HEADER OXIDOREDUCTASE 28-MAR-02 1GX7
TITLE BEST MODEL OF THE ELECTRON TRANSFER COMPLEX BETWEEN
TITLE 2 CYTOCHROME C3 AND [FE]-HYDROGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC [FE] HYDROGENASE LARGE SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.18.99.1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PERIPLASMIC [FE] HYDROGENASE SMALL SUBUNIT;
COMPND 7 CHAIN: D;
COMPND 8 EC: 1.18.99.1;
COMPND 9 MOL_ID: 3;
COMPND 10 MOLECULE: CYTOCHROME C3;
COMPND 11 CHAIN: E
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 3 ORGANISM_TAXID: 882;
SOURCE 4 STRAIN: HILDENBOROUGH;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 7 ORGANISM_TAXID: 882;
SOURCE 8 STRAIN: HILDENBOROUGH;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS;
SOURCE 11 ORGANISM_TAXID: 882;
SOURCE 12 STRAIN: HILDENBOROUGH
KEYWDS OXIDOREDUCTASE, ELECTRON TRANSFER COMPLEX, HYDROGENASE,
KEYWDS 2 MULTIHEME CYTOCHROME, NMR, SOFT DOCKING, OXIDOREDUCTASE
KEYWDS 3 ELECTRON TRANSPORT, 4FE-4S, IRON-SULFUR,
EXPDTA SOLUTION NMR; THEORETICAL MODEL
MDLTYP MINIMIZED AVERAGE
AUTHOR L.ELANTAK,X.MORELLI,O.BORNET,C.HATCHIKIAN,M.CZJZEK,A.DOLLA,
AUTHOR 2 F.GUERLESQUIN
REVDAT 2 24-FEB-09 1GX7 1 VERSN
REVDAT 1 31-JUL-03 1GX7 0
JRNL AUTH L.ELANTAK,X.MORELLI,O.BORNET,C.HATCHIKIAN,M.CZJZEK,
JRNL AUTH 2 A.DOLLA,F.GUERLESQUIN
JRNL TITL THE CYTOCHROME C(3)-[FE]-HYDROGENASE
JRNL TITL 2 ELECTRON-TRANSFER COMPLEX: STRUCTURAL MODEL BY NMR
JRNL TITL 3 RESTRAINED DOCKING
JRNL REF FEBS LETT. V. 548 1 2003
JRNL REFN ISSN 0014-5793
JRNL PMID 12885397
JRNL DOI 10.1016/S0014-5793(03)00718-X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A MOLECULAR DYNAMICS CALCULATION
REMARK 3 (AMBER FORCE FIELD) WITH SHAKE RESTRAINTS FOR THE HETEROATOMS
REMARK 3 WAS PERFORMED HEAT-BATH TEMPERATURE: 280 K INITIAL VELOCITIES
REMARK 3 FROM A MAXWELL-BOLTZMAN DISTRIBUTION AT 280K. SHAKE RESTRAINTS
REMARK 3 WITH A TOLERANCE OF 0.0004. THIS IS A MODEL COMPLEX OBTAINED
REMARK 3 BY NMR-RESTRAINED SOFT DOCKING AND MINIMIZATION.
REMARK 4
REMARK 4 1GX7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-APR-02.
REMARK 100 THE PDBE ID CODE IS EBI-9632.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 10 MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500; 500
REMARK 210 SPECTROMETER MODEL : DRX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : NULL
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE COMPLEX MODEL WAS DETERMINED WITH
REMARK 210 NMR-RESTRAINED (HSQC) SOFT DOCKING, THEN MINIMIZED BY
REMARK 210 MOLECULAR DYNAMICS
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 220
REMARK 220 EXPERIMENTAL DETAILS
REMARK 220 EXPERIMENT TYPE: THEORETICAL MODELLING
REMARK 220 MODELLING PROGRAM: BIGGER; X-PLOR3.851
REMARK 220 PROGRAM AUTHORS: NUNO PALMA, AXEL BRUENGER
REMARK 220 MODELLING EXPERIMENT: THE SOFT DOCKING WITH BIGGER WAS
REMARK 220 RESTRAINED BY NMR DATA
REMARK 225
REMARK 225 THEORETICAL MODEL
REMARK 225 THE COORDINATES IN THIS ENTRY REPRESENT A MODEL STRUCTURE.
REMARK 225 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT CRYST1 AND
REMARK 225 SCALE RECORDS BE INCLUDED, BUT THE VALUES ON THESE
REMARK 225 RECORDS ARE MEANINGLESS.
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 GLN A 71 - HD1 HIS A 75 1.58
REMARK 500 O PRO A 173 - HD1 HIS A 196 1.59
REMARK 500 O PHE A 197 - HE1 TRP D 92 1.58
REMARK 500 HZ3 LYS A 238 - HG1 THR A 259 1.53
REMARK 500 O LEU D 76 - HD1 HIS D 82 1.58
REMARK 500 O PRO E 5 - HD1 HIS E 22 1.59
REMARK 500 HD1 HIS E 52 - O ALA E 62 1.54
REMARK 500 H LYS E 102 - OXT GLU E 107 1.59
REMARK 500 S1 PDT A 4 - C CMO A 10 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 CYS A 35 CA - CB - SG ANGL. DEV. = -7.2 DEGREES
REMARK 500 TYR A 311 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 SER A 321 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 CYS A 360 CA - CB - SG ANGL. DEV. = -7.4 DEGREES
REMARK 500 CYS A 382 CA - CB - SG ANGL. DEV. = -12.1 DEGREES
REMARK 500 ALA A 397 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 GLU D 123 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 CYS E 46 CA - CB - SG ANGL. DEV. = -8.9 DEGREES
REMARK 500 GLU E 107 N - CA - C ANGL. DEV. = -18.3 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 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 33 -40.26 -168.98
REMARK 500 ASP A 39 -1.43 82.09
REMARK 500 PRO A 57 -97.02 -72.14
REMARK 500 ALA A 65 -50.88 -123.26
REMARK 500 ILE A 67 31.11 -79.08
REMARK 500 GLN A 71 -65.77 68.20
REMARK 500 ASN A 79 69.33 60.43
REMARK 500 GLN A 85 41.64 -151.16
REMARK 500 MET A 105 75.47 -119.29
REMARK 500 PHE A 139 49.94 -89.06
REMARK 500 HIS A 141 60.61 -158.94
REMARK 500 THR A 145 5.56 -68.46
REMARK 500 PHE A 197 78.95 -101.83
REMARK 500 SER A 198 97.04 -34.73
REMARK 500 SER A 202 124.35 -29.99
REMARK 500 THR A 213 -79.67 -119.72
REMARK 500 PRO A 244 39.70 -73.02
REMARK 500 LEU A 246 58.09 -95.52
REMARK 500 SER A 284 28.32 -67.63
REMARK 500 SER A 289 48.31 -89.11
REMARK 500 ALA A 293 -46.51 -159.19
REMARK 500 THR A 294 35.75 -82.24
REMARK 500 ILE A 295 48.23 -163.07
REMARK 500 TYR A 311 42.96 -88.15
REMARK 500 GLU A 312 -68.64 -148.54
REMARK 500 ALA A 313 48.45 -104.19
REMARK 500 SER A 321 47.92 -57.28
REMARK 500 ALA A 326 -54.40 -144.01
REMARK 500 VAL A 327 56.79 -93.54
REMARK 500 ALA A 377 73.09 -156.61
REMARK 500 VAL A 394 -52.46 -132.73
REMARK 500 ILE D 39 -70.15 -26.47
REMARK 500 TYR D 75 -56.01 -156.90
REMARK 500 GLU D 77 -48.09 77.73
REMARK 500 HIS D 82 -131.24 69.18
REMARK 500 THR D 90 -169.27 -160.23
REMARK 500 TYR D 122 -44.37 -132.97
REMARK 500 GLU E 12 51.50 -158.31
REMARK 500 LYS E 15 39.90 -95.29
REMARK 500 SER E 23 -80.82 -25.78
REMARK 500 LYS E 29 -5.81 65.86
REMARK 500 ASP E 32 39.21 -141.56
REMARK 500 CYS E 33 -47.16 -168.67
REMARK 500 ASP E 53 -47.01 -152.96
REMARK 500 ASP E 59 53.73 71.07
REMARK 500 ALA E 62 -55.75 57.50
REMARK 500 THR E 74 -145.26 -127.78
REMARK 500 PHE E 76 -165.10 -109.86
REMARK 500 ALA E 89 -150.85 -178.36
REMARK 500 ASP E 90 70.24 82.86
REMARK 500 ALA E 91 -71.74 13.56
REMARK 500 CYS E 100 -33.95 113.93
REMARK 500 CYS E 105 -27.20 176.85
REMARK 500 HIS E 106 -77.60 -126.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 36 GLY A 37 149.74
REMARK 500 GLY A 37 CYS A 38 -92.50
REMARK 500 ASN A 68 CYS A 69 -149.76
REMARK 500 GLN A 71 CYS A 72 -142.21
REMARK 500 PHE A 147 THR A 148 -145.44
REMARK 500 THR A 199 CYS A 200 148.54
REMARK 500 MET A 232 PRO A 233 -129.28
REMARK 500 LYS A 247 SER A 248 -143.09
REMARK 500 ARG A 252 ASP A 253 -147.63
REMARK 500 LEU A 330 ASP A 331 147.39
REMARK 500 TYR A 370 HIS A 371 -133.49
REMARK 500 CYS A 384 GLY A 385 -147.21
REMARK 500 GLN A 388 PRO A 389 -137.36
REMARK 500 GLU A 396 ALA A 397 139.37
REMARK 500 PRO D 119 TYR D 120 119.41
REMARK 500 THR E 14 LYS E 15 -141.74
REMARK 500 CYS E 33 HIS E 34 144.19
REMARK 500 ASP E 42 TYR E 43 147.20
REMARK 500 ALA E 62 LYS E 63 -147.62
REMARK 500 LYS E 72 ASN E 73 145.65
REMARK 500 HIS E 106 GLU E 107 -145.78
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 82 0.09 SIDE CHAIN
REMARK 500 ARG A 111 0.08 SIDE CHAIN
REMARK 500 TYR A 112 0.10 SIDE CHAIN
REMARK 500 TYR A 185 0.10 SIDE CHAIN
REMARK 500 TYR A 227 0.14 SIDE CHAIN
REMARK 500 TYR A 370 0.16 SIDE CHAIN
REMARK 500 TYR D 42 0.06 SIDE CHAIN
REMARK 500 TYR D 120 0.09 SIDE CHAIN
REMARK 500 TYR D 122 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 FE2 A 5 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT A 4 S1
REMARK 620 2 CYN A 7 C 78.8
REMARK 620 3 CMO A 10 C 67.4 115.7
REMARK 620 4 MET A 232 SD 164.8 86.2 121.8
REMARK 620 5 PDT A 4 S2 33.6 84.8 93.5 143.9
REMARK 620 6 CMO A 9 C 83.0 44.1 148.4 85.1 64.4
REMARK 620 7 CYN A 8 C 70.5 145.9 65.5 123.5 61.4 115.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A 6 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT A 4 S1
REMARK 620 2 CMO A 10 C 55.4
REMARK 620 3 MET A 232 SD 143.5 89.1
REMARK 620 4 PDT A 4 S2 32.1 76.0 140.8
REMARK 620 5 CYN A 8 C 57.7 41.1 90.7 54.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 1 FE2
REMARK 620 2 CYS A 76 SG 137.6
REMARK 620 3 SF4 A 1 S3 56.2 109.0
REMARK 620 4 SF4 A 1 FE3 61.6 144.8 105.7
REMARK 620 5 SF4 A 1 FE4 59.0 151.1 56.2 59.3
REMARK 620 6 SF4 A 1 S2 105.2 117.2 107.7 55.7 56.4
REMARK 620 7 SF4 A 1 S4 56.2 106.0 109.2 55.4 102.5 107.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 41 SG
REMARK 620 2 SF4 A 1 FE1 148.6
REMARK 620 3 SF4 A 1 S3 113.7 56.2
REMARK 620 4 SF4 A 1 FE3 141.9 59.9 104.3
REMARK 620 5 SF4 A 1 FE4 143.8 60.4 56.7 59.1
REMARK 620 6 SF4 A 1 S1 106.6 104.8 110.0 54.8 56.8
REMARK 620 7 SF4 A 1 S4 112.1 56.3 109.2 54.8 103.6 104.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 1 FE2
REMARK 620 2 SF4 A 1 FE1 58.5
REMARK 620 3 CYS A 38 SG 145.9 145.0
REMARK 620 4 SF4 A 1 FE4 58.1 59.5 145.7
REMARK 620 5 SF4 A 1 S1 55.2 103.9 111.1 56.5
REMARK 620 6 SF4 A 1 S2 102.8 55.7 111.3 56.5 109.5
REMARK 620 7 SF4 A 1 S4 55.1 55.8 111.3 103.0 105.5 108.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 1 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 1 FE2
REMARK 620 2 CYS A 35 SG 143.3
REMARK 620 3 SF4 A 1 FE1 60.6 143.1
REMARK 620 4 SF4 A 1 S3 56.8 107.6 56.3
REMARK 620 5 SF4 A 1 FE3 62.8 144.9 61.2 107.4
REMARK 620 6 SF4 A 1 S1 56.9 111.8 105.1 110.3 56.2
REMARK 620 7 SF4 A 1 S2 106.5 110.1 56.4 107.8 56.4 109.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 72 SG
REMARK 620 2 SF4 A 2 FE3 146.2
REMARK 620 3 SF4 A 2 FE4 137.0 63.4
REMARK 620 4 SF4 A 2 S2 107.3 56.8 56.7
REMARK 620 5 SF4 A 2 FE2 149.2 58.6 60.3 103.2
REMARK 620 6 SF4 A 2 S3 108.3 105.3 56.4 110.6 55.4
REMARK 620 7 SF4 A 2 S4 115.4 56.9 107.5 110.3 55.6 104.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 2 FE1
REMARK 620 2 SF4 A 2 FE3 58.4
REMARK 620 3 SF4 A 2 FE4 58.3 62.5
REMARK 620 4 CYS A 45 SG 152.7 142.2 139.4
REMARK 620 5 SF4 A 2 S1 101.8 57.0 55.8 105.4
REMARK 620 6 SF4 A 2 S3 55.3 105.1 55.6 112.5 108.2
REMARK 620 7 SF4 A 2 S4 55.4 56.8 105.6 114.9 111.1 104.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 66 SG
REMARK 620 2 SF4 A 2 FE1 141.0
REMARK 620 3 SF4 A 2 FE4 148.3 58.8
REMARK 620 4 SF4 A 2 S2 109.3 57.4 55.1
REMARK 620 5 SF4 A 2 FE2 143.6 62.9 60.2 107.1
REMARK 620 6 SF4 A 2 S1 113.5 105.4 55.0 103.6 57.2
REMARK 620 7 SF4 A 2 S4 107.5 57.2 104.1 111.2 57.3 111.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 2 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 69 SG
REMARK 620 2 SF4 A 2 FE1 142.7
REMARK 620 3 SF4 A 2 FE3 150.6 57.8
REMARK 620 4 SF4 A 2 S2 112.7 56.9 54.7
REMARK 620 5 SF4 A 2 FE2 143.1 61.4 57.2 104.2
REMARK 620 6 SF4 A 2 S1 112.9 104.4 55.0 103.2 56.0
REMARK 620 7 SF4 A 2 S3 108.3 56.7 101.1 111.0 55.9 108.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 3 FE2
REMARK 620 2 SF4 A 3 FE3 60.0
REMARK 620 3 SF4 A 3 S4 56.2 55.6
REMARK 620 4 CYS A 234 SG 142.0 141.7 105.6
REMARK 620 5 SF4 A 3 FE4 59.9 61.5 105.3 149.2
REMARK 620 6 SF4 A 3 S2 104.5 55.6 107.2 113.1 57.6
REMARK 620 7 SF4 A 3 S3 56.1 106.5 107.4 111.3 57.6 111.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 179 SG
REMARK 620 2 SF4 A 3 FE3 142.7
REMARK 620 3 SF4 A 3 S1 116.3 56.0
REMARK 620 4 SF4 A 3 S4 104.1 56.0 108.3
REMARK 620 5 SF4 A 3 FE1 139.1 60.6 104.3 56.6
REMARK 620 6 SF4 A 3 FE4 150.9 61.3 57.4 104.6 58.7
REMARK 620 7 SF4 A 3 S3 109.1 107.2 110.5 108.0 56.4 57.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 382 SG
REMARK 620 2 SF4 A 3 FE2 147.0
REMARK 620 3 SF4 A 3 S1 108.7 56.4
REMARK 620 4 SF4 A 3 S4 115.1 56.2 108.9
REMARK 620 5 SF4 A 3 FE1 147.2 59.5 103.7 56.2
REMARK 620 6 SF4 A 3 FE4 142.5 58.4 56.3 102.4 57.4
REMARK 620 7 SF4 A 3 S2 108.3 104.5 107.4 108.2 56.2 56.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A 3 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SF4 A 3 FE2
REMARK 620 2 SF4 A 3 FE3 60.3
REMARK 620 3 SF4 A 3 S1 56.9 55.5
REMARK 620 4 CYS A 378 SG 144.3 142.6 108.4
REMARK 620 5 SF4 A 3 FE1 61.4 61.1 106.1 145.5
REMARK 620 6 SF4 A 3 S2 105.5 55.4 106.0 109.9 57.4
REMARK 620 7 SF4 A 3 S3 56.6 105.9 109.5 111.5 57.2 111.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC E 109 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC E 109 NA
REMARK 620 2 HIS E 106 NE2 88.2
REMARK 620 3 HEC E 109 NB 90.5 87.5
REMARK 620 4 HEC E 109 NC 179.6 92.2 89.5
REMARK 620 5 HIS E 70 NE2 89.6 177.7 93.2 90.1
REMARK 620 6 HEC E 109 ND 89.7 91.7 179.1 90.3 87.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC E 110 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 52 NE2
REMARK 620 2 HEC E 110 NA 88.1
REMARK 620 3 HEC E 110 ND 89.5 90.3
REMARK 620 4 HIS E 35 NE2 176.9 89.5 88.6
REMARK 620 5 HEC E 110 NB 90.5 89.9 179.8 91.4
REMARK 620 6 HEC E 110 NC 92.7 179.2 89.9 89.7 89.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC E 111 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HEC E 111 NC
REMARK 620 2 HIS E 34 NE2 87.6
REMARK 620 3 HEC E 111 ND 90.7 88.0
REMARK 620 4 HIS E 22 NE2 90.5 176.6 89.1
REMARK 620 5 HEC E 111 NB 89.8 91.9 179.6 90.9
REMARK 620 6 HEC E 111 NA 176.0 88.4 89.6 93.5 90.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC E 112 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 83 NE2
REMARK 620 2 HEC E 112 NC 90.9
REMARK 620 3 HEC E 112 NA 91.9 177.2
REMARK 620 4 HEC E 112 NB 92.2 90.0 90.0
REMARK 620 5 HIS E 25 NE2 175.3 93.0 84.2 90.4
REMARK 620 6 HEC E 112 ND 87.0 89.8 90.3 179.2 90.4
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 FE2 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN A 8
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDT A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 9
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 110
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 111
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 112
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HFE RELATED DB: PDB
REMARK 900 1.6 A RESOLUTION STRUCTURE OF THE FE-
REMARK 900 ONLY HYDROGENASE FROM DESULFOVIBRIO
REMARK 900 DESULFURICANS
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: 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 C3
DBREF 1GX7 A 27 397 UNP P07598 PHFL_DESVH 27 397
DBREF 1GX7 D 36 123 UNP P07603 PHFS_DESVH 36 123
DBREF 1GX7 E 1 107 UNP P00131 CYC3_DESVH 23 129
SEQRES 1 A 371 PHE VAL GLN ILE ASP GLU ALA LYS CYS ILE GLY CYS ASP
SEQRES 2 A 371 THR CYS SER GLN TYR CYS PRO THR ALA ALA ILE PHE GLY
SEQRES 3 A 371 GLU MET GLY GLU PRO HIS SER ILE PRO HIS ILE GLU ALA
SEQRES 4 A 371 CYS ILE ASN CYS GLY GLN CYS LEU THR HIS CYS PRO GLU
SEQRES 5 A 371 ASN ALA ILE TYR GLU ALA GLN SER TRP VAL PRO GLU VAL
SEQRES 6 A 371 GLU LYS LYS LEU LYS ASP GLY LYS VAL LYS CYS ILE ALA
SEQRES 7 A 371 MET PRO ALA PRO ALA VAL ARG TYR ALA LEU GLY ASP ALA
SEQRES 8 A 371 PHE GLY MET PRO VAL GLY SER VAL THR THR GLY LYS MET
SEQRES 9 A 371 LEU ALA ALA LEU GLN LYS LEU GLY PHE ALA HIS CYS TRP
SEQRES 10 A 371 ASP THR GLU PHE THR ALA ASP VAL THR ILE TRP GLU GLU
SEQRES 11 A 371 GLY SER GLU PHE VAL GLU ARG LEU THR LYS LYS SER ASP
SEQRES 12 A 371 MET PRO LEU PRO GLN PHE THR SER CYS CYS PRO GLY TRP
SEQRES 13 A 371 GLN LYS TYR ALA GLU THR TYR TYR PRO GLU LEU LEU PRO
SEQRES 14 A 371 HIS PHE SER THR CYS LYS SER PRO ILE GLY MET ASN GLY
SEQRES 15 A 371 ALA LEU ALA LYS THR TYR GLY ALA GLU ARG MET LYS TYR
SEQRES 16 A 371 ASP PRO LYS GLN VAL TYR THR VAL SER ILE MET PRO CYS
SEQRES 17 A 371 ILE ALA LYS LYS TYR GLU GLY LEU ARG PRO GLU LEU LYS
SEQRES 18 A 371 SER SER GLY MET ARG ASP ILE ASP ALA THR LEU THR THR
SEQRES 19 A 371 ARG GLU LEU ALA TYR MET ILE LYS LYS ALA GLY ILE ASP
SEQRES 20 A 371 PHE ALA LYS LEU PRO ASP GLY LYS ARG ASP SER LEU MET
SEQRES 21 A 371 GLY GLU SER THR GLY GLY ALA THR ILE PHE GLY VAL THR
SEQRES 22 A 371 GLY GLY VAL MET GLU ALA ALA LEU ARG PHE ALA TYR GLU
SEQRES 23 A 371 ALA VAL THR GLY LYS LYS PRO ASP SER TRP ASP PHE LYS
SEQRES 24 A 371 ALA VAL ARG GLY LEU ASP GLY ILE LYS GLU ALA THR VAL
SEQRES 25 A 371 ASN VAL GLY GLY THR ASP VAL LYS VAL ALA VAL VAL HIS
SEQRES 26 A 371 GLY ALA LYS ARG PHE LYS GLN VAL CYS ASP ASP VAL LYS
SEQRES 27 A 371 ALA GLY LYS SER PRO TYR HIS PHE ILE GLU TYR MET ALA
SEQRES 28 A 371 CYS PRO GLY GLY CYS VAL CYS GLY GLY GLY GLN PRO VAL
SEQRES 29 A 371 MET PRO GLY VAL LEU GLU ALA
SEQRES 1 D 88 VAL LYS GLN ILE LYS ASP TYR MET LEU ASP ARG ILE ASN
SEQRES 2 D 88 GLY VAL TYR GLY ALA ASP ALA LYS PHE PRO VAL ARG ALA
SEQRES 3 D 88 SER GLN ASP ASN THR GLN VAL LYS ALA LEU TYR LYS SER
SEQRES 4 D 88 TYR LEU GLU LYS PRO LEU GLY HIS LYS SER HIS ASP LEU
SEQRES 5 D 88 LEU HIS THR HIS TRP PHE ASP LYS SER LYS GLY VAL LYS
SEQRES 6 D 88 GLU LEU THR THR ALA GLY LYS LEU PRO ASN PRO ARG ALA
SEQRES 7 D 88 SER GLU PHE GLU GLY PRO TYR PRO TYR GLU
SEQRES 1 E 107 ALA PRO LYS ALA PRO ALA ASP GLY LEU LYS MET GLU ALA
SEQRES 2 E 107 THR LYS GLN PRO VAL VAL PHE ASN HIS SER THR HIS LYS
SEQRES 3 E 107 SER VAL LYS CYS GLY ASP CYS HIS HIS PRO VAL ASN GLY
SEQRES 4 E 107 LYS GLU ASP TYR ARG LYS CYS GLY THR ALA GLY CYS HIS
SEQRES 5 E 107 ASP SER MET ASP LYS LYS ASP LYS SER ALA LYS GLY TYR
SEQRES 6 E 107 TYR HIS VAL MET HIS ASP LYS ASN THR LYS PHE LYS SER
SEQRES 7 E 107 CYS VAL GLY CYS HIS VAL GLU VAL ALA GLY ALA ASP ALA
SEQRES 8 E 107 ALA LYS LYS LYS ASP LEU THR GLY CYS LYS LYS SER LYS
SEQRES 9 E 107 CYS HIS GLU
HET FE2 A 5 1
HET FE2 A 6 1
HET CYN A 7 2
HET CYN A 8 2
HET SF4 A 1 8
HET SF4 A 2 8
HET SF4 A 3 8
HET PDT A 4 5
HET CMO A 9 2
HET CMO A 10 2
HET HEC E 109 47
HET HEC E 110 47
HET HEC E 111 47
HET HEC E 112 47
HETNAM FE2 FE (II) ION
HETNAM CYN CYANIDE ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM PDT 1,3-PROPANEDITHIOL
HETNAM CMO CARBON MONOXIDE
HETNAM HEC HEME C
HETSYN HEC 3,7,12,17-TETRAMETHYL-8,13-DIVINYL-2,18-
HETSYN 2 HEC PORPHINEDIPROPIONIC ACID
FORMUL 4 FE2 2(FE 2+)
FORMUL 6 CYN 2(C N 1-)
FORMUL 8 SF4 3(FE4 S4 2+)
FORMUL 11 PDT C3 H8 S2
FORMUL 12 CMO 2(C O)
FORMUL 14 HEC 4(C34 H34 FE N4 O4)
HELIX 1 1 THR A 40 CYS A 45 5 6
HELIX 2 2 TRP A 87 ASP A 97 1 11
HELIX 3 3 ALA A 107 GLY A 115 1 9
HELIX 4 4 ASP A 116 GLY A 119 5 4
HELIX 5 5 THR A 126 LEU A 137 1 12
HELIX 6 6 ASP A 144 THR A 165 1 22
HELIX 7 7 CYS A 179 TYR A 190 1 12
HELIX 8 8 PRO A 191 PHE A 197 5 7
HELIX 9 9 SER A 202 LYS A 212 1 11
HELIX 10 10 THR A 213 MET A 219 1 7
HELIX 11 11 ASP A 222 LYS A 224 5 3
HELIX 12 12 ILE A 235 LEU A 242 1 8
HELIX 13 13 THR A 259 ALA A 270 1 12
HELIX 14 14 ASP A 273 LEU A 277 5 5
HELIX 15 15 GLY A 300 TYR A 311 1 12
HELIX 16 16 GLY A 352 LYS A 354 5 3
HELIX 17 17 ARG A 355 ALA A 365 1 11
HELIX 18 18 GLY A 381 GLY A 385 5 5
HELIX 19 19 GLN D 38 ALA D 55 1 18
HELIX 20 20 ASN D 65 SER D 74 1 10
HELIX 21 21 LYS D 83 LEU D 88 1 6
HELIX 22 22 LYS D 97 LEU D 102 1 6
HELIX 23 23 ARG D 112 PHE D 116 5 5
HELIX 24 24 GLY E 64 ASP E 71 1 8
HELIX 25 25 SER E 78 GLY E 88 1 11
HELIX 26 26 ALA E 91 GLY E 99 1 9
SHEET 1 AA 2 VAL A 28 ILE A 30 0
SHEET 2 AA 2 ILE A 81 GLU A 83 -1 O TYR A 82 N GLN A 29
SHEET 1 AB 3 LYS A 101 MET A 105 0
SHEET 2 AB 3 VAL A 226 ILE A 231 1 O TYR A 227 N ILE A 103
SHEET 3 AB 3 ALA A 256 LEU A 258 1 O ALA A 256 N SER A 230
SHEET 1 AC 4 GLN A 174 PHE A 175 0
SHEET 2 AC 4 PHE A 372 TYR A 375 1 N ILE A 373 O GLN A 174
SHEET 3 AC 4 ASP A 344 VAL A 350 1 O ALA A 348 N GLU A 374
SHEET 4 AC 4 ILE A 333 ASN A 339 -1 O LYS A 334 N VAL A 349
SHEET 1 EA 2 LEU E 9 MET E 11 0
SHEET 2 EA 2 VAL E 18 PHE E 20 -1 O VAL E 18 N MET E 11
LINK FE1 SF4 A 1 SG CYS A 76 1555 1555 2.22
LINK FE2 SF4 A 1 SG CYS A 41 1555 1555 2.21
LINK FE3 SF4 A 1 SG CYS A 38 1555 1555 2.25
LINK FE4 SF4 A 1 SG CYS A 35 1555 1555 2.21
LINK FE1 SF4 A 2 SG CYS A 72 1555 1555 2.19
LINK FE2 SF4 A 2 SG CYS A 45 1555 1555 2.24
LINK FE3 SF4 A 2 SG CYS A 66 1555 1555 2.22
LINK FE4 SF4 A 2 SG CYS A 69 1555 1555 2.19
LINK FE1 SF4 A 3 SG CYS A 234 1555 1555 2.26
LINK FE2 SF4 A 3 SG CYS A 179 1555 1555 2.27
LINK FE3 SF4 A 3 SG CYS A 382 1555 1555 2.27
LINK FE4 SF4 A 3 SG CYS A 378 1555 1555 2.22
LINK FE FE2 A 5 C CYN A 8 1555 1555 1.41
LINK FE FE2 A 5 S1 PDT A 4 1555 1555 2.29
LINK FE FE2 A 5 C CYN A 7 1555 1555 2.16
LINK FE FE2 A 5 C CMO A 10 1555 1555 1.42
LINK FE FE2 A 5 SD MET A 232 1555 1555 1.78
LINK FE FE2 A 5 S2 PDT A 4 1555 1555 2.41
LINK FE FE2 A 5 C CMO A 9 1555 1555 2.16
LINK FE FE2 A 6 C CMO A 9 1555 1555 1.37
LINK FE FE2 A 6 C CYN A 8 1555 1555 2.16
LINK FE FE2 A 6 S1 PDT A 4 1555 1555 2.47
LINK FE FE2 A 6 C CMO A 10 1555 1555 2.19
LINK FE FE2 A 6 SD MET A 232 1555 1555 1.78
LINK FE FE2 A 6 S2 PDT A 4 1555 1555 2.45
LINK FE FE2 A 6 C CYN A 7 1555 1555 1.40
LINK C CYN A 7 C CMO A 9 1555 1555 1.62
LINK C CYN A 8 C CMO A 10 1555 1555 1.53
LINK SG CYS E 30 CAB HEC E 111 1555 1555 1.82
LINK SG CYS E 33 CAC HEC E 111 1555 1555 1.83
LINK SG CYS E 46 CAB HEC E 110 1555 1555 1.82
LINK SG CYS E 51 CAC HEC E 110 1555 1555 1.83
LINK SG CYS E 79 CAB HEC E 112 1555 1555 1.82
LINK SG CYS E 82 CAC HEC E 112 1555 1555 1.83
LINK SG CYS E 100 CAB HEC E 109 1555 1555 1.83
LINK SG CYS E 105 CAC HEC E 109 1555 1555 1.82
LINK FE HEC E 109 NE2 HIS E 70 1555 1555 2.21
LINK FE HEC E 109 NE2 HIS E 106 1555 1555 2.28
LINK FE HEC E 110 NE2 HIS E 35 1555 1555 2.17
LINK FE HEC E 110 NE2 HIS E 52 1555 1555 2.17
LINK FE HEC E 111 NE2 HIS E 22 1555 1555 2.24
LINK FE HEC E 111 NE2 HIS E 34 1555 1555 2.21
LINK FE HEC E 112 NE2 HIS E 25 1555 1555 2.20
LINK FE HEC E 112 NE2 HIS E 83 1555 1555 2.20
CISPEP 1 LEU A 172 PRO A 173 0 1.72
CISPEP 2 LEU D 108 PRO D 109 0 5.83
SITE 1 AC1 7 PDT A 4 FE2 A 6 CYN A 7 CYN A 8
SITE 2 AC1 7 CMO A 9 CMO A 10 MET A 232
SITE 1 AC2 7 PDT A 4 FE2 A 5 CYN A 7 CYN A 8
SITE 2 AC2 7 CMO A 9 CMO A 10 MET A 232
SITE 1 AC3 9 PDT A 4 FE2 A 5 FE2 A 6 CYN A 8
SITE 2 AC3 9 CMO A 9 CMO A 10 PRO A 203 ILE A 204
SITE 3 AC3 9 MET A 232
SITE 1 AC4 10 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 AC4 10 CMO A 9 CMO A 10 ALA A 107 PRO A 108
SITE 3 AC4 10 ALA A 109 MET A 232
SITE 1 AC5 12 LYS A 34 CYS A 35 ILE A 36 CYS A 38
SITE 2 AC5 12 ASP A 39 CYS A 41 SER A 42 HIS A 58
SITE 3 AC5 12 HIS A 75 CYS A 76 ILE A 81 HEC E 109
SITE 1 AC6 9 TYR A 44 CYS A 45 ILE A 50 ALA A 65
SITE 2 AC6 9 CYS A 66 ILE A 67 CYS A 69 GLY A 70
SITE 3 AC6 9 CYS A 72
SITE 1 AC7 10 CYS A 69 CYS A 179 PRO A 180 CYS A 234
SITE 2 AC7 10 MET A 376 ALA A 377 CYS A 378 CYS A 382
SITE 3 AC7 10 GLY A 385 GLY A 386
SITE 1 AC8 11 FE2 A 5 FE2 A 6 CYN A 7 CYN A 8
SITE 2 AC8 11 CMO A 9 CMO A 10 PRO A 203 PHE A 296
SITE 3 AC8 11 GLY A 297 MET A 376 CYS A 382
SITE 1 AC9 9 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 AC9 9 CYN A 8 CMO A 10 MET A 232 PRO A 233
SITE 3 AC9 9 LYS A 237
SITE 1 BC1 9 PDT A 4 FE2 A 5 FE2 A 6 CYN A 7
SITE 2 BC1 9 CYN A 8 CMO A 9 PRO A 108 THR A 145
SITE 3 BC1 9 MET A 232
SITE 1 BC2 19 SF4 A 1 ILE A 36 CYS A 38 MET A 54
SITE 2 BC2 19 MET E 11 GLU E 12 ALA E 13 THR E 14
SITE 3 BC2 19 LYS E 15 GLN E 16 VAL E 18 TYR E 65
SITE 4 BC2 19 HIS E 70 CYS E 79 VAL E 80 LEU E 97
SITE 5 BC2 19 CYS E 100 CYS E 105 HIS E 106
SITE 1 BC3 17 HIS E 34 HIS E 35 PRO E 36 VAL E 37
SITE 2 BC3 17 ASN E 38 ASP E 42 CYS E 46 THR E 48
SITE 3 BC3 17 CYS E 51 HIS E 52 SER E 61 ALA E 62
SITE 4 BC3 17 HIS E 67 VAL E 68 THR E 74 LYS E 75
SITE 5 BC3 17 PHE E 76
SITE 1 BC4 15 PRO E 2 LYS E 3 ALA E 4 PHE E 20
SITE 2 BC4 15 HIS E 22 HIS E 25 LYS E 26 CYS E 30
SITE 3 BC4 15 CYS E 33 HIS E 34 ARG E 44 LYS E 45
SITE 4 BC4 15 CYS E 46 GLY E 47 HEC E 112
SITE 1 BC5 14 VAL E 19 PHE E 20 ASN E 21 SER E 23
SITE 2 BC5 14 THR E 24 HIS E 25 CYS E 33 MET E 69
SITE 3 BC5 14 CYS E 79 CYS E 82 HIS E 83 LYS E 104
SITE 4 BC5 14 CYS E 105 HEC E 111
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
(ATOM LINES ARE NOT SHOWN.)
END
