Header list of 2bpn.pdb file
Complete list - r 25 2 Bytes
HEADER ELECTRON TRANSPORT 21-APR-05 2BPN
TITLE SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH)
TITLE 2 FERRICYTOCHROME C3, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOCHROME C3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CYTOCHROME C3, RESIDUES 23-129
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 3 ORGANISM_TAXID: 882;
SOURCE 4 STRAIN: HILDENBOROUGH
KEYWDS ELECTRON TRANSPORT, HEMEPROTEIN, CYTOCHROME C3, REDOX
KEYWDS 2 COOPERATIVITY, REDOX-BOHR COOPERATIVITY, TRANSDUCTION,
KEYWDS 3 PARAMAGNETIC
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.C.MESSIAS,A.P.AGUIAR,L.BRENNAN,A.V.XAVIER,D.L.TURNER
REVDAT 3 24-FEB-09 2BPN 1 VERSN
REVDAT 2 22-MAR-06 2BPN 1 JRNL
REVDAT 1 15-MAR-06 2BPN 0
JRNL AUTH A.C.MESSIAS,A.P.AGUIAR,L.BRENNAN,C.A.SALGUEIRO,
JRNL AUTH 2 L.M.SARAIVA,A.V.XAVIER,D.L.TURNER
JRNL TITL SOLUTION STRUCTURES OF TETRAHAEM FERRICYTOCHROME
JRNL TITL 2 C(3) FROM DESULFOVIBRIO VULGARIS (HILDENBOROUGH)
JRNL TITL 3 AND ITS K45Q MUTANT: THE MOLECULAR BASIS OF
JRNL TITL 4 COOPERATIVITY.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1757 143 2006
JRNL REFN ISSN 0006-3002
JRNL PMID 16527248
JRNL DOI 10.1016/J.BBABIO.2006.01.007
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.C.MESSIAS,D.H.W.KASTRAU,H.S.COSTA,J.LEGALL,
REMARK 1 AUTH 2 D.L.TURNER,H.SANTOS,A.V.XAVIER
REMARK 1 TITL SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (
REMARK 1 TITL 2 HILDENBOROUGH) FERROCYTOCHROME C3: STRUCTURAL
REMARK 1 TITL 3 BASIS FOR FUNCTIONAL COOPERATIVITY.
REMARK 1 REF J.MOL.BIOL. V. 281 719 1998
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 9710542
REMARK 1 DOI 10.1006/JMBI.1998.1974
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.SIMOES,P.M.MATIAS,J.MORAIS,K.WILSON,Z.DAUTER,
REMARK 1 AUTH 2 M.A.CARRONDO
REMARK 1 TITL REFINEMENT OF THE THREE-DIMENSIONAL STRUCTURES OF
REMARK 1 TITL 2 CYTOCHROMES C3 FROM DESULFOVIBRIO VULGARIS
REMARK 1 TITL 3 HILDENBOROUGH AT 1.67 A RESOLUTION AND FROM
REMARK 1 TITL 4 DESULFOVIBRIO DESULFURICANS ATCC27774 AT 1.6 A
REMARK 1 TITL 5 RESOLUTION
REMARK 1 REF INORG.CHIM.ACTA. V. 273 213 1998
REMARK 1 REFN ISSN 0020-1693
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PARADYANA
REMARK 3 AUTHORS : D.L.TURNER,L,BRENNAN,S.G.CHAMBERLIN, R.O.LOURO,
REMARK 3 A.V.XAVIER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2BPN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-APR-05.
REMARK 100 THE PDBE ID CODE IS EBI-23675.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.0
REMARK 210 PH : 7.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 92% WATER/8% D2O AND 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-1H-NOESY,
REMARK 210 2D-1H-TOCSY,
REMARK 210 2D-1H-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500
REMARK 210 SPECTROMETER MODEL : DRX-500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PARADYANA
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210 WITH SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 155
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NONE
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 400
REMARK 400 COMPOUND
REMARK 400 PARTICIPATES IN SULFATE RESPIRATION COUPLED WITH
REMARK 400 PHOSPHORYLATION BY TRANSFERRING ELECTRONS FROM
REMARK 400 THE ENZYME DEHYDROGENASE TO FERREDOXIN.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 O MET A 11 - H VAL A 18 1.52
REMARK 500 O HIS A 83 - H ALA A 87 1.47
REMARK 500 O LYS A 93 - H ASP A 96 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 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 99.09 -37.40
REMARK 500 1 PRO A 5 165.71 -49.21
REMARK 500 1 GLU A 12 57.67 -147.39
REMARK 500 1 THR A 14 -156.72 -91.06
REMARK 500 1 HIS A 25 48.32 -144.33
REMARK 500 1 LYS A 40 103.93 178.88
REMARK 500 1 GLU A 41 124.23 -33.37
REMARK 500 1 LYS A 45 136.91 -37.59
REMARK 500 1 THR A 48 167.98 53.74
REMARK 500 1 CYS A 51 -135.37 -107.94
REMARK 500 1 HIS A 52 86.09 -64.94
REMARK 500 1 LYS A 57 79.70 -107.99
REMARK 500 1 LYS A 58 -80.40 163.21
REMARK 500 1 LYS A 60 -137.07 -103.09
REMARK 500 1 SER A 61 167.99 86.48
REMARK 500 1 MET A 69 29.30 -152.47
REMARK 500 1 HIS A 70 -73.27 -155.29
REMARK 500 1 ASN A 73 46.48 -87.61
REMARK 500 1 SER A 78 -148.99 -115.52
REMARK 500 1 LYS A 102 -8.32 86.49
REMARK 500 1 HIS A 106 62.73 -101.58
REMARK 500 2 GLU A 12 58.64 -147.70
REMARK 500 2 THR A 14 -156.67 -93.26
REMARK 500 2 HIS A 25 49.76 -147.30
REMARK 500 2 SER A 27 31.43 -97.35
REMARK 500 2 LYS A 40 103.40 176.46
REMARK 500 2 GLU A 41 129.33 -31.87
REMARK 500 2 LYS A 45 123.95 -39.77
REMARK 500 2 THR A 48 149.73 56.46
REMARK 500 2 CYS A 51 -138.16 -133.27
REMARK 500 2 HIS A 52 87.38 -60.58
REMARK 500 2 LYS A 58 -73.11 170.08
REMARK 500 2 MET A 69 30.00 -153.38
REMARK 500 2 HIS A 70 -75.08 -155.38
REMARK 500 2 ASP A 71 155.93 -44.68
REMARK 500 2 ASN A 73 50.95 -94.18
REMARK 500 2 SER A 78 -154.60 -120.22
REMARK 500 2 ALA A 92 -70.85 -117.27
REMARK 500 2 ASP A 96 -46.37 -136.67
REMARK 500 2 CYS A 100 -75.58 -109.94
REMARK 500 2 LYS A 104 30.74 -91.37
REMARK 500 2 CYS A 105 -62.42 -152.19
REMARK 500 2 HIS A 106 59.03 -99.44
REMARK 500 3 ALA A 4 127.02 -39.60
REMARK 500 3 GLU A 12 55.95 -144.24
REMARK 500 3 THR A 14 -157.27 -97.03
REMARK 500 3 HIS A 25 48.83 -146.17
REMARK 500 3 LYS A 40 102.75 176.69
REMARK 500 3 GLU A 41 123.36 -35.26
REMARK 500 3 THR A 48 150.83 54.87
REMARK 500 3 CYS A 51 -136.58 -125.98
REMARK 500 3 HIS A 52 88.13 -61.71
REMARK 500 3 LYS A 58 -74.82 165.61
REMARK 500 3 MET A 69 30.92 -152.00
REMARK 500 3 HIS A 70 -73.05 -156.95
REMARK 500 3 ASP A 71 151.62 -45.41
REMARK 500 3 ASN A 73 48.77 -86.58
REMARK 500 3 SER A 78 -149.65 -116.39
REMARK 500 3 LYS A 102 7.49 90.62
REMARK 500 4 GLU A 12 59.04 -148.83
REMARK 500 4 THR A 14 -156.91 -101.66
REMARK 500 4 HIS A 25 49.44 -146.71
REMARK 500 4 LYS A 40 102.66 -178.10
REMARK 500 4 GLU A 41 124.94 -34.91
REMARK 500 4 LYS A 45 136.74 -37.63
REMARK 500 4 THR A 48 167.74 54.17
REMARK 500 4 CYS A 51 -137.77 -108.34
REMARK 500 4 HIS A 52 78.13 -63.08
REMARK 500 4 LYS A 58 -74.80 165.48
REMARK 500 4 ASP A 59 128.06 -39.61
REMARK 500 4 MET A 69 29.11 -152.47
REMARK 500 4 HIS A 70 -72.04 -156.06
REMARK 500 4 ASN A 73 47.22 -87.21
REMARK 500 4 SER A 78 -155.09 -115.72
REMARK 500 4 LYS A 102 -1.32 90.32
REMARK 500 4 HIS A 106 64.58 -103.96
REMARK 500 5 LYS A 3 -179.71 -51.02
REMARK 500 5 GLU A 12 55.38 -144.13
REMARK 500 5 THR A 14 -157.53 -103.97
REMARK 500 5 HIS A 25 47.35 -142.50
REMARK 500 5 LYS A 40 103.25 -179.81
REMARK 500 5 GLU A 41 124.08 -34.84
REMARK 500 5 CYS A 51 -133.36 -150.98
REMARK 500 5 HIS A 52 91.50 -69.52
REMARK 500 5 LYS A 58 -74.33 170.23
REMARK 500 5 MET A 69 34.57 -154.46
REMARK 500 5 HIS A 70 -63.58 -156.54
REMARK 500 5 ASP A 71 170.69 -55.70
REMARK 500 5 THR A 74 162.59 -40.91
REMARK 500 5 SER A 78 -149.41 -113.83
REMARK 500 5 ALA A 92 -66.37 -108.50
REMARK 500 5 ASP A 96 -43.71 -132.42
REMARK 500 5 LYS A 102 -3.25 81.03
REMARK 500 5 HIS A 106 64.61 -105.96
REMARK 500 6 LYS A 3 -168.86 -70.38
REMARK 500 6 PRO A 5 161.78 -40.08
REMARK 500 6 GLU A 12 57.62 -146.51
REMARK 500 6 THR A 14 -157.90 -91.99
REMARK 500 6 LYS A 15 30.05 -90.50
REMARK 500 6 HIS A 25 48.84 -147.33
REMARK 500 6 VAL A 37 -76.38 -135.80
REMARK 500 6 LYS A 40 135.37 -176.83
REMARK 500 6 GLU A 41 119.05 -35.74
REMARK 500 6 LYS A 45 130.53 -39.27
REMARK 500 6 THR A 48 150.87 55.17
REMARK 500 6 CYS A 51 -139.21 -133.52
REMARK 500 6 HIS A 52 76.40 -61.30
REMARK 500 6 ASP A 56 -166.43 -121.56
REMARK 500 6 LYS A 58 -41.12 164.39
REMARK 500 6 LYS A 60 48.43 -104.73
REMARK 500 6 MET A 69 26.91 -151.44
REMARK 500 6 HIS A 70 -70.44 -154.60
REMARK 500 6 ASP A 71 152.99 -45.88
REMARK 500 6 ASN A 73 49.34 -97.20
REMARK 500 6 SER A 78 -148.22 -119.97
REMARK 500 6 ALA A 89 28.57 -161.49
REMARK 500 6 ALA A 92 -55.59 -123.63
REMARK 500 6 LYS A 102 -6.64 87.73
REMARK 500 7 LYS A 3 137.17 62.46
REMARK 500 7 THR A 14 -158.86 -110.97
REMARK 500 7 HIS A 25 50.59 -149.52
REMARK 500 7 SER A 27 32.72 -91.21
REMARK 500 7 LYS A 40 103.26 -171.28
REMARK 500 7 GLU A 41 127.59 -33.34
REMARK 500 7 LYS A 45 126.13 -39.58
REMARK 500 7 THR A 48 150.66 55.56
REMARK 500 7 CYS A 51 -140.52 -138.73
REMARK 500 7 HIS A 52 81.40 -60.24
REMARK 500 7 LYS A 57 79.74 -110.23
REMARK 500 7 LYS A 58 -77.66 163.82
REMARK 500 7 ASP A 59 119.78 -39.78
REMARK 500 7 LYS A 60 -141.96 -97.01
REMARK 500 7 SER A 61 173.48 86.83
REMARK 500 7 MET A 69 28.12 -159.12
REMARK 500 7 HIS A 70 -74.57 -147.71
REMARK 500 7 THR A 74 165.03 -44.12
REMARK 500 7 HIS A 106 62.04 -101.50
REMARK 500 8 PRO A 5 163.32 -41.00
REMARK 500 8 GLU A 12 58.90 -148.55
REMARK 500 8 THR A 14 -156.94 -93.02
REMARK 500 8 HIS A 25 47.68 -143.11
REMARK 500 8 LYS A 40 104.35 178.58
REMARK 500 8 GLU A 41 123.85 -33.16
REMARK 500 8 LYS A 45 136.83 -37.17
REMARK 500 8 THR A 48 168.20 54.02
REMARK 500 8 CYS A 51 -138.44 -110.76
REMARK 500 8 HIS A 52 81.32 -62.26
REMARK 500 8 LYS A 58 -76.57 171.44
REMARK 500 8 MET A 69 27.73 -154.15
REMARK 500 8 HIS A 70 -80.41 -153.18
REMARK 500 8 ASP A 71 154.14 -41.94
REMARK 500 8 ASN A 73 41.80 -90.23
REMARK 500 8 SER A 78 -95.57 -115.54
REMARK 500 8 CYS A 79 -47.58 -153.13
REMARK 500 8 ALA A 92 -63.10 -109.29
REMARK 500 8 ASP A 96 -43.60 -134.80
REMARK 500 8 LYS A 102 -6.91 87.42
REMARK 500 8 HIS A 106 65.52 -107.92
REMARK 500 9 PRO A 2 -176.11 -61.07
REMARK 500 9 ALA A 4 102.45 -40.49
REMARK 500 9 PRO A 5 166.92 -45.16
REMARK 500 9 GLU A 12 56.24 -147.14
REMARK 500 9 THR A 14 -158.36 -90.93
REMARK 500 9 LYS A 15 30.89 -90.61
REMARK 500 9 HIS A 25 49.70 -146.69
REMARK 500 9 SER A 27 -44.91 149.66
REMARK 500 9 VAL A 37 -75.80 -133.37
REMARK 500 9 LYS A 40 134.25 -176.86
REMARK 500 9 GLU A 41 117.12 -36.91
REMARK 500 9 LYS A 45 133.45 -39.81
REMARK 500 9 THR A 48 150.05 55.05
REMARK 500 9 CYS A 51 -139.52 -138.44
REMARK 500 9 HIS A 52 75.40 -60.90
REMARK 500 9 ASP A 56 -167.82 -121.95
REMARK 500 9 LYS A 58 -83.24 170.88
REMARK 500 9 SER A 61 -167.65 -67.00
REMARK 500 9 MET A 69 25.41 -152.69
REMARK 500 9 HIS A 70 -61.30 -149.44
REMARK 500 9 ASP A 71 177.65 -51.59
REMARK 500 9 LYS A 72 -46.46 -136.58
REMARK 500 9 THR A 74 164.21 -41.69
REMARK 500 9 ALA A 92 -70.76 -118.60
REMARK 500 9 HIS A 106 61.85 -100.12
REMARK 500 10 LYS A 3 -124.72 -61.87
REMARK 500 10 PRO A 5 162.05 -40.53
REMARK 500 10 THR A 14 -159.58 -104.39
REMARK 500 10 LYS A 15 30.70 -92.84
REMARK 500 10 HIS A 25 50.76 -150.47
REMARK 500 10 SER A 27 37.59 -90.28
REMARK 500 10 LYS A 40 103.50 171.97
REMARK 500 10 GLU A 41 126.95 -29.25
REMARK 500 10 LYS A 45 141.52 -37.64
REMARK 500 10 THR A 48 167.00 54.57
REMARK 500 10 CYS A 51 -139.08 -120.16
REMARK 500 10 HIS A 52 87.40 -61.18
REMARK 500 10 ASP A 56 -168.95 -125.92
REMARK 500 10 LYS A 58 -85.01 164.28
REMARK 500 10 SER A 61 174.03 -57.30
REMARK 500 10 MET A 69 26.18 -151.18
REMARK 500 10 HIS A 70 -80.99 -150.32
REMARK 500 10 ASP A 71 156.81 -43.14
REMARK 500 10 ASN A 73 43.22 -92.13
REMARK 500 10 SER A 78 -114.07 -111.10
REMARK 500 10 CYS A 79 -48.40 -138.04
REMARK 500 10 ALA A 89 19.52 -147.46
REMARK 500 10 LYS A 102 -7.88 87.80
REMARK 500 10 HIS A 106 65.73 -109.82
REMARK 500 11 ALA A 4 98.32 -36.40
REMARK 500 11 THR A 14 -155.55 -112.22
REMARK 500 11 HIS A 25 43.74 -151.48
REMARK 500 11 SER A 27 -47.79 85.51
REMARK 500 11 LYS A 40 104.37 -178.21
REMARK 500 11 GLU A 41 127.53 -32.67
REMARK 500 11 THR A 48 151.07 55.76
REMARK 500 11 CYS A 51 -139.87 -136.15
REMARK 500 11 HIS A 52 81.62 -59.75
REMARK 500 11 ASP A 56 -167.52 -122.35
REMARK 500 11 LYS A 58 -67.67 167.96
REMARK 500 11 MET A 69 30.95 -153.83
REMARK 500 11 HIS A 70 -74.40 -152.68
REMARK 500 11 ALA A 89 22.20 -151.10
REMARK 500 11 LYS A 102 -8.46 87.68
REMARK 500 11 HIS A 106 66.05 -107.58
REMARK 500 12 ALA A 4 88.75 38.85
REMARK 500 12 PRO A 5 162.30 -40.29
REMARK 500 12 GLU A 12 53.79 -143.41
REMARK 500 12 THR A 14 -158.02 -106.30
REMARK 500 12 HIS A 25 46.98 -144.29
REMARK 500 12 LYS A 40 103.50 179.46
REMARK 500 12 GLU A 41 123.47 -35.37
REMARK 500 12 CYS A 51 -131.88 -150.91
REMARK 500 12 LYS A 58 -75.37 163.81
REMARK 500 12 SER A 61 166.52 -43.70
REMARK 500 12 MET A 69 34.54 -150.73
REMARK 500 12 HIS A 70 -66.29 -158.33
REMARK 500 12 THR A 74 163.33 -41.75
REMARK 500 12 ALA A 89 32.72 -151.73
REMARK 500 12 ASP A 96 -43.32 -130.47
REMARK 500 12 HIS A 106 58.04 -94.21
REMARK 500 13 PRO A 5 161.72 -40.30
REMARK 500 13 GLU A 12 58.39 -146.59
REMARK 500 13 THR A 14 -159.68 -112.62
REMARK 500 13 HIS A 25 44.51 -142.68
REMARK 500 13 SER A 27 -45.06 148.34
REMARK 500 13 VAL A 37 -77.04 -127.57
REMARK 500 13 LYS A 40 131.89 -172.22
REMARK 500 13 GLU A 41 120.92 -36.37
REMARK 500 13 LYS A 45 137.18 -37.77
REMARK 500 13 THR A 48 167.30 54.16
REMARK 500 13 CYS A 51 -139.28 -110.88
REMARK 500 13 HIS A 52 76.18 -60.99
REMARK 500 13 LYS A 58 -67.41 164.94
REMARK 500 13 MET A 69 23.26 -150.30
REMARK 500 13 HIS A 70 -55.63 -151.16
REMARK 500 13 ASP A 71 -176.35 -52.58
REMARK 500 13 LYS A 72 -47.22 -147.12
REMARK 500 13 THR A 74 164.36 -42.05
REMARK 500 13 ASP A 96 -43.50 -137.94
REMARK 500 13 LYS A 102 -8.22 87.89
REMARK 500 13 HIS A 106 64.96 -103.73
REMARK 500 14 ALA A 4 76.90 -117.98
REMARK 500 14 PRO A 5 163.77 -41.44
REMARK 500 14 THR A 14 -160.04 -106.51
REMARK 500 14 HIS A 25 49.70 -145.98
REMARK 500 14 SER A 27 36.56 -98.14
REMARK 500 14 LYS A 40 104.37 170.51
REMARK 500 14 GLU A 41 126.51 -30.60
REMARK 500 14 LYS A 45 142.43 -37.42
REMARK 500 14 THR A 48 167.42 54.76
REMARK 500 14 CYS A 51 -140.00 -120.48
REMARK 500 14 HIS A 52 82.52 -61.05
REMARK 500 14 ASP A 56 -169.78 -120.26
REMARK 500 14 LYS A 58 -58.17 170.45
REMARK 500 14 SER A 61 -178.75 -59.97
REMARK 500 14 MET A 69 26.85 -151.05
REMARK 500 14 HIS A 70 -76.22 -153.76
REMARK 500 14 ASP A 71 152.93 -45.47
REMARK 500 14 ASN A 73 43.01 -90.21
REMARK 500 14 SER A 78 -124.71 -113.46
REMARK 500 14 ASP A 96 -43.81 -135.35
REMARK 500 14 LYS A 102 -8.52 87.49
REMARK 500 14 HIS A 106 68.69 -112.93
REMARK 500 15 PRO A 2 88.56 -48.33
REMARK 500 15 LYS A 3 44.26 -106.46
REMARK 500 15 ALA A 4 90.15 39.02
REMARK 500 15 PRO A 5 162.14 -40.14
REMARK 500 15 GLU A 12 54.50 -142.38
REMARK 500 15 THR A 14 -158.18 -93.82
REMARK 500 15 LYS A 15 31.87 -90.89
REMARK 500 15 HIS A 25 48.19 -147.06
REMARK 500 15 LYS A 40 103.79 178.29
REMARK 500 15 GLU A 41 126.28 -31.50
REMARK 500 15 THR A 48 150.47 55.44
REMARK 500 15 CYS A 51 -138.06 -136.57
REMARK 500 15 HIS A 52 88.01 -60.91
REMARK 500 15 LYS A 58 -74.26 165.84
REMARK 500 15 MET A 69 24.37 -148.35
REMARK 500 15 HIS A 70 -79.91 -151.11
REMARK 500 15 ASP A 71 151.71 -41.11
REMARK 500 15 ASN A 73 47.04 -87.34
REMARK 500 15 SER A 78 -121.89 -113.74
REMARK 500 15 LYS A 102 -0.83 78.79
REMARK 500 15 HIS A 106 61.81 -101.28
REMARK 500 16 PRO A 2 -161.86 -78.87
REMARK 500 16 LYS A 3 -60.14 -96.18
REMARK 500 16 THR A 14 -157.05 -113.92
REMARK 500 16 LYS A 15 32.43 -92.93
REMARK 500 16 HIS A 25 48.92 -146.24
REMARK 500 16 LYS A 40 103.59 -176.63
REMARK 500 16 GLU A 41 129.10 -32.02
REMARK 500 16 LYS A 45 123.27 -39.63
REMARK 500 16 THR A 48 150.67 55.88
REMARK 500 16 CYS A 51 -138.79 -135.98
REMARK 500 16 HIS A 52 89.46 -60.01
REMARK 500 16 LYS A 58 -83.95 163.14
REMARK 500 16 LYS A 60 -141.86 -105.24
REMARK 500 16 SER A 61 164.80 85.44
REMARK 500 16 MET A 69 30.74 -149.94
REMARK 500 16 HIS A 70 -82.11 -151.39
REMARK 500 16 ASP A 71 150.81 -49.84
REMARK 500 16 SER A 78 -95.00 -116.78
REMARK 500 16 CYS A 79 -47.69 -153.10
REMARK 500 16 LYS A 102 -5.79 84.51
REMARK 500 16 HIS A 106 67.75 -112.61
REMARK 500 17 LYS A 3 153.27 87.78
REMARK 500 17 PRO A 5 162.21 -40.53
REMARK 500 17 THR A 14 -156.59 -112.58
REMARK 500 17 LYS A 15 30.29 -91.00
REMARK 500 17 HIS A 25 50.66 -149.30
REMARK 500 17 LYS A 40 102.91 -179.90
REMARK 500 17 GLU A 41 123.99 -34.83
REMARK 500 17 LYS A 45 136.79 -37.77
REMARK 500 17 THR A 48 167.44 54.03
REMARK 500 17 CYS A 51 -137.66 -114.49
REMARK 500 17 HIS A 52 79.24 -63.22
REMARK 500 17 ASP A 56 -166.46 -128.96
REMARK 500 17 LYS A 58 -81.81 166.02
REMARK 500 17 SER A 61 -164.31 -56.17
REMARK 500 17 MET A 69 31.31 -159.29
REMARK 500 17 HIS A 70 -77.26 -157.00
REMARK 500 17 ASN A 73 44.24 -88.94
REMARK 500 17 SER A 78 -148.90 -115.19
REMARK 500 17 ALA A 89 30.80 -160.03
REMARK 500 17 ALA A 92 -52.02 -126.10
REMARK 500 17 LYS A 102 -2.84 81.14
REMARK 500 17 CYS A 105 -72.91 -81.57
REMARK 500 17 HIS A 106 56.51 -90.76
REMARK 500 18 THR A 14 -160.34 -112.97
REMARK 500 18 SER A 27 -44.04 149.67
REMARK 500 18 LYS A 40 103.61 -176.53
REMARK 500 18 GLU A 41 126.75 -31.99
REMARK 500 18 LYS A 45 140.62 -37.23
REMARK 500 18 THR A 48 167.77 53.97
REMARK 500 18 CYS A 51 -139.60 -120.07
REMARK 500 18 HIS A 52 74.16 -62.20
REMARK 500 18 LYS A 58 -84.55 171.99
REMARK 500 18 MET A 69 25.81 -151.88
REMARK 500 18 HIS A 70 -72.02 -152.18
REMARK 500 18 ASP A 71 155.30 -40.22
REMARK 500 18 SER A 78 -95.39 -117.45
REMARK 500 18 CYS A 79 -47.59 -152.28
REMARK 500 18 ASP A 96 -43.83 -134.15
REMARK 500 18 LYS A 102 -4.91 89.38
REMARK 500 18 HIS A 106 62.21 -102.44
REMARK 500 19 LYS A 3 158.23 75.34
REMARK 500 19 PRO A 5 178.64 -53.28
REMARK 500 19 GLU A 12 54.66 -140.71
REMARK 500 19 THR A 14 -159.75 -104.82
REMARK 500 19 HIS A 25 50.02 -147.16
REMARK 500 19 VAL A 37 -74.79 -136.49
REMARK 500 19 LYS A 40 105.97 -176.81
REMARK 500 19 GLU A 41 115.82 -20.46
REMARK 500 19 LYS A 45 140.58 -37.54
REMARK 500 19 THR A 48 167.78 54.32
REMARK 500 19 CYS A 51 -139.02 -114.18
REMARK 500 19 HIS A 52 77.87 -61.80
REMARK 500 19 ASP A 56 -169.86 -122.75
REMARK 500 19 LYS A 58 -61.73 168.46
REMARK 500 19 MET A 69 29.59 -155.68
REMARK 500 19 HIS A 70 -76.55 -153.61
REMARK 500 19 ASP A 71 153.90 -45.94
REMARK 500 19 ASN A 73 44.79 -88.51
REMARK 500 19 SER A 78 -149.12 -114.64
REMARK 500 19 LYS A 102 -7.61 86.34
REMARK 500 19 HIS A 106 65.37 -107.46
REMARK 500 20 ALA A 4 101.59 -38.42
REMARK 500 20 PRO A 5 162.24 -43.83
REMARK 500 20 GLU A 12 56.83 -146.21
REMARK 500 20 THR A 14 -156.93 -91.69
REMARK 500 20 HIS A 25 51.27 -151.17
REMARK 500 20 SER A 27 40.46 -93.77
REMARK 500 20 LYS A 40 102.92 171.62
REMARK 500 20 GLU A 41 127.35 -28.72
REMARK 500 20 LYS A 45 141.20 -37.64
REMARK 500 20 THR A 48 166.90 54.33
REMARK 500 20 CYS A 51 -139.83 -121.02
REMARK 500 20 HIS A 52 75.38 -61.59
REMARK 500 20 LYS A 58 -36.59 164.28
REMARK 500 20 LYS A 60 -119.91 -68.89
REMARK 500 20 SER A 61 173.65 84.85
REMARK 500 20 MET A 69 26.42 -151.96
REMARK 500 20 HIS A 70 -80.92 -151.99
REMARK 500 20 ASP A 71 152.72 -40.72
REMARK 500 20 ASN A 73 45.61 -88.01
REMARK 500 20 SER A 78 -95.46 -111.88
REMARK 500 20 CYS A 79 -47.23 -153.69
REMARK 500 20 ALA A 89 49.96 -80.76
REMARK 500 20 ASP A 96 -44.40 -135.32
REMARK 500 20 LYS A 102 -1.11 85.13
REMARK 500 20 HIS A 106 67.14 -112.05
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 108 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 22 NE2
REMARK 620 2 HIS A 34 NE2 176.3
REMARK 620 3 HEC A 108 NA 88.1 91.9
REMARK 620 4 HEC A 108 ND 87.8 88.5 88.0
REMARK 620 5 HEC A 108 NB 90.6 93.1 90.7 178.0
REMARK 620 6 HEC A 108 NC 87.2 92.5 174.1 88.2 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC A 109 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC A 109 NC
REMARK 620 2 HIS A 52 NE2 92.4
REMARK 620 3 HEC A 109 NA 174.2 90.4
REMARK 620 4 HEC A 109 NB 93.8 95.0 91.0
REMARK 620 5 HEC A 109 ND 88.3 86.3 86.8 177.5
REMARK 620 6 HIS A 35 NE2 88.9 173.2 87.7 91.6 87.0
REMARK 620 N 1 2 3 4 5
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 25 NE2
REMARK 620 2 HEC A 110 NA 86.4
REMARK 620 3 HEC A 110 ND 89.9 85.7
REMARK 620 4 HIS A 83 NE2 172.5 86.1 88.9
REMARK 620 5 HEC A 110 NB 88.9 86.9 172.6 91.4
REMARK 620 6 HEC A 110 NC 92.9 178.2 92.7 94.6 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 111 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC A 111 ND
REMARK 620 2 HIS A 106 NE2 91.2
REMARK 620 3 HEC A 111 NA 87.7 91.8
REMARK 620 4 HEC A 111 NC 90.0 92.8 174.9
REMARK 620 5 HIS A 70 NE2 86.7 177.8 87.7 87.7
REMARK 620 6 HEC A 111 NB 175.7 91.8 89.3 92.8 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 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC A 111
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A2I RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (
REMARK 900 HILDENBOROUGH) FERROCYTOCHROME C3, NMR, 20
REMARK 900 STRUCTURES
REMARK 900 RELATED ID: 1GX7 RELATED DB: PDB
REMARK 900 BEST MODEL OF THE ELECTRON TRANSFER COMPLEX
REMARK 900 BETWEEN CYTOCHROME C3 AND [FE]-HYDROGENASE
REMARK 900 RELATED ID: 1MDV RELATED DB: PDB
REMARK 900 KEY ROLE OF PHENYLALANINE 20 IN CYTOCHROME
REMARK 900 C3: STRUCTURE, STABILITY AND FUNCTION STUDIES
REMARK 900 RELATED ID: 2CTH RELATED DB: PDB
REMARK 900 CYTOCHROME C3 FROM DESULFOVIBRIO VULGARIS
REMARK 900 HILDENBOROUGH
REMARK 900 RELATED ID: 2CYM RELATED DB: PDB
REMARK 900 CYTOCHROME C=3=
DBREF 2BPN A 1 107 UNP P00131 CYC3_DESVH 23 129
SEQRES 1 A 107 ALA PRO LYS ALA PRO ALA ASP GLY LEU LYS MET GLU ALA
SEQRES 2 A 107 THR LYS GLN PRO VAL VAL PHE ASN HIS SER THR HIS LYS
SEQRES 3 A 107 SER VAL LYS CYS GLY ASP CYS HIS HIS PRO VAL ASN GLY
SEQRES 4 A 107 LYS GLU ASP TYR ARG LYS CYS GLY THR ALA GLY CYS HIS
SEQRES 5 A 107 ASP SER MET ASP LYS LYS ASP LYS SER ALA LYS GLY TYR
SEQRES 6 A 107 TYR HIS VAL MET HIS ASP LYS ASN THR LYS PHE LYS SER
SEQRES 7 A 107 CYS VAL GLY CYS HIS VAL GLU VAL ALA GLY ALA ASP ALA
SEQRES 8 A 107 ALA LYS LYS LYS ASP LEU THR GLY CYS LYS LYS SER LYS
SEQRES 9 A 107 CYS HIS GLU
HET HEC A 108 75
HET HEC A 109 75
HET HEC A 110 75
HET HEC A 111 75
HETNAM HEC HEME C
HETSYN HEC 3,7,12,17-TETRAMETHYL-8,13-DIVINYL-2,18-
HETSYN 2 HEC PORPHINEDIPROPIONIC ACID
FORMUL 2 HEC 4(C34 H34 FE N4 O4)
HELIX 1 1 ASN A 21 LYS A 26 5 6
HELIX 2 2 LYS A 29 HIS A 34 1 6
HELIX 3 3 CYS A 79 GLU A 85 1 7
HELIX 4 4 ALA A 92 ASP A 96 5 5
SHEET 1 AA 2 LYS A 10 MET A 11 0
SHEET 2 AA 2 VAL A 18 VAL A 19 -1 O VAL A 18 N MET A 11
LINK NE2 HIS A 22 FE HEC A 108 1555 1555 2.00
LINK NE2 HIS A 25 FE HEC A 110 1555 1555 2.00
LINK SG CYS A 30 CAB HEC A 108 1555 1555 1.83
LINK SG CYS A 33 CAC HEC A 108 1555 1555 1.81
LINK NE2 HIS A 34 FE HEC A 108 1555 1555 1.89
LINK NE2 HIS A 35 FE HEC A 109 1555 1555 2.00
LINK SG CYS A 46 CAB HEC A 109 1555 1555 1.81
LINK SG CYS A 51 CAC HEC A 109 1555 1555 1.81
LINK NE2 HIS A 52 FE HEC A 109 1555 1555 1.91
LINK NE2 HIS A 70 FE HEC A 111 1555 1555 2.00
LINK SG CYS A 79 CAB HEC A 110 1555 1555 1.84
LINK SG CYS A 82 CAC HEC A 110 1555 1555 1.81
LINK NE2 HIS A 83 FE HEC A 110 1555 1555 1.94
LINK SG CYS A 100 CAB HEC A 111 1555 1555 1.91
LINK SG CYS A 105 CAC HEC A 111 1555 1555 1.81
LINK NE2 HIS A 106 FE HEC A 111 1555 1555 1.88
SITE 1 AC1 9 PRO A 5 LEU A 9 MET A 11 PHE A 20
SITE 2 AC1 9 HIS A 22 CYS A 30 CYS A 33 HIS A 34
SITE 3 AC1 9 TYR A 43
SITE 1 AC2 14 CYS A 33 HIS A 35 VAL A 37 ASP A 42
SITE 2 AC2 14 LYS A 45 CYS A 46 CYS A 51 HIS A 52
SITE 3 AC2 14 ALA A 62 HIS A 67 VAL A 68 THR A 74
SITE 4 AC2 14 LYS A 75 PHE A 76
SITE 1 AC3 9 VAL A 18 THR A 24 HIS A 25 ASP A 32
SITE 2 AC3 9 SER A 78 CYS A 79 CYS A 82 HIS A 83
SITE 3 AC3 9 LYS A 104
SITE 1 AC4 18 GLU A 12 ALA A 13 THR A 14 GLN A 16
SITE 2 AC4 18 VAL A 18 MET A 55 TYR A 65 TYR A 66
SITE 3 AC4 18 HIS A 70 CYS A 79 VAL A 80 HIS A 83
SITE 4 AC4 18 LEU A 97 THR A 98 GLY A 99 CYS A 100
SITE 5 AC4 18 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 - r 25 2 Bytes