Header list of 1fi7.pdb file
Complete list - 23 20 Bytes
HEADER ELECTRON TRANSPORT 03-AUG-00 1FI7
TITLE SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF CYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: EQUUS CABALLUS;
SOURCE 3 ORGANISM_COMMON: HORSE;
SOURCE 4 ORGANISM_TAXID: 9796;
SOURCE 5 TISSUE: HEART
KEYWDS CYTOCHROME C, SOLUTION STRUCTURE, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,G.LIU,J.LU,T.REDDIG,W.TANG,Y.WU,D.ZHU
REVDAT 5 23-FEB-22 1FI7 1 REMARK LINK
REVDAT 4 24-FEB-09 1FI7 1 VERSN
REVDAT 3 29-MAR-05 1FI7 1 JRNL
REVDAT 2 13-SEP-00 1FI7 1 DBREF
REVDAT 1 23-AUG-00 1FI7 0
JRNL AUTH L.BANCI,I.BERTINI,G.LIU,J.LU,T.REDDIG,W.TANG,Y.WU,Y.YAO,
JRNL AUTH 2 D.ZHU
JRNL TITL EFFECTS OF EXTRINSIC IMIDAZOLE LIGATION ON THE MOLECULAR AND
JRNL TITL 2 ELECTRONIC STRUCTURE OF CYTOCHROME C
JRNL REF J.BIOL.INORG.CHEM. V. 6 628 2001
JRNL REFN ISSN 0949-8257
JRNL PMID 11472026
JRNL DOI 10.1007/S007750100240
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 5.0, AMBER 5.0, PSEUDOREM 5.0
REMARK 3 AUTHORS : WUTHRICH ET AL (DYANA), PEARLMAN, CASE, CALDWELL,
REMARK 3 ROSS, CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER,
REMARK 3 KOLLMAN (AMBER), BANCI, BERTINI, GORI SAVELLINI,
REMARK 3 ROMAGNOLI, TURANO, CREMONINI, LUCHINAT,GARY
REMARK 3 (PSEUDOREM)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: OTHER REFINEMENT REMARKS: DYNAMICS
REMARK 3 SIMULATED ANNEALING,RESTRAINED ENERGY MINIMIZATION;
REMARK 3 PSEUDOCONTACT SHIFTS WERE USED IN THE CALCULATION AND IN THE
REMARK 3 MINIMIZATION AS FURTHER NON-CLASSICAL CONSTRAINTS
REMARK 4
REMARK 4 1FI7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011613.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 6MM CYTOCHROME C, 1.2M
REMARK 210 IMIDAZOLE; 6MM CYTOCHROME C,
REMARK 210 1.2M IMIDAZOLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PSEUDODYANA 5.0
REMARK 210 METHOD USED : AMBER
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: 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 TYR A 48 CB - CG - CD2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 TYR A 48 CB - CG - CD1 ANGL. DEV. = 3.7 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 ALA A 15 -71.96 -0.70
REMARK 500 CYS A 17 -44.09 -164.88
REMARK 500 LYS A 27 -126.37 37.22
REMARK 500 ASN A 31 102.64 -59.50
REMARK 500 GLN A 42 58.05 -149.06
REMARK 500 ASP A 50 14.50 -62.73
REMARK 500 LYS A 60 -11.32 -155.67
REMARK 500 GLU A 61 -52.07 134.91
REMARK 500 ASN A 70 56.68 -152.30
REMARK 500 LYS A 72 48.03 -83.96
REMARK 500 LYS A 73 -49.10 -145.40
REMARK 500 ILE A 75 117.75 -162.08
REMARK 500 THR A 78 -67.77 -127.59
REMARK 500 LYS A 79 -31.50 -174.79
REMARK 500 MET A 80 83.81 55.86
REMARK 500 ILE A 81 -118.18 -98.98
REMARK 500 ILE A 85 -81.49 -54.68
REMARK 500 LYS A 86 -50.69 -148.70
REMARK 500 LYS A 87 -153.20 -166.40
REMARK 500 THR A 89 -70.54 -49.51
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 74 0.06 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 HEC A 110 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 110 NA 93.1
REMARK 620 3 HEC A 110 NB 89.9 89.7
REMARK 620 4 HEC A 110 NC 86.9 179.5 89.8
REMARK 620 5 HEC A 110 ND 85.5 89.9 175.4 90.6
REMARK 620 6 IMD A 105 N3 172.2 93.4 94.3 86.6 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 IMD A 105
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 110
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FI9 RELATED DB: PDB
REMARK 900 1FI9 CONTAINS THE ENSEMBLE OF STRUCTURES.
DBREF 1FI7 A 1 104 UNP P00004 CYC_HORSE 1 104
SEQRES 1 A 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE VAL GLN LYS
SEQRES 2 A 104 CYS ALA GLN CYS HIS THR VAL GLU LYS GLY GLY LYS HIS
SEQRES 3 A 104 LYS THR GLY PRO ASN LEU HIS GLY LEU PHE GLY ARG LYS
SEQRES 4 A 104 THR GLY GLN ALA PRO GLY PHE THR TYR THR ASP ALA ASN
SEQRES 5 A 104 LYS ASN LYS GLY ILE THR TRP LYS GLU GLU THR LEU MET
SEQRES 6 A 104 GLU TYR LEU GLU ASN PRO LYS LYS TYR ILE PRO GLY THR
SEQRES 7 A 104 LYS MET ILE PHE ALA GLY ILE LYS LYS LYS THR GLU ARG
SEQRES 8 A 104 GLU ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
HET IMD A 105 9
HET HEC A 110 75
HETNAM IMD IMIDAZOLE
HETNAM HEC HEME C
FORMUL 2 IMD C3 H5 N2 1+
FORMUL 3 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 ALA A 51 GLY A 56 1 6
HELIX 3 3 GLU A 61 ASN A 70 1 10
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 GLU A 104 1 18
LINK SG CYS A 14 CAB HEC A 110 1555 1555 1.82
LINK SG CYS A 17 CAC HEC A 110 1555 1555 1.81
LINK NE2 HIS A 18 FE HEC A 110 1555 1555 1.94
LINK N3 IMD A 105 FE HEC A 110 1555 1555 1.97
SITE 1 AC1 3 TYR A 67 LYS A 79 HEC A 110
SITE 1 AC2 16 CYS A 14 CYS A 17 HIS A 18 THR A 28
SITE 2 AC2 16 GLY A 29 PRO A 30 LEU A 32 THR A 40
SITE 3 AC2 16 THR A 49 ASN A 52 TRP A 59 LEU A 64
SITE 4 AC2 16 LEU A 68 THR A 78 LYS A 79 IMD A 105
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 - 23 20 Bytes