HEADER OXIDOREDUCTASE 01-MAR-05 1Z01
TITLE 2-OXOQUINOLINE 8-MONOOXYGENASE COMPONENT: ACTIVE SITE MODULATION BY
TITLE 2 RIESKE-[2FE-2S] CENTER OXIDATION/REDUCTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-OXO-1,2-DIHYDROQUINOLINE 8-MONOOXYGENASE, OXYGENASE
COMPND 3 COMPONENT;
COMPND 4 CHAIN: A, B, C, D, E, F;
COMPND 5 EC: 1.14.13.61
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303
KEYWDS MONOOXYGENASE, RIESKE CENTER, OXYGEN BINDING/ACTIVATION, SUBSTRATE
KEYWDS 2 BOUND COMPLEX, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.M.MARTINS,T.SVETLITCHNAIA,H.DOBBEK
REVDAT 5 13-MAR-24 1Z01 1 REMARK LINK
REVDAT 4 18-JUL-18 1Z01 1 REMARK
REVDAT 3 11-OCT-17 1Z01 1 REMARK
REVDAT 2 24-FEB-09 1Z01 1 VERSN
REVDAT 1 24-MAY-05 1Z01 0
JRNL AUTH B.M.MARTINS,T.SVETLITCHNAIA,H.DOBBEK
JRNL TITL 2-OXOQUINOLINE 8-MONOOXYGENASE OXYGENASE COMPONENT: ACTIVE
JRNL TITL 2 SITE MODULATION BY RIESKE-[2FE-2S] CENTER
JRNL TITL 3 OXIDATION/REDUCTION
JRNL REF STRUCTURE V. 13 817 2005
JRNL REFN ISSN 0969-2126
JRNL PMID 15893671
JRNL DOI 10.1016/J.STR.2005.03.008
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 275820
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 13790
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20724
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 3763
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Z01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 275832
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
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 52.23000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.73000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 83.48000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.73000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.23000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 83.48000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 89870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -334.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 104.46000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -83.48000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 86.73000
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 MET A 1
REMARK 465 SER A 2
REMARK 465 ASP A 3
REMARK 465 GLN A 4
REMARK 465 PRO A 5
REMARK 465 ILE A 6
REMARK 465 ILE A 7
REMARK 465 ARG A 8
REMARK 465 ARG A 9
REMARK 465 ARG A 10
REMARK 465 GLN A 11
REMARK 465 VAL A 12
REMARK 465 LYS A 13
REMARK 465 THR A 14
REMARK 465 GLY A 15
REMARK 465 LYS A 443
REMARK 465 GLU A 444
REMARK 465 ASP A 445
REMARK 465 HIS A 446
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 ASP B 3
REMARK 465 GLN B 4
REMARK 465 PRO B 5
REMARK 465 ILE B 6
REMARK 465 ILE B 7
REMARK 465 ARG B 8
REMARK 465 ARG B 9
REMARK 465 ARG B 10
REMARK 465 GLN B 11
REMARK 465 VAL B 12
REMARK 465 LYS B 13
REMARK 465 THR B 14
REMARK 465 GLY B 15
REMARK 465 LYS B 443
REMARK 465 GLU B 444
REMARK 465 ASP B 445
REMARK 465 HIS B 446
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 ASP C 3
REMARK 465 GLN C 4
REMARK 465 PRO C 5
REMARK 465 ILE C 6
REMARK 465 ILE C 7
REMARK 465 ARG C 8
REMARK 465 ARG C 9
REMARK 465 ARG C 10
REMARK 465 GLN C 11
REMARK 465 VAL C 12
REMARK 465 LYS C 13
REMARK 465 THR C 14
REMARK 465 GLY C 15
REMARK 465 LYS C 443
REMARK 465 GLU C 444
REMARK 465 ASP C 445
REMARK 465 HIS C 446
REMARK 465 MET D 1
REMARK 465 SER D 2
REMARK 465 ASP D 3
REMARK 465 GLN D 4
REMARK 465 PRO D 5
REMARK 465 ILE D 6
REMARK 465 ILE D 7
REMARK 465 ARG D 8
REMARK 465 ARG D 9
REMARK 465 ARG D 10
REMARK 465 GLN D 11
REMARK 465 VAL D 12
REMARK 465 LYS D 13
REMARK 465 THR D 14
REMARK 465 GLY D 15
REMARK 465 LYS D 443
REMARK 465 GLU D 444
REMARK 465 ASP D 445
REMARK 465 HIS D 446
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ASP E 3
REMARK 465 GLN E 4
REMARK 465 PRO E 5
REMARK 465 ILE E 6
REMARK 465 ILE E 7
REMARK 465 ARG E 8
REMARK 465 ARG E 9
REMARK 465 ARG E 10
REMARK 465 GLN E 11
REMARK 465 VAL E 12
REMARK 465 LYS E 13
REMARK 465 THR E 14
REMARK 465 GLY E 15
REMARK 465 LYS E 443
REMARK 465 GLU E 444
REMARK 465 ASP E 445
REMARK 465 HIS E 446
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 GLN F 4
REMARK 465 PRO F 5
REMARK 465 ILE F 6
REMARK 465 ILE F 7
REMARK 465 ARG F 8
REMARK 465 ARG F 9
REMARK 465 ARG F 10
REMARK 465 GLN F 11
REMARK 465 VAL F 12
REMARK 465 LYS F 13
REMARK 465 THR F 14
REMARK 465 GLY F 15
REMARK 465 LYS F 443
REMARK 465 GLU F 444
REMARK 465 ASP F 445
REMARK 465 HIS F 446
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 GLU A 178 CG CD OE1 OE2
REMARK 470 GLU B 178 CG CD OE1 OE2
REMARK 470 GLU C 178 CG CD OE1 OE2
REMARK 470 GLU D 178 CG CD OE1 OE2
REMARK 470 GLU E 178 CG CD OE1 OE2
REMARK 470 GLU F 178 CG CD OE1 OE2
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 PRO B 239 O HOH B 1071 2.12
REMARK 500 O PRO E 239 O HOH E 980 2.19
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 ARG D 342 NE - CZ - NH2 ANGL. DEV. = 3.1 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 ALA A 36 42.75 -94.60
REMARK 500 ASN A 42 43.22 72.86
REMARK 500 HIS A 86 -74.07 -71.44
REMARK 500 PRO A 95 119.52 -38.72
REMARK 500 ASN A 125 56.30 -160.82
REMARK 500 VAL A 237 78.53 -117.37
REMARK 500 GLU A 254 37.34 -148.51
REMARK 500 HIS A 311 -7.86 77.37
REMARK 500 THR A 322 -163.01 -129.54
REMARK 500 MET A 352 -72.89 -149.89
REMARK 500 CYS A 357 -62.75 -100.83
REMARK 500 TYR A 437 -59.23 -134.83
REMARK 500 ALA B 36 45.33 -97.62
REMARK 500 ASN B 42 44.48 72.72
REMARK 500 HIS B 86 -75.43 -75.46
REMARK 500 TYR B 107 -70.12 -86.69
REMARK 500 ASN B 125 57.00 -160.06
REMARK 500 GLU B 254 36.20 -146.22
REMARK 500 GLU B 279 -99.12 -60.04
REMARK 500 LEU B 280 -39.49 -32.22
REMARK 500 LYS B 283 128.20 -172.05
REMARK 500 LEU B 287 39.55 -83.92
REMARK 500 HIS B 311 -7.22 76.47
REMARK 500 MET B 352 -68.66 -147.04
REMARK 500 CYS B 357 -62.31 -99.33
REMARK 500 VAL B 388 -167.50 -126.57
REMARK 500 TYR B 437 -57.17 -133.79
REMARK 500 ALA C 36 45.52 -97.85
REMARK 500 ASN C 42 46.89 71.78
REMARK 500 HIS C 86 -76.97 -73.22
REMARK 500 LYS C 94 77.00 -150.76
REMARK 500 THR C 121 176.24 178.11
REMARK 500 VAL C 123 -59.48 -29.80
REMARK 500 ASN C 125 55.46 -160.42
REMARK 500 ASP C 235 38.47 27.96
REMARK 500 ASP C 248 34.26 -99.56
REMARK 500 GLU C 254 33.25 -146.39
REMARK 500 LYS C 283 129.37 -171.71
REMARK 500 LEU C 287 39.35 -77.40
REMARK 500 HIS C 311 -5.56 78.71
REMARK 500 MET C 352 -72.88 -142.58
REMARK 500 CYS C 357 -64.73 -97.53
REMARK 500 VAL C 388 -167.28 -125.19
REMARK 500 TYR C 437 -55.21 -134.21
REMARK 500 ALA D 36 40.06 -92.28
REMARK 500 ASN D 42 43.11 75.69
REMARK 500 HIS D 86 -72.30 -73.43
REMARK 500 PRO D 95 119.22 -39.70
REMARK 500 VAL D 123 -58.44 -29.23
REMARK 500 ASN D 125 57.33 -158.58
REMARK 500
REMARK 500 THIS ENTRY HAS 84 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 84 SG
REMARK 620 2 FES A 500 S1 104.4
REMARK 620 3 FES A 500 S2 111.8 109.1
REMARK 620 4 CYS A 105 SG 105.1 105.3 120.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 86 ND1
REMARK 620 2 FES A 500 S1 112.2
REMARK 620 3 FES A 500 S2 115.7 105.3
REMARK 620 4 HIS A 108 ND1 96.1 115.1 112.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 221 NE2
REMARK 620 2 HIS A 225 NE2 114.1
REMARK 620 3 ASP A 365 OD1 138.3 95.3
REMARK 620 4 ASP A 365 OD2 94.3 89.1 55.6
REMARK 620 5 HOH A1169 O 95.9 108.3 102.5 154.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 84 SG
REMARK 620 2 FES B 500 S1 104.6
REMARK 620 3 FES B 500 S2 114.1 107.9
REMARK 620 4 CYS B 105 SG 105.2 108.1 116.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 86 ND1
REMARK 620 2 FES B 500 S1 111.5
REMARK 620 3 FES B 500 S2 113.8 105.1
REMARK 620 4 HIS B 108 ND1 96.2 117.4 113.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 221 NE2
REMARK 620 2 HIS B 225 NE2 108.5
REMARK 620 3 ASP B 365 OD1 146.6 92.3
REMARK 620 4 ASP B 365 OD2 95.8 93.3 56.2
REMARK 620 5 HOH B1121 O 96.3 97.8 106.7 160.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 84 SG
REMARK 620 2 FES C 500 S1 105.5
REMARK 620 3 FES C 500 S2 113.1 106.5
REMARK 620 4 CYS C 105 SG 104.1 109.7 117.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 86 ND1
REMARK 620 2 FES C 500 S1 107.0
REMARK 620 3 FES C 500 S2 116.2 106.4
REMARK 620 4 HIS C 108 ND1 95.8 118.2 113.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE C 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 221 NE2
REMARK 620 2 HIS C 225 NE2 108.3
REMARK 620 3 ASP C 365 OD1 144.2 95.8
REMARK 620 4 ASP C 365 OD2 95.6 90.3 57.3
REMARK 620 5 HOH C1104 O 97.5 114.4 96.0 146.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 84 SG
REMARK 620 2 FES D 500 S1 103.6
REMARK 620 3 FES D 500 S2 113.6 104.7
REMARK 620 4 CYS D 105 SG 107.1 107.9 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES D 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 86 ND1
REMARK 620 2 FES D 500 S1 110.8
REMARK 620 3 FES D 500 S2 114.2 106.0
REMARK 620 4 HIS D 108 ND1 93.0 120.8 112.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE D 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 221 NE2
REMARK 620 2 HIS D 225 NE2 114.8
REMARK 620 3 ASP D 365 OD1 145.1 90.3
REMARK 620 4 ASP D 365 OD2 97.9 92.2 55.3
REMARK 620 5 HOH D1164 O 92.8 96.1 108.9 162.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 84 SG
REMARK 620 2 FES E 500 S1 106.8
REMARK 620 3 FES E 500 S2 112.4 111.1
REMARK 620 4 CYS E 105 SG 105.5 105.6 114.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 86 ND1
REMARK 620 2 FES E 500 S1 111.1
REMARK 620 3 FES E 500 S2 112.3 106.7
REMARK 620 4 HIS E 108 ND1 93.1 116.7 116.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE E 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 221 NE2
REMARK 620 2 HIS E 225 NE2 109.2
REMARK 620 3 ASP E 365 OD1 142.8 93.8
REMARK 620 4 ASP E 365 OD2 91.4 96.0 56.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 500 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 84 SG
REMARK 620 2 FES F 500 S1 105.4
REMARK 620 3 FES F 500 S2 113.6 106.1
REMARK 620 4 CYS F 105 SG 106.9 107.7 116.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 500 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 86 ND1
REMARK 620 2 FES F 500 S1 109.3
REMARK 620 3 FES F 500 S2 115.4 105.3
REMARK 620 4 HIS F 108 ND1 91.9 118.8 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE F 501 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 221 NE2
REMARK 620 2 HIS F 225 NE2 111.4
REMARK 620 3 ASP F 365 OD1 143.4 92.7
REMARK 620 4 ASP F 365 OD2 94.8 91.9 55.9
REMARK 620 5 HOH F1120 O 105.8 113.9 87.7 137.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES D 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 500
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z02 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH FE(II)
REMARK 900 RELATED ID: 1Z03 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH FE(II)
DBREF 1Z01 A 1 446 UNP O05935 O05935_PSEPU 1 446
DBREF 1Z01 B 1 446 UNP O05935 O05935_PSEPU 1 446
DBREF 1Z01 C 1 446 UNP O05935 O05935_PSEPU 1 446
DBREF 1Z01 D 1 446 UNP O05935 O05935_PSEPU 1 446
DBREF 1Z01 E 1 446 UNP O05935 O05935_PSEPU 1 446
DBREF 1Z01 F 1 446 UNP O05935 O05935_PSEPU 1 446
SEQRES 1 A 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 A 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 A 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 A 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 A 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 A 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 A 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 A 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 A 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 A 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 A 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 A 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 A 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 A 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 A 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 A 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 A 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 A 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 A 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 A 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 A 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 A 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 A 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 A 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 A 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 A 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 A 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 A 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 A 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 A 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 A 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 A 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 A 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 A 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 A 446 LYS GLU ASP HIS
SEQRES 1 B 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 B 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 B 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 B 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 B 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 B 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 B 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 B 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 B 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 B 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 B 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 B 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 B 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 B 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 B 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 B 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 B 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 B 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 B 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 B 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 B 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 B 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 B 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 B 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 B 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 B 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 B 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 B 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 B 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 B 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 B 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 B 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 B 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 B 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 B 446 LYS GLU ASP HIS
SEQRES 1 C 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 C 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 C 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 C 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 C 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 C 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 C 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 C 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 C 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 C 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 C 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 C 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 C 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 C 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 C 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 C 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 C 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 C 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 C 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 C 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 C 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 C 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 C 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 C 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 C 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 C 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 C 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 C 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 C 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 C 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 C 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 C 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 C 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 C 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 C 446 LYS GLU ASP HIS
SEQRES 1 D 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 D 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 D 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 D 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 D 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 D 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 D 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 D 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 D 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 D 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 D 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 D 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 D 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 D 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 D 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 D 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 D 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 D 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 D 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 D 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 D 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 D 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 D 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 D 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 D 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 D 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 D 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 D 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 D 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 D 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 D 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 D 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 D 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 D 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 D 446 LYS GLU ASP HIS
SEQRES 1 E 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 E 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 E 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 E 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 E 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 E 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 E 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 E 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 E 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 E 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 E 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 E 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 E 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 E 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 E 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 E 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 E 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 E 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 E 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 E 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 E 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 E 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 E 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 E 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 E 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 E 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 E 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 E 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 E 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 E 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 E 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 E 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 E 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 E 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 E 446 LYS GLU ASP HIS
SEQRES 1 F 446 MET SER ASP GLN PRO ILE ILE ARG ARG ARG GLN VAL LYS
SEQRES 2 F 446 THR GLY ILE SER ASP ALA ARG ALA ASN ASN ALA LYS THR
SEQRES 3 F 446 GLN SER GLN TYR GLN PRO TYR LYS ASP ALA ALA TRP GLY
SEQRES 4 F 446 PHE ILE ASN HIS TRP TYR PRO ALA LEU PHE THR HIS GLU
SEQRES 5 F 446 LEU GLU GLU ASP GLN VAL GLN GLY ILE GLN ILE CYS GLY
SEQRES 6 F 446 VAL PRO ILE VAL LEU ARG ARG VAL ASN GLY LYS VAL PHE
SEQRES 7 F 446 ALA LEU LYS ASP GLN CYS LEU HIS ARG GLY VAL ARG LEU
SEQRES 8 F 446 SER GLU LYS PRO THR CYS PHE THR LYS SER THR ILE SER
SEQRES 9 F 446 CYS TRP TYR HIS GLY PHE THR PHE ASP LEU GLU THR GLY
SEQRES 10 F 446 LYS LEU VAL THR ILE VAL ALA ASN PRO GLU ASP LYS LEU
SEQRES 11 F 446 ILE GLY THR THR GLY VAL THR THR TYR PRO VAL HIS GLU
SEQRES 12 F 446 VAL ASN GLY MET ILE PHE VAL PHE VAL ARG GLU ASP ASP
SEQRES 13 F 446 PHE PRO ASP GLU ASP VAL PRO PRO LEU ALA HIS ASP LEU
SEQRES 14 F 446 PRO PHE ARG PHE PRO GLU ARG SER GLU GLN PHE PRO HIS
SEQRES 15 F 446 PRO LEU TRP PRO SER SER PRO SER VAL LEU ASP ASP ASN
SEQRES 16 F 446 ALA VAL VAL HIS GLY MET HIS ARG THR GLY PHE GLY ASN
SEQRES 17 F 446 TRP ARG ILE ALA CYS GLU ASN GLY PHE ASP ASN ALA HIS
SEQRES 18 F 446 ILE LEU VAL HIS LYS ASP ASN THR ILE VAL HIS ALA MET
SEQRES 19 F 446 ASP TRP VAL LEU PRO LEU GLY LEU LEU PRO THR SER ASP
SEQRES 20 F 446 ASP CYS ILE ALA VAL VAL GLU ASP ASP ASP GLY PRO LYS
SEQRES 21 F 446 GLY MET MET GLN TRP LEU PHE THR ASP LYS TRP ALA PRO
SEQRES 22 F 446 VAL LEU GLU ASN GLN GLU LEU GLY LEU LYS VAL GLU GLY
SEQRES 23 F 446 LEU LYS GLY ARG HIS TYR ARG THR SER VAL VAL LEU PRO
SEQRES 24 F 446 GLY VAL LEU MET VAL GLU ASN TRP PRO GLU GLU HIS VAL
SEQRES 25 F 446 VAL GLN TYR GLU TRP TYR VAL PRO ILE THR ASP ASP THR
SEQRES 26 F 446 HIS GLU TYR TRP GLU ILE LEU VAL ARG VAL CYS PRO THR
SEQRES 27 F 446 ASP GLU ASP ARG LYS LYS PHE GLN TYR ARG TYR ASP HIS
SEQRES 28 F 446 MET TYR LYS PRO LEU CYS LEU HIS GLY PHE ASN ASP SER
SEQRES 29 F 446 ASP LEU TYR ALA ARG GLU ALA MET GLN ASN PHE TYR TYR
SEQRES 30 F 446 ASP GLY THR GLY TRP ASP ASP GLU GLN LEU VAL ALA THR
SEQRES 31 F 446 ASP ILE SER PRO ILE THR TRP ARG LYS LEU ALA SER ARG
SEQRES 32 F 446 TRP ASN ARG GLY ILE ALA LYS PRO GLY ARG GLY VAL ALA
SEQRES 33 F 446 GLY ALA VAL LYS ASP THR SER LEU ILE PHE LYS GLN THR
SEQRES 34 F 446 ALA ASP GLY LYS ARG PRO GLY TYR LYS VAL GLU GLN ILE
SEQRES 35 F 446 LYS GLU ASP HIS
HET FE A 501 1
HET FES A 500 4
HET FE B 501 1
HET FES B 500 4
HET FE C 501 1
HET FES C 500 4
HET FE D 501 1
HET FES D 500 4
HET FE E 501 1
HET FES E 500 4
HET FE F 501 1
HET FES F 500 4
HETNAM FE FE (III) ION
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
FORMUL 7 FE 6(FE 3+)
FORMUL 8 FES 6(FE2 S2)
FORMUL 19 HOH *3763(H2 O)
HELIX 1 1 ASN A 23 SER A 28 1 6
HELIX 2 2 TYR A 30 ALA A 36 1 7
HELIX 3 3 HIS A 51 LEU A 53 5 3
HELIX 4 4 ARG A 90 LYS A 94 5 5
HELIX 5 5 PRO A 158 VAL A 162 5 5
HELIX 6 6 PRO A 164 LEU A 169 5 6
HELIX 7 7 ASN A 208 GLU A 214 1 7
HELIX 8 8 ALA A 220 LYS A 226 5 7
HELIX 9 9 ASN A 228 MET A 234 1 7
HELIX 10 10 THR A 338 HIS A 351 1 14
HELIX 11 11 MET A 352 CYS A 357 1 6
HELIX 12 12 GLY A 360 ASP A 378 1 19
HELIX 13 13 GLY A 379 GLU A 385 1 7
HELIX 14 14 VAL A 388 THR A 390 5 3
HELIX 15 15 ASP A 391 ASN A 405 1 15
HELIX 16 16 THR A 422 ASP A 431 1 10
HELIX 17 17 ASN B 23 GLN B 29 1 7
HELIX 18 18 TYR B 30 ASP B 35 1 6
HELIX 19 19 HIS B 51 LEU B 53 5 3
HELIX 20 20 ARG B 90 LYS B 94 5 5
HELIX 21 21 PRO B 158 VAL B 162 5 5
HELIX 22 22 PRO B 164 LEU B 169 5 6
HELIX 23 23 ASN B 208 GLY B 216 1 9
HELIX 24 24 ALA B 220 LYS B 226 5 7
HELIX 25 25 ASN B 228 MET B 234 1 7
HELIX 26 26 THR B 338 MET B 352 1 15
HELIX 27 27 MET B 352 CYS B 357 1 6
HELIX 28 28 GLY B 360 ASP B 378 1 19
HELIX 29 29 GLY B 379 GLU B 385 1 7
HELIX 30 30 VAL B 388 THR B 390 5 3
HELIX 31 31 ASP B 391 ASN B 405 1 15
HELIX 32 32 THR B 422 ASP B 431 1 10
HELIX 33 33 ASN C 23 GLN C 29 1 7
HELIX 34 34 TYR C 30 ALA C 36 1 7
HELIX 35 35 HIS C 51 LEU C 53 5 3
HELIX 36 36 ARG C 90 LYS C 94 5 5
HELIX 37 37 PRO C 158 VAL C 162 5 5
HELIX 38 38 PRO C 164 LEU C 169 5 6
HELIX 39 39 ASN C 208 GLY C 216 1 9
HELIX 40 40 ALA C 220 LYS C 226 5 7
HELIX 41 41 ASN C 228 MET C 234 1 7
HELIX 42 42 THR C 338 MET C 352 1 15
HELIX 43 43 MET C 352 CYS C 357 1 6
HELIX 44 44 GLY C 360 ASP C 378 1 19
HELIX 45 45 GLY C 379 GLU C 385 1 7
HELIX 46 46 VAL C 388 THR C 390 5 3
HELIX 47 47 ASP C 391 ASN C 405 1 15
HELIX 48 48 THR C 422 ASP C 431 1 10
HELIX 49 49 ASN D 23 SER D 28 1 6
HELIX 50 50 TYR D 30 ALA D 36 1 7
HELIX 51 51 HIS D 51 LEU D 53 5 3
HELIX 52 52 ARG D 90 LYS D 94 5 5
HELIX 53 53 PRO D 158 VAL D 162 5 5
HELIX 54 54 PRO D 164 LEU D 169 5 6
HELIX 55 55 ASN D 208 GLU D 214 1 7
HELIX 56 56 ALA D 220 LYS D 226 5 7
HELIX 57 57 ASN D 228 MET D 234 1 7
HELIX 58 58 THR D 338 MET D 352 1 15
HELIX 59 59 MET D 352 CYS D 357 1 6
HELIX 60 60 GLY D 360 ASP D 378 1 19
HELIX 61 61 THR D 380 GLU D 385 1 6
HELIX 62 62 VAL D 388 THR D 390 5 3
HELIX 63 63 ASP D 391 ASN D 405 1 15
HELIX 64 64 THR D 422 ASP D 431 1 10
HELIX 65 65 ASN E 23 GLN E 29 1 7
HELIX 66 66 TYR E 30 ASP E 35 1 6
HELIX 67 67 HIS E 51 LEU E 53 5 3
HELIX 68 68 ARG E 90 LYS E 94 5 5
HELIX 69 69 PRO E 158 VAL E 162 5 5
HELIX 70 70 PRO E 164 LEU E 169 5 6
HELIX 71 71 ASN E 208 GLY E 216 1 9
HELIX 72 72 ALA E 220 LYS E 226 5 7
HELIX 73 73 ASN E 228 MET E 234 1 7
HELIX 74 74 THR E 338 MET E 352 1 15
HELIX 75 75 MET E 352 CYS E 357 1 6
HELIX 76 76 GLY E 360 ASP E 378 1 19
HELIX 77 77 GLY E 379 GLU E 385 1 7
HELIX 78 78 VAL E 388 THR E 390 5 3
HELIX 79 79 ASP E 391 ASN E 405 1 15
HELIX 80 80 THR E 422 ASP E 431 1 10
HELIX 81 81 ASN F 23 GLN F 29 1 7
HELIX 82 82 TYR F 30 ASP F 35 1 6
HELIX 83 83 HIS F 51 LEU F 53 5 3
HELIX 84 84 ARG F 90 LYS F 94 5 5
HELIX 85 85 PRO F 158 VAL F 162 5 5
HELIX 86 86 PRO F 164 LEU F 169 5 6
HELIX 87 87 ASN F 208 GLY F 216 1 9
HELIX 88 88 ALA F 220 LYS F 226 5 7
HELIX 89 89 ASN F 228 MET F 234 1 7
HELIX 90 90 THR F 338 MET F 352 1 15
HELIX 91 91 MET F 352 CYS F 357 1 6
HELIX 92 92 GLY F 360 ASP F 378 1 19
HELIX 93 93 THR F 380 GLU F 385 1 6
HELIX 94 94 VAL F 388 THR F 390 5 3
HELIX 95 95 ASP F 391 ASN F 405 1 15
HELIX 96 96 THR F 422 ASP F 431 1 10
SHEET 1 A 3 HIS A 43 PHE A 49 0
SHEET 2 A 3 MET A 147 VAL A 152 -1 O ILE A 148 N ALA A 47
SHEET 3 A 3 VAL A 141 VAL A 144 -1 N HIS A 142 O PHE A 149
SHEET 1 B 4 VAL A 58 ILE A 63 0
SHEET 2 B 4 VAL A 66 VAL A 73 -1 O ILE A 68 N ILE A 61
SHEET 3 B 4 LYS A 76 LYS A 81 -1 O LYS A 76 N VAL A 73
SHEET 4 B 4 THR A 138 TYR A 139 -1 O TYR A 139 N ALA A 79
SHEET 1 C 3 THR A 102 SER A 104 0
SHEET 2 C 3 PHE A 110 ASP A 113 -1 O PHE A 112 N ILE A 103
SHEET 3 C 3 LEU A 119 ILE A 122 -1 O THR A 121 N THR A 111
SHEET 1 D 7 ALA A 196 PHE A 206 0
SHEET 2 D 7 THR A 325 VAL A 335 -1 O HIS A 326 N GLY A 205
SHEET 3 D 7 VAL A 313 PRO A 320 -1 N VAL A 319 O GLU A 327
SHEET 4 D 7 VAL A 301 GLU A 305 -1 N LEU A 302 O GLU A 316
SHEET 5 D 7 ARG A 293 VAL A 297 -1 N VAL A 297 O VAL A 301
SHEET 6 D 7 GLY A 261 GLN A 264 -1 N MET A 262 O VAL A 296
SHEET 7 D 7 ILE A 250 VAL A 253 -1 N VAL A 253 O GLY A 261
SHEET 1 E 2 GLY A 241 PRO A 244 0
SHEET 2 E 2 TRP A 271 VAL A 274 -1 O VAL A 274 N GLY A 241
SHEET 1 F 2 GLU A 276 ASN A 277 0
SHEET 2 F 2 LEU A 282 LYS A 283 -1 O LEU A 282 N ASN A 277
SHEET 1 G 3 HIS B 43 PHE B 49 0
SHEET 2 G 3 MET B 147 VAL B 152 -1 O ILE B 148 N ALA B 47
SHEET 3 G 3 VAL B 141 VAL B 144 -1 N VAL B 144 O MET B 147
SHEET 1 H 3 VAL B 58 ILE B 63 0
SHEET 2 H 3 VAL B 66 VAL B 73 -1 O ILE B 68 N ILE B 61
SHEET 3 H 3 LYS B 76 LYS B 81 -1 O LYS B 76 N VAL B 73
SHEET 1 I 3 THR B 102 SER B 104 0
SHEET 2 I 3 PHE B 110 ASP B 113 -1 O PHE B 112 N ILE B 103
SHEET 3 I 3 LEU B 119 ILE B 122 -1 O THR B 121 N THR B 111
SHEET 1 J 7 ALA B 196 PHE B 206 0
SHEET 2 J 7 THR B 325 VAL B 335 -1 O HIS B 326 N GLY B 205
SHEET 3 J 7 VAL B 313 PRO B 320 -1 N VAL B 313 O VAL B 333
SHEET 4 J 7 VAL B 301 GLU B 305 -1 N VAL B 304 O GLN B 314
SHEET 5 J 7 ARG B 293 VAL B 297 -1 N VAL B 297 O VAL B 301
SHEET 6 J 7 GLY B 261 GLN B 264 -1 N MET B 262 O VAL B 296
SHEET 7 J 7 ILE B 250 VAL B 253 -1 N ALA B 251 O MET B 263
SHEET 1 K 2 GLY B 241 PRO B 244 0
SHEET 2 K 2 TRP B 271 VAL B 274 -1 O VAL B 274 N GLY B 241
SHEET 1 L 2 GLU B 276 ASN B 277 0
SHEET 2 L 2 LEU B 282 LYS B 283 -1 O LEU B 282 N ASN B 277
SHEET 1 M 3 HIS C 43 PHE C 49 0
SHEET 2 M 3 MET C 147 VAL C 152 -1 O ILE C 148 N ALA C 47
SHEET 3 M 3 VAL C 141 VAL C 144 -1 N VAL C 144 O MET C 147
SHEET 1 N 4 VAL C 58 ILE C 63 0
SHEET 2 N 4 VAL C 66 VAL C 73 -1 O ILE C 68 N ILE C 61
SHEET 3 N 4 LYS C 76 LYS C 81 -1 O LYS C 76 N VAL C 73
SHEET 4 N 4 THR C 138 TYR C 139 -1 O TYR C 139 N ALA C 79
SHEET 1 O 3 THR C 102 SER C 104 0
SHEET 2 O 3 PHE C 110 ASP C 113 -1 O PHE C 112 N ILE C 103
SHEET 3 O 3 LEU C 119 ILE C 122 -1 O THR C 121 N THR C 111
SHEET 1 P 7 ALA C 196 PHE C 206 0
SHEET 2 P 7 THR C 325 VAL C 335 -1 O HIS C 326 N GLY C 205
SHEET 3 P 7 VAL C 313 PRO C 320 -1 N VAL C 319 O GLU C 327
SHEET 4 P 7 VAL C 301 GLU C 305 -1 N VAL C 304 O GLN C 314
SHEET 5 P 7 ARG C 293 VAL C 297 -1 N VAL C 297 O VAL C 301
SHEET 6 P 7 GLY C 261 GLN C 264 -1 N MET C 262 O VAL C 296
SHEET 7 P 7 ILE C 250 VAL C 253 -1 N ALA C 251 O MET C 263
SHEET 1 Q 2 GLY C 241 PRO C 244 0
SHEET 2 Q 2 TRP C 271 VAL C 274 -1 O VAL C 274 N GLY C 241
SHEET 1 R 2 GLU C 276 ASN C 277 0
SHEET 2 R 2 LEU C 282 LYS C 283 -1 O LEU C 282 N ASN C 277
SHEET 1 S 3 HIS D 43 PHE D 49 0
SHEET 2 S 3 MET D 147 VAL D 152 -1 O ILE D 148 N ALA D 47
SHEET 3 S 3 VAL D 141 VAL D 144 -1 N VAL D 144 O MET D 147
SHEET 1 T 4 VAL D 58 ILE D 63 0
SHEET 2 T 4 VAL D 66 VAL D 73 -1 O ILE D 68 N ILE D 61
SHEET 3 T 4 LYS D 76 LYS D 81 -1 O LYS D 76 N VAL D 73
SHEET 4 T 4 THR D 138 TYR D 139 -1 O TYR D 139 N ALA D 79
SHEET 1 U 3 THR D 102 SER D 104 0
SHEET 2 U 3 PHE D 110 ASP D 113 -1 O PHE D 112 N ILE D 103
SHEET 3 U 3 LEU D 119 ILE D 122 -1 O THR D 121 N THR D 111
SHEET 1 V 7 ALA D 196 PHE D 206 0
SHEET 2 V 7 THR D 325 VAL D 335 -1 O HIS D 326 N GLY D 205
SHEET 3 V 7 VAL D 313 PRO D 320 -1 N VAL D 319 O GLU D 327
SHEET 4 V 7 VAL D 301 GLU D 305 -1 N VAL D 304 O GLN D 314
SHEET 5 V 7 ARG D 293 VAL D 297 -1 N VAL D 297 O VAL D 301
SHEET 6 V 7 GLY D 261 GLN D 264 -1 N MET D 262 O VAL D 296
SHEET 7 V 7 ILE D 250 VAL D 253 -1 N ALA D 251 O MET D 263
SHEET 1 W 2 GLY D 241 PRO D 244 0
SHEET 2 W 2 TRP D 271 VAL D 274 -1 O VAL D 274 N GLY D 241
SHEET 1 X 2 GLU D 276 ASN D 277 0
SHEET 2 X 2 LEU D 282 LYS D 283 -1 O LEU D 282 N ASN D 277
SHEET 1 Y 3 HIS E 43 PHE E 49 0
SHEET 2 Y 3 MET E 147 VAL E 152 -1 O ILE E 148 N ALA E 47
SHEET 3 Y 3 VAL E 141 VAL E 144 -1 N VAL E 144 O MET E 147
SHEET 1 Z 3 VAL E 58 ILE E 63 0
SHEET 2 Z 3 VAL E 66 VAL E 73 -1 O ILE E 68 N ILE E 61
SHEET 3 Z 3 LYS E 76 LYS E 81 -1 O LYS E 76 N VAL E 73
SHEET 1 AA 3 THR E 102 SER E 104 0
SHEET 2 AA 3 PHE E 110 ASP E 113 -1 O PHE E 112 N ILE E 103
SHEET 3 AA 3 LEU E 119 ILE E 122 -1 O THR E 121 N THR E 111
SHEET 1 AB 7 ALA E 196 PHE E 206 0
SHEET 2 AB 7 THR E 325 VAL E 335 -1 O HIS E 326 N GLY E 205
SHEET 3 AB 7 VAL E 313 PRO E 320 -1 N VAL E 313 O VAL E 333
SHEET 4 AB 7 VAL E 301 GLU E 305 -1 N VAL E 304 O GLN E 314
SHEET 5 AB 7 ARG E 293 VAL E 297 -1 N VAL E 297 O VAL E 301
SHEET 6 AB 7 GLY E 261 GLN E 264 -1 N MET E 262 O VAL E 296
SHEET 7 AB 7 ILE E 250 VAL E 253 -1 N ALA E 251 O MET E 263
SHEET 1 AC 2 GLY E 241 PRO E 244 0
SHEET 2 AC 2 TRP E 271 VAL E 274 -1 O VAL E 274 N GLY E 241
SHEET 1 AD 2 GLU E 276 ASN E 277 0
SHEET 2 AD 2 LEU E 282 LYS E 283 -1 O LEU E 282 N ASN E 277
SHEET 1 AE 3 HIS F 43 PHE F 49 0
SHEET 2 AE 3 MET F 147 VAL F 152 -1 O ILE F 148 N ALA F 47
SHEET 3 AE 3 VAL F 141 VAL F 144 -1 N VAL F 144 O MET F 147
SHEET 1 AF 4 VAL F 58 ILE F 63 0
SHEET 2 AF 4 VAL F 66 VAL F 73 -1 O ILE F 68 N ILE F 61
SHEET 3 AF 4 LYS F 76 LYS F 81 -1 O LYS F 76 N VAL F 73
SHEET 4 AF 4 THR F 138 TYR F 139 -1 O TYR F 139 N ALA F 79
SHEET 1 AG 3 THR F 102 SER F 104 0
SHEET 2 AG 3 PHE F 110 ASP F 113 -1 O PHE F 112 N ILE F 103
SHEET 3 AG 3 LEU F 119 ILE F 122 -1 O THR F 121 N THR F 111
SHEET 1 AH 7 ALA F 196 PHE F 206 0
SHEET 2 AH 7 THR F 325 VAL F 335 -1 O HIS F 326 N GLY F 205
SHEET 3 AH 7 VAL F 313 PRO F 320 -1 N VAL F 319 O GLU F 327
SHEET 4 AH 7 VAL F 301 GLU F 305 -1 N VAL F 304 O GLN F 314
SHEET 5 AH 7 ARG F 293 VAL F 297 -1 N VAL F 297 O VAL F 301
SHEET 6 AH 7 GLY F 261 GLN F 264 -1 N MET F 262 O VAL F 296
SHEET 7 AH 7 ILE F 250 VAL F 253 -1 N VAL F 253 O GLY F 261
SHEET 1 AI 2 GLY F 241 PRO F 244 0
SHEET 2 AI 2 TRP F 271 VAL F 274 -1 O VAL F 274 N GLY F 241
SHEET 1 AJ 2 GLU F 276 ASN F 277 0
SHEET 2 AJ 2 LEU F 282 LYS F 283 -1 O LEU F 282 N ASN F 277
LINK SG CYS A 84 FE2 FES A 500 1555 1555 2.37
LINK ND1 HIS A 86 FE1 FES A 500 1555 1555 2.16
LINK SG CYS A 105 FE2 FES A 500 1555 1555 2.33
LINK ND1 HIS A 108 FE1 FES A 500 1555 1555 2.20
LINK NE2 HIS A 221 FE FE A 501 1555 1555 2.23
LINK NE2 HIS A 225 FE FE A 501 1555 1555 2.06
LINK OD1 ASP A 365 FE FE A 501 1555 1555 2.47
LINK OD2 ASP A 365 FE FE A 501 1555 1555 2.21
LINK FE FE A 501 O HOH A1169 1555 1555 2.26
LINK SG CYS B 84 FE2 FES B 500 1555 1555 2.39
LINK ND1 HIS B 86 FE1 FES B 500 1555 1555 2.18
LINK SG CYS B 105 FE2 FES B 500 1555 1555 2.41
LINK ND1 HIS B 108 FE1 FES B 500 1555 1555 2.19
LINK NE2 HIS B 221 FE FE B 501 1555 1555 2.23
LINK NE2 HIS B 225 FE FE B 501 1555 1555 2.18
LINK OD1 ASP B 365 FE FE B 501 1555 1555 2.49
LINK OD2 ASP B 365 FE FE B 501 1555 1555 2.12
LINK FE FE B 501 O HOH B1121 1555 1555 2.56
LINK SG CYS C 84 FE2 FES C 500 1555 1555 2.32
LINK ND1 HIS C 86 FE1 FES C 500 1555 1555 2.28
LINK SG CYS C 105 FE2 FES C 500 1555 1555 2.37
LINK ND1 HIS C 108 FE1 FES C 500 1555 1555 2.18
LINK NE2 HIS C 221 FE FE C 501 1555 1555 2.31
LINK NE2 HIS C 225 FE FE C 501 1555 1555 2.17
LINK OD1 ASP C 365 FE FE C 501 1555 1555 2.44
LINK OD2 ASP C 365 FE FE C 501 1555 1555 2.13
LINK FE FE C 501 O HOH C1104 1555 1555 2.40
LINK SG CYS D 84 FE2 FES D 500 1555 1555 2.36
LINK ND1 HIS D 86 FE1 FES D 500 1555 1555 2.19
LINK SG CYS D 105 FE2 FES D 500 1555 1555 2.35
LINK ND1 HIS D 108 FE1 FES D 500 1555 1555 2.20
LINK NE2 HIS D 221 FE FE D 501 1555 1555 2.18
LINK NE2 HIS D 225 FE FE D 501 1555 1555 2.12
LINK OD1 ASP D 365 FE FE D 501 1555 1555 2.51
LINK OD2 ASP D 365 FE FE D 501 1555 1555 2.17
LINK FE FE D 501 O HOH D1164 1555 1555 2.56
LINK SG CYS E 84 FE2 FES E 500 1555 1555 2.36
LINK ND1 HIS E 86 FE1 FES E 500 1555 1555 2.21
LINK SG CYS E 105 FE2 FES E 500 1555 1555 2.42
LINK ND1 HIS E 108 FE1 FES E 500 1555 1555 2.20
LINK NE2 HIS E 221 FE FE E 501 1555 1555 2.23
LINK NE2 HIS E 225 FE FE E 501 1555 1555 2.18
LINK OD1 ASP E 365 FE FE E 501 1555 1555 2.44
LINK OD2 ASP E 365 FE FE E 501 1555 1555 2.19
LINK SG CYS F 84 FE2 FES F 500 1555 1555 2.32
LINK ND1 HIS F 86 FE1 FES F 500 1555 1555 2.31
LINK SG CYS F 105 FE2 FES F 500 1555 1555 2.37
LINK ND1 HIS F 108 FE1 FES F 500 1555 1555 2.21
LINK NE2 HIS F 221 FE FE F 501 1555 1555 2.24
LINK NE2 HIS F 225 FE FE F 501 1555 1555 2.17
LINK OD1 ASP F 365 FE FE F 501 1555 1555 2.52
LINK OD2 ASP F 365 FE FE F 501 1555 1555 2.12
LINK FE FE F 501 O HOH F1120 1555 1555 2.29
CISPEP 1 PHE A 173 PRO A 174 0 0.30
CISPEP 2 LEU A 298 PRO A 299 0 0.52
CISPEP 3 TRP A 307 PRO A 308 0 0.08
CISPEP 4 PHE B 173 PRO B 174 0 -0.32
CISPEP 5 LEU B 298 PRO B 299 0 0.54
CISPEP 6 TRP B 307 PRO B 308 0 0.11
CISPEP 7 PHE C 173 PRO C 174 0 0.18
CISPEP 8 LEU C 298 PRO C 299 0 0.17
CISPEP 9 TRP C 307 PRO C 308 0 -0.19
CISPEP 10 PHE D 173 PRO D 174 0 0.20
CISPEP 11 LEU D 298 PRO D 299 0 0.18
CISPEP 12 TRP D 307 PRO D 308 0 0.15
CISPEP 13 PHE E 173 PRO E 174 0 0.08
CISPEP 14 LEU E 298 PRO E 299 0 0.79
CISPEP 15 TRP E 307 PRO E 308 0 -0.06
CISPEP 16 PHE F 173 PRO F 174 0 0.17
CISPEP 17 LEU F 298 PRO F 299 0 0.10
CISPEP 18 TRP F 307 PRO F 308 0 0.09
SITE 1 AC1 4 HIS A 221 HIS A 225 ASP A 365 HOH A1169
SITE 1 AC2 4 HIS B 221 HIS B 225 ASP B 365 HOH B1121
SITE 1 AC3 4 HIS C 221 HIS C 225 ASP C 365 HOH C1104
SITE 1 AC4 4 HIS D 221 HIS D 225 ASP D 365 HOH D1164
SITE 1 AC5 4 HIS E 221 HIS E 225 ASP E 365 HOH E1091
SITE 1 AC6 4 HIS F 221 HIS F 225 ASP F 365 HOH F1120
SITE 1 AC7 6 CYS A 84 HIS A 86 ARG A 87 CYS A 105
SITE 2 AC7 6 HIS A 108 PHE A 110
SITE 1 AC8 7 CYS B 84 HIS B 86 ARG B 87 CYS B 105
SITE 2 AC8 7 HIS B 108 GLY B 109 PHE B 110
SITE 1 AC9 7 CYS C 84 HIS C 86 ARG C 87 CYS C 105
SITE 2 AC9 7 HIS C 108 GLY C 109 PHE C 110
SITE 1 BC1 7 CYS D 84 HIS D 86 ARG D 87 CYS D 105
SITE 2 BC1 7 HIS D 108 GLY D 109 PHE D 110
SITE 1 BC2 7 CYS E 84 HIS E 86 ARG E 87 CYS E 105
SITE 2 BC2 7 HIS E 108 GLY E 109 PHE E 110
SITE 1 BC3 6 CYS F 84 HIS F 86 ARG F 87 CYS F 105
SITE 2 BC3 6 HIS F 108 PHE F 110
CRYST1 104.460 166.960 173.460 90.00 90.00 90.00 P 21 21 21 24
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 0.009573 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005989 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005765 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
