Header list of 1i5u.pdb file
Complete list - 10 20 Bytes
HEADER ELECTRON TRANSPORT 28-FEB-01 1I5U
TITLE SOLUTION STRUCTURE OF CYTOCHROME B5 TRIPLE MUTANT (E48A/E56A/D60A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME B5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SOLUBLE DOMAIN (RESIDUES 8-89);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PUC19
KEYWDS ELECTRON TRANSPORT, TRANSMEMBRANE, HEME, MICROSOME
EXPDTA SOLUTION NMR
AUTHOR C.QIAN,Y.YAO,W.TANG,J.WANG,H.ZHONGXIAN
REVDAT 4 10-NOV-21 1I5U 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1I5U 1 VERSN
REVDAT 2 31-DEC-02 1I5U 1 REMARK
REVDAT 1 21-MAR-01 1I5U 0
JRNL AUTH C.QIAN,Y.YAO,K.YE,J.WANG,W.TANG,Y.WANG,W.WANG,J.LU,Y.XIE,
JRNL AUTH 2 Z.HUANG
JRNL TITL EFFECTS OF CHARGED AMINO-ACID MUTATION ON THE SOLUTION
JRNL TITL 2 STRUCTURE OF CYTOCHROME B(5) AND BINDING BETWEEN CYTOCHROME
JRNL TITL 3 B(5) AND CYTOCHROME C.
JRNL REF PROTEIN SCI. V. 10 2451 2001
JRNL REFN ISSN 0961-8368
JRNL PMID 11714912
JRNL DOI 10.1110/PS.PS.12401
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, AMBER
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1522 MEANINGFUL NOE-DERIVED DISTANCE CONSTRAINTS, TOGETHER WITH
REMARK 3 190 PSEUDOCONTACT SHIFT CONSTRAINTS.
REMARK 4
REMARK 4 1I5U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012941.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303; 303
REMARK 210 PH : 7.0; 7.0; 7.0; 7.0
REMARK 210 IONIC STRENGTH : NULL; NULL; NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 4MM CYTOCHROME B5 TRIPLE
REMARK 210 MUTANT(E48A/E56A/D60A)
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, AURELIA, PSEUDYANA,
REMARK 210 XEASY
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 36
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED AVERAGE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 20 106.54 -168.93
REMARK 500 HIS A 63 118.62 62.66
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 TYR A 27 0.09 SIDE CHAIN
REMARK 500 ARG A 68 0.11 SIDE CHAIN
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 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 39 NE2
REMARK 620 2 HEM A 201 NA 91.6
REMARK 620 3 HEM A 201 NB 95.0 89.9
REMARK 620 4 HEM A 201 NC 88.0 179.4 89.7
REMARK 620 5 HEM A 201 ND 85.8 90.9 178.9 89.4
REMARK 620 6 HIS A 63 NE2 175.9 90.6 88.5 89.9 90.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I5T RELATED DB: PDB
REMARK 900 1I5T CONTAINS SOLUTION STRUCTURE OF CYANOFERRICYTOCHROME C
REMARK 900 RELATED ID: 1AW3 RELATED DB: PDB
REMARK 900 1AW3 CONTAINS SOLUTION NMR STRUCTURE OF OXIDIZED RAT MICROSOMAL
REMARK 900 CYTOCHROME B5
REMARK 900 RELATED ID: 1F04 RELATED DB: PDB
REMARK 900 1F04 CONTAINS SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL
REMARK 900 CYTOCHROME B5 MUTANT (E44A/E48A/E56A/D60A)
DBREF 1I5U A 3 84 UNP P00171 CYB5_BOVIN 8 89
SEQADV 1I5U ALA A 48 UNP P00171 GLU 53 ENGINEERED MUTATION
SEQADV 1I5U ALA A 56 UNP P00171 GLU 61 ENGINEERED MUTATION
SEQADV 1I5U ALA A 60 UNP P00171 ASP 65 ENGINEERED MUTATION
SEQRES 1 A 82 ALA VAL LYS TYR TYR THR LEU GLU GLU ILE GLN LYS HIS
SEQRES 2 A 82 ASN ASN SER LYS SER THR TRP LEU ILE LEU HIS TYR LYS
SEQRES 3 A 82 VAL TYR ASP LEU THR LYS PHE LEU GLU GLU HIS PRO GLY
SEQRES 4 A 82 GLY GLU GLU VAL LEU ARG ALA GLN ALA GLY GLY ASP ALA
SEQRES 5 A 82 THR ALA ASN PHE GLU ALA VAL GLY HIS SER THR ASP ALA
SEQRES 6 A 82 ARG GLU LEU SER LYS THR PHE ILE ILE GLY GLU LEU HIS
SEQRES 7 A 82 PRO ASP ASP ARG
HET HEM A 201 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 LEU A 36 5 4
HELIX 3 3 GLY A 42 ALA A 50 1 9
HELIX 4 4 ALA A 54 VAL A 61 1 8
HELIX 5 5 SER A 64 PHE A 74 1 11
HELIX 6 6 PRO A 81 ARG A 84 5 4
SHEET 1 A 5 TYR A 6 TYR A 7 0
SHEET 2 A 5 ILE A 75 LEU A 79 1 O GLU A 78 N TYR A 7
SHEET 3 A 5 LYS A 28 ASP A 31 -1 N VAL A 29 O GLY A 77
SHEET 4 A 5 SER A 20 LEU A 25 -1 O LEU A 23 N TYR A 30
SHEET 5 A 5 ASN A 16 ASN A 17 -1 N ASN A 17 O SER A 20
LINK NE2 HIS A 39 FE HEM A 201 1555 1555 2.00
LINK NE2 HIS A 63 FE HEM A 201 1555 1555 1.99
SITE 1 AC1 13 LEU A 32 PHE A 35 HIS A 39 PRO A 40
SITE 2 AC1 13 GLY A 41 VAL A 45 ASN A 57 PHE A 58
SITE 3 AC1 13 HIS A 63 SER A 64 ALA A 67 LEU A 70
SITE 4 AC1 13 SER A 71
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 - 10 20 Bytes