSPORT 14-OCT-93 1APC
TITLE SOLUTION STRUCTURE OF APOCYTOCHROME B562
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B562;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR A.J.WAND,Y.FENG,S.G.SLIGAR
REVDAT 4 29-NOV-17 1APC 1 REMARK HELIX
REVDAT 3 24-FEB-09 1APC 1 VERSN
REVDAT 2 01-APR-03 1APC 1 JRNL
REVDAT 1 31-JAN-94 1APC 0
JRNL AUTH Y.FENG,S.G.SLIGAR,A.J.WAND
JRNL TITL SOLUTION STRUCTURE OF APOCYTOCHROME B562.
JRNL REF NAT.STRUCT.BIOL. V. 1 30 1994
JRNL REFN ISSN 1072-8368
JRNL PMID 7656004
JRNL DOI 10.1038/NSB0194-30
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.FENG,A.J.WAND,S.G.SLIGAR
REMARK 1 TITL 1H AND 15N NMR RESONANCE ASSIGNMENTS AND PRELIMINARY
REMARK 1 TITL 2 STRUCTURAL CHARACTERIZATION OF ESCHERICHIA COLI
REMARK 1 TITL 3 APOCYTOCHROME B562
REMARK 1 REF BIOCHEMISTRY V. 30 7711 1991
REMARK 1 REFN ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : HARE RESEARCH INC. (DSPACE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1APC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171092.
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 : 1
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: 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 THR A 44 HD3 PRO A 46 0.36
REMARK 500 O ASP A 50 H SER A 52 0.90
REMARK 500 HB3 SER A 55 HD3 PRO A 56 0.95
REMARK 500 HE2 PHE A 61 HE2 PHE A 65 1.09
REMARK 500 HD13 LEU A 78 HB3 LYS A 83 1.12
REMARK 500 O ALA A 43 HD3 PRO A 45 1.13
REMARK 500 HB3 ALA A 79 HG21 VAL A 84 1.18
REMARK 500 O ASP A 2 H GLU A 4 1.23
REMARK 500 CD1 LEU A 78 HB3 LYS A 83 1.23
REMARK 500 HE21 GLN A 25 H VAL A 26 1.24
REMARK 500 O PRO A 46 H GLU A 49 1.24
REMARK 500 HD11 LEU A 78 HB3 LYS A 83 1.30
REMARK 500 O MET A 58 H PHE A 61 1.31
REMARK 500 HE21 GLN A 25 N VAL A 26 1.32
REMARK 500 O LEU A 3 H ASP A 5 1.33
REMARK 500 HB2 ASN A 22 HG2 GLN A 25 1.33
REMARK 500 O THR A 44 CD PRO A 46 1.43
REMARK 500 O SER A 55 H GLU A 57 1.43
REMARK 500 O GLN A 93 HB2 LEU A 94 1.44
REMARK 500 C THR A 44 HD3 PRO A 46 1.48
REMARK 500 O ALA A 87 H ALA A 90 1.49
REMARK 500 O LEU A 78 HB2 LYS A 83 1.51
REMARK 500 O ALA A 23 HE22 GLN A 25 1.52
REMARK 500 CG ASP A 2 H LEU A 3 1.54
REMARK 500 O ASP A 39 H ALA A 43 1.54
REMARK 500 C ALA A 23 HE22 GLN A 25 1.55
REMARK 500 O MET A 33 H ALA A 37 1.58
REMARK 500 O LEU A 3 N ASP A 5 1.64
REMARK 500 O ASP A 50 N SER A 52 1.65
REMARK 500 O ASP A 2 N GLU A 4 1.97
REMARK 500 O ALA A 87 N ALA A 89 2.03
REMARK 500 O VAL A 16 CB ALA A 20 2.10
REMARK 500 O PRO A 46 N GLU A 49 2.11
REMARK 500 O PHE A 65 N ILE A 67 2.14
REMARK 500 O ALA A 43 CD PRO A 45 2.16
REMARK 500 O ILE A 17 O ALA A 20 2.16
REMARK 500 N ALA A 23 OE1 GLN A 25 2.18
REMARK 500 O LEU A 78 CB LYS A 83 2.19
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 ASP A 2 -133.56 -142.35
REMARK 500 LEU A 3 20.11 -49.18
REMARK 500 GLU A 4 -15.96 -19.85
REMARK 500 ASP A 5 -81.23 -73.52
REMARK 500 GLU A 18 -77.80 -51.94
REMARK 500 ASP A 21 -35.83 164.21
REMARK 500 ASN A 22 -168.45 -46.23
REMARK 500 GLN A 25 -87.72 -52.32
REMARK 500 VAL A 26 -30.37 -34.92
REMARK 500 PRO A 45 69.00 -60.87
REMARK 500 GLU A 49 103.87 83.91
REMARK 500 LYS A 51 48.75 -34.53
REMARK 500 SER A 52 87.62 -24.31
REMARK 500 SER A 55 -81.37 156.16
REMARK 500 PRO A 56 40.09 -60.94
REMARK 500 GLU A 57 -79.99 -80.36
REMARK 500 MET A 58 -81.54 -33.66
REMARK 500 LYS A 59 -34.66 -27.60
REMARK 500 ASP A 66 -41.75 -20.60
REMARK 500 LEU A 76 -81.19 -78.75
REMARK 500 LYS A 77 -15.13 -43.43
REMARK 500 GLN A 88 -31.50 -24.18
REMARK 500 LEU A 94 -178.01 104.24
REMARK 500 LYS A 95 -44.11 -133.62
REMARK 500 THR A 96 77.79 7.70
REMARK 500 THR A 97 117.76 -13.83
REMARK 500 ALA A 100 89.65 -19.35
REMARK 500 TYR A 101 159.49 -38.55
REMARK 500 LYS A 104 -89.81 171.47
REMARK 500 TYR A 105 47.40 -90.77
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 ARG A 98 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1APC A 1 106 UNP P0ABE7 C562_ECOLI 23 128
SEQRES 1 A 106 ALA ASP LEU GLU ASP ASN MET GLU THR LEU ASN ASP ASN
SEQRES 2 A 106 LEU LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL
SEQRES 3 A 106 LYS ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP
SEQRES 4 A 106 ALA GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER
SEQRES 5 A 106 PRO ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE
SEQRES 6 A 106 ASP ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU
SEQRES 7 A 106 ALA ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA
SEQRES 8 A 106 GLU GLN LEU LYS THR THR ARG ASN ALA TYR HIS GLN LYS
SEQRES 9 A 106 TYR ARG
HELIX 1 BA ALA A 23 GLN A 41 1 19
HELIX 2 LA PRO A 46 LEU A 48 1 3
HELIX 3 CA MET A 58 ALA A 79 1 22
HELIX 4 DA VAL A 84 GLN A 93 1 10
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
Complete list - 29 20 Bytes