Header list of 1it1.pdb file
Complete list - b 23 2 Bytes
HEADER ELECTRON TRANSPORT 29-DEC-01 1IT1
TITLE SOLUTION STRUCTURES OF FERROCYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS
TITLE 2 MIYAZAKI F
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C3;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS STR. 'MIYAZAKI F';
SOURCE 3 ORGANISM_TAXID: 883;
SOURCE 4 STRAIN: MIYAZAKI F
KEYWDS ELECTRON TRANSFER, TETRAHEME PROTEIN, ELECTRON TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.HARADA,Y.FUKUOKA,T.OHMURA,A.FUKUNISHI,G.KAWAI,T.FUJIWARA,H.AKUTSU
REVDAT 4 23-FEB-22 1IT1 1 REMARK LINK
REVDAT 3 24-FEB-09 1IT1 1 VERSN
REVDAT 2 07-JAN-03 1IT1 1 REMARK
REVDAT 1 10-JUL-02 1IT1 0
JRNL AUTH E.HARADA,Y.FUKUOKA,T.OHMURA,A.FUKUNISHI,G.KAWAI,T.FUJIWARA,
JRNL AUTH 2 H.AKUTSU
JRNL TITL REDOX-COUPLED CONFORMATIONAL ALTERNATIONS IN CYTOCHROME C(3)
JRNL TITL 2 FROM D. VULGARIS MIYAZAKI F ON THE BASIS OF ITS REDUCED
JRNL TITL 3 SOLUTION STRUCTURE.
JRNL REF J.MOL.BIOL. V. 319 767 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 12054869
JRNL DOI 10.1016/S0022-2836(02)00367-4
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8.5.1, X-PLOR 3.8.5.1
REMARK 3 AUTHORS : BRUNGER, A.T. (X-PLOR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IT1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000005250.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 56MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : U-15N CYTOCHROME C3 IN THE FULLY
REMARK 210 REDUCED STATE; 30MM SODIUM
REMARK 210 PHOSPHATE BUFFER; CYTOCHROME C3
REMARK 210 IN THE FULLY REDUCED STATE; 30MM
REMARK 210 SODIUM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 2D
REMARK 210 NOESY; DQF-COSY; E-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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: 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 SG CYS A 30 HAB HEC A 201 1.03
REMARK 500 SG CYS A 79 HAB HEC A 203 1.04
REMARK 500 SG CYS A 105 HAC HEC A 204 1.07
REMARK 500 SG CYS A 51 HAC HEC A 202 1.08
REMARK 500 SG CYS A 100 HAB HEC A 204 1.30
REMARK 500 SG CYS A 46 HAB HEC A 202 1.32
REMARK 500 O ASP A 71 HG SER A 78 1.40
REMARK 500 O LEU A 9 H PHE A 20 1.42
REMARK 500 O LYS A 29 H ASP A 32 1.43
REMARK 500 HD1 HIS A 83 O LEU A 97 1.44
REMARK 500 H MET A 11 O VAL A 18 1.44
REMARK 500 O VAL A 37 H LYS A 40 1.45
REMARK 500 O HIS A 25 H VAL A 28 1.50
REMARK 500 O LYS A 72 H THR A 74 1.55
REMARK 500 O HIS A 22 H HIS A 25 1.58
REMARK 500 O THR A 48 H GLY A 50 1.58
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 1 ALA A 4 137.55 -39.86
REMARK 500 1 HIS A 34 46.00 -88.20
REMARK 500 1 HIS A 35 163.83 -35.01
REMARK 500 1 ASN A 38 21.76 47.79
REMARK 500 1 ALA A 47 48.69 -89.64
REMARK 500 1 THR A 48 168.66 -45.36
REMARK 500 1 ALA A 49 63.83 -65.72
REMARK 500 1 CYS A 51 -80.67 -120.98
REMARK 500 1 LYS A 57 24.02 44.49
REMARK 500 1 ASP A 59 103.50 -51.06
REMARK 500 1 LYS A 60 31.61 -87.15
REMARK 500 1 SER A 61 -160.11 -110.96
REMARK 500 1 HIS A 67 -80.28 -39.17
REMARK 500 1 LYS A 75 -32.04 -38.86
REMARK 500 1 ALA A 89 57.28 39.70
REMARK 500 1 ALA A 91 -28.35 -38.06
REMARK 500 1 SER A 103 -148.82 -127.57
REMARK 500 2 ALA A 6 173.96 -58.42
REMARK 500 2 HIS A 34 38.88 -88.34
REMARK 500 2 HIS A 35 157.79 -31.36
REMARK 500 2 PRO A 36 99.10 -64.74
REMARK 500 2 ASN A 38 -85.59 58.39
REMARK 500 2 ALA A 47 52.97 -106.51
REMARK 500 2 THR A 48 -165.83 -51.43
REMARK 500 2 CYS A 51 -132.09 -104.04
REMARK 500 2 MET A 55 20.50 -79.47
REMARK 500 2 LYS A 57 23.36 45.53
REMARK 500 2 SER A 61 -156.49 -80.51
REMARK 500 2 HIS A 67 -72.37 -86.31
REMARK 500 2 ALA A 68 -19.37 -49.11
REMARK 500 2 LYS A 72 -167.18 -102.75
REMARK 500 2 LYS A 75 -34.47 -38.84
REMARK 500 2 ALA A 89 48.06 -95.09
REMARK 500 2 ALA A 91 -26.55 -38.87
REMARK 500 2 SER A 103 -149.51 -124.34
REMARK 500 3 ALA A 6 -179.56 -58.65
REMARK 500 3 HIS A 34 37.67 -90.26
REMARK 500 3 HIS A 35 165.18 -33.39
REMARK 500 3 ASN A 38 -84.47 174.89
REMARK 500 3 ALA A 47 52.22 -108.76
REMARK 500 3 THR A 48 -168.43 -50.22
REMARK 500 3 CYS A 51 -132.34 -106.03
REMARK 500 3 HIS A 52 49.51 -79.14
REMARK 500 3 LYS A 57 17.40 54.07
REMARK 500 3 SER A 61 -156.56 -103.93
REMARK 500 3 HIS A 67 -79.77 -39.35
REMARK 500 3 LYS A 75 -33.96 -38.87
REMARK 500 3 ALA A 89 49.28 -92.85
REMARK 500 3 ALA A 91 -27.14 -38.81
REMARK 500 3 SER A 103 -152.31 -82.15
REMARK 500
REMARK 500 THIS ENTRY HAS 306 RAMACHANDRAN OUTLIERS.
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 201 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 22 NE2
REMARK 620 2 HEC A 201 NA 89.8
REMARK 620 3 HEC A 201 NB 90.0 89.9
REMARK 620 4 HEC A 201 NC 89.4 179.1 89.7
REMARK 620 5 HEC A 201 ND 89.3 89.3 178.9 91.1
REMARK 620 6 HIS A 34 NE2 178.8 91.2 90.6 89.6 90.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 203 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 25 NE2
REMARK 620 2 HEC A 203 NA 88.5
REMARK 620 3 HEC A 203 NB 87.9 89.7
REMARK 620 4 HEC A 203 NC 88.6 177.1 89.8
REMARK 620 5 HEC A 203 ND 86.7 90.4 174.6 89.8
REMARK 620 6 HIS A 83 NE2 177.4 89.3 90.8 93.6 94.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 202 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 35 NE2
REMARK 620 2 HEC A 202 NA 91.5
REMARK 620 3 HEC A 202 NB 92.2 89.6
REMARK 620 4 HEC A 202 NC 89.8 178.7 90.5
REMARK 620 5 HEC A 202 ND 87.1 89.0 178.5 90.9
REMARK 620 6 HIS A 52 NE2 176.7 89.4 91.1 89.3 89.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 204 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 70 NE2
REMARK 620 2 HEC A 204 NA 90.6
REMARK 620 3 HEC A 204 NB 87.2 90.8
REMARK 620 4 HEC A 204 NC 90.3 178.8 89.9
REMARK 620 5 HEC A 204 ND 89.9 89.7 177.1 89.6
REMARK 620 6 HIS A 106 NE2 177.1 92.2 92.1 86.9 90.7
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 204
DBREF 1IT1 A 1 107 UNP P00132 CYC3_DESVM 24 130
SEQRES 1 A 107 ALA PRO LYS ALA PRO ALA ASP GLY LEU LYS MET ASP LYS
SEQRES 2 A 107 THR LYS GLN PRO VAL VAL PHE ASN HIS SER THR HIS LYS
SEQRES 3 A 107 ALA VAL LYS CYS GLY ASP CYS HIS HIS PRO VAL ASN GLY
SEQRES 4 A 107 LYS GLU ASP TYR GLN LYS CYS ALA THR ALA GLY CYS HIS
SEQRES 5 A 107 ASP ASN MET ASP LYS LYS ASP LYS SER ALA LYS GLY TYR
SEQRES 6 A 107 TYR HIS ALA MET HIS ASP LYS GLY THR LYS PHE LYS SER
SEQRES 7 A 107 CYS VAL GLY CYS HIS LEU GLU THR ALA GLY ALA ASP ALA
SEQRES 8 A 107 ALA LYS LYS LYS GLU LEU THR GLY CYS LYS GLY SER LYS
SEQRES 9 A 107 CYS HIS SER
HET HEC A 201 75
HET HEC A 202 75
HET HEC A 203 75
HET HEC A 204 75
HETNAM HEC HEME C
FORMUL 2 HEC 4(C34 H34 FE N4 O4)
HELIX 1 1 ASN A 21 HIS A 25 5 5
HELIX 2 2 LYS A 29 HIS A 34 1 6
HELIX 3 3 GLY A 64 ASP A 71 1 8
HELIX 4 4 SER A 78 ALA A 87 1 10
HELIX 5 5 ASP A 90 LEU A 97 1 8
SHEET 1 A 2 LEU A 9 MET A 11 0
SHEET 2 A 2 VAL A 18 PHE A 20 -1 O VAL A 18 N MET A 11
SHEET 1 B 2 PRO A 36 VAL A 37 0
SHEET 2 B 2 LYS A 40 GLU A 41 -1 O LYS A 40 N VAL A 37
LINK SG CYS A 30 CAB HEC A 201 1555 1555 1.81
LINK SG CYS A 33 CAC HEC A 201 1555 1555 1.81
LINK SG CYS A 46 CAB HEC A 202 1555 1555 1.81
LINK SG CYS A 51 CAC HEC A 202 1555 1555 1.81
LINK SG CYS A 79 CAB HEC A 203 1555 1555 1.81
LINK SG CYS A 82 CAC HEC A 203 1555 1555 1.81
LINK SG CYS A 100 CAB HEC A 204 1555 1555 1.81
LINK SG CYS A 105 CAC HEC A 204 1555 1555 1.81
LINK NE2 HIS A 22 FE HEC A 201 1555 1555 2.20
LINK NE2 HIS A 25 FE HEC A 203 1555 1555 2.23
LINK NE2 HIS A 34 FE HEC A 201 1555 1555 2.18
LINK NE2 HIS A 35 FE HEC A 202 1555 1555 2.19
LINK NE2 HIS A 52 FE HEC A 202 1555 1555 2.21
LINK NE2 HIS A 70 FE HEC A 204 1555 1555 2.19
LINK NE2 HIS A 83 FE HEC A 203 1555 1555 2.27
LINK NE2 HIS A 106 FE HEC A 204 1555 1555 2.16
SITE 1 AC1 19 PRO A 2 ALA A 4 PRO A 5 LEU A 9
SITE 2 AC1 19 LYS A 10 MET A 11 PHE A 20 HIS A 22
SITE 3 AC1 19 HIS A 25 VAL A 28 CYS A 30 CYS A 33
SITE 4 AC1 19 HIS A 34 TYR A 43 GLN A 44 LYS A 45
SITE 5 AC1 19 CYS A 46 HEC A 202 HEC A 203
SITE 1 AC2 18 CYS A 33 HIS A 34 HIS A 35 ASP A 42
SITE 2 AC2 18 GLN A 44 LYS A 45 CYS A 46 THR A 48
SITE 3 AC2 18 CYS A 51 HIS A 52 SER A 61 ALA A 62
SITE 4 AC2 18 HIS A 67 ALA A 68 THR A 74 LYS A 75
SITE 5 AC2 18 SER A 78 HEC A 201
SITE 1 AC3 16 VAL A 18 PHE A 20 THR A 24 HIS A 25
SITE 2 AC3 16 VAL A 28 CYS A 33 LYS A 77 SER A 78
SITE 3 AC3 16 CYS A 79 CYS A 82 HIS A 83 THR A 86
SITE 4 AC3 16 GLU A 96 LYS A 104 CYS A 105 HEC A 201
SITE 1 AC4 22 MET A 11 ASP A 12 LYS A 13 THR A 14
SITE 2 AC4 22 LYS A 15 GLN A 16 PRO A 17 VAL A 18
SITE 3 AC4 22 LYS A 57 TYR A 65 TYR A 66 MET A 69
SITE 4 AC4 22 HIS A 70 CYS A 79 VAL A 80 HIS A 83
SITE 5 AC4 22 LEU A 97 THR A 98 GLY A 99 CYS A 100
SITE 6 AC4 22 CYS A 105 HIS 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
MODEL 1
Complete list - b 23 2 Bytes