Header list of 1nmi.pdb file
Complete list - 23 20 Bytes
HEADER ELECTRON TRANSPORT 10-JAN-03 1NMI
TITLE SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF ISO-1 CYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C, ISO-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LIGAND-PROTEIN COMPLEX, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR Y.YAO,Y.TONG,G.LIU,J.WANG,J.ZHENG,W.TANG
REVDAT 3 23-FEB-22 1NMI 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1NMI 1 VERSN
REVDAT 1 04-FEB-03 1NMI 0
JRNL AUTH Y.YAO,Y.TONG,G.LIU,J.WANG,J.ZHENG,W.TANG
JRNL TITL SOLUTION STRUCTURE OF THE IMIDAZOLE COMPLEX OF ISO-1
JRNL TITL 2 CYTOCHROME C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, DYANA 1.5
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NMI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-03.
REMARK 100 THE DEPOSITION ID IS D_1000018004.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1MM ISO-1 CYTOCHROME C, 120MM
REMARK 210 D5IMIDAZOLE; 1MM 15N LABELED ISO-
REMARK 210 1 CYTOCHROME C, 120MM D5IMIDAZOLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY;
REMARK 210 3D_15N-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : RESTRAINED ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 ARG A 13 NE - CZ - NH2 ANGL. DEV. = -3.2 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 SER A 2 -62.60 -104.78
REMARK 500 ARG A 13 -60.76 -133.47
REMARK 500 LYS A 22 96.07 -65.39
REMARK 500 VAL A 28 -51.40 -121.52
REMARK 500 ARG A 38 -102.99 -142.16
REMARK 500 HIS A 39 -177.59 -179.40
REMARK 500 SER A 40 82.18 -66.10
REMARK 500 GLN A 42 46.17 -92.84
REMARK 500 LYS A 54 -77.70 -53.76
REMARK 500 LYS A 55 46.01 26.71
REMARK 500 ASN A 56 68.63 15.23
REMARK 500 THR A 69 -65.00 -104.80
REMARK 500 LYS A 72 -137.47 51.92
REMARK 500 LYS A 73 -33.36 70.57
REMARK 500 ILE A 75 56.92 20.12
REMARK 500 THR A 78 -66.22 -21.77
REMARK 500 LYS A 79 -71.40 -167.78
REMARK 500 LYS A 86 -49.56 -162.00
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 13 0.14 SIDE CHAIN
REMARK 500 HIS A 18 0.11 SIDE CHAIN
REMARK 500 ARG A 38 0.09 SIDE CHAIN
REMARK 500 TYR A 48 0.11 SIDE CHAIN
REMARK 500 TYR A 74 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 HEC A1018 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A1018 NA 91.0
REMARK 620 3 HEC A1018 NB 88.9 90.7
REMARK 620 4 HEC A1018 NC 88.5 179.3 89.9
REMARK 620 5 HEC A1018 ND 87.5 89.9 176.4 89.5
REMARK 620 6 IMD A 104 N1 176.7 91.7 92.9 88.7 90.6
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 104
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 1018
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YIC RELATED DB: PDB
DBREF 1NMI A -5 103 UNP P00044 CYC1_YEAST 1 108
SEQADV 1NMI THR A 102 UNP P00044 CYS 107 CONFLICT
SEQRES 1 A 108 THR GLU PHE LYS ALA GLY SER ALA LYS LYS GLY ALA THR
SEQRES 2 A 108 LEU PHE LYS THR ARG CYS LEU GLN CYS HIS THR VAL GLU
SEQRES 3 A 108 LYS GLY GLY PRO HIS LYS VAL GLY PRO ASN LEU HIS GLY
SEQRES 4 A 108 ILE PHE GLY ARG HIS SER GLY GLN ALA GLU GLY TYR SER
SEQRES 5 A 108 TYR THR ASP ALA ASN ILE LYS LYS ASN VAL LEU TRP ASP
SEQRES 6 A 108 GLU ASN ASN MET SER GLU TYR LEU THR ASN PRO LYS LYS
SEQRES 7 A 108 TYR ILE PRO GLY THR LYS MET ALA PHE GLY GLY LEU LYS
SEQRES 8 A 108 LYS GLU LYS ASP ARG ASN ASP LEU ILE THR TYR LEU LYS
SEQRES 9 A 108 LYS ALA THR GLU
HET IMD A 104 9
HET HEC A1018 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 LYS A 5 THR A 12 1 8
HELIX 2 2 ASP A 50 LYS A 55 1 6
HELIX 3 3 ASP A 60 LEU A 68 1 9
HELIX 4 4 LYS A 87 GLU A 103 1 17
LINK SG CYS A 14 CAB HEC A1018 1555 1555 1.83
LINK SG CYS A 17 CAC HEC A1018 1555 1555 1.84
LINK NE2 HIS A 18 FE HEC A1018 1555 1555 1.94
LINK N1 IMD A 104 FE HEC A1018 1555 1555 1.99
SITE 1 AC1 3 TYR A 67 ALA A 81 HEC A1018
SITE 1 AC2 21 ARG A 13 CYS A 14 CYS A 17 HIS A 18
SITE 2 AC2 21 PRO A 30 LEU A 32 ILE A 35 TYR A 48
SITE 3 AC2 21 ASP A 50 TRP A 59 MET A 64 LEU A 68
SITE 4 AC2 21 PRO A 76 THR A 78 LYS A 79 MET A 80
SITE 5 AC2 21 ALA A 81 PHE A 82 LEU A 94 LEU A 98
SITE 6 AC2 21 IMD A 104
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