HEADER OXIDOREDUCTASE 12-APR-09 3H1I
TITLE STIGMATELLIN AND ANTIMYCIN BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN I,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A, N;
COMPND 5 SYNONYM: CYTOCHROME BC1 COMPLEX, COMPLEX III;
COMPND 6 EC: 1.10.2.2;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CORE PROTEIN 2,
COMPND 9 MITOCHONDRIAL;
COMPND 10 CHAIN: B, O;
COMPND 11 SYNONYM: COMPLEX III SUBUNIT II;
COMPND 12 EC: 1.10.2.2;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CYTOCHROME B;
COMPND 15 CHAIN: C, P;
COMPND 16 SYNONYM: UBIQUINOL-CYTOCHROME-C REDUCTASE COMPLEX CYTOCHROME B
COMPND 17 SUBUNIT, CYTOCHROME B-C1 COMPLEX SUBUNIT 3, COMPLEX III SUBUNIT 3,
COMPND 18 COMPLEX III SUBUNIT III;
COMPND 19 EC: 1.10.2.2;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL;
COMPND 22 CHAIN: D, Q;
COMPND 23 SYNONYM: CYTOCHROME C-1;
COMPND 24 EC: 1.10.2.2;
COMPND 25 MOL_ID: 5;
COMPND 26 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL;
COMPND 27 CHAIN: E, R;
COMPND 28 FRAGMENT: SEQUENCE DATABASE RESIDUES 77-272;
COMPND 29 SYNONYM: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, RIESKE
COMPND 30 IRON-SULFUR PROTEIN, RISP, COMPLEX III SUBUNIT 5;
COMPND 31 EC: 1.10.2.2;
COMPND 32 MOL_ID: 6;
COMPND 33 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KDA PROTEIN;
COMPND 34 CHAIN: F, S;
COMPND 35 SYNONYM: COMPLEX III SUBUNIT VI;
COMPND 36 EC: 1.10.2.2;
COMPND 37 MOL_ID: 7;
COMPND 38 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING
COMPND 39 PROTEIN QP-C;
COMPND 40 CHAIN: G, T;
COMPND 41 SYNONYM: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 9.5 KDA PROTEIN,
COMPND 42 COMPLEX III SUBUNIT VII;
COMPND 43 EC: 1.10.2.2;
COMPND 44 MOL_ID: 8;
COMPND 45 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN;
COMPND 46 CHAIN: H, U;
COMPND 47 SYNONYM: MITOCHONDRIAL HINGE PROTEIN, CYTOCHROME C1, NONHEME 11 KDA
COMPND 48 PROTEIN, COMPLEX III SUBUNIT VIII;
COMPND 49 EC: 1.10.2.2;
COMPND 50 MOL_ID: 9;
COMPND 51 MOLECULE: CYTOCHROME B-C1 COMPLEX SUBUNIT RIESKE, MITOCHONDRIAL;
COMPND 52 CHAIN: I, V;
COMPND 53 FRAGMENT: SEQUENCE DATABASE RESIDUES 1-76;
COMPND 54 SYNONYM: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, RIESKE
COMPND 55 IRON-SULFUR PROTEIN, RISP, COMPLEX III SUBUNIT 5;
COMPND 56 EC: 1.10.2.2;
COMPND 57 MOL_ID: 10;
COMPND 58 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.2 KDA PROTEIN;
COMPND 59 CHAIN: J, W;
COMPND 60 SYNONYM: CYTOCHROME C1, NONHEME 7 KDA PROTEIN, COMPLEX III SUBUNIT X;
COMPND 61 EC: 1.10.2.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 7 ORGANISM_COMMON: CHICKEN;
SOURCE 8 ORGANISM_TAXID: 9031;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 11 ORGANISM_COMMON: CHICKEN;
SOURCE 12 ORGANISM_TAXID: 9031;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 15 ORGANISM_COMMON: CHICKEN;
SOURCE 16 ORGANISM_TAXID: 9031;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 19 ORGANISM_COMMON: CHICKEN;
SOURCE 20 ORGANISM_TAXID: 9031;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 23 ORGANISM_COMMON: CHICKEN;
SOURCE 24 ORGANISM_TAXID: 9031;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 27 ORGANISM_COMMON: CHICKEN;
SOURCE 28 ORGANISM_TAXID: 9031;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 31 ORGANISM_COMMON: CHICKEN;
SOURCE 32 ORGANISM_TAXID: 9031;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 35 ORGANISM_COMMON: CHICKEN;
SOURCE 36 ORGANISM_TAXID: 9031;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 39 ORGANISM_COMMON: CHICKEN;
SOURCE 40 ORGANISM_TAXID: 9031
KEYWDS CYTOCHROME BC1, MEMBRANE PROTEIN, HEME PROTEIN, RIESKE IRON SULFUR
KEYWDS 2 PROTEIN, CYTOCHROME B, CYTOCHROME C1, COMPLEX III, MITOCHONDRIAL
KEYWDS 3 PROCESSING PROTEASE, UBIQUINONE, OXIDOREDUCTASE, REDOX ENZYME,
KEYWDS 4 RESPIRATORY CHAIN, STIGMATELLIN, ANTIMYCIN, ELECTRON TRANSPORT,
KEYWDS 5 HEME, IRON, MEMBRANE, METAL-BINDING, MITOCHONDRION, MITOCHONDRION
KEYWDS 6 INNER MEMBRANE, TRANSMEMBRANE, TRANSPORT, DISULFIDE BOND, IRON-
KEYWDS 7 SULFUR, TRANSIT PEPTIDE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.ZHANG,L.HUANG,V.M.SHULMEISTER,Y.I.CHI,K.K.KIM,L.W.HUNG,A.R.CROFTS,
AUTHOR 2 E.A.BERRY,S.H.KIM
REVDAT 3 06-SEP-23 3H1I 1 COMPND REMARK HETNAM FORMUL
REVDAT 3 2 1 ATOM
REVDAT 2 13-JUL-11 3H1I 1 VERSN
REVDAT 1 28-APR-09 3H1I 0
JRNL AUTH Z.ZHANG,L.HUANG,V.M.SHULMEISTER,Y.I.CHI,K.K.KIM,L.W.HUNG,
JRNL AUTH 2 A.R.CROFTS,E.A.BERRY,S.H.KIM
JRNL TITL ELECTRON TRANSFER BY DOMAIN MOVEMENT IN CYTOCHROME BC1
JRNL REF NATURE V. 392 677 1998
JRNL REFN ISSN 0028-0836
JRNL PMID 9565029
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH L.S.HUANG,D.COBESSI,E.Y.TUNG,E.A.BERRY
REMARK 1 TITL BINDING OF THE RESPIRATORY CHAIN INHIBITOR ANTIMYCIN TO THE
REMARK 1 TITL 2 MITOCHONDRIAL BC(1) COMPLEX: A NEW CRYSTAL STRUCTURE REVEALS
REMARK 1 TITL 3 AN ALTERED INTRAMOLECULAR HYDROGEN-BONDING PATTERN.
REMARK 1 REF J.MOL.BIOL. V. 351 573 2005
REMARK 1 REFN ISSN 0022-2836
REMARK 1 REFERENCE 2
REMARK 1 AUTH E.A.BERRY,L.S.HUANG,Z.ZHANG,S.H.KIM
REMARK 1 TITL THE STRUCTURE OF THE AVIAN MITOCHONDRIAL CYTOCHROME BC1
REMARK 1 TITL 2 COMPLEX.
REMARK 1 REF J.BIOENERG.BIOMEMBR. V. 31 177 1999
REMARK 1 REFN ISSN 0145-479X
REMARK 2
REMARK 2 RESOLUTION. 3.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 6933881.310
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 85111
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.263
REMARK 3 FREE R VALUE : 0.306
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2551
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.71
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10734
REMARK 3 BIN R VALUE (WORKING SET) : 0.3810
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 351
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.022
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31797
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 904
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 89.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 34.71000
REMARK 3 B22 (A**2) : -20.96000
REMARK 3 B33 (A**2) : -13.76000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.53
REMARK 3 ESD FROM SIGMAA (A) : 1.00
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.62
REMARK 3 ESD FROM C-V SIGMAA (A) : 1.10
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.300 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.450 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.23
REMARK 3 BSOL : 14.40
REMARK 3
REMARK 3 NCS MODEL : CONSTR
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : HETERO10.PAR
REMARK 3 PARAMETER FILE 3 : FNMFMX.PAR
REMARK 3 PARAMETER FILE 4 : WATER.PARAM
REMARK 3 PARAMETER FILE 5 : PROSTHW.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : &_1_TOPOLOGY_INFILE_1
REMARK 3 TOPOLOGY FILE 2 : &_1_TOPOLOGY_INFILE_2
REMARK 3 TOPOLOGY FILE 3 : &_1_TOPOLOGY_INFILE_3
REMARK 3 TOPOLOGY FILE 4 : &_1_TOPOLOGY_INFILE_4
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H1I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052573.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-SEP-96
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5412
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90316
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 87.039
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.22900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.99700
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.340
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ALMN, TFFC (CCP4 PACKAGE), RAVE
REMARK 200 STARTING MODEL: PDB ENTRY 1BCC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM KMES PH 6.7, 75MM NACL, 10%
REMARK 280 GLYCEROL, AND 6% PEG4000, INHIBITORS WERE ADDED FROM ETHANOLIC
REMARK 280 SOLUTION, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 87.34650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 120.36600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 90.83300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 120.36600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 87.34650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 90.83300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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: EICOSAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: EICOSAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 109030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 152830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -716.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: N, O, P, Q, R, S, T, U, V, W
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 1
REMARK 465 ARG A 445
REMARK 465 PHE A 446
REMARK 465 SER B -1
REMARK 465 LEU B 0
REMARK 465 LYS B 1
REMARK 465 VAL B 2
REMARK 465 ALA B 3
REMARK 465 PRO B 4
REMARK 465 LYS B 5
REMARK 465 VAL B 6
REMARK 465 ALA B 7
REMARK 465 VAL B 8
REMARK 465 SER B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 ALA B 12
REMARK 465 GLU B 13
REMARK 465 ARG B 14
REMARK 465 VAL B 15
REMARK 465 LYS B 16
REMARK 465 LEU B 17
REMARK 465 CYS B 18
REMARK 465 ALA F 1
REMARK 465 ALA F 2
REMARK 465 ARG F 3
REMARK 465 ALA F 4
REMARK 465 THR F 5
REMARK 465 VAL F 6
REMARK 465 ALA F 7
REMARK 465 GLY F 8
REMARK 465 GLY F 9
REMARK 465 LEU H 2
REMARK 465 ARG H 3
REMARK 465 GLY H 4
REMARK 465 SER H 5
REMARK 465 GLY H 6
REMARK 465 GLU H 7
REMARK 465 GLU H 8
REMARK 465 TYR I 78
REMARK 465 ALA N 1
REMARK 465 ALA N 2
REMARK 465 ARG N 445
REMARK 465 PHE N 446
REMARK 465 SER O -1
REMARK 465 LEU O 0
REMARK 465 LYS O 1
REMARK 465 VAL O 2
REMARK 465 ALA O 3
REMARK 465 PRO O 4
REMARK 465 LYS O 5
REMARK 465 VAL O 6
REMARK 465 ALA O 7
REMARK 465 VAL O 8
REMARK 465 SER O 9
REMARK 465 ALA O 10
REMARK 465 ALA O 11
REMARK 465 ALA O 12
REMARK 465 GLU O 13
REMARK 465 ARG O 14
REMARK 465 VAL O 15
REMARK 465 LYS O 16
REMARK 465 LEU O 17
REMARK 465 MET P 1
REMARK 465 ALA S 1
REMARK 465 ALA S 2
REMARK 465 ARG S 3
REMARK 465 ALA S 4
REMARK 465 THR S 5
REMARK 465 VAL S 6
REMARK 465 ALA S 7
REMARK 465 GLY S 8
REMARK 465 GLY S 9
REMARK 465 ASP T 80
REMARK 465 GLN T 81
REMARK 465 LEU U 2
REMARK 465 ARG U 3
REMARK 465 GLY U 4
REMARK 465 SER U 5
REMARK 465 GLY U 6
REMARK 465 GLU U 7
REMARK 465 GLU U 8
REMARK 465 GLU U 9
REMARK 465 GLU U 10
REMARK 465 GLU U 11
REMARK 465 UNK V 26
REMARK 465 UNK V 27
REMARK 465 TYR V 78
REMARK 465 GLU W 63
REMARK 465 GLU W 64
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ILE A 444 C O CB CG1 CG2 CD1
REMARK 470 GLU H 9 N CB CG CD OE1 OE2
REMARK 470 ARG I 47 N CB CG CD NE CZ NH1
REMARK 470 ARG I 47 NH2
REMARK 470 ARG I 61 CG CD NE CZ NH1 NH2
REMARK 470 ILE N 444 O CG1 CG2 CD1
REMARK 470 ARG V 47 N CB CG CD NE CZ NH1
REMARK 470 ARG V 47 NH2
REMARK 470 ARG V 61 CG CD NE CZ NH1 NH2
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 SG CYS Q 37 CAB HEC Q 501 1.77
REMARK 500 SG CYS D 37 CAB HEC D 501 1.78
REMARK 500 SG CYS Q 40 CAC HEC Q 501 1.84
REMARK 500 SG CYS D 40 CAC HEC D 501 1.85
REMARK 500 OD1 ASP S 35 OH TYR S 89 2.17
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 PRO B 134 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO C 271 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO O 19 C - N - CA ANGL. DEV. = 10.3 DEGREES
REMARK 500 PRO O 134 C - N - CA ANGL. DEV. = 10.4 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 TYR A 4 -78.42 -34.62
REMARK 500 ALA A 5 -70.00 -19.11
REMARK 500 LEU A 23 157.43 -42.61
REMARK 500 CYS A 35 -162.17 -165.96
REMARK 500 TRP A 40 76.76 -113.40
REMARK 500 ASN A 49 -160.12 -110.93
REMARK 500 ALA A 55 -73.39 1.46
REMARK 500 PRO A 71 -172.26 -55.66
REMARK 500 CYS A 72 -92.97 -33.64
REMARK 500 SER A 81 -19.94 -49.53
REMARK 500 TYR A 89 -168.37 -161.64
REMARK 500 THR A 90 94.77 -162.43
REMARK 500 SER A 91 -159.27 -86.55
REMARK 500 GLN A 94 115.63 160.89
REMARK 500 ALA A 96 140.66 -174.88
REMARK 500 MET A 106 -56.21 -18.13
REMARK 500 GLN A 118 -73.71 -91.57
REMARK 500 GLU A 128 1.67 -60.88
REMARK 500 VAL A 148 -34.93 -38.23
REMARK 500 GLN A 159 140.14 -13.66
REMARK 500 ALA A 164 16.65 -65.77
REMARK 500 LEU A 177 134.03 -34.06
REMARK 500 ASP A 181 -35.87 -38.80
REMARK 500 PHE A 190 79.12 -65.19
REMARK 500 PHE A 216 48.94 -90.37
REMARK 500 PHE A 221 -86.59 -80.04
REMARK 500 THR A 222 -173.91 -58.60
REMARK 500 SER A 239 -170.45 -175.32
REMARK 500 ASP A 245 89.24 -163.71
REMARK 500 TRP A 262 -61.27 -22.16
REMARK 500 ALA A 263 -71.91 -30.84
REMARK 500 ASP A 264 125.60 -36.40
REMARK 500 ASN A 267 -38.29 -38.31
REMARK 500 VAL A 268 -73.74 -50.40
REMARK 500 ASN A 274 -17.00 -45.29
REMARK 500 ASP A 281 127.95 -174.71
REMARK 500 ARG A 282 -51.29 -11.91
REMARK 500 LYS A 288 -12.12 -41.61
REMARK 500 LEU A 290 156.11 -34.08
REMARK 500 SER A 306 157.37 178.78
REMARK 500 THR A 317 -155.16 -124.90
REMARK 500 ASP A 332 -78.87 -58.92
REMARK 500 MET A 334 -71.82 -52.49
REMARK 500 LEU A 369 65.24 -109.88
REMARK 500 ARG A 388 -146.52 -122.88
REMARK 500 ALA A 404 -82.83 -46.37
REMARK 500 ARG A 405 -54.99 -22.42
REMARK 500 ASP A 433 116.20 55.72
REMARK 500 TRP A 443 99.90 81.32
REMARK 500 GLU B 22 -144.79 -89.59
REMARK 500
REMARK 500 THIS ENTRY HAS 538 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 TYR C 104 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 PEE A 2008
REMARK 610 ANY C 2002
REMARK 610 CDL C 2004
REMARK 610 PEE C 2007
REMARK 610 CDL D 2003
REMARK 610 PEE E 2005
REMARK 610 PLC E 2009
REMARK 610 PEE N 3008
REMARK 610 ANY P 3002
REMARK 610 CDL P 3004
REMARK 610 PEE P 3005
REMARK 610 PEE P 3007
REMARK 610 CDL Q 3003
REMARK 610 PLC R 3009
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 HEM C 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 84 NE2
REMARK 620 2 HEM C 501 NA 88.5
REMARK 620 3 HEM C 501 NB 92.2 90.5
REMARK 620 4 HEM C 501 NC 90.5 178.0 91.3
REMARK 620 5 HEM C 501 ND 91.3 89.3 176.5 88.9
REMARK 620 6 HIS C 183 NE2 176.3 93.7 84.9 87.3 91.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 98 NE2
REMARK 620 2 HEM C 502 NA 91.0
REMARK 620 3 HEM C 502 NB 92.4 90.9
REMARK 620 4 HEM C 502 NC 86.4 177.2 88.0
REMARK 620 5 HEM C 502 ND 90.5 91.1 176.4 90.1
REMARK 620 6 HIS C 197 NE2 172.5 91.8 94.4 90.8 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 41 NE2
REMARK 620 2 HEC D 501 NA 86.9
REMARK 620 3 HEC D 501 NB 91.9 91.1
REMARK 620 4 HEC D 501 NC 92.7 177.8 86.8
REMARK 620 5 HEC D 501 ND 91.1 87.8 176.7 94.4
REMARK 620 6 MET D 160 SD 173.6 90.9 94.1 89.7 82.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 139 SG
REMARK 620 2 FES E 501 S1 112.9
REMARK 620 3 FES E 501 S2 108.9 106.5
REMARK 620 4 CYS E 158 SG 108.8 109.7 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 141 ND1
REMARK 620 2 FES E 501 S1 114.5
REMARK 620 3 FES E 501 S2 113.3 106.6
REMARK 620 4 HIS E 161 ND1 93.5 115.5 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM P 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 84 NE2
REMARK 620 2 HEM P 501 NA 83.6
REMARK 620 3 HEM P 501 NB 86.2 89.9
REMARK 620 4 HEM P 501 NC 96.3 177.2 92.9
REMARK 620 5 HEM P 501 ND 93.2 87.4 177.2 89.9
REMARK 620 6 HIS P 183 NE2 173.3 94.4 87.5 86.1 93.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM P 502 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 98 NE2
REMARK 620 2 HEM P 502 NA 86.0
REMARK 620 3 HEM P 502 NB 92.0 89.0
REMARK 620 4 HEM P 502 NC 91.6 177.6 90.6
REMARK 620 5 HEM P 502 ND 90.7 88.0 175.8 92.5
REMARK 620 6 HIS P 197 NE2 171.3 89.7 95.5 92.7 81.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC Q 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 41 NE2
REMARK 620 2 HEC Q 501 NA 89.5
REMARK 620 3 HEC Q 501 NB 91.5 92.0
REMARK 620 4 HEC Q 501 NC 91.4 177.7 85.8
REMARK 620 5 HEC Q 501 ND 88.6 87.5 179.5 94.6
REMARK 620 6 MET Q 160 SD 172.6 91.4 95.9 88.1 84.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES R 501 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS R 139 SG
REMARK 620 2 FES R 501 S1 114.1
REMARK 620 3 FES R 501 S2 107.8 107.1
REMARK 620 4 CYS R 158 SG 110.4 108.4 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES R 501 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS R 141 ND1
REMARK 620 2 FES R 501 S1 115.1
REMARK 620 3 FES R 501 S2 113.9 104.9
REMARK 620 4 HIS R 161 ND1 92.7 117.2 113.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM P 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC Q 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES R 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANY C 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL D 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 2004
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE E 2005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE C 2007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE A 2008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLC E 2009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 2011
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 2015
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL R 2103
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 2104
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL E 2105
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SMA P 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANY P 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL Q 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE P 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE P 3007
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEE N 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLC R 3009
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 3010
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL P 3011
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL C 3015
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL E 3103
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL P 3104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BCC RELATED DB: PDB
REMARK 900 STIGMATELLIN-BOUND CYTOCHROME BC1 COMPLEX FROM CHICKEN. THE CURRENT
REMARK 900 ENTRY IS A FURTHER REFINEMENT OF THIS STRUCTURE, WHICH IT WILL MAKE
REMARK 900 OBSOLETE.
REMARK 900 RELATED ID: 1PPJ RELATED DB: PDB
REMARK 900 BOVINE BC1 COMPLEX WITH ANTIMYCIN AND STIGMATELLIN BOUND
REMARK 900 RELATED ID: 3H1H RELATED DB: PDB
REMARK 900 RELATED ID: 3H1J RELATED DB: PDB
REMARK 900 RELATED ID: 3H1K RELATED DB: PDB
REMARK 900 RELATED ID: 3H1L RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 IN THE COORDINATES THE FIRST 15 RESIDUES IN CHAINS I AND V ARE
REMARK 999 MODELED AS UNK BECAUSE THE SEQUENCE ALIGNMENT IS UNKNOWN FOR THE
REMARK 999 FIRST 42 RESIDUES IN CHAINS I AND V.
DBREF 3H1I C 1 380 UNP P18946 CYB_CHICK 1 380
DBREF 3H1I E 1 196 UNP Q5ZLR5 UCRI_CHICK 77 272
DBREF 3H1I I 47 78 UNP Q5ZLR5 UCRI_CHICK 45 76
DBREF 3H1I P 1 380 UNP P18946 CYB_CHICK 1 380
DBREF 3H1I R 1 196 UNP Q5ZLR5 UCRI_CHICK 77 272
DBREF 3H1I V 47 78 UNP Q5ZLR5 UCRI_CHICK 45 76
DBREF 3H1I A 1 446 PDB 3H1I 3H1I 1 446
DBREF 3H1I N 1 446 PDB 3H1I 3H1I 1 446
DBREF 3H1I B -1 439 PDB 3H1I 3H1I -1 439
DBREF 3H1I O -1 439 PDB 3H1I 3H1I -1 439
DBREF 3H1I D 1 241 PDB 3H1I 3H1I 1 241
DBREF 3H1I Q 1 241 PDB 3H1I 3H1I 1 241
DBREF 3H1I F 1 110 PDB 3H1I 3H1I 1 110
DBREF 3H1I S 1 110 PDB 3H1I 3H1I 1 110
DBREF 3H1I G 1 81 PDB 3H1I 3H1I 1 81
DBREF 3H1I T 1 81 PDB 3H1I 3H1I 1 81
DBREF 3H1I H 2 78 PDB 3H1I 3H1I 2 78
DBREF 3H1I U 2 78 PDB 3H1I 3H1I 2 78
DBREF 3H1I J 4 64 PDB 3H1I 3H1I 4 64
DBREF 3H1I W 4 64 PDB 3H1I 3H1I 4 64
SEQRES 1 A 446 ALA ALA THR TYR ALA GLN THR LEU GLN ASN ILE PRO GLU
SEQRES 2 A 446 THR ASN VAL THR THR LEU ASP ASN GLY LEU ARG VAL ALA
SEQRES 3 A 446 SER GLU GLU SER SER GLN PRO THR CYS THR VAL GLY VAL
SEQRES 4 A 446 TRP ILE GLY ALA GLY SER ARG TYR GLU ASN GLU LYS ASN
SEQRES 5 A 446 ASN GLY ALA GLY TYR PHE VAL GLU HIS LEU ALA PHE LYS
SEQRES 6 A 446 GLY THR LYS LYS ARG PRO CYS ALA ALA PHE GLU LYS GLU
SEQRES 7 A 446 VAL GLU SER MET GLY ALA HIS PHE ASN GLY TYR THR SER
SEQRES 8 A 446 ARG GLU GLN THR ALA PHE TYR ILE LYS ALA LEU SER LYS
SEQRES 9 A 446 ASP MET PRO LYS VAL VAL GLU LEU LEU ALA ASP VAL VAL
SEQRES 10 A 446 GLN ASN CYS ALA LEU GLU GLU SER GLN ILE GLU LYS GLU
SEQRES 11 A 446 ARG GLY VAL ILE LEU GLN GLU LEU LYS GLU MET ASP ASN
SEQRES 12 A 446 ASP MET THR ASN VAL THR PHE ASP TYR LEU HIS ALA THR
SEQRES 13 A 446 ALA PHE GLN GLY THR ALA LEU ALA ARG THR VAL GLU GLY
SEQRES 14 A 446 THR THR GLU ASN ILE LYS HIS LEU THR ARG ALA ASP LEU
SEQRES 15 A 446 ALA SER TYR ILE ASP THR HIS PHE LYS ALA PRO ARG MET
SEQRES 16 A 446 VAL LEU ALA ALA ALA GLY GLY ILE SER HIS LYS GLU LEU
SEQRES 17 A 446 VAL ASP ALA ALA ARG GLN HIS PHE SER GLY VAL SER PHE
SEQRES 18 A 446 THR TYR LYS GLU ASP ALA VAL PRO ILE LEU PRO ARG CYS
SEQRES 19 A 446 ARG PHE THR GLY SER GLU ILE ARG ALA ARG ASP ASP ALA
SEQRES 20 A 446 LEU PRO VAL ALA HIS VAL ALA LEU ALA VAL GLU GLY PRO
SEQRES 21 A 446 GLY TRP ALA ASP PRO ASP ASN VAL VAL LEU HIS VAL ALA
SEQRES 22 A 446 ASN ALA ILE ILE GLY ARG TYR ASP ARG THR PHE GLY GLY
SEQRES 23 A 446 GLY LYS HIS LEU SER SER ARG LEU ALA ALA LEU ALA VAL
SEQRES 24 A 446 GLU HIS LYS LEU CYS HIS SER PHE GLN THR PHE ASN THR
SEQRES 25 A 446 SER TYR SER ASP THR GLY LEU PHE GLY PHE HIS PHE VAL
SEQRES 26 A 446 ALA ASP PRO LEU SER ILE ASP ASP MET MET PHE CYS ALA
SEQRES 27 A 446 GLN GLY GLU TRP MET ARG LEU CYS THR SER THR THR GLU
SEQRES 28 A 446 SER GLU VAL LYS ARG ALA LYS ASN HIS LEU ARG SER ALA
SEQRES 29 A 446 MET VAL ALA GLN LEU ASP GLY THR THR PRO VAL CYS GLU
SEQRES 30 A 446 THR ILE GLY SER HIS LEU LEU ASN TYR GLY ARG ARG ILE
SEQRES 31 A 446 SER LEU GLU GLU TRP ASP SER ARG ILE SER ALA VAL ASP
SEQRES 32 A 446 ALA ARG MET VAL ARG ASP VAL CYS SER LYS TYR ILE TYR
SEQRES 33 A 446 ASP LYS CYS PRO ALA LEU ALA ALA VAL GLY PRO ILE GLU
SEQRES 34 A 446 GLN LEU LEU ASP TYR ASN ARG ILE ARG SER GLY MET TYR
SEQRES 35 A 446 TRP ILE ARG PHE
SEQRES 1 B 441 SER LEU LYS VAL ALA PRO LYS VAL ALA VAL SER ALA ALA
SEQRES 2 B 441 ALA GLU ARG VAL LYS LEU CYS PRO GLY ALA GLU ASP LEU
SEQRES 3 B 441 GLU ILE THR LYS LEU PRO ASN GLY LEU ILE ILE ALA SER
SEQRES 4 B 441 LEU GLU ASN PHE SER PRO ALA SER ARG ILE GLY VAL PHE
SEQRES 5 B 441 ILE LYS ALA GLY SER ARG TYR GLU THR THR ALA ASN LEU
SEQRES 6 B 441 GLY THR ALA HIS LEU LEU ARG LEU ALA SER PRO LEU THR
SEQRES 7 B 441 THR LYS GLY ALA SER SER PHE ARG ILE THR ARG GLY ILE
SEQRES 8 B 441 GLU ALA VAL GLY GLY SER LEU SER VAL TYR SER THR ARG
SEQRES 9 B 441 GLU LYS MET THR TYR CYS VAL GLU CYS LEU ARG ASP HIS
SEQRES 10 B 441 VAL ASP THR VAL MET GLU TYR LEU LEU ASN VAL THR THR
SEQRES 11 B 441 ALA PRO GLU PHE ARG PRO TRP GLU VAL THR ASP LEU GLN
SEQRES 12 B 441 PRO GLN LEU LYS VAL ASP LYS ALA VAL ALA PHE GLN SER
SEQRES 13 B 441 PRO GLN VAL GLY VAL LEU GLU ASN LEU HIS ALA ALA ALA
SEQRES 14 B 441 TYR LYS THR ALA LEU ALA ASN PRO LEU TYR CYS PRO ASP
SEQRES 15 B 441 TYR ARG ILE GLY LYS ILE THR SER GLU GLN LEU HIS HIS
SEQRES 16 B 441 PHE VAL GLN ASN ASN PHE THR SER ALA ARG MET ALA LEU
SEQRES 17 B 441 VAL GLY ILE GLY VAL LYS HIS SER ASP LEU LYS GLN VAL
SEQRES 18 B 441 ALA GLU GLN PHE LEU ASN ILE ARG SER GLY ALA GLY THR
SEQRES 19 B 441 SER SER ALA LYS ALA THR TYR TRP GLY GLY GLU ILE ARG
SEQRES 20 B 441 GLU GLN ASN GLY HIS SER LEU VAL HIS ALA ALA VAL VAL
SEQRES 21 B 441 THR GLU GLY ALA ALA VAL GLY SER ALA GLU ALA ASN ALA
SEQRES 22 B 441 PHE SER VAL LEU GLN HIS VAL LEU GLY ALA GLY PRO LEU
SEQRES 23 B 441 ILE LYS ARG GLY SER SER VAL THR SER LYS LEU TYR GLN
SEQRES 24 B 441 GLY VAL ALA LYS ALA THR THR GLN PRO PHE ASP ALA SER
SEQRES 25 B 441 ALA PHE ASN VAL ASN TYR SER ASP SER GLY LEU PHE GLY
SEQRES 26 B 441 PHE TYR THR ILE SER GLN ALA ALA HIS ALA GLY GLU VAL
SEQRES 27 B 441 ILE ARG ALA ALA MET ASN GLN LEU LYS ALA ALA ALA GLN
SEQRES 28 B 441 GLY GLY VAL THR GLU GLU ASP VAL THR LYS ALA LYS ASN
SEQRES 29 B 441 GLN LEU LYS ALA THR TYR LEU MET SER VAL GLU THR ALA
SEQRES 30 B 441 GLN GLY LEU LEU ASN GLU ILE GLY SER GLU ALA LEU LEU
SEQRES 31 B 441 SER GLY THR HIS THR ALA PRO SER VAL VAL ALA GLN LYS
SEQRES 32 B 441 ILE ASP SER VAL THR SER ALA ASP VAL VAL ASN ALA ALA
SEQRES 33 B 441 LYS LYS PHE VAL SER GLY LYS LYS SER MET ALA ALA SER
SEQRES 34 B 441 GLY ASP LEU GLY SER THR PRO PHE LEU ASP GLU LEU
SEQRES 1 C 380 MET ALA PRO ASN ILE ARG LYS SER HIS PRO LEU LEU LYS
SEQRES 2 C 380 MET ILE ASN ASN SER LEU ILE ASP LEU PRO ALA PRO SER
SEQRES 3 C 380 ASN ILE SER ALA TRP TRP ASN PHE GLY SER LEU LEU ALA
SEQRES 4 C 380 VAL CYS LEU MET THR GLN ILE LEU THR GLY LEU LEU LEU
SEQRES 5 C 380 ALA MET HIS TYR THR ALA ASP THR SER LEU ALA PHE SER
SEQRES 6 C 380 SER VAL ALA HIS THR CYS ARG ASN VAL GLN TYR GLY TRP
SEQRES 7 C 380 LEU ILE ARG ASN LEU HIS ALA ASN GLY ALA SER PHE PHE
SEQRES 8 C 380 PHE ILE CYS ILE PHE LEU HIS ILE GLY ARG GLY LEU TYR
SEQRES 9 C 380 TYR GLY SER TYR LEU TYR LYS GLU THR TRP ASN THR GLY
SEQRES 10 C 380 VAL ILE LEU LEU LEU THR LEU MET ALA THR ALA PHE VAL
SEQRES 11 C 380 GLY TYR VAL LEU PRO TRP GLY GLN MET SER PHE TRP GLY
SEQRES 12 C 380 ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO TYR
SEQRES 13 C 380 ILE GLY HIS THR LEU VAL GLU TRP ALA TRP GLY GLY PHE
SEQRES 14 C 380 SER VAL ASP ASN PRO THR LEU THR ARG PHE PHE ALA LEU
SEQRES 15 C 380 HIS PHE LEU LEU PRO PHE ALA ILE ALA GLY ILE THR ILE
SEQRES 16 C 380 ILE HIS LEU THR PHE LEU HIS GLU SER GLY SER ASN ASN
SEQRES 17 C 380 PRO LEU GLY ILE SER SER ASP SER ASP LYS ILE PRO PHE
SEQRES 18 C 380 HIS PRO TYR TYR SER PHE LYS ASP ILE LEU GLY LEU THR
SEQRES 19 C 380 LEU MET LEU THR PRO PHE LEU THR LEU ALA LEU PHE SER
SEQRES 20 C 380 PRO ASN LEU LEU GLY ASP PRO GLU ASN PHE THR PRO ALA
SEQRES 21 C 380 ASN PRO LEU VAL THR PRO PRO HIS ILE LYS PRO GLU TRP
SEQRES 22 C 380 TYR PHE LEU PHE ALA TYR ALA ILE LEU ARG SER ILE PRO
SEQRES 23 C 380 ASN LYS LEU GLY GLY VAL LEU ALA LEU ALA ALA SER VAL
SEQRES 24 C 380 LEU ILE LEU PHE LEU ILE PRO PHE LEU HIS LYS SER LYS
SEQRES 25 C 380 GLN ARG THR MET THR PHE ARG PRO LEU SER GLN THR LEU
SEQRES 26 C 380 PHE TRP LEU LEU VAL ALA ASN LEU LEU ILE LEU THR TRP
SEQRES 27 C 380 ILE GLY SER GLN PRO VAL GLU HIS PRO PHE ILE ILE ILE
SEQRES 28 C 380 GLY GLN MET ALA SER LEU SER TYR PHE THR ILE LEU LEU
SEQRES 29 C 380 ILE LEU PHE PRO THR ILE GLY THR LEU GLU ASN LYS MET
SEQRES 30 C 380 LEU ASN TYR
SEQRES 1 D 241 GLY GLU LEU GLU LEU HIS PRO PRO ALA PHE PRO TRP SER
SEQRES 2 D 241 HIS GLY GLY PRO LEU SER ALA LEU ASP HIS SER SER VAL
SEQRES 3 D 241 ARG ARG GLY PHE GLN VAL TYR LYS GLN VAL CYS SER ALA
SEQRES 4 D 241 CYS HIS SER MET ASP TYR VAL ALA PHE ARG ASN LEU ILE
SEQRES 5 D 241 GLY VAL THR HIS THR GLU ALA GLU ALA LYS ALA LEU ALA
SEQRES 6 D 241 GLU GLU VAL GLU VAL GLN ASP GLY PRO ASP GLU ASN GLY
SEQRES 7 D 241 GLU LEU PHE MET ARG PRO GLY LYS ILE SER ASP TYR PHE
SEQRES 8 D 241 PRO LYS PRO TYR PRO ASN PRO GLU ALA ALA ARG ALA ALA
SEQRES 9 D 241 ASN ASN GLY ALA LEU PRO PRO ASP LEU SER TYR ILE VAL
SEQRES 10 D 241 ASN ALA ARG HIS GLY GLY GLU ASP TYR VAL PHE SER LEU
SEQRES 11 D 241 LEU THR GLY TYR CYS ASP PRO PRO ALA GLY VAL VAL VAL
SEQRES 12 D 241 ARG GLU GLY LEU HIS TYR ASN PRO TYR PHE PRO GLY GLN
SEQRES 13 D 241 ALA ILE GLY MET ALA PRO PRO ILE TYR ASN GLU ILE LEU
SEQRES 14 D 241 GLU TYR ASP ASP GLY THR PRO ALA THR MET SER GLN ILE
SEQRES 15 D 241 ALA LYS ASP VAL CYS THR PHE LEU ARG TRP ALA ALA GLU
SEQRES 16 D 241 PRO GLU HIS ASP GLN ARG LYS ARG MET GLY LEU LYS MET
SEQRES 17 D 241 LEU LEU ILE SER ALA LEU LEU THR SER LEU LEU TYR TYR
SEQRES 18 D 241 MET LYS ARG HIS LYS TRP SER VAL LEU LYS SER ARG LYS
SEQRES 19 D 241 MET ALA TYR ARG PRO PRO LYS
SEQRES 1 E 196 VAL HIS ASN ASP VAL THR VAL PRO ASP PHE SER ALA TYR
SEQRES 2 E 196 ARG ARG GLU ASP VAL MET ASP ALA THR THR SER SER GLN
SEQRES 3 E 196 THR SER SER GLU ASP ARG LYS GLY PHE SER TYR LEU VAL
SEQRES 4 E 196 THR ALA THR ALA CYS VAL ALA THR ALA TYR ALA ALA LYS
SEQRES 5 E 196 ASN VAL VAL THR GLN PHE ILE SER SER LEU SER ALA SER
SEQRES 6 E 196 ALA ASP VAL LEU ALA LEU SER LYS ILE GLU ILE LYS LEU
SEQRES 7 E 196 SER ASP ILE PRO GLU GLY LYS ASN VAL ALA PHE LYS TRP
SEQRES 8 E 196 ARG GLY LYS PRO LEU PHE VAL ARG HIS ARG THR GLN ALA
SEQRES 9 E 196 GLU ILE ASN GLN GLU ALA GLU VAL ASP VAL SER LYS LEU
SEQRES 10 E 196 ARG ASP PRO GLN HIS ASP LEU ASP ARG VAL LYS LYS PRO
SEQRES 11 E 196 GLU TRP VAL ILE LEU VAL GLY VAL CYS THR HIS LEU GLY
SEQRES 12 E 196 CYS VAL PRO ILE ALA ASN SER GLY ASP PHE GLY GLY TYR
SEQRES 13 E 196 TYR CYS PRO CYS HIS GLY SER HIS TYR ASP ALA SER GLY
SEQRES 14 E 196 ARG ILE ARG LYS GLY PRO ALA PRO TYR ASN LEU GLU VAL
SEQRES 15 E 196 PRO THR TYR GLN PHE VAL GLY ASP ASP LEU VAL VAL VAL
SEQRES 16 E 196 GLY
SEQRES 1 F 110 ALA ALA ARG ALA THR VAL ALA GLY GLY GLY ARG LEU MET
SEQRES 2 F 110 ASP ARG ILE ARG LYS TRP TYR TYR ASN ALA ALA GLY PHE
SEQRES 3 F 110 ASN LYS TYR GLY LEU MET ARG ASP ASP THR LEU TYR GLU
SEQRES 4 F 110 ASP ASP ASP VAL LYS GLU ALA LEU LYS ARG LEU PRO GLU
SEQRES 5 F 110 ASP LEU TYR ASN GLU ARG MET PHE ARG ILE LYS ARG ALA
SEQRES 6 F 110 LEU ASP LEU SER LEU LYS HIS ARG ILE LEU PRO LYS GLU
SEQRES 7 F 110 GLN TRP VAL LYS TYR GLU GLU ASP LYS PRO TYR LEU GLU
SEQRES 8 F 110 PRO TYR LEU LYS GLU VAL ILE ARG GLU ARG LEU GLU ARG
SEQRES 9 F 110 GLU ALA TRP ASN LYS LYS
SEQRES 1 G 81 GLY ILE HIS PHE GLY ASN LEU ALA ARG VAL ARG HIS ILE
SEQRES 2 G 81 ILE THR TYR SER LEU SER PRO PHE GLU GLN ARG ALA ILE
SEQRES 3 G 81 PRO ASN ILE PHE SER ASP ALA LEU PRO ASN VAL TRP ARG
SEQRES 4 G 81 ARG PHE SER SER GLN VAL PHE LYS VAL ALA PRO PRO PHE
SEQRES 5 G 81 LEU GLY ALA TYR LEU LEU TYR SER TRP GLY THR GLN GLU
SEQRES 6 G 81 PHE GLU ARG LEU LYS ARG LYS ASN PRO ALA ASP TYR GLU
SEQRES 7 G 81 ASN ASP GLN
SEQRES 1 H 77 LEU ARG GLY SER GLY GLU GLU GLU GLU GLU GLU LEU VAL
SEQRES 2 H 77 ASP PRO LEU THR THR ILE ARG GLU HIS CYS GLU GLN THR
SEQRES 3 H 77 GLU LYS CYS VAL LYS ALA ARG GLU ARG LEU GLU LEU CYS
SEQRES 4 H 77 ASP ALA ARG VAL SER SER ARG SER HIS THR GLU GLU GLN
SEQRES 5 H 77 CYS THR GLU GLU LEU PHE ASP PHE LEU HIS ALA ARG ASP
SEQRES 6 H 77 HIS CYS VAL ALA HIS LYS LEU PHE ASN LYS LEU LYS
SEQRES 1 I 47 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 I 47 UNK UNK ARG PRO LEU LEU CYS ARG GLU SER MET SER GLY
SEQRES 3 I 47 ARG SER ALA ARG ARG ASP LEU VAL ALA GLY ILE SER LEU
SEQRES 4 I 47 ASN ALA PRO ALA SER VAL ARG TYR
SEQRES 1 J 61 ALA LEU LEU ARG GLN ALA TYR SER ALA LEU PHE ARG ARG
SEQRES 2 J 61 THR SER THR PHE ALA LEU THR VAL VAL LEU GLY ALA VAL
SEQRES 3 J 61 LEU PHE GLU ARG ALA PHE ASP GLN GLY ALA ASP ALA ILE
SEQRES 4 J 61 PHE GLU HIS LEU ASN GLU GLY LYS LEU TRP LYS HIS ILE
SEQRES 5 J 61 LYS HIS LYS TYR GLU ALA SER GLU GLU
SEQRES 1 N 446 ALA ALA THR TYR ALA GLN THR LEU GLN ASN ILE PRO GLU
SEQRES 2 N 446 THR ASN VAL THR THR LEU ASP ASN GLY LEU ARG VAL ALA
SEQRES 3 N 446 SER GLU GLU SER SER GLN PRO THR CYS THR VAL GLY VAL
SEQRES 4 N 446 TRP ILE GLY ALA GLY SER ARG TYR GLU ASN GLU LYS ASN
SEQRES 5 N 446 ASN GLY ALA GLY TYR PHE VAL GLU HIS LEU ALA PHE LYS
SEQRES 6 N 446 GLY THR LYS LYS ARG PRO CYS ALA ALA PHE GLU LYS GLU
SEQRES 7 N 446 VAL GLU SER MET GLY ALA HIS PHE ASN GLY TYR THR SER
SEQRES 8 N 446 ARG GLU GLN THR ALA PHE TYR ILE LYS ALA LEU SER LYS
SEQRES 9 N 446 ASP MET PRO LYS VAL VAL GLU LEU LEU ALA ASP VAL VAL
SEQRES 10 N 446 GLN ASN CYS ALA LEU GLU GLU SER GLN ILE GLU LYS GLU
SEQRES 11 N 446 ARG GLY VAL ILE LEU GLN GLU LEU LYS GLU MET ASP ASN
SEQRES 12 N 446 ASP MET THR ASN VAL THR PHE ASP TYR LEU HIS ALA THR
SEQRES 13 N 446 ALA PHE GLN GLY THR ALA LEU ALA ARG THR VAL GLU GLY
SEQRES 14 N 446 THR THR GLU ASN ILE LYS HIS LEU THR ARG ALA ASP LEU
SEQRES 15 N 446 ALA SER TYR ILE ASP THR HIS PHE LYS ALA PRO ARG MET
SEQRES 16 N 446 VAL LEU ALA ALA ALA GLY GLY ILE SER HIS LYS GLU LEU
SEQRES 17 N 446 VAL ASP ALA ALA ARG GLN HIS PHE SER GLY VAL SER PHE
SEQRES 18 N 446 THR TYR LYS GLU ASP ALA VAL PRO ILE LEU PRO ARG CYS
SEQRES 19 N 446 ARG PHE THR GLY SER GLU ILE ARG ALA ARG ASP ASP ALA
SEQRES 20 N 446 LEU PRO VAL ALA HIS VAL ALA LEU ALA VAL GLU GLY PRO
SEQRES 21 N 446 GLY TRP ALA ASP PRO ASP ASN VAL VAL LEU HIS VAL ALA
SEQRES 22 N 446 ASN ALA ILE ILE GLY ARG TYR ASP ARG THR PHE GLY GLY
SEQRES 23 N 446 GLY LYS HIS LEU SER SER ARG LEU ALA ALA LEU ALA VAL
SEQRES 24 N 446 GLU HIS LYS LEU CYS HIS SER PHE GLN THR PHE ASN THR
SEQRES 25 N 446 SER TYR SER ASP THR GLY LEU PHE GLY PHE HIS PHE VAL
SEQRES 26 N 446 ALA ASP PRO LEU SER ILE ASP ASP MET MET PHE CYS ALA
SEQRES 27 N 446 GLN GLY GLU TRP MET ARG LEU CYS THR SER THR THR GLU
SEQRES 28 N 446 SER GLU VAL LYS ARG ALA LYS ASN HIS LEU ARG SER ALA
SEQRES 29 N 446 MET VAL ALA GLN LEU ASP GLY THR THR PRO VAL CYS GLU
SEQRES 30 N 446 THR ILE GLY SER HIS LEU LEU ASN TYR GLY ARG ARG ILE
SEQRES 31 N 446 SER LEU GLU GLU TRP ASP SER ARG ILE SER ALA VAL ASP
SEQRES 32 N 446 ALA ARG MET VAL ARG ASP VAL CYS SER LYS TYR ILE TYR
SEQRES 33 N 446 ASP LYS CYS PRO ALA LEU ALA ALA VAL GLY PRO ILE GLU
SEQRES 34 N 446 GLN LEU LEU ASP TYR ASN ARG ILE ARG SER GLY MET TYR
SEQRES 35 N 446 TRP ILE ARG PHE
SEQRES 1 O 441 SER LEU LYS VAL ALA PRO LYS VAL ALA VAL SER ALA ALA
SEQRES 2 O 441 ALA GLU ARG VAL LYS LEU CYS PRO GLY ALA GLU ASP LEU
SEQRES 3 O 441 GLU ILE THR LYS LEU PRO ASN GLY LEU ILE ILE ALA SER
SEQRES 4 O 441 LEU GLU ASN PHE SER PRO ALA SER ARG ILE GLY VAL PHE
SEQRES 5 O 441 ILE LYS ALA GLY SER ARG TYR GLU THR THR ALA ASN LEU
SEQRES 6 O 441 GLY THR ALA HIS LEU LEU ARG LEU ALA SER PRO LEU THR
SEQRES 7 O 441 THR LYS GLY ALA SER SER PHE ARG ILE THR ARG GLY ILE
SEQRES 8 O 441 GLU ALA VAL GLY GLY SER LEU SER VAL TYR SER THR ARG
SEQRES 9 O 441 GLU LYS MET THR TYR CYS VAL GLU CYS LEU ARG ASP HIS
SEQRES 10 O 441 VAL ASP THR VAL MET GLU TYR LEU LEU ASN VAL THR THR
SEQRES 11 O 441 ALA PRO GLU PHE ARG PRO TRP GLU VAL THR ASP LEU GLN
SEQRES 12 O 441 PRO GLN LEU LYS VAL ASP LYS ALA VAL ALA PHE GLN SER
SEQRES 13 O 441 PRO GLN VAL GLY VAL LEU GLU ASN LEU HIS ALA ALA ALA
SEQRES 14 O 441 TYR LYS THR ALA LEU ALA ASN PRO LEU TYR CYS PRO ASP
SEQRES 15 O 441 TYR ARG ILE GLY LYS ILE THR SER GLU GLN LEU HIS HIS
SEQRES 16 O 441 PHE VAL GLN ASN ASN PHE THR SER ALA ARG MET ALA LEU
SEQRES 17 O 441 VAL GLY ILE GLY VAL LYS HIS SER ASP LEU LYS GLN VAL
SEQRES 18 O 441 ALA GLU GLN PHE LEU ASN ILE ARG SER GLY ALA GLY THR
SEQRES 19 O 441 SER SER ALA LYS ALA THR TYR TRP GLY GLY GLU ILE ARG
SEQRES 20 O 441 GLU GLN ASN GLY HIS SER LEU VAL HIS ALA ALA VAL VAL
SEQRES 21 O 441 THR GLU GLY ALA ALA VAL GLY SER ALA GLU ALA ASN ALA
SEQRES 22 O 441 PHE SER VAL LEU GLN HIS VAL LEU GLY ALA GLY PRO LEU
SEQRES 23 O 441 ILE LYS ARG GLY SER SER VAL THR SER LYS LEU TYR GLN
SEQRES 24 O 441 GLY VAL ALA LYS ALA THR THR GLN PRO PHE ASP ALA SER
SEQRES 25 O 441 ALA PHE ASN VAL ASN TYR SER ASP SER GLY LEU PHE GLY
SEQRES 26 O 441 PHE TYR THR ILE SER GLN ALA ALA HIS ALA GLY GLU VAL
SEQRES 27 O 441 ILE ARG ALA ALA MET ASN GLN LEU LYS ALA ALA ALA GLN
SEQRES 28 O 441 GLY GLY VAL THR GLU GLU ASP VAL THR LYS ALA LYS ASN
SEQRES 29 O 441 GLN LEU LYS ALA THR TYR LEU MET SER VAL GLU THR ALA
SEQRES 30 O 441 GLN GLY LEU LEU ASN GLU ILE GLY SER GLU ALA LEU LEU
SEQRES 31 O 441 SER GLY THR HIS THR ALA PRO SER VAL VAL ALA GLN LYS
SEQRES 32 O 441 ILE ASP SER VAL THR SER ALA ASP VAL VAL ASN ALA ALA
SEQRES 33 O 441 LYS LYS PHE VAL SER GLY LYS LYS SER MET ALA ALA SER
SEQRES 34 O 441 GLY ASP LEU GLY SER THR PRO PHE LEU ASP GLU LEU
SEQRES 1 P 380 MET ALA PRO ASN ILE ARG LYS SER HIS PRO LEU LEU LYS
SEQRES 2 P 380 MET ILE ASN ASN SER LEU ILE ASP LEU PRO ALA PRO SER
SEQRES 3 P 380 ASN ILE SER ALA TRP TRP ASN PHE GLY SER LEU LEU ALA
SEQRES 4 P 380 VAL CYS LEU MET THR GLN ILE LEU THR GLY LEU LEU LEU
SEQRES 5 P 380 ALA MET HIS TYR THR ALA ASP THR SER LEU ALA PHE SER
SEQRES 6 P 380 SER VAL ALA HIS THR CYS ARG ASN VAL GLN TYR GLY TRP
SEQRES 7 P 380 LEU ILE ARG ASN LEU HIS ALA ASN GLY ALA SER PHE PHE
SEQRES 8 P 380 PHE ILE CYS ILE PHE LEU HIS ILE GLY ARG GLY LEU TYR
SEQRES 9 P 380 TYR GLY SER TYR LEU TYR LYS GLU THR TRP ASN THR GLY
SEQRES 10 P 380 VAL ILE LEU LEU LEU THR LEU MET ALA THR ALA PHE VAL
SEQRES 11 P 380 GLY TYR VAL LEU PRO TRP GLY GLN MET SER PHE TRP GLY
SEQRES 12 P 380 ALA THR VAL ILE THR ASN LEU PHE SER ALA ILE PRO TYR
SEQRES 13 P 380 ILE GLY HIS THR LEU VAL GLU TRP ALA TRP GLY GLY PHE
SEQRES 14 P 380 SER VAL ASP ASN PRO THR LEU THR ARG PHE PHE ALA LEU
SEQRES 15 P 380 HIS PHE LEU LEU PRO PHE ALA ILE ALA GLY ILE THR ILE
SEQRES 16 P 380 ILE HIS LEU THR PHE LEU HIS GLU SER GLY SER ASN ASN
SEQRES 17 P 380 PRO LEU GLY ILE SER SER ASP SER ASP LYS ILE PRO PHE
SEQRES 18 P 380 HIS PRO TYR TYR SER PHE LYS ASP ILE LEU GLY LEU THR
SEQRES 19 P 380 LEU MET LEU THR PRO PHE LEU THR LEU ALA LEU PHE SER
SEQRES 20 P 380 PRO ASN LEU LEU GLY ASP PRO GLU ASN PHE THR PRO ALA
SEQRES 21 P 380 ASN PRO LEU VAL THR PRO PRO HIS ILE LYS PRO GLU TRP
SEQRES 22 P 380 TYR PHE LEU PHE ALA TYR ALA ILE LEU ARG SER ILE PRO
SEQRES 23 P 380 ASN LYS LEU GLY GLY VAL LEU ALA LEU ALA ALA SER VAL
SEQRES 24 P 380 LEU ILE LEU PHE LEU ILE PRO PHE LEU HIS LYS SER LYS
SEQRES 25 P 380 GLN ARG THR MET THR PHE ARG PRO LEU SER GLN THR LEU
SEQRES 26 P 380 PHE TRP LEU LEU VAL ALA ASN LEU LEU ILE LEU THR TRP
SEQRES 27 P 380 ILE GLY SER GLN PRO VAL GLU HIS PRO PHE ILE ILE ILE
SEQRES 28 P 380 GLY GLN MET ALA SER LEU SER TYR PHE THR ILE LEU LEU
SEQRES 29 P 380 ILE LEU PHE PRO THR ILE GLY THR LEU GLU ASN LYS MET
SEQRES 30 P 380 LEU ASN TYR
SEQRES 1 Q 241 GLY GLU LEU GLU LEU HIS PRO PRO ALA PHE PRO TRP SER
SEQRES 2 Q 241 HIS GLY GLY PRO LEU SER ALA LEU ASP HIS SER SER VAL
SEQRES 3 Q 241 ARG ARG GLY PHE GLN VAL TYR LYS GLN VAL CYS SER ALA
SEQRES 4 Q 241 CYS HIS SER MET ASP TYR VAL ALA PHE ARG ASN LEU ILE
SEQRES 5 Q 241 GLY VAL THR HIS THR GLU ALA GLU ALA LYS ALA LEU ALA
SEQRES 6 Q 241 GLU GLU VAL GLU VAL GLN ASP GLY PRO ASP GLU ASN GLY
SEQRES 7 Q 241 GLU LEU PHE MET ARG PRO GLY LYS ILE SER ASP TYR PHE
SEQRES 8 Q 241 PRO LYS PRO TYR PRO ASN PRO GLU ALA ALA ARG ALA ALA
SEQRES 9 Q 241 ASN ASN GLY ALA LEU PRO PRO ASP LEU SER TYR ILE VAL
SEQRES 10 Q 241 ASN ALA ARG HIS GLY GLY GLU ASP TYR VAL PHE SER LEU
SEQRES 11 Q 241 LEU THR GLY TYR CYS ASP PRO PRO ALA GLY VAL VAL VAL
SEQRES 12 Q 241 ARG GLU GLY LEU HIS TYR ASN PRO TYR PHE PRO GLY GLN
SEQRES 13 Q 241 ALA ILE GLY MET ALA PRO PRO ILE TYR ASN GLU ILE LEU
SEQRES 14 Q 241 GLU TYR ASP ASP GLY THR PRO ALA THR MET SER GLN ILE
SEQRES 15 Q 241 ALA LYS ASP VAL CYS THR PHE LEU ARG TRP ALA ALA GLU
SEQRES 16 Q 241 PRO GLU HIS ASP GLN ARG LYS ARG MET GLY LEU LYS MET
SEQRES 17 Q 241 LEU LEU ILE SER ALA LEU LEU THR SER LEU LEU TYR TYR
SEQRES 18 Q 241 MET LYS ARG HIS LYS TRP SER VAL LEU LYS SER ARG LYS
SEQRES 19 Q 241 MET ALA TYR ARG PRO PRO LYS
SEQRES 1 R 196 VAL HIS ASN ASP VAL THR VAL PRO ASP PHE SER ALA TYR
SEQRES 2 R 196 ARG ARG GLU ASP VAL MET ASP ALA THR THR SER SER GLN
SEQRES 3 R 196 THR SER SER GLU ASP ARG LYS GLY PHE SER TYR LEU VAL
SEQRES 4 R 196 THR ALA THR ALA CYS VAL ALA THR ALA TYR ALA ALA LYS
SEQRES 5 R 196 ASN VAL VAL THR GLN PHE ILE SER SER LEU SER ALA SER
SEQRES 6 R 196 ALA ASP VAL LEU ALA LEU SER LYS ILE GLU ILE LYS LEU
SEQRES 7 R 196 SER ASP ILE PRO GLU GLY LYS ASN VAL ALA PHE LYS TRP
SEQRES 8 R 196 ARG GLY LYS PRO LEU PHE VAL ARG HIS ARG THR GLN ALA
SEQRES 9 R 196 GLU ILE ASN GLN GLU ALA GLU VAL ASP VAL SER LYS LEU
SEQRES 10 R 196 ARG ASP PRO GLN HIS ASP LEU ASP ARG VAL LYS LYS PRO
SEQRES 11 R 196 GLU TRP VAL ILE LEU VAL GLY VAL CYS THR HIS LEU GLY
SEQRES 12 R 196 CYS VAL PRO ILE ALA ASN SER GLY ASP PHE GLY GLY TYR
SEQRES 13 R 196 TYR CYS PRO CYS HIS GLY SER HIS TYR ASP ALA SER GLY
SEQRES 14 R 196 ARG ILE ARG LYS GLY PRO ALA PRO TYR ASN LEU GLU VAL
SEQRES 15 R 196 PRO THR TYR GLN PHE VAL GLY ASP ASP LEU VAL VAL VAL
SEQRES 16 R 196 GLY
SEQRES 1 S 110 ALA ALA ARG ALA THR VAL ALA GLY GLY GLY ARG LEU MET
SEQRES 2 S 110 ASP ARG ILE ARG LYS TRP TYR TYR ASN ALA ALA GLY PHE
SEQRES 3 S 110 ASN LYS TYR GLY LEU MET ARG ASP ASP THR LEU TYR GLU
SEQRES 4 S 110 ASP ASP ASP VAL LYS GLU ALA LEU LYS ARG LEU PRO GLU
SEQRES 5 S 110 ASP LEU TYR ASN GLU ARG MET PHE ARG ILE LYS ARG ALA
SEQRES 6 S 110 LEU ASP LEU SER LEU LYS HIS ARG ILE LEU PRO LYS GLU
SEQRES 7 S 110 GLN TRP VAL LYS TYR GLU GLU ASP LYS PRO TYR LEU GLU
SEQRES 8 S 110 PRO TYR LEU LYS GLU VAL ILE ARG GLU ARG LEU GLU ARG
SEQRES 9 S 110 GLU ALA TRP ASN LYS LYS
SEQRES 1 T 81 GLY ILE HIS PHE GLY ASN LEU ALA ARG VAL ARG HIS ILE
SEQRES 2 T 81 ILE THR TYR SER LEU SER PRO PHE GLU GLN ARG ALA ILE
SEQRES 3 T 81 PRO ASN ILE PHE SER ASP ALA LEU PRO ASN VAL TRP ARG
SEQRES 4 T 81 ARG PHE SER SER GLN VAL PHE LYS VAL ALA PRO PRO PHE
SEQRES 5 T 81 LEU GLY ALA TYR LEU LEU TYR SER TRP GLY THR GLN GLU
SEQRES 6 T 81 PHE GLU ARG LEU LYS ARG LYS ASN PRO ALA ASP TYR GLU
SEQRES 7 T 81 ASN ASP GLN
SEQRES 1 U 77 LEU ARG GLY SER GLY GLU GLU GLU GLU GLU GLU LEU VAL
SEQRES 2 U 77 ASP PRO LEU THR THR ILE ARG GLU HIS CYS GLU GLN THR
SEQRES 3 U 77 GLU LYS CYS VAL LYS ALA ARG GLU ARG LEU GLU LEU CYS
SEQRES 4 U 77 ASP ALA ARG VAL SER SER ARG SER HIS THR GLU GLU GLN
SEQRES 5 U 77 CYS THR GLU GLU LEU PHE ASP PHE LEU HIS ALA ARG ASP
SEQRES 6 U 77 HIS CYS VAL ALA HIS LYS LEU PHE ASN LYS LEU LYS
SEQRES 1 V 47 UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK
SEQRES 2 V 47 UNK UNK ARG PRO LEU LEU CYS ARG GLU SER MET SER GLY
SEQRES 3 V 47 ARG SER ALA ARG ARG ASP LEU VAL ALA GLY ILE SER LEU
SEQRES 4 V 47 ASN ALA PRO ALA SER VAL ARG TYR
SEQRES 1 W 61 ALA LEU LEU ARG GLN ALA TYR SER ALA LEU PHE ARG ARG
SEQRES 2 W 61 THR SER THR PHE ALA LEU THR VAL VAL LEU GLY ALA VAL
SEQRES 3 W 61 LEU PHE GLU ARG ALA PHE ASP GLN GLY ALA ASP ALA ILE
SEQRES 4 W 61 PHE GLU HIS LEU ASN GLU GLY LYS LEU TRP LYS HIS ILE
SEQRES 5 W 61 LYS HIS LYS TYR GLU ALA SER GLU GLU
HET PEE A2008 21
HET UNL A3016 1
HET HEM C 501 43
HET HEM C 502 43
HET SMA C2001 37
HET ANY C2002 37
HET CDL C2004 40
HET PEE C2007 49
HET UNL C2010 1
HET GOL C2011 6
HET UNL C2104 1
HET UNL C3015 1
HET HEC D 501 43
HET CDL D2003 50
HET FES E 501 4
HET PEE E2005 50
HET PLC E2009 32
HET UNL E2105 1
HET UNL E3103 1
HET PEE N3008 5
HET HEM P 501 43
HET HEM P 502 43
HET UNL P2015 1
HET SMA P3001 37
HET ANY P3002 37
HET CDL P3004 40
HET PEE P3005 50
HET PEE P3007 49
HET UNL P3010 1
HET GOL P3011 6
HET UNL P3104 1
HET HEC Q 501 43
HET CDL Q3003 50
HET FES R 501 4
HET UNL R2103 1
HET PLC R3009 32
HETNAM PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE
HETNAM UNL UNKNOWN LIGAND
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM SMA STIGMATELLIN A
HETNAM ANY 2-METHYL-BUTYRIC ACID 3-(3-FORMYLAMINO-2-HYDROXY-
HETNAM 2 ANY BENZOYLAMINO)-8-HEPTYL-2,6-DIMETHYL-4,9-DIOXO-[1,
HETNAM 3 ANY 5]DIOXONAN-7-YL ESTER
HETNAM CDL CARDIOLIPIN
HETNAM GOL GLYCEROL
HETNAM HEC HEME C
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM PLC DIUNDECYL PHOSPHATIDYL CHOLINE
HETSYN PEE DOPE
HETSYN HEM HEME
HETSYN ANY ANTIMYCIN
HETSYN CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-
HETSYN 2 CDL PHOSPHO)-1',3'-SN-GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 21 PEE 6(C41 H78 N O8 P)
FORMUL 23 HEM 4(C34 H32 FE N4 O4)
FORMUL 25 SMA 2(C30 H42 O7)
FORMUL 26 ANY 2(C29 H42 N2 O9)
FORMUL 27 CDL 4(C81 H156 O17 P2 2-)
FORMUL 30 GOL 2(C3 H8 O3)
FORMUL 33 HEC 2(C34 H34 FE N4 O4)
FORMUL 35 FES 2(FE2 S2)
FORMUL 37 PLC 2(C32 H65 N O8 P 1+)
HELIX 1 1 THR A 3 ILE A 11 1 9
HELIX 2 2 TYR A 57 ALA A 63 1 7
HELIX 3 3 PRO A 71 SER A 81 1 11
HELIX 4 4 ASP A 105 GLN A 118 1 14
HELIX 5 5 GLU A 123 ASP A 142 1 20
HELIX 6 6 ASP A 144 PHE A 158 1 15
HELIX 7 7 THR A 170 LEU A 177 1 8
HELIX 8 8 THR A 178 PHE A 190 1 13
HELIX 9 9 LYS A 191 ARG A 194 5 4
HELIX 10 10 SER A 204 PHE A 216 1 13
HELIX 11 11 TYR A 223 ALA A 227 5 5
HELIX 12 12 PRO A 265 ILE A 277 1 13
HELIX 13 13 GLY A 286 LEU A 290 5 5
HELIX 14 14 SER A 292 HIS A 301 1 10
HELIX 15 15 SER A 330 THR A 349 1 20
HELIX 16 16 THR A 350 GLN A 368 1 19
HELIX 17 17 GLY A 371 GLY A 387 1 17
HELIX 18 18 SER A 391 VAL A 402 1 12
HELIX 19 19 ASP A 403 TYR A 416 1 14
HELIX 20 20 ASP A 433 GLY A 440 1 8
HELIX 21 21 GLY B 64 ALA B 72 1 9
HELIX 22 22 SER B 81 ALA B 91 1 11
HELIX 23 23 LEU B 112 ASP B 114 5 3
HELIX 24 24 HIS B 115 ALA B 129 1 15
HELIX 25 25 ARG B 133 GLN B 141 1 9
HELIX 26 26 GLN B 143 PHE B 152 1 10
HELIX 27 27 SER B 154 ALA B 167 1 14
HELIX 28 28 THR B 170 ASN B 174 5 5
HELIX 29 29 THR B 187 ASN B 197 1 11
HELIX 30 30 LYS B 212 LEU B 224 1 13
HELIX 31 31 SER B 266 GLY B 280 1 15
HELIX 32 32 SER B 293 LYS B 301 1 9
HELIX 33 33 HIS B 332 ALA B 346 1 15
HELIX 34 34 THR B 353 SER B 371 1 19
HELIX 35 35 THR B 374 SER B 389 1 16
HELIX 36 36 SER B 396 SER B 404 1 9
HELIX 37 37 THR B 406 GLY B 420 1 15
HELIX 38 38 PHE B 435 LEU B 439 5 5
HELIX 39 39 ASN C 4 HIS C 9 1 6
HELIX 40 40 LEU C 11 ILE C 20 1 10
HELIX 41 41 SER C 29 TRP C 32 5 4
HELIX 42 42 ASN C 33 MET C 54 1 22
HELIX 43 43 ASP C 59 ASN C 73 1 15
HELIX 44 44 TYR C 76 TYR C 105 1 30
HELIX 45 45 GLY C 106 LEU C 109 5 4
HELIX 46 46 TYR C 110 LEU C 134 1 25
HELIX 47 47 GLY C 137 LEU C 150 1 14
HELIX 48 48 PHE C 151 ILE C 154 5 4
HELIX 49 49 TYR C 156 GLY C 167 1 12
HELIX 50 50 ASP C 172 GLY C 205 1 34
HELIX 51 51 SER C 214 SER C 216 5 3
HELIX 52 52 PHE C 221 SER C 247 1 27
HELIX 53 53 ASP C 253 THR C 258 5 6
HELIX 54 54 GLU C 272 TYR C 274 5 3
HELIX 55 55 PHE C 275 ILE C 285 1 11
HELIX 56 56 ASN C 287 ILE C 301 1 15
HELIX 57 57 LEU C 302 LEU C 308 5 7
HELIX 58 58 THR C 315 PHE C 318 5 4
HELIX 59 59 ARG C 319 SER C 341 1 23
HELIX 60 60 PRO C 347 ILE C 365 1 19
HELIX 61 61 ILE C 365 ASN C 379 1 15
HELIX 62 62 ASP D 22 CYS D 37 1 16
HELIX 63 63 ALA D 47 ILE D 52 1 6
HELIX 64 64 THR D 57 GLU D 67 1 11
HELIX 65 65 ASN D 97 ALA D 104 1 8
HELIX 66 66 TYR D 115 ARG D 120 1 6
HELIX 67 67 GLY D 123 TYR D 134 1 12
HELIX 68 68 THR D 178 GLU D 195 1 18
HELIX 69 69 GLU D 197 ARG D 233 1 37
HELIX 70 70 ARG E 15 MET E 19 5 5
HELIX 71 71 SER E 24 THR E 27 5 4
HELIX 72 72 SER E 28 SER E 61 1 34
HELIX 73 73 THR E 102 ASN E 107 1 6
HELIX 74 74 ARG F 11 GLY F 25 1 15
HELIX 75 75 PHE F 26 TYR F 29 5 4
HELIX 76 76 MET F 32 LEU F 37 1 6
HELIX 77 77 ASP F 40 LEU F 50 1 11
HELIX 78 78 PRO F 51 HIS F 72 1 22
HELIX 79 79 PRO F 76 TRP F 80 5 5
HELIX 80 80 LYS F 82 ASP F 86 5 5
HELIX 81 81 LEU F 90 ASN F 108 1 19
HELIX 82 82 PRO G 20 GLN G 23 5 4
HELIX 83 83 ASP G 32 LEU G 69 1 38
HELIX 84 84 ASN G 73 TYR G 77 5 5
HELIX 85 85 ASP H 15 GLN H 26 1 12
HELIX 86 86 THR H 27 ARG H 47 1 21
HELIX 87 87 CYS H 54 HIS H 71 1 18
HELIX 88 88 CYS I 51 SER I 56 1 6
HELIX 89 89 ALA J 4 LEU J 13 1 10
HELIX 90 90 ARG J 16 ASN J 47 1 32
HELIX 91 91 LEU J 51 LYS J 56 1 6
HELIX 92 92 HIS J 57 TYR J 59 5 3
HELIX 93 93 THR N 3 ILE N 11 1 9
HELIX 94 94 TYR N 57 ALA N 63 1 7
HELIX 95 95 PRO N 71 SER N 81 1 11
HELIX 96 96 ASP N 105 GLN N 118 1 14
HELIX 97 97 GLU N 123 ASP N 142 1 20
HELIX 98 98 ASP N 144 PHE N 158 1 15
HELIX 99 99 THR N 170 LEU N 177 1 8
HELIX 100 100 THR N 178 PHE N 190 1 13
HELIX 101 101 LYS N 191 ARG N 194 5 4
HELIX 102 102 SER N 204 PHE N 216 1 13
HELIX 103 103 TYR N 223 ALA N 227 5 5
HELIX 104 104 PRO N 265 ILE N 277 1 13
HELIX 105 105 GLY N 286 LEU N 290 5 5
HELIX 106 106 SER N 292 HIS N 301 1 10
HELIX 107 107 SER N 330 THR N 349 1 20
HELIX 108 108 THR N 350 GLN N 368 1 19
HELIX 109 109 GLY N 371 GLY N 387 1 17
HELIX 110 110 SER N 391 VAL N 402 1 12
HELIX 111 111 ASP N 403 TYR N 416 1 14
HELIX 112 112 ASP N 433 GLY N 440 1 8
HELIX 113 113 GLY O 64 ALA O 72 1 9
HELIX 114 114 SER O 81 ALA O 91 1 11
HELIX 115 115 LEU O 112 ASP O 114 5 3
HELIX 116 116 HIS O 115 ALA O 129 1 15
HELIX 117 117 ARG O 133 GLN O 141 1 9
HELIX 118 118 GLN O 143 PHE O 152 1 10
HELIX 119 119 SER O 154 ALA O 167 1 14
HELIX 120 120 THR O 170 ASN O 174 5 5
HELIX 121 121 THR O 187 ASN O 197 1 11
HELIX 122 122 LYS O 212 LEU O 224 1 13
HELIX 123 123 ALA O 267 GLY O 280 1 14
HELIX 124 124 SER O 293 LYS O 301 1 9
HELIX 125 125 HIS O 332 ALA O 346 1 15
HELIX 126 126 THR O 353 VAL O 372 1 20
HELIX 127 127 THR O 374 SER O 389 1 16
HELIX 128 128 SER O 396 SER O 404 1 9
HELIX 129 129 THR O 406 GLY O 420 1 15
HELIX 130 130 PHE O 435 LEU O 439 5 5
HELIX 131 131 ASN P 4 HIS P 9 1 6
HELIX 132 132 LEU P 11 ILE P 20 1 10
HELIX 133 133 SER P 29 TRP P 32 5 4
HELIX 134 134 ASN P 33 MET P 54 1 22
HELIX 135 135 ASP P 59 ASN P 73 1 15
HELIX 136 136 TYR P 76 TYR P 105 1 30
HELIX 137 137 GLY P 106 LEU P 109 5 4
HELIX 138 138 TYR P 110 LEU P 134 1 25
HELIX 139 139 GLY P 137 LEU P 150 1 14
HELIX 140 140 PHE P 151 ILE P 154 5 4
HELIX 141 141 GLY P 158 GLY P 167 1 10
HELIX 142 142 ASP P 172 GLY P 205 1 34
HELIX 143 143 SER P 214 SER P 216 5 3
HELIX 144 144 PRO P 223 SER P 247 1 25
HELIX 145 145 ASP P 253 THR P 258 5 6
HELIX 146 146 GLU P 272 TYR P 274 5 3
HELIX 147 147 PHE P 275 ILE P 285 1 11
HELIX 148 148 ASN P 287 ILE P 301 1 15
HELIX 149 149 LEU P 302 LEU P 308 5 7
HELIX 150 150 THR P 315 PHE P 318 5 4
HELIX 151 151 ARG P 319 SER P 341 1 23
HELIX 152 152 PRO P 347 ILE P 365 1 19
HELIX 153 153 ILE P 365 ASN P 379 1 15
HELIX 154 154 ASP Q 22 CYS Q 37 1 16
HELIX 155 155 ALA Q 47 LEU Q 51 5 5
HELIX 156 156 THR Q 57 GLU Q 67 1 11
HELIX 157 157 ASN Q 97 ALA Q 104 1 8
HELIX 158 158 TYR Q 115 ARG Q 120 1 6
HELIX 159 159 GLY Q 123 TYR Q 134 1 12
HELIX 160 160 THR Q 178 ALA Q 193 1 16
HELIX 161 161 ALA Q 194 PRO Q 196 5 3
HELIX 162 162 GLU Q 197 SER Q 232 1 36
HELIX 163 163 ARG R 15 MET R 19 5 5
HELIX 164 164 SER R 24 THR R 27 5 4
HELIX 165 165 SER R 28 SER R 61 1 34
HELIX 166 166 THR R 102 ASN R 107 1 6
HELIX 167 167 HIS R 122 VAL R 127 1 6
HELIX 168 168 LEU S 12 GLY S 25 1 14
HELIX 169 169 PHE S 26 GLY S 30 5 5
HELIX 170 170 MET S 32 LEU S 37 1 6
HELIX 171 171 ASP S 40 LEU S 50 1 11
HELIX 172 172 PRO S 51 HIS S 72 1 22
HELIX 173 173 PRO S 76 TRP S 80 5 5
HELIX 174 174 LYS S 82 ASP S 86 5 5
HELIX 175 175 LEU S 90 LYS S 110 1 21
HELIX 176 176 PRO T 20 GLN T 23 5 4
HELIX 177 177 ASP T 32 LEU T 69 1 38
HELIX 178 178 ASN T 73 TYR T 77 5 5
HELIX 179 179 ASP U 15 GLN U 26 1 12
HELIX 180 180 THR U 27 ARG U 47 1 21
HELIX 181 181 CYS U 54 HIS U 71 1 18
HELIX 182 182 CYS V 51 MET V 55 5 5
HELIX 183 183 ALA W 4 LEU W 13 1 10
HELIX 184 184 ARG W 16 ASN W 47 1 32
HELIX 185 185 LEU W 51 LYS W 56 1 6
HELIX 186 186 HIS W 57 TYR W 59 5 3
SHEET 1 A 6 ASN A 15 THR A 18 0
SHEET 2 A 6 ARG A 24 GLU A 29 -1 O VAL A 25 N THR A 17
SHEET 3 A 6 VAL A 196 GLY A 201 1 O LEU A 197 N ALA A 26
SHEET 4 A 6 THR A 34 VAL A 39 -1 N GLY A 38 O ALA A 198
SHEET 5 A 6 THR A 95 LEU A 102 -1 O ILE A 99 N VAL A 37
SHEET 6 A 6 HIS A 85 THR A 90 -1 N HIS A 85 O LYS A 100
SHEET 1 B 8 ARG A 279 ASP A 281 0
SHEET 2 B 8 SER A 306 SER A 313 -1 O PHE A 307 N TYR A 280
SHEET 3 B 8 GLY A 318 ALA A 326 -1 O LEU A 319 N THR A 312
SHEET 4 B 8 ALA A 251 GLU A 258 -1 N VAL A 257 O PHE A 320
SHEET 5 B 8 ALA A 421 GLY A 426 -1 O VAL A 425 N HIS A 252
SHEET 6 B 8 SER A 239 ASP A 245 1 N ALA A 243 O ALA A 424
SHEET 7 B 8 ARG G 11 LEU G 18 -1 O THR G 15 N ARG A 242
SHEET 8 B 8 LYS D 234 ALA D 236 -1 N LYS D 234 O TYR G 16
SHEET 1 C 6 MET B 204 VAL B 207 0
SHEET 2 C 6 GLY B 48 ILE B 51 -1 N PHE B 50 O ALA B 205
SHEET 3 C 6 LYS B 104 VAL B 109 -1 O MET B 105 N ILE B 51
SHEET 4 C 6 LEU B 96 THR B 101 -1 N TYR B 99 O THR B 106
SHEET 5 C 6 ALA I 66 SER I 69 -1 O ILE I 68 N VAL B 98
SHEET 6 C 6 ALA I 74 VAL I 76 -1 O SER I 75 N GLY I 67
SHEET 1 D 5 GLU B 243 ARG B 245 0
SHEET 2 D 5 LYS B 422 SER B 427 1 O MET B 424 N ILE B 244
SHEET 3 D 5 LEU B 252 GLU B 260 -1 N VAL B 258 O SER B 423
SHEET 4 D 5 SER B 319 GLN B 329 -1 O PHE B 322 N THR B 259
SHEET 5 D 5 PHE B 307 TYR B 316 -1 N PHE B 312 O GLY B 323
SHEET 1 E 2 PRO C 23 PRO C 25 0
SHEET 2 E 2 LYS C 218 PRO C 220 -1 O ILE C 219 N ALA C 24
SHEET 1 F 2 GLU D 69 ASP D 72 0
SHEET 2 F 2 PHE D 81 PRO D 84 -1 O ARG D 83 N VAL D 70
SHEET 1 G 2 HIS D 148 TYR D 149 0
SHEET 2 G 2 ALA D 157 ILE D 158 -1 O ILE D 158 N HIS D 148
SHEET 1 H 3 ILE E 74 LYS E 77 0
SHEET 2 H 3 LEU E 192 VAL E 195 -1 O VAL E 193 N ILE E 76
SHEET 3 H 3 TYR E 185 GLN E 186 -1 N GLN E 186 O VAL E 194
SHEET 1 I 3 ASN E 86 ALA E 88 0
SHEET 2 I 3 PHE E 97 HIS E 100 -1 O VAL E 98 N VAL E 87
SHEET 3 I 3 TRP E 132 LEU E 135 -1 O VAL E 133 N ARG E 99
SHEET 1 J 4 ILE E 147 ALA E 148 0
SHEET 2 J 4 GLY E 154 CYS E 158 -1 O TYR E 157 N ILE E 147
SHEET 3 J 4 SER E 163 ASP E 166 -1 O TYR E 165 N TYR E 156
SHEET 4 J 4 ILE E 171 LYS E 173 -1 O LYS E 173 N HIS E 164
SHEET 1 K 6 ASN N 15 THR N 18 0
SHEET 2 K 6 ARG N 24 GLU N 29 -1 O VAL N 25 N THR N 17
SHEET 3 K 6 VAL N 196 GLY N 201 1 O LEU N 197 N ALA N 26
SHEET 4 K 6 THR N 34 VAL N 39 -1 N GLY N 38 O ALA N 198
SHEET 5 K 6 GLN N 94 LEU N 102 -1 O ILE N 99 N VAL N 37
SHEET 6 K 6 HIS N 85 SER N 91 -1 N SER N 91 O GLN N 94
SHEET 1 L 8 ARG N 279 ASP N 281 0
SHEET 2 L 8 SER N 306 SER N 313 -1 O PHE N 307 N TYR N 280
SHEET 3 L 8 GLY N 318 ALA N 326 -1 O VAL N 325 N SER N 306
SHEET 4 L 8 ALA N 251 GLU N 258 -1 N VAL N 257 O PHE N 320
SHEET 5 L 8 ALA N 421 GLY N 426 -1 O ALA N 421 N ALA N 256
SHEET 6 L 8 SER N 239 ASP N 245 1 N ALA N 243 O ALA N 424
SHEET 7 L 8 ARG T 11 LEU T 18 -1 O THR T 15 N ARG N 242
SHEET 8 L 8 LYS Q 234 ALA Q 236 -1 N LYS Q 234 O TYR T 16
SHEET 1 M 2 THR O 27 LYS O 28 0
SHEET 2 M 2 ILE O 34 ILE O 35 -1 O ILE O 35 N THR O 27
SHEET 1 N 7 SER O 37 LEU O 38 0
SHEET 2 N 7 MET O 204 ILE O 209 1 O GLY O 208 N LEU O 38
SHEET 3 N 7 ARG O 46 ILE O 51 -1 N PHE O 50 O ALA O 205
SHEET 4 N 7 LYS O 104 VAL O 109 -1 O MET O 105 N ILE O 51
SHEET 5 N 7 LEU O 96 THR O 101 -1 N TYR O 99 O THR O 106
SHEET 6 N 7 ALA V 66 SER V 69 -1 O ILE V 68 N VAL O 98
SHEET 7 N 7 ALA V 74 VAL V 76 -1 O SER V 75 N GLY V 67
SHEET 1 O 5 GLU O 243 GLN O 247 0
SHEET 2 O 5 LYS O 422 GLY O 428 1 O MET O 424 N ILE O 244
SHEET 3 O 5 LEU O 252 GLU O 260 -1 N VAL O 258 O SER O 423
SHEET 4 O 5 SER O 319 GLN O 329 -1 O THR O 326 N ALA O 255
SHEET 5 O 5 PHE O 307 TYR O 316 -1 N PHE O 312 O GLY O 323
SHEET 1 P 2 PRO P 23 PRO P 25 0
SHEET 2 P 2 LYS P 218 PRO P 220 -1 O ILE P 219 N ALA P 24
SHEET 1 Q 2 GLU Q 69 ASP Q 72 0
SHEET 2 Q 2 PHE Q 81 PRO Q 84 -1 O ARG Q 83 N VAL Q 70
SHEET 1 R 2 HIS Q 148 TYR Q 149 0
SHEET 2 R 2 ALA Q 157 ILE Q 158 -1 O ILE Q 158 N HIS Q 148
SHEET 1 S 3 ILE R 74 LYS R 77 0
SHEET 2 S 3 LEU R 192 VAL R 195 -1 O VAL R 193 N ILE R 76
SHEET 3 S 3 TYR R 185 GLN R 186 -1 N GLN R 186 O VAL R 194
SHEET 1 T 3 LYS R 85 ALA R 88 0
SHEET 2 T 3 PHE R 97 HIS R 100 -1 O HIS R 100 N LYS R 85
SHEET 3 T 3 TRP R 132 LEU R 135 -1 O VAL R 133 N ARG R 99
SHEET 1 U 4 ILE R 147 ALA R 148 0
SHEET 2 U 4 GLY R 154 CYS R 158 -1 O TYR R 157 N ILE R 147
SHEET 3 U 4 SER R 163 ASP R 166 -1 O TYR R 165 N TYR R 156
SHEET 4 U 4 ILE R 171 LYS R 173 -1 O LYS R 173 N HIS R 164
SSBOND 1 CYS E 144 CYS E 160 1555 1555 2.03
SSBOND 2 CYS H 24 CYS H 68 1555 1555 2.02
SSBOND 3 CYS H 40 CYS H 54 1555 1555 2.03
SSBOND 4 CYS R 144 CYS R 160 1555 1555 2.02
SSBOND 5 CYS U 24 CYS U 68 1555 1555 2.03
SSBOND 6 CYS U 40 CYS U 54 1555 1555 2.04
LINK NE2 HIS C 84 FE HEM C 501 1555 1555 2.00
LINK NE2 HIS C 98 FE HEM C 502 1555 1555 2.01
LINK NE2 HIS C 183 FE HEM C 501 1555 1555 1.99
LINK NE2 HIS C 197 FE HEM C 502 1555 1555 2.01
LINK NE2 HIS D 41 FE HEC D 501 1555 1555 2.00
LINK SD MET D 160 FE HEC D 501 1555 1555 2.13
LINK SG CYS E 139 FE1 FES E 501 1555 1555 2.26
LINK ND1 HIS E 141 FE2 FES E 501 1555 1555 2.07
LINK SG CYS E 158 FE1 FES E 501 1555 1555 2.25
LINK ND1 HIS E 161 FE2 FES E 501 1555 1555 2.07
LINK NE2 HIS P 84 FE HEM P 501 1555 1555 2.00
LINK NE2 HIS P 98 FE HEM P 502 1555 1555 2.02
LINK NE2 HIS P 183 FE HEM P 501 1555 1555 2.01
LINK NE2 HIS P 197 FE HEM P 502 1555 1555 2.00
LINK NE2 HIS Q 41 FE HEC Q 501 1555 1555 2.01
LINK SD MET Q 160 FE HEC Q 501 1555 1555 2.10
LINK SG CYS R 139 FE1 FES R 501 1555 1555 2.27
LINK ND1 HIS R 141 FE2 FES R 501 1555 1555 2.10
LINK SG CYS R 158 FE1 FES R 501 1555 1555 2.24
LINK ND1 HIS R 161 FE2 FES R 501 1555 1555 2.10
CISPEP 1 HIS C 222 PRO C 223 0 0.35
CISPEP 2 HIS C 346 PRO C 347 0 0.03
CISPEP 3 GLY D 73 PRO D 74 0 0.17
CISPEP 4 ALA P 2 PRO P 3 0 -0.06
CISPEP 5 HIS P 222 PRO P 223 0 0.24
CISPEP 6 HIS P 346 PRO P 347 0 -0.08
CISPEP 7 GLY Q 73 PRO Q 74 0 0.16
SITE 1 AC1 18 GLN C 45 ILE C 46 GLY C 49 LEU C 52
SITE 2 AC1 18 ALA C 53 TYR C 56 ARG C 81 HIS C 84
SITE 3 AC1 18 ALA C 85 LEU C 124 THR C 127 GLY C 131
SITE 4 AC1 18 TYR C 132 LEU C 134 PRO C 135 HIS C 183
SITE 5 AC1 18 PHE C 184 PRO C 187
SITE 1 AC2 20 TRP C 32 GLY C 35 LEU C 38 ALA C 39
SITE 2 AC2 20 HIS C 98 ARG C 101 SER C 107 THR C 113
SITE 3 AC2 20 TRP C 114 GLY C 117 VAL C 118 LEU C 120
SITE 4 AC2 20 LEU C 121 ILE C 190 THR C 194 HIS C 197
SITE 5 AC2 20 LEU C 201 SER C 206 ASN C 207 ANY C2002
SITE 1 AC3 14 VAL D 32 VAL D 36 CYS D 37 CYS D 40
SITE 2 AC3 14 HIS D 41 ASN D 105 ALA D 108 PRO D 110
SITE 3 AC3 14 ARG D 120 TYR D 126 PHE D 153 GLY D 159
SITE 4 AC3 14 MET D 160 PRO D 163
SITE 1 AC4 7 CYS E 139 HIS E 141 LEU E 142 CYS E 144
SITE 2 AC4 7 CYS E 158 HIS E 161 SER E 163
SITE 1 AC5 17 GLN P 45 ILE P 46 GLY P 49 LEU P 52
SITE 2 AC5 17 ALA P 53 ARG P 81 HIS P 84 ALA P 85
SITE 3 AC5 17 LEU P 124 THR P 127 GLY P 131 TYR P 132
SITE 4 AC5 17 LEU P 134 PRO P 135 HIS P 183 PHE P 184
SITE 5 AC5 17 PRO P 187
SITE 1 AC6 18 TRP P 32 GLY P 35 LEU P 38 ALA P 39
SITE 2 AC6 18 HIS P 98 ARG P 101 SER P 107 THR P 113
SITE 3 AC6 18 TRP P 114 GLY P 117 VAL P 118 LEU P 120
SITE 4 AC6 18 LEU P 121 THR P 194 HIS P 197 LEU P 201
SITE 5 AC6 18 ASN P 207 ANY P3002
SITE 1 AC7 14 VAL Q 32 VAL Q 36 CYS Q 37 CYS Q 40
SITE 2 AC7 14 HIS Q 41 ASN Q 105 ALA Q 108 PRO Q 110
SITE 3 AC7 14 ARG Q 120 TYR Q 126 PHE Q 153 GLY Q 159
SITE 4 AC7 14 MET Q 160 PRO Q 163
SITE 1 AC8 8 CYS R 139 HIS R 141 LEU R 142 GLY R 143
SITE 2 AC8 8 CYS R 144 CYS R 158 HIS R 161 SER R 163
SITE 1 AC9 12 LEU C 122 MET C 125 ALA C 126 PHE C 129
SITE 2 AC9 12 GLY C 143 VAL C 146 ILE C 147 PRO C 271
SITE 3 AC9 12 GLU C 272 PHE C 275 TYR C 279 HIS R 161
SITE 1 BC1 14 SER C 18 LEU C 19 ILE C 28 TRP C 32
SITE 2 BC1 14 SER C 36 ALA C 39 LEU C 42 THR C 194
SITE 3 BC1 14 ILE C 195 LEU C 198 PHE C 221 TYR C 225
SITE 4 BC1 14 ASP C 229 HEM C 502
SITE 1 BC2 12 ALA C 30 ASN C 33 LEU C 231 GLY C 232
SITE 2 BC2 12 MET C 236 CDL C2004 TYR D 220 LYS D 223
SITE 3 BC2 12 ARG D 224 HIS F 72 ARG F 73 ARG G 40
SITE 1 BC3 8 SER C 29 ALA C 30 TRP C 31 PEE C2007
SITE 2 BC3 8 CDL D2003 ARG G 40 PHE G 41 GLN G 44
SITE 1 BC4 8 PEE A2008 PHE C 227 ILE C 230 LYS D 226
SITE 2 BC4 8 TYR E 37 THR E 40 THR E 47 PHE J 14
SITE 1 BC5 11 TRP C 31 PHE C 96 ARG C 101 TYR C 104
SITE 2 BC5 11 TYR C 105 PHE C 277 THR C 317 TRP C 327
SITE 3 BC5 11 CDL C2004 TYR F 29 GLN G 44
SITE 1 BC6 3 TYR A 442 HIS C 222 PEE E2005
SITE 1 BC7 11 LEU C 79 LEU C 241 GLN D 200 MET D 204
SITE 2 BC7 11 LYS D 207 MET D 208 TYR E 49 ALA E 50
SITE 3 BC7 11 VAL E 54 GLN E 57 ASP J 36
SITE 1 BC8 5 PHE C 64 ARG C 81 ASN C 256 PHE C 257
SITE 2 BC8 5 TYR D 115
SITE 1 BC9 1 THR P 199
SITE 1 CC1 1 THR R 140
SITE 1 CC2 1 ASN C 149
SITE 1 CC3 1 TYR E 178
SITE 1 CC4 14 HIS E 161 LEU P 122 MET P 125 ALA P 126
SITE 2 CC4 14 PHE P 129 GLY P 143 VAL P 146 ILE P 147
SITE 3 CC4 14 LEU P 182 LYS P 270 PRO P 271 GLU P 272
SITE 4 CC4 14 PHE P 275 TYR P 279
SITE 1 CC5 13 LEU P 19 ILE P 28 TRP P 32 SER P 36
SITE 2 CC5 13 ALA P 39 LEU P 42 THR P 194 ILE P 195
SITE 3 CC5 13 LEU P 198 PHE P 221 TYR P 225 ASP P 229
SITE 4 CC5 13 HEM P 502
SITE 1 CC6 12 ALA P 30 ASN P 33 LEU P 231 GLY P 232
SITE 2 CC6 12 MET P 236 CDL P3004 TYR Q 220 LYS Q 223
SITE 3 CC6 12 ARG Q 224 HIS S 72 ARG S 73 ARG T 40
SITE 1 CC7 9 SER P 29 ALA P 30 TRP P 31 PEE P3007
SITE 2 CC7 9 CDL Q3003 HIS S 72 ARG T 40 PHE T 41
SITE 3 CC7 9 GLN T 44
SITE 1 CC8 8 PHE P 227 ILE P 230 LYS Q 226 TYR R 37
SITE 2 CC8 8 THR R 40 THR R 47 PHE W 14 GLU W 32
SITE 1 CC9 12 TRP P 31 PHE P 96 ARG P 101 TYR P 104
SITE 2 CC9 12 TYR P 105 PHE P 277 THR P 317 TRP P 327
SITE 3 CC9 12 LEU P 333 CDL P3004 TYR S 29 GLN T 44
SITE 1 DC1 2 TYR N 442 HIS P 222
SITE 1 DC2 10 THR P 44 TYR P 76 LEU P 79 GLN Q 200
SITE 2 DC2 10 MET Q 204 LYS Q 207 TYR R 49 ALA R 50
SITE 3 DC2 10 VAL R 54 GLN R 57
SITE 1 DC3 1 ALA P 85
SITE 1 DC4 4 PHE P 64 ARG P 81 ASN P 256 TYR Q 115
SITE 1 DC5 2 THR C 199 HIS C 202
SITE 1 DC6 1 THR E 140
SITE 1 DC7 2 ASN P 149 HIS P 159
CRYST1 174.693 181.666 240.732 90.00 90.00 90.00 P 21 21 21 8
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 0.005724 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005505 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004154 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
