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HEADER HYDROGENASE 11-NOV-98 1HFE
TITLE 1.6 A RESOLUTION STRUCTURE OF THE FE-ONLY HYDROGENASE FROM
TITLE 2 DESULFOVIBRIO DESULFURICANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (FE-ONLY HYDROGENASE (E.C.1.18.99.1) (SMALLER
COMPND 3 SUBUNIT));
COMPND 4 CHAIN: S, T;
COMPND 5 EC: 1.18.99.1;
COMPND 6 OTHER_DETAILS: THE FE-ONLY HYDROGENASE FROM DESULFOVIBRIO
COMPND 7 DESULFURICANS HAS EXACTLY THE SAME SEQUENCE AS THE FE-ONLY
COMPND 8 HYDROGENASE FROM DESULFOVIBRIO VULGARIS (STRAIN HILDENBOROUGH);
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PROTEIN (FE-ONLY HYDROGENASE (E.C.1.18.99.1) (LARGER
COMPND 11 SUBUNIT));
COMPND 12 CHAIN: L, M;
COMPND 13 EC: 1.18.99.1;
COMPND 14 OTHER_DETAILS: THE FE-ONLY HYDROGENASE FROM DESULFOVIBRIO
COMPND 15 DESULFURICANS HAS EXACTLY THE SAME SEQUENCE AS THE FE-ONLY
COMPND 16 HYDROGENASE FROM DESULFOVIBRIO VULGARIS (STRAIN HILDENBOROUGH)
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP. VULGARIS STR.
SOURCE 3 HILDENBOROUGH;
SOURCE 4 ORGANISM_TAXID: 882;
SOURCE 5 STRAIN: HILDENBOROUGH / ATCC 29579 / NCIMB 8303;
SOURCE 6 ATCC: 7757;
SOURCE 7 CELLULAR_LOCATION: PERIPLASM;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP. VULGARIS STR.
SOURCE 10 HILDENBOROUGH;
SOURCE 11 ORGANISM_TAXID: 882;
SOURCE 12 STRAIN: HILDENBOROUGH / ATCC 29579 / NCIMB 8303;
SOURCE 13 ATCC: 7757;
SOURCE 14 CELLULAR_LOCATION: PERIPLASM
KEYWDS FE-ONLY HYDROGENASE, HYDROGENE METABOLISM, PERIPLASM, HYDROGENASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NICOLET,C.PIRAS,P.LEGRAND,E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS
REVDAT 7 20-NOV-19 1HFE 1 REMARK LINK
REVDAT 6 02-MAR-10 1HFE 1 REMARK HELIX SHEET HETATM
REVDAT 5 24-FEB-09 1HFE 1 VERSN
REVDAT 4 01-APR-03 1HFE 1 JRNL
REVDAT 3 02-FEB-00 1HFE 1 LINK
REVDAT 2 22-JUN-99 1HFE 1 REVDAT
REVDAT 1 20-APR-99 1HFE 0
JRNL AUTH Y.NICOLET,C.PIRAS,P.LEGRAND,C.E.HATCHIKIAN,
JRNL AUTH 2 J.C.FONTECILLA-CAMPS
JRNL TITL DESULFOVIBRIO DESULFURICANS IRON HYDROGENASE: THE STRUCTURE
JRNL TITL 2 SHOWS UNUSUAL COORDINATION TO AN ACTIVE SITE FE BINUCLEAR
JRNL TITL 3 CENTER.
JRNL REF STRUCTURE FOLD.DES. V. 7 13 1999
JRNL REFN ISSN 0969-2126
JRNL PMID 10368269
JRNL DOI 10.1016/S0969-2126(99)80005-7
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.8
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 7.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 124375
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) : 0.158
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6295
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.67
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12049
REMARK 3 BIN R VALUE (WORKING SET) : 0.2275
REMARK 3 BIN FREE R VALUE : 0.2423
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 633
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7456
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 93
REMARK 3 SOLVENT ATOMS : 1179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.27
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.64000
REMARK 3 B22 (A**2) : 1.72000
REMARK 3 B33 (A**2) : -0.07000
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) : 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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.740
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.510
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) : NULL ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPH19X.PEP
REMARK 3 TOPOLOGY FILE 2 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 2 MOLECULES OF THE ASYMMETRIC UNIT WERE NEVER CONSTRAINT WITH
REMARK 3 THE NON
REMARK 3 CRYSTALLOGRAPHIC SYMMETRY DURING REFINEMENT.
REMARK 4
REMARK 4 1HFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-98.
REMARK 100 THE DEPOSITION ID IS D_1000000080.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : MAY-98
REMARK 200 TEMPERATURE (KELVIN) : 100.00
REMARK 200 PH : 7.60
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.947375
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 158363
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.510
REMARK 200 RESOLUTION RANGE LOW (A) : 21.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.51
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 89.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 64.48500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.53500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 64.48500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.53500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -146.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: T, M
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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 19570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -332.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, L, T, M
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 MET S 1
REMARK 465 GLN S 2
REMARK 465 ILE S 3
REMARK 465 ALA S 4
REMARK 465 SER S 5
REMARK 465 ILE S 6
REMARK 465 THR S 7
REMARK 465 ARG S 8
REMARK 465 ARG S 9
REMARK 465 GLY S 10
REMARK 465 PHE S 11
REMARK 465 LEU S 12
REMARK 465 LYS S 13
REMARK 465 VAL S 14
REMARK 465 ALA S 15
REMARK 465 CYS S 16
REMARK 465 VAL S 17
REMARK 465 THR S 18
REMARK 465 THR S 19
REMARK 465 GLY S 20
REMARK 465 ALA S 21
REMARK 465 ALA S 22
REMARK 465 LEU S 23
REMARK 465 ILE S 24
REMARK 465 GLY S 25
REMARK 465 ILE S 26
REMARK 465 ARG S 27
REMARK 465 MET S 28
REMARK 465 THR S 29
REMARK 465 GLY S 30
REMARK 465 LYS S 31
REMARK 465 ALA S 32
REMARK 465 VAL S 33
REMARK 465 ALA S 34
REMARK 465 ALA S 35
REMARK 465 MET L 1
REMARK 465 ASP L 399
REMARK 465 ARG L 400
REMARK 465 THR L 401
REMARK 465 THR L 402
REMARK 465 THR L 403
REMARK 465 ARG L 404
REMARK 465 LEU L 405
REMARK 465 TYR L 406
REMARK 465 ALA L 407
REMARK 465 GLY L 408
REMARK 465 LEU L 409
REMARK 465 LYS L 410
REMARK 465 LYS L 411
REMARK 465 ARG L 412
REMARK 465 LEU L 413
REMARK 465 ALA L 414
REMARK 465 MET L 415
REMARK 465 ALA L 416
REMARK 465 SER L 417
REMARK 465 ALA L 418
REMARK 465 ASN L 419
REMARK 465 LYS L 420
REMARK 465 ALA L 421
REMARK 465 MET T 1
REMARK 465 GLN T 2
REMARK 465 ILE T 3
REMARK 465 ALA T 4
REMARK 465 SER T 5
REMARK 465 ILE T 6
REMARK 465 THR T 7
REMARK 465 ARG T 8
REMARK 465 ARG T 9
REMARK 465 GLY T 10
REMARK 465 PHE T 11
REMARK 465 LEU T 12
REMARK 465 LYS T 13
REMARK 465 VAL T 14
REMARK 465 ALA T 15
REMARK 465 CYS T 16
REMARK 465 VAL T 17
REMARK 465 THR T 18
REMARK 465 THR T 19
REMARK 465 GLY T 20
REMARK 465 ALA T 21
REMARK 465 ALA T 22
REMARK 465 LEU T 23
REMARK 465 ILE T 24
REMARK 465 GLY T 25
REMARK 465 ILE T 26
REMARK 465 ARG T 27
REMARK 465 MET T 28
REMARK 465 THR T 29
REMARK 465 GLY T 30
REMARK 465 LYS T 31
REMARK 465 ALA T 32
REMARK 465 VAL T 33
REMARK 465 ALA T 34
REMARK 465 ALA T 35
REMARK 465 MET M 1
REMARK 465 ASP M 399
REMARK 465 ARG M 400
REMARK 465 THR M 401
REMARK 465 THR M 402
REMARK 465 THR M 403
REMARK 465 ARG M 404
REMARK 465 LEU M 405
REMARK 465 TYR M 406
REMARK 465 ALA M 407
REMARK 465 GLY M 408
REMARK 465 LEU M 409
REMARK 465 LYS M 410
REMARK 465 LYS M 411
REMARK 465 ARG M 412
REMARK 465 LEU M 413
REMARK 465 ALA M 414
REMARK 465 MET M 415
REMARK 465 ALA M 416
REMARK 465 SER M 417
REMARK 465 ALA M 418
REMARK 465 ASN M 419
REMARK 465 LYS M 420
REMARK 465 ALA M 421
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 MET L 398 CA C O CB CG SD CE
REMARK 470 MET M 398 CA C O CB CG SD CE
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN S 38 OE1 NE2
REMARK 480 LYS S 40 NZ
REMARK 480 LYS S 56 CD CE NZ
REMARK 480 LYS S 73 CE NZ
REMARK 480 GLU S 77 CD OE1
REMARK 480 LYS S 78 CD NZ
REMARK 480 LYS S 97 NZ
REMARK 480 GLU S 101 OE1 OE2
REMARK 480 LYS L 19 CE NZ
REMARK 480 LYS L 24 NZ
REMARK 480 LYS L 34 NZ
REMARK 480 GLU L 53 CD OE1 OE2
REMARK 480 MET L 54 SD
REMARK 480 LYS L 93 CD CE NZ
REMARK 480 LYS L 96 CE NZ
REMARK 480 LYS L 99 CD CE NZ
REMARK 480 GLN L 135 OE1
REMARK 480 LYS L 136 NZ
REMARK 480 THR L 165 O
REMARK 480 LYS L 166 CG CD CE NZ
REMARK 480 LYS L 167 CG CD CE NZ
REMARK 480 ASP L 169 CG OD1 OD2
REMARK 480 LYS L 220 NZ
REMARK 480 LYS L 247 NZ
REMARK 480 LYS L 269 CE NZ
REMARK 480 LYS L 276 CD CE NZ
REMARK 480 LYS L 281 CG CD CE NZ
REMARK 480 LYS L 317 CB CG CD CE NZ
REMARK 480 LYS L 318 CG CD CE NZ
REMARK 480 ASP L 320 CB
REMARK 480 THR L 343 CG2
REMARK 480 ASP L 344 OD2
REMARK 480 LYS L 346 CE
REMARK 480 LYS L 367 CA O CB CG CD CE NZ
REMARK 480 GLU L 396 CG CD OE1 OE2
REMARK 480 LYS T 56 CD CE NZ
REMARK 480 LYS T 69 CE NZ
REMARK 480 LYS T 73 CD CE NZ
REMARK 480 GLU T 77 CD OE1 OE2
REMARK 480 LYS T 78 CD CE
REMARK 480 GLU T 117 CD OE1 OE2
REMARK 480 LYS M 19 NZ
REMARK 480 LYS M 34 CE NZ
REMARK 480 GLU M 53 CD OE1 OE2
REMARK 480 MET M 54 SD CE
REMARK 480 LYS M 93 CG CD CE NZ
REMARK 480 LYS M 96 CE NZ
REMARK 480 LYS M 101 CE NZ
REMARK 480 LYS M 136 CD CE NZ
REMARK 480 LYS M 166 CB CG CD CE NZ
REMARK 480 LYS M 167 CB CG CD CE NZ
REMARK 480 ASP M 169 CB CG OD1 OD2
REMARK 480 LYS M 220 NZ
REMARK 480 LYS M 269 CG CD CE NZ
REMARK 480 LYS M 276 CB CG CD CE NZ
REMARK 480 LYS M 281 CG CD CE NZ
REMARK 480 LYS M 317 CB CG CD CE NZ
REMARK 480 LYS M 318 NZ
REMARK 480 ASN M 339 ND2
REMARK 480 LYS M 346 CE NZ
REMARK 480 LYS M 367 CB CG CD CE NZ
REMARK 480 GLU M 396 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 FE FE2 M 426 C CMO M 430 1.71
REMARK 500 FE FE2 L 426 C CMO L 430 1.75
REMARK 500 FE FE2 L 427 C CMO L 431 1.76
REMARK 500 FE FE2 M 427 C CMO M 431 1.80
REMARK 500 FE FE2 L 426 C CYN L 429 1.81
REMARK 500 FE FE2 L 427 C CYN L 428 1.82
REMARK 500 FE FE2 M 426 C CYN M 429 1.85
REMARK 500 FE FE2 M 427 C CYN M 428 1.87
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 S 75 -58.61 -140.76
REMARK 500 GLU S 77 -67.41 78.57
REMARK 500 ARG L 8 -23.71 76.66
REMARK 500 ALA L 113 -11.43 -140.10
REMARK 500 THR L 213 -79.27 -123.55
REMARK 500 LYS L 247 34.24 -146.41
REMARK 500 MET L 286 49.63 -140.10
REMARK 500 LYS L 367 30.94 -92.88
REMARK 500 TYR T 75 -60.37 -143.12
REMARK 500 GLU T 77 -67.48 77.44
REMARK 500 ARG M 8 -22.47 77.38
REMARK 500 ALA M 113 -10.76 -140.68
REMARK 500 ALA M 113 -7.58 -140.68
REMARK 500 THR M 213 -79.77 -122.49
REMARK 500 LYS M 247 35.83 -146.91
REMARK 500 LYS M 247 39.52 -146.91
REMARK 500 PHE M 324 79.23 -116.88
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 ZN S 500 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP S 86 OD2
REMARK 620 2 HIS T 82 NE2 119.7
REMARK 620 3 ASP T 86 OD2 104.2 104.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 422 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 35 SG
REMARK 620 2 SF4 L 422 S1 119.8
REMARK 620 3 SF4 L 422 S2 114.3 106.9
REMARK 620 4 SF4 L 422 S4 102.9 104.2 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 422 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 38 SG
REMARK 620 2 SF4 L 422 S1 118.4
REMARK 620 3 SF4 L 422 S3 99.6 107.4
REMARK 620 4 SF4 L 422 S4 120.0 104.7 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 422 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 41 SG
REMARK 620 2 SF4 L 422 S2 119.7
REMARK 620 3 SF4 L 422 S3 111.7 105.3
REMARK 620 4 SF4 L 422 S4 104.4 109.4 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 423 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 45 SG
REMARK 620 2 SF4 L 423 S2 114.1
REMARK 620 3 SF4 L 423 S3 115.2 105.7
REMARK 620 4 SF4 L 423 S4 110.7 105.1 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 423 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 66 SG
REMARK 620 2 SF4 L 423 S1 104.3
REMARK 620 3 SF4 L 423 S3 118.9 106.1
REMARK 620 4 SF4 L 423 S4 115.3 104.7 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 423 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 69 SG
REMARK 620 2 SF4 L 423 S1 116.7
REMARK 620 3 SF4 L 423 S2 99.3 104.7
REMARK 620 4 SF4 L 423 S4 125.9 103.5 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 423 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 72 SG
REMARK 620 2 SF4 L 423 S1 109.7
REMARK 620 3 SF4 L 423 S2 107.1 105.6
REMARK 620 4 SF4 L 423 S3 123.8 103.7 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 422 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 76 SG
REMARK 620 2 SF4 L 422 S1 112.6
REMARK 620 3 SF4 L 422 S2 117.2 105.8
REMARK 620 4 SF4 L 422 S3 110.3 105.3 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 424 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 179 SG
REMARK 620 2 SF4 L 424 S2 107.8
REMARK 620 3 SF4 L 424 S3 113.3 105.7
REMARK 620 4 SF4 L 424 S4 115.7 106.2 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 424 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 234 SG
REMARK 620 2 SF4 L 424 S1 105.7
REMARK 620 3 SF4 L 424 S2 107.5 108.0
REMARK 620 4 SF4 L 424 S3 123.7 106.7 104.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 424 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 378 SG
REMARK 620 2 SF4 L 424 S1 114.8
REMARK 620 3 SF4 L 424 S2 107.1 108.3
REMARK 620 4 SF4 L 424 S4 117.5 103.2 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 L 426 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 382 SG
REMARK 620 2 PDT L 425 S1 91.3
REMARK 620 3 PDT L 425 S2 97.1 86.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L 424 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 382 SG
REMARK 620 2 SF4 L 424 S1 118.0
REMARK 620 3 SF4 L 424 S3 105.9 104.7
REMARK 620 4 SF4 L 424 S4 119.1 102.4 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 422 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 35 SG
REMARK 620 2 SF4 M 422 S1 118.7
REMARK 620 3 SF4 M 422 S2 114.8 106.4
REMARK 620 4 SF4 M 422 S4 102.3 104.4 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 422 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 38 SG
REMARK 620 2 SF4 M 422 S1 118.9
REMARK 620 3 SF4 M 422 S3 99.7 106.9
REMARK 620 4 SF4 M 422 S4 120.2 104.5 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 422 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 41 SG
REMARK 620 2 SF4 M 422 S2 117.7
REMARK 620 3 SF4 M 422 S3 112.9 105.3
REMARK 620 4 SF4 M 422 S4 104.9 108.8 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 423 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 45 SG
REMARK 620 2 SF4 M 423 S2 114.7
REMARK 620 3 SF4 M 423 S3 116.3 105.1
REMARK 620 4 SF4 M 423 S4 110.8 104.4 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 423 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 66 SG
REMARK 620 2 SF4 M 423 S1 105.3
REMARK 620 3 SF4 M 423 S3 117.8 107.2
REMARK 620 4 SF4 M 423 S4 114.7 103.6 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 423 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 69 SG
REMARK 620 2 SF4 M 423 S1 116.9
REMARK 620 3 SF4 M 423 S2 97.8 105.2
REMARK 620 4 SF4 M 423 S4 125.1 104.1 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 423 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 72 SG
REMARK 620 2 SF4 M 423 S1 110.1
REMARK 620 3 SF4 M 423 S2 106.9 104.8
REMARK 620 4 SF4 M 423 S3 123.6 103.2 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 422 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 76 SG
REMARK 620 2 SF4 M 422 S1 109.7
REMARK 620 3 SF4 M 422 S2 118.1 105.5
REMARK 620 4 SF4 M 422 S3 109.9 107.1 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 424 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 179 SG
REMARK 620 2 SF4 M 424 S2 107.7
REMARK 620 3 SF4 M 424 S3 114.3 105.3
REMARK 620 4 SF4 M 424 S4 115.8 105.6 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 424 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 234 SG
REMARK 620 2 SF4 M 424 S1 106.2
REMARK 620 3 SF4 M 424 S2 107.3 109.4
REMARK 620 4 SF4 M 424 S3 123.2 105.8 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 424 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 378 SG
REMARK 620 2 SF4 M 424 S1 115.7
REMARK 620 3 SF4 M 424 S2 107.7 107.7
REMARK 620 4 SF4 M 424 S4 116.5 102.8 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M 424 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 382 SG
REMARK 620 2 SF4 M 424 S1 117.1
REMARK 620 3 SF4 M 424 S3 104.9 106.3
REMARK 620 4 SF4 M 424 S4 118.1 103.4 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 M 426 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 382 SG
REMARK 620 2 PDT M 425 S1 89.8
REMARK 620 3 PDT M 425 S2 95.3 81.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 L 427 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT L 425 S1
REMARK 620 2 PDT L 425 S2 86.6
REMARK 620 3 HOH L 433 O 104.4 101.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 M 427 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PDT M 425 S1
REMARK 620 2 HOH M 434 O 108.3
REMARK 620 3 PDT M 425 S2 82.1 100.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 L 426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 L 427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN L 428
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN L 429
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 M 426
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 M 427
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN M 428
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYN M 429
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 L 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 L 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 L 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDT L 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO L 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO L 431
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 M 422
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 M 423
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 M 424
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PDT M 425
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO M 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMO M 431
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS L 432
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CYS M 433
DBREF 1HFE S 1 123 UNP P07603 PHFS_DESVH 1 123
DBREF 1HFE T 1 123 UNP P07603 PHFS_DESVH 1 123
DBREF 1HFE L 1 421 UNP P07598 PHFL_DESVH 1 421
DBREF 1HFE M 1 421 UNP P07598 PHFL_DESVH 1 421
SEQRES 1 S 123 MET GLN ILE ALA SER ILE THR ARG ARG GLY PHE LEU LYS
SEQRES 2 S 123 VAL ALA CYS VAL THR THR GLY ALA ALA LEU ILE GLY ILE
SEQRES 3 S 123 ARG MET THR GLY LYS ALA VAL ALA ALA VAL LYS GLN ILE
SEQRES 4 S 123 LYS ASP TYR MET LEU ASP ARG ILE ASN GLY VAL TYR GLY
SEQRES 5 S 123 ALA ASP ALA LYS PHE PRO VAL ARG ALA SER GLN ASP ASN
SEQRES 6 S 123 THR GLN VAL LYS ALA LEU TYR LYS SER TYR LEU GLU LYS
SEQRES 7 S 123 PRO LEU GLY HIS LYS SER HIS ASP LEU LEU HIS THR HIS
SEQRES 8 S 123 TRP PHE ASP LYS SER LYS GLY VAL LYS GLU LEU THR THR
SEQRES 9 S 123 ALA GLY LYS LEU PRO ASN PRO ARG ALA SER GLU PHE GLU
SEQRES 10 S 123 GLY PRO TYR PRO TYR GLU
SEQRES 1 L 421 MET SER ARG THR VAL MET GLU ARG ILE GLU TYR GLU MET
SEQRES 2 L 421 HIS THR PRO ASP PRO LYS ALA ASP PRO ASP LYS LEU HIS
SEQRES 3 L 421 PHE VAL GLN ILE ASP GLU ALA LYS CYS ILE GLY CYS ASP
SEQRES 4 L 421 THR CYS SER GLN TYR CYS PRO THR ALA ALA ILE PHE GLY
SEQRES 5 L 421 GLU MET GLY GLU PRO HIS SER ILE PRO HIS ILE GLU ALA
SEQRES 6 L 421 CYS ILE ASN CYS GLY GLN CYS LEU THR HIS CYS PRO GLU
SEQRES 7 L 421 ASN ALA ILE TYR GLU ALA GLN SER TRP VAL PRO GLU VAL
SEQRES 8 L 421 GLU LYS LYS LEU LYS ASP GLY LYS VAL LYS CYS ILE ALA
SEQRES 9 L 421 MET PRO ALA PRO ALA VAL ARG TYR ALA LEU GLY ASP ALA
SEQRES 10 L 421 PHE GLY MET PRO VAL GLY SER VAL THR THR GLY LYS MET
SEQRES 11 L 421 LEU ALA ALA LEU GLN LYS LEU GLY PHE ALA HIS CYS TRP
SEQRES 12 L 421 ASP THR GLU PHE THR ALA ASP VAL THR ILE TRP GLU GLU
SEQRES 13 L 421 GLY SER GLU PHE VAL GLU ARG LEU THR LYS LYS SER ASP
SEQRES 14 L 421 MET PRO LEU PRO GLN PHE THR SER CYS CYS PRO GLY TRP
SEQRES 15 L 421 GLN LYS TYR ALA GLU THR TYR TYR PRO GLU LEU LEU PRO
SEQRES 16 L 421 HIS PHE SER THR CYS LYS SER PRO ILE GLY MET ASN GLY
SEQRES 17 L 421 ALA LEU ALA LYS THR TYR GLY ALA GLU ARG MET LYS TYR
SEQRES 18 L 421 ASP PRO LYS GLN VAL TYR THR VAL SER ILE MET PRO CYS
SEQRES 19 L 421 ILE ALA LYS LYS TYR GLU GLY LEU ARG PRO GLU LEU LYS
SEQRES 20 L 421 SER SER GLY MET ARG ASP ILE ASP ALA THR LEU THR THR
SEQRES 21 L 421 ARG GLU LEU ALA TYR MET ILE LYS LYS ALA GLY ILE ASP
SEQRES 22 L 421 PHE ALA LYS LEU PRO ASP GLY LYS ARG ASP SER LEU MET
SEQRES 23 L 421 GLY GLU SER THR GLY GLY ALA THR ILE PHE GLY VAL THR
SEQRES 24 L 421 GLY GLY VAL MET GLU ALA ALA LEU ARG PHE ALA TYR GLU
SEQRES 25 L 421 ALA VAL THR GLY LYS LYS PRO ASP SER TRP ASP PHE LYS
SEQRES 26 L 421 ALA VAL ARG GLY LEU ASP GLY ILE LYS GLU ALA THR VAL
SEQRES 27 L 421 ASN VAL GLY GLY THR ASP VAL LYS VAL ALA VAL VAL HIS
SEQRES 28 L 421 GLY ALA LYS ARG PHE LYS GLN VAL CYS ASP ASP VAL LYS
SEQRES 29 L 421 ALA GLY LYS SER PRO TYR HIS PHE ILE GLU TYR MET ALA
SEQRES 30 L 421 CYS PRO GLY GLY CYS VAL CYS GLY GLY GLY GLN PRO VAL
SEQRES 31 L 421 MET PRO GLY VAL LEU GLU ALA MET ASP ARG THR THR THR
SEQRES 32 L 421 ARG LEU TYR ALA GLY LEU LYS LYS ARG LEU ALA MET ALA
SEQRES 33 L 421 SER ALA ASN LYS ALA
SEQRES 1 T 123 MET GLN ILE ALA SER ILE THR ARG ARG GLY PHE LEU LYS
SEQRES 2 T 123 VAL ALA CYS VAL THR THR GLY ALA ALA LEU ILE GLY ILE
SEQRES 3 T 123 ARG MET THR GLY LYS ALA VAL ALA ALA VAL LYS GLN ILE
SEQRES 4 T 123 LYS ASP TYR MET LEU ASP ARG ILE ASN GLY VAL TYR GLY
SEQRES 5 T 123 ALA ASP ALA LYS PHE PRO VAL ARG ALA SER GLN ASP ASN
SEQRES 6 T 123 THR GLN VAL LYS ALA LEU TYR LYS SER TYR LEU GLU LYS
SEQRES 7 T 123 PRO LEU GLY HIS LYS SER HIS ASP LEU LEU HIS THR HIS
SEQRES 8 T 123 TRP PHE ASP LYS SER LYS GLY VAL LYS GLU LEU THR THR
SEQRES 9 T 123 ALA GLY LYS LEU PRO ASN PRO ARG ALA SER GLU PHE GLU
SEQRES 10 T 123 GLY PRO TYR PRO TYR GLU
SEQRES 1 M 421 MET SER ARG THR VAL MET GLU ARG ILE GLU TYR GLU MET
SEQRES 2 M 421 HIS THR PRO ASP PRO LYS ALA ASP PRO ASP LYS LEU HIS
SEQRES 3 M 421 PHE VAL GLN ILE ASP GLU ALA LYS CYS ILE GLY CYS ASP
SEQRES 4 M 421 THR CYS SER GLN TYR CYS PRO THR ALA ALA ILE PHE GLY
SEQRES 5 M 421 GLU MET GLY GLU PRO HIS SER ILE PRO HIS ILE GLU ALA
SEQRES 6 M 421 CYS ILE ASN CYS GLY GLN CYS LEU THR HIS CYS PRO GLU
SEQRES 7 M 421 ASN ALA ILE TYR GLU ALA GLN SER TRP VAL PRO GLU VAL
SEQRES 8 M 421 GLU LYS LYS LEU LYS ASP GLY LYS VAL LYS CYS ILE ALA
SEQRES 9 M 421 MET PRO ALA PRO ALA VAL ARG TYR ALA LEU GLY ASP ALA
SEQRES 10 M 421 PHE GLY MET PRO VAL GLY SER VAL THR THR GLY LYS MET
SEQRES 11 M 421 LEU ALA ALA LEU GLN LYS LEU GLY PHE ALA HIS CYS TRP
SEQRES 12 M 421 ASP THR GLU PHE THR ALA ASP VAL THR ILE TRP GLU GLU
SEQRES 13 M 421 GLY SER GLU PHE VAL GLU ARG LEU THR LYS LYS SER ASP
SEQRES 14 M 421 MET PRO LEU PRO GLN PHE THR SER CYS CYS PRO GLY TRP
SEQRES 15 M 421 GLN LYS TYR ALA GLU THR TYR TYR PRO GLU LEU LEU PRO
SEQRES 16 M 421 HIS PHE SER THR CYS LYS SER PRO ILE GLY MET ASN GLY
SEQRES 17 M 421 ALA LEU ALA LYS THR TYR GLY ALA GLU ARG MET LYS TYR
SEQRES 18 M 421 ASP PRO LYS GLN VAL TYR THR VAL SER ILE MET PRO CYS
SEQRES 19 M 421 ILE ALA LYS LYS TYR GLU GLY LEU ARG PRO GLU LEU LYS
SEQRES 20 M 421 SER SER GLY MET ARG ASP ILE ASP ALA THR LEU THR THR
SEQRES 21 M 421 ARG GLU LEU ALA TYR MET ILE LYS LYS ALA GLY ILE ASP
SEQRES 22 M 421 PHE ALA LYS LEU PRO ASP GLY LYS ARG ASP SER LEU MET
SEQRES 23 M 421 GLY GLU SER THR GLY GLY ALA THR ILE PHE GLY VAL THR
SEQRES 24 M 421 GLY GLY VAL MET GLU ALA ALA LEU ARG PHE ALA TYR GLU
SEQRES 25 M 421 ALA VAL THR GLY LYS LYS PRO ASP SER TRP ASP PHE LYS
SEQRES 26 M 421 ALA VAL ARG GLY LEU ASP GLY ILE LYS GLU ALA THR VAL
SEQRES 27 M 421 ASN VAL GLY GLY THR ASP VAL LYS VAL ALA VAL VAL HIS
SEQRES 28 M 421 GLY ALA LYS ARG PHE LYS GLN VAL CYS ASP ASP VAL LYS
SEQRES 29 M 421 ALA GLY LYS SER PRO TYR HIS PHE ILE GLU TYR MET ALA
SEQRES 30 M 421 CYS PRO GLY GLY CYS VAL CYS GLY GLY GLY GLN PRO VAL
SEQRES 31 M 421 MET PRO GLY VAL LEU GLU ALA MET ASP ARG THR THR THR
SEQRES 32 M 421 ARG LEU TYR ALA GLY LEU LYS LYS ARG LEU ALA MET ALA
SEQRES 33 M 421 SER ALA ASN LYS ALA
HET ZN S 500 1
HET FE2 L 426 1
HET FE2 L 427 1
HET CYN L 428 2
HET CYN L 429 2
HET SF4 L 422 8
HET SF4 L 423 8
HET SF4 L 424 8
HET PDT L 425 5
HET CMO L 430 2
HET CMO L 431 2
HET CYS L 432 7
HET FE2 M 426 1
HET FE2 M 427 1
HET CYN M 428 2
HET CYN M 429 2
HET SF4 M 422 8
HET SF4 M 423 8
HET SF4 M 424 8