Header list of 1qpu.pdb file
Complete list - 2 20 Bytes
HEADER ELECTRON TRANSPORT 30-MAY-99 1QPU
TITLE SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI CYTOCHROME 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;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR HELIX BUNDLE, HEMOPROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
AUTHOR F.ARNESANO,L.BANCI,I.BERTINI,J.FARAONE-MENNELLA,A.ROSATO,P.D.BARKER,
AUTHOR 2 A.R.FERSHT
REVDAT 4 02-MAR-22 1QPU 1 REMARK LINK
REVDAT 3 24-FEB-09 1QPU 1 VERSN
REVDAT 2 29-DEC-99 1QPU 1 JRNL REMARK
REVDAT 1 02-JUN-99 1QPU 0
JRNL AUTH F.ARNESANO,L.BANCI,I.BERTINI,J.FARAONE-MENNELLA,A.ROSATO,
JRNL AUTH 2 P.D.BARKER,A.R.FERSHT
JRNL TITL THE SOLUTION STRUCTURE OF OXIDIZED ESCHERICHIA COLI
JRNL TITL 2 CYTOCHROME B562.
JRNL REF BIOCHEMISTRY V. 38 8657 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10393541
JRNL DOI 10.1021/BI982785F
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 5.0
REMARK 3 AUTHORS : GUNTERT, P., MUMENTHALER, C. & WUTHRICH, K
REMARK 3 (DYANA), PEARLMAN, D.A. ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QPU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-99.
REMARK 100 THE DEPOSITION ID IS D_1000009123.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 4.8; 4.8; 4.8
REMARK 210 IONIC STRENGTH : 500 MM PHOSPHATE; 500 MM
REMARK 210 PHOSPHATE; 500 MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3 MM CYTOCHROME B562, 500 MM
REMARK 210 PHOSPHATE BUFFER, PH 4.8; 3 MM
REMARK 210 CYTOCHROME B562 U-15N, 500 MM
REMARK 210 PHOSPHATE BUFFER, PH 4.8; 3 MM
REMARK 210 CYTOCHROME B562, 500 MM
REMARK 210 PHOSPHATE BUFFER, PH 4.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS FOLLOWED
REMARK 210 BY ENERGY MINIMIZATION
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: 1D NOE EXPERIMENTS WERE USED TO OBTAIN CONSTRAINTS FOR THE
REMARK 210 IRON AXIAL LIGANDS
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: 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 ARG A 106 CB - CA - C ANGL. DEV. = 19.0 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 ASP A 2 -90.91 -84.92
REMARK 500 LEU A 3 -41.79 173.79
REMARK 500 ARG A 62 -26.63 -24.16
REMARK 500 LYS A 83 44.89 -75.76
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 0.13 SIDE CHAIN
REMARK 500 TYR A 105 0.07 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 107 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 7 SD
REMARK 620 2 HEM A 107 NA 83.9
REMARK 620 3 HEM A 107 NB 94.1 90.0
REMARK 620 4 HEM A 107 NC 92.8 175.6 93.2
REMARK 620 5 HEM A 107 ND 81.8 90.3 175.8 86.3
REMARK 620 6 HIS A 102 NE2 170.9 91.7 93.9 91.1 90.3
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 107
DBREF 1QPU 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
HET HEM A 107 73
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN HEM HEME
FORMUL 2 HEM C34 H32 FE N4 O4
HELIX 1 1 LEU A 3 GLU A 18 1 16
HELIX 2 2 ASN A 22 GLN A 41 1 20
HELIX 3 3 PRO A 45 GLU A 49 5 5
HELIX 4 4 ARG A 62 ASN A 80 1 19
HELIX 5 5 LYS A 83 ARG A 106 1 24
LINK SD MET A 7 FE HEM A 107 1555 1555 2.30
LINK NE2 HIS A 102 FE HEM A 107 1555 1555 1.98
SITE 1 AC1 14 LEU A 3 GLU A 4 MET A 7 LEU A 10
SITE 2 AC1 14 ASN A 11 PRO A 45 PHE A 61 GLY A 64
SITE 3 AC1 14 LEU A 68 THR A 97 ARG A 98 HIS A 102
SITE 4 AC1 14 TYR A 105 ARG A 106
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 - 2 20 Bytes