Header list of 1aqa.pdb file
Complete list - 16 20 Bytes
HEADER ELECTRON TRANSPORT 28-JUL-97 1AQA
TITLE SOLUTION STRUCTURE OF REDUCED MICROSOMAL RAT CYTOCHROME B5, NMR,
TITLE 2 MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 STRAIN: NM522;
SOURCE 6 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 7 GENE: CYB5;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 10 EXPRESSION_SYSTEM_STRAIN: NM522;
SOURCE 11 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_PLASMID: PUC 13;
SOURCE 14 EXPRESSION_SYSTEM_GENE: SYNRATCYB5;
SOURCE 15 OTHER_DETAILS: CLONING VECTOR PUC13
KEYWDS CYTOCHROME B5, PROTEIN RECOGNITION, SOLUTION STRUCTURES, SECONDARY
KEYWDS 2 STRUCTURES, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR L.BANCI,I.BERTINI,F.FERRONI,A.ROSATO
REVDAT 3 16-FEB-22 1AQA 1 REMARK LINK
REVDAT 2 24-FEB-09 1AQA 1 VERSN
REVDAT 1 17-SEP-97 1AQA 0
JRNL AUTH L.BANCI,I.BERTINI,F.FERRONI,A.ROSATO
JRNL TITL SOLUTION STRUCTURE OF REDUCED MICROSOMAL RAT CYTOCHROME B5.
JRNL REF EUR.J.BIOCHEM. V. 249 270 1997
JRNL REFN ISSN 0014-2956
JRNL PMID 9363779
JRNL DOI 10.1111/J.1432-1033.1997.T01-1-00270.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER
REMARK 3 AUTHORS : WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1AQA 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_1000171124.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY WATERGATE; TOCSY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE 800 MHZ; AMX 600 MHZ
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, AMBER
REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR DYNAMICS
REMARK 210 SIMULATED ANNEALING, RESTRAINED
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 40
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 LYS A 2
REMARK 465 ASP A 3
REMARK 465 VAL A 4
REMARK 465 LYS A 89
REMARK 465 PRO A 90
REMARK 465 SER A 91
REMARK 465 GLU A 92
REMARK 465 THR A 93
REMARK 465 LEU A 94
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 SER A 18 94.89 78.79
REMARK 500 LYS A 19 -8.53 76.97
REMARK 500 THR A 33 57.30 -64.93
REMARK 500 LYS A 34 -51.10 -174.23
REMARK 500 GLU A 44 -65.11 -29.04
REMARK 500 THR A 55 -59.89 -17.53
REMARK 500 PHE A 58 -71.87 -74.93
REMARK 500 TYR A 74 -83.86 -80.25
REMARK 500 ILE A 75 97.03 55.32
REMARK 500 GLU A 78 -84.57 -103.75
REMARK 500 LEU A 79 162.00 169.17
REMARK 500 ASP A 82 -53.14 -150.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM A 95A FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 95A NA 93.4
REMARK 620 3 HEM A 95A NB 91.3 89.5
REMARK 620 4 HEM A 95A NC 85.6 178.9 90.9
REMARK 620 5 HEM A 95A ND 89.2 88.9 178.3 90.7
REMARK 620 6 HIS A 63 NE2 171.7 94.1 92.2 86.8 87.5
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: S1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 95A
DBREF 1AQA A 1 94 UNP P00173 CYB5_RAT 5 98
SEQRES 1 A 94 ASP LYS ASP VAL LYS TYR TYR THR LEU GLU GLU ILE GLN
SEQRES 2 A 94 LYS HIS LYS ASP SER LYS SER THR TRP VAL ILE LEU HIS
SEQRES 3 A 94 HIS LYS VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS
SEQRES 4 A 94 PRO GLY GLY GLU GLU VAL LEU ARG GLU GLN ALA GLY GLY
SEQRES 5 A 94 ASP ALA THR GLU ASN PHE GLU ASP VAL GLY HIS SER THR
SEQRES 6 A 94 ASP ALA ARG GLU LEU SER LYS THR TYR ILE ILE GLY GLU
SEQRES 7 A 94 LEU HIS PRO ASP ASP ARG SER LYS ILE ALA LYS PRO SER
SEQRES 8 A 94 GLU THR LEU
HET HEM A 95A 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 THR A 8 HIS A 15 1 8
HELIX 2 2 THR A 33 GLU A 38 5 6
HELIX 3 3 GLY A 42 GLU A 48 1 7
HELIX 4 4 ALA A 54 ASP A 60 1 7
HELIX 5 5 SER A 64 ILE A 75 1 12
HELIX 6 6 ASP A 82 LYS A 86 1 5
SHEET 1 A 2 TRP A 22 ILE A 24 0
SHEET 2 A 2 VAL A 29 ASP A 31 -1 N TYR A 30 O VAL A 23
LINK NE2 HIS A 39 FE HEM A 95A 1555 1555 2.01
LINK NE2 HIS A 63 FE HEM A 95A 1555 1555 2.02
SITE 1 S1 2 HIS A 39 HEM A 95A
SITE 1 AC1 9 PHE A 35 HIS A 39 VAL A 45 LEU A 46
SITE 2 AC1 9 ASN A 57 VAL A 61 HIS A 63 ALA A 67
SITE 3 AC1 9 LEU A 70
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 - 16 20 Bytes