Header list of 1fi3.pdb file
Complete list - 3 20 Bytes
HEADER ELECTRON TRANSPORT 03-AUG-00 1FI3
TITLE SOLUTION STRUCTURE OF THE M61H MUTANT OF PSEUDOMONAS STUTZERI
TITLE 2 SUBSTRAIN ZOBELL FERROCYTOCHROME C-551
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C-551;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: C551, CYTOCHROME C8;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI ZOBELL;
SOURCE 3 ORGANISM_TAXID: 96564;
SOURCE 4 STRAIN: ZOBELL;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PCATNIRMM61H
KEYWDS C-551 FAMILY, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR G.T.MILLER,J.K.HARDMAN,R.TIMKOVICH
REVDAT 4 03-NOV-21 1FI3 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1FI3 1 VERSN
REVDAT 2 06-JUN-01 1FI3 1 JRNL
REVDAT 1 14-MAR-01 1FI3 0
JRNL AUTH G.T.MILLER,J.K.HARDMAN,R.TIMKOVICH
JRNL TITL SOLUTION CONFORMATION OF THE MET 61 TO HIS 61 MUTANT OF
JRNL TITL 2 PSEUDOMONAS STUTZERI ZOBELL FERROCYTOCHROME C-551.
JRNL REF BIOPHYS.J. V. 80 2928 2001
JRNL REFN ISSN 0006-3495
JRNL PMID 11371465
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 95.0, CNSSOLVE 0.9A
REMARK 3 AUTHORS : HARE/REED (FELIX), BRUNGER (CNSSOLVE)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1039 NOE DISTANCE CONSTRAINTS
REMARK 3 35 H-BOND CONSTRAINTS
REMARK 3 72 TORSION ANGLE MAIN CHAIN CONSTRAINTS
REMARK 4
REMARK 4 1FI3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011609.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 333
REMARK 210 PH : 9.2
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 5 MM C-551; 50 MM PHOSPHATE
REMARK 210 BUFFER, SODIUM DITHIONITE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY, HOHAHA, DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AM
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNSSOLVE 0.9A
REMARK 210 METHOD USED : SIMULATED ANNEALING
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 : 1
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: 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 H TRP A 56 O1D HEC A 83 1.50
REMARK 500 HE1 TRP A 56 O2A HEC A 83 1.59
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 LYS A 8 -71.04 -79.71
REMARK 500 PRO A 11 22.77 -58.81
REMARK 500 ASP A 19 46.59 -142.51
REMARK 500 THR A 20 -50.21 -154.19
REMARK 500 LYS A 21 135.43 67.45
REMARK 500 MET A 22 -58.31 -147.20
REMARK 500 SER A 52 139.61 -176.27
REMARK 500 VAL A 55 -74.85 -120.48
REMARK 500 LEU A 81 -88.95 50.35
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 HEC A 83 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 16 NE2
REMARK 620 2 HEC A 83 NA 89.4
REMARK 620 3 HEC A 83 NB 92.3 90.0
REMARK 620 4 HEC A 83 NC 92.3 178.3 90.1
REMARK 620 5 HEC A 83 ND 89.0 90.2 178.7 89.7
REMARK 620 6 HIS A 61 NE2 178.4 92.0 88.5 86.3 90.2
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 HEC A 83
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CCH RELATED DB: PDB
REMARK 900 1CCH IS THE WILD TYPE SOLUTION STRUCTURE
DBREF 1FI3 A 1 82 UNP P00101 CY551_PSEST 23 104
SEQADV 1FI3 HIS A 61 UNP P00101 MET 83 ENGINEERED MUTATION
SEQRES 1 A 82 GLN ASP GLY GLU ALA LEU PHE LYS SER LYS PRO CYS ALA
SEQRES 2 A 82 ALA CYS HIS SER VAL ASP THR LYS MET VAL GLY PRO ALA
SEQRES 3 A 82 LEU LYS GLU VAL ALA ALA LYS ASN ALA GLY VAL GLU GLY
SEQRES 4 A 82 ALA ALA ASP THR LEU ALA LEU HIS ILE LYS ASN GLY SER
SEQRES 5 A 82 GLN GLY VAL TRP GLY PRO ILE PRO HIS PRO PRO ASN PRO
SEQRES 6 A 82 VAL THR GLU GLU GLU ALA LYS ILE LEU ALA GLU TRP VAL
SEQRES 7 A 82 LEU SER LEU LYS
HET HEC A 83 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 GLN A 1 LYS A 10 1 10
HELIX 2 2 PRO A 11 HIS A 16 1 6
HELIX 3 3 ALA A 26 ASN A 34 1 9
HELIX 4 4 GLY A 39 LYS A 49 1 11
HELIX 5 5 THR A 67 LEU A 81 1 15
LINK SG CYS A 12 CAB HEC A 83 1555 1555 1.81
LINK SG CYS A 15 CAC HEC A 83 1555 1555 1.83
LINK NE2 HIS A 16 FE HEC A 83 1555 1555 1.95
LINK NE2 HIS A 61 FE HEC A 83 1555 1555 1.92
SITE 1 AC1 15 CYS A 12 CYS A 15 HIS A 16 VAL A 23
SITE 2 AC1 15 GLY A 24 VAL A 30 LEU A 44 HIS A 47
SITE 3 AC1 15 ILE A 48 SER A 52 VAL A 55 TRP A 56
SITE 4 AC1 15 GLY A 57 ILE A 59 HIS A 61
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 - 3 20 Bytes