Header list of 1j3s.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 12-FEB-03 1J3S
TITLE SOLUTION STRUCTURE OF REDUCED RECOMBINANT HUMAN CYTOCHROME C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FERROCYTOCHROME C;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B1-21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS FERROCYTOCHROME C, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.-Y.JENG,J.-H.SHIU,Y.-H.TSAI,W.-J.CHUANG
REVDAT 3 23-FEB-22 1J3S 1 REMARK LINK
REVDAT 2 24-FEB-09 1J3S 1 VERSN
REVDAT 1 18-MAY-04 1J3S 0
JRNL AUTH W.-Y.JENG,J.-H.SHIU,Y.-H.TSAI,W.-J.CHUANG
JRNL TITL SOLUTION STRUCTURE OF REDUCED RECOMBINANT HUMAN CYTOCHROME C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.-Y.JENG,J.-H.SHIU,Y.-H.TSAI,W.-J.CHUANG
REMARK 1 TITL EXPRESSION AND CHARACTERIZATION OF RECOMBINANT HUMAN
REMARK 1 TITL 2 CYTOCHROME C IN E. COLI
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1562 RESTRAINTS, 1449 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 80
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,33 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1J3S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000005594.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 125
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM CYTOCHROME C; 25MM PHOSPHATE
REMARK 210 BUFFER; 2MM CYTOCHROME C; 25MM
REMARK 210 PHOSPHATE BUFFER; 2MM CYTOCHROME
REMARK 210 C U-15N; 25MM PHOSPHATE BUFFER;
REMARK 210 2MM CYTOCHROME C U-15N; 25MM
REMARK 210 PHOSPHATE BUFFER; 2MM CYTOCHROME
REMARK 210 C U-15N, 13C; 25MM PHOSPHATE
REMARK 210 BUFFER; 2MM CYTOCHROME C U-15N,
REMARK 210 13C; 25MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 3D_15N-SEPARATED_NOESY; HNCBCA,
REMARK 210 CBCA(CO)NH, HBHA(CBCA)NH,
REMARK 210 HBHA(CBCACO)NH, HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.5.9, XWINNMR 2.6
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210 METHOD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
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: 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 1 LYS A 13 -64.25 -120.79
REMARK 500 1 GLU A 21 31.60 -149.15
REMARK 500 1 LYS A 22 -77.04 -97.59
REMARK 500 1 LYS A 27 -73.85 -82.11
REMARK 500 1 ASN A 31 103.02 -53.03
REMARK 500 1 GLN A 42 -48.32 -149.05
REMARK 500 1 TYR A 46 118.50 -160.01
REMARK 500 1 TYR A 48 177.26 -44.26
REMARK 500 1 THR A 49 88.62 -58.56
REMARK 500 1 ALA A 51 -72.51 -52.45
REMARK 500 1 GLU A 61 -74.12 -75.78
REMARK 500 1 ASN A 70 102.46 -171.84
REMARK 500 1 THR A 78 151.55 -42.58
REMARK 500 1 LYS A 87 86.90 -159.29
REMARK 500 1 ASN A 103 29.03 -156.82
REMARK 500 2 VAL A 20 31.80 -83.93
REMARK 500 2 GLU A 21 22.35 -160.49
REMARK 500 2 LYS A 27 -72.63 -150.72
REMARK 500 2 ASN A 31 100.22 -44.22
REMARK 500 2 LEU A 32 41.21 -82.25
REMARK 500 2 THR A 40 -174.84 -65.05
REMARK 500 2 GLN A 42 -56.46 -156.39
REMARK 500 2 SER A 47 92.24 -68.56
REMARK 500 2 TYR A 48 176.90 -46.17
REMARK 500 2 THR A 49 87.45 -59.67
REMARK 500 2 ALA A 50 -31.68 -35.71
REMARK 500 2 TRP A 59 107.28 -42.41
REMARK 500 2 GLU A 61 -75.99 -76.58
REMARK 500 2 ASN A 70 97.27 -170.98
REMARK 500 2 THR A 78 160.70 -49.94
REMARK 500 2 ILE A 81 58.36 -91.04
REMARK 500 2 LYS A 87 96.15 -67.13
REMARK 500 2 ALA A 96 -39.35 -39.98
REMARK 500 2 ASN A 103 45.08 -177.50
REMARK 500 3 LYS A 13 -65.46 -134.14
REMARK 500 3 ASN A 31 99.60 -52.40
REMARK 500 3 LYS A 39 -174.50 -64.68
REMARK 500 3 THR A 40 -169.95 -53.50
REMARK 500 3 GLN A 42 54.30 -161.82
REMARK 500 3 ALA A 43 169.66 -44.34
REMARK 500 3 TYR A 48 176.17 -44.19
REMARK 500 3 THR A 49 86.86 -59.26
REMARK 500 3 ALA A 51 -70.57 -49.26
REMARK 500 3 TRP A 59 103.23 -49.04
REMARK 500 3 ASN A 70 88.52 -176.00
REMARK 500 3 TYR A 74 -72.59 -83.37
REMARK 500 4 LYS A 13 -68.40 -122.44
REMARK 500 4 HIS A 18 74.12 -115.51
REMARK 500 4 LYS A 22 -86.67 -85.23
REMARK 500 4 LYS A 27 -73.15 -91.41
REMARK 500
REMARK 500 THIS ENTRY HAS 321 RAMACHANDRAN OUTLIERS.
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 1 ARG A 38 0.31 SIDE CHAIN
REMARK 500 2 ARG A 38 0.25 SIDE CHAIN
REMARK 500 2 ARG A 91 0.32 SIDE CHAIN
REMARK 500 3 ARG A 91 0.13 SIDE CHAIN
REMARK 500 4 ARG A 38 0.11 SIDE CHAIN
REMARK 500 4 ARG A 91 0.16 SIDE CHAIN
REMARK 500 5 ARG A 38 0.28 SIDE CHAIN
REMARK 500 5 ARG A 91 0.15 SIDE CHAIN
REMARK 500 6 ARG A 38 0.25 SIDE CHAIN
REMARK 500 6 ARG A 91 0.30 SIDE CHAIN
REMARK 500 7 ARG A 38 0.31 SIDE CHAIN
REMARK 500 7 ARG A 91 0.21 SIDE CHAIN
REMARK 500 8 ARG A 38 0.32 SIDE CHAIN
REMARK 500 8 ARG A 91 0.16 SIDE CHAIN
REMARK 500 9 ARG A 38 0.28 SIDE CHAIN
REMARK 500 9 ARG A 91 0.23 SIDE CHAIN
REMARK 500 10 ARG A 38 0.30 SIDE CHAIN
REMARK 500 10 ARG A 91 0.22 SIDE CHAIN
REMARK 500 11 ARG A 38 0.08 SIDE CHAIN
REMARK 500 11 ARG A 91 0.30 SIDE CHAIN
REMARK 500 12 ARG A 38 0.32 SIDE CHAIN
REMARK 500 12 ARG A 91 0.24 SIDE CHAIN
REMARK 500 13 ARG A 38 0.32 SIDE CHAIN
REMARK 500 13 ARG A 91 0.10 SIDE CHAIN
REMARK 500 14 ARG A 38 0.32 SIDE CHAIN
REMARK 500 14 ARG A 91 0.15 SIDE CHAIN
REMARK 500 15 ARG A 38 0.32 SIDE CHAIN
REMARK 500 15 ARG A 91 0.19 SIDE CHAIN
REMARK 500 16 ARG A 38 0.13 SIDE CHAIN
REMARK 500 16 ARG A 91 0.30 SIDE CHAIN
REMARK 500 18 ARG A 38 0.18 SIDE CHAIN
REMARK 500 18 ARG A 91 0.23 SIDE CHAIN
REMARK 500 19 ARG A 38 0.30 SIDE CHAIN
REMARK 500 19 ARG A 91 0.13 SIDE CHAIN
REMARK 500 20 ARG A 38 0.12 SIDE CHAIN
REMARK 500 20 ARG A 91 0.32 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 105 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HEC A 105 NA 90.1
REMARK 620 3 HEC A 105 NB 88.9 90.1
REMARK 620 4 HEC A 105 NC 89.3 179.4 90.0
REMARK 620 5 HEC A 105 ND 90.3 89.7 179.1 90.1
REMARK 620 6 MET A 80 SD 178.1 90.4 89.3 90.2 91.6
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 HEC A 105
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5406 RELATED DB: BMRB
DBREF 1J3S A 1 104 UNP P99999 CYC_HUMAN 1 104
SEQRES 1 A 104 GLY ASP VAL GLU LYS GLY LYS LYS ILE PHE ILE MET LYS
SEQRES 2 A 104 CYS SER 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 TYR SER TYR THR ALA ALA ASN
SEQRES 5 A 104 LYS ASN LYS GLY ILE ILE TRP GLY GLU ASP 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 VAL GLY ILE LYS LYS LYS GLU GLU ARG
SEQRES 8 A 104 ALA ASP LEU ILE ALA TYR LEU LYS LYS ALA THR ASN GLU
HET HEC A 105 75
HETNAM HEC HEME C
FORMUL 2 HEC C34 H34 FE N4 O4
HELIX 1 1 ASP A 2 CYS A 14 1 13
HELIX 2 2 THR A 49 GLY A 56 1 8
HELIX 3 3 GLY A 60 ASN A 70 1 11
HELIX 4 4 ASN A 70 ILE A 75 1 6
HELIX 5 5 LYS A 87 THR A 102 1 16
LINK SG CYS A 14 CAB HEC A 105 1555 1555 1.81
LINK SG CYS A 17 CAC HEC A 105 1555 1555 1.82
LINK NE2 HIS A 18 FE HEC A 105 1555 1555 1.99
LINK SD MET A 80 FE HEC A 105 1555 1555 2.38
SITE 1 AC1 19 CYS A 14 CYS A 17 HIS A 18 THR A 28
SITE 2 AC1 19 PRO A 30 LEU A 35 ARG A 38 THR A 40
SITE 3 AC1 19 TYR A 46 TYR A 48 THR A 49 TRP A 59
SITE 4 AC1 19 TYR A 67 LEU A 68 THR A 78 LYS A 79
SITE 5 AC1 19 MET A 80 PHE A 82 ARG A 91
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
MODEL 1
Complete list - b 23 2 Bytes