HEADER OXIDOREDUCTASE 13-FEB-95 1AOR
TITLE STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME,
TITLE 2 ALDEHYDE FERREDOXIN OXIDOREDUCTASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE FERREDOXIN OXIDOREDUCTASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;
SOURCE 3 ORGANISM_TAXID: 2261
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.CHAN,S.MUKUND,A.KLETZIN,M.W.W.ADAMS,D.C.REES
REVDAT 4 24-MAR-09 1AOR 1 LINK ATOM CONECT
REVDAT 3 24-FEB-09 1AOR 1 VERSN
REVDAT 2 01-APR-03 1AOR 1 JRNL
REVDAT 1 20-APR-95 1AOR 0
JRNL AUTH M.K.CHAN,S.MUKUND,A.KLETZIN,M.W.ADAMS,D.C.REES
JRNL TITL STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN
JRNL TITL 2 ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE.
JRNL REF SCIENCE V. 267 1463 1995
JRNL REFN ISSN 0036-8075
JRNL PMID 7878465
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.KLETZIN,S.MUKUND,T.L.KELLEY-CROUSE,M.K.CHAN,
REMARK 1 AUTH 2 D.C.REES,M.W.W.ADAMS
REMARK 1 TITL MOLECULAR CHARACTERIZATION OF THE GENES ENCODING
REMARK 1 TITL 2 TWO TUNGSTEN-CONTAINING ENZYMES FROM
REMARK 1 TITL 3 HYPERTHERMOPHILIC ARCHAEA: ALDEHYDE FERREDOXIN
REMARK 1 TITL 4 OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS AND
REMARK 1 TITL 5 FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM
REMARK 1 TITL 6 THERMOCOCCUS LITORALIS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
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) (%) : 89.0
REMARK 3 NUMBER OF REFLECTIONS : 55520
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 9386
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 129
REMARK 3 SOLVENT ATOMS : 373
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 2.58
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 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:
REMARK 3 PLEASE NOTE THAT ALL RESIDUES WERE BUILT TO FIT THE BEST
REMARK 3 POSSIBLE OBSERVED DENSITY. THOSE SIDE CHAIN ATOMS WHICH
REMARK 3 SEEMED UNRELIABLE HAD THEIR OCCUPANCIES FIXED AT 0.0.
REMARK 4
REMARK 4 1AOR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : NULL
REMARK 200 RADIATION SOURCE : NULL
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56373
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 40.46950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.89600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.16600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.89600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.46950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.16600
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 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 ARG A 7 NE CZ NH1 NH2
REMARK 480 GLU A 26 CG CD OE1 OE2
REMARK 480 LYS A 151 CG CD CE NZ
REMARK 480 GLU A 156 CG CD OE1 OE2
REMARK 480 LYS A 214 CG CD CE NZ
REMARK 480 ARG A 229 NE CZ NH1 NH2
REMARK 480 ASN A 230 CG OD1 ND2
REMARK 480 ARG A 300 NE CZ NH1 NH2
REMARK 480 GLU A 366 CG CD OE1 OE2
REMARK 480 ASP A 517 CG OD1 OD2
REMARK 480 ARG A 547 NE CZ NH1 NH2
REMARK 480 GLU A 587 CG CD OE1 OE2
REMARK 480 GLU A 594 CG CD OE1 OE2
REMARK 480 GLU A 597 CG CD OE1 OE2
REMARK 480 GLU A 603 CG CD OE1 OE2
REMARK 480 ARG B 7 NE CZ NH1 NH2
REMARK 480 GLU B 26 CG CD OE1 OE2
REMARK 480 GLU B 117 CG CD OE1 OE2
REMARK 480 LYS B 118 CG CD CE NZ
REMARK 480 LYS B 125 CG CD CE NZ
REMARK 480 LYS B 151 CG CD CE NZ
REMARK 480 GLU B 156 CG CD OE1 OE2
REMARK 480 LYS B 157 CG CD CE NZ
REMARK 480 LYS B 214 CG CD CE NZ
REMARK 480 GLN B 215 CG CD OE1 NE2
REMARK 480 ARG B 300 NE CZ NH1 NH2
REMARK 480 GLU B 366 CG CD OE1 OE2
REMARK 480 ASP B 517 CG OD1 OD2
REMARK 480 ARG B 547 NE CZ NH1 NH2
REMARK 480 GLU B 587 CG CD OE1 OE2
REMARK 480 GLU B 594 CG CD OE1 OE2
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 ALA A 184 N - CA - C ANGL. DEV. = -19.8 DEGREES
REMARK 500 GLY A 185 N - CA - C ANGL. DEV. = 19.2 DEGREES
REMARK 500 LEU A 255 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 ALA B 184 N - CA - C ANGL. DEV. = -23.6 DEGREES
REMARK 500 GLY B 185 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 LEU B 255 CA - CB - CG ANGL. DEV. = 17.2 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 LEU A 32 -61.45 67.08
REMARK 500 SER A 34 -113.07 43.83
REMARK 500 PRO A 48 -9.72 -57.64
REMARK 500 ASP A 126 -117.52 58.57
REMARK 500 ALA A 184 77.72 -101.75
REMARK 500 ASP A 326 101.19 -54.49
REMARK 500 ALA A 426 40.59 -66.28
REMARK 500 ALA A 432 84.97 -161.53
REMARK 500 ASN A 451 71.02 -163.12
REMARK 500 LEU B 32 -60.73 59.54
REMARK 500 SER B 34 -110.67 32.91
REMARK 500 ASP B 126 -119.54 58.19
REMARK 500 ARG B 284 -179.15 -173.14
REMARK 500 ASP B 326 101.20 -53.60
REMARK 500 ALA B 426 35.93 -64.78
REMARK 500 ALA B 432 83.23 -163.71
REMARK 500 ASN B 451 65.34 -165.80
REMARK 500 TYR B 452 71.30 -66.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ALA A 184 45.2 L L OUTSIDE RANGE
REMARK 500 ILE A 449 22.8 L L OUTSIDE RANGE
REMARK 500 ALA B 184 47.2 L L OUTSIDE RANGE
REMARK 500 ILE B 449 22.8 L L OUTSIDE RANGE
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 PTE A 609 MG1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 93 O
REMARK 620 2 ALA A 183 O 89.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 606 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 332 OE1
REMARK 620 2 HIS A 383 NE2 91.3
REMARK 620 3 GLU B 332 OE1 134.7 111.9
REMARK 620 4 HIS B 383 NE2 109.7 118.5 93.0
REMARK 620 5 GLU A 332 OE2 52.4 141.7 91.2 88.7
REMARK 620 6 GLU B 332 OE2 92.4 88.4 52.2 143.6 82.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 PTE B 608 MG1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN B 93 O
REMARK 620 2 ALA B 183 O 90.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 607 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 181 O
REMARK 620 2 PTE A 609 O8 126.2
REMARK 620 3 HOH A5011 O 108.2 88.3
REMARK 620 4 HOH A5013 O 96.1 137.6 79.5
REMARK 620 5 HOH A5012 O 112.9 75.8 137.7 86.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 606 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 181 O
REMARK 620 2 PTE B 608 O8 102.7
REMARK 620 3 HOH B5026 O 106.7 76.0
REMARK 620 4 HOH B5024 O 123.2 133.2 82.4
REMARK 620 5 HOH B5025 O 105.5 80.1 143.3 94.6
REMARK 620 N 1 2 3 4
REMARK 700
REMARK 700 SHEET
REMARK 700 HELIX AND SHEET ENTRIES HAVE BEEN AUTOMATICALLY GENERATED
REMARK 700 BY THE PDB USING A PROGRAM BASED ON DSSP OF W. KABSCH AND
REMARK 700 C. SANDER
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PT1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE
REMARK 800 TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT A)
REMARK 800 SITE_IDENTIFIER: PT2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE
REMARK 800 TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT B).
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 606
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 607
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 606
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 608
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTE A 609
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 607
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTE B 608
DBREF 1AOR A 1 605 UNP Q51739 AOR_PYRFU 1 605
DBREF 1AOR B 1 605 UNP Q51739 AOR_PYRFU 1 605
SEQRES 1 A 605 MET TYR GLY ASN TRP GLY ARG PHE ILE ARG VAL ASN LEU
SEQRES 2 A 605 SER THR GLY ASP ILE LYS VAL GLU GLU TYR ASP GLU GLU
SEQRES 3 A 605 LEU ALA LYS LYS TRP LEU GLY SER ARG GLY LEU ALA ILE
SEQRES 4 A 605 TYR LEU LEU LEU LYS GLU MET ASP PRO THR VAL ASP PRO
SEQRES 5 A 605 LEU SER PRO GLU ASN LYS LEU ILE ILE ALA ALA GLY PRO
SEQRES 6 A 605 LEU THR GLY THR SER ALA PRO THR GLY GLY ARG TYR ASN
SEQRES 7 A 605 VAL VAL THR LYS SER PRO LEU THR GLY PHE ILE THR MET
SEQRES 8 A 605 ALA ASN SER GLY GLY TYR PHE GLY ALA GLU LEU LYS PHE
SEQRES 9 A 605 ALA GLY TYR ASP ALA ILE VAL VAL GLU GLY LYS ALA GLU
SEQRES 10 A 605 LYS PRO VAL TYR ILE TYR ILE LYS ASP GLU HIS ILE GLU
SEQRES 11 A 605 ILE ARG ASP ALA SER HIS ILE TRP GLY LYS LYS VAL SER
SEQRES 12 A 605 GLU THR GLU ALA THR ILE ARG LYS GLU VAL GLY SER GLU
SEQRES 13 A 605 LYS VAL LYS ILE ALA SER ILE GLY PRO ALA GLY GLU ASN
SEQRES 14 A 605 LEU VAL LYS PHE ALA ALA ILE MET ASN ASP GLY HIS ARG
SEQRES 15 A 605 ALA ALA GLY ARG GLY GLY VAL GLY ALA VAL MET GLY SER
SEQRES 16 A 605 LYS ASN LEU LYS ALA ILE ALA VAL GLU GLY SER LYS THR
SEQRES 17 A 605 VAL PRO ILE ALA ASP LYS GLN LYS PHE MET LEU VAL VAL
SEQRES 18 A 605 ARG GLU LYS VAL ASN LYS LEU ARG ASN ASP PRO VAL ALA
SEQRES 19 A 605 GLY GLY GLY LEU PRO LYS TYR GLY THR ALA VAL LEU VAL
SEQRES 20 A 605 ASN ILE ILE ASN GLU ASN GLY LEU TYR PRO VAL LYS ASN
SEQRES 21 A 605 PHE GLN THR GLY VAL TYR PRO TYR ALA TYR GLU GLN SER
SEQRES 22 A 605 GLY GLU ALA MET ALA ALA LYS TYR LEU VAL ARG ASN LYS
SEQRES 23 A 605 PRO CYS TYR ALA CYS PRO ILE GLY CYS GLY ARG VAL ASN
SEQRES 24 A 605 ARG LEU PRO THR VAL GLY GLU THR GLU GLY PRO GLU TYR
SEQRES 25 A 605 GLU SER VAL TRP ALA LEU GLY ALA ASN LEU GLY ILE ASN
SEQRES 26 A 605 ASP LEU ALA SER ILE ILE GLU ALA ASN HIS MET CYS ASP
SEQRES 27 A 605 GLU LEU GLY LEU ASP THR ILE SER THR GLY GLY THR LEU
SEQRES 28 A 605 ALA THR ALA MET GLU LEU TYR GLU LYS GLY HIS ILE LYS
SEQRES 29 A 605 ASP GLU GLU LEU GLY ASP ALA PRO PRO PHE ARG TRP GLY
SEQRES 30 A 605 ASN THR GLU VAL LEU HIS TYR TYR ILE GLU LYS ILE ALA
SEQRES 31 A 605 LYS ARG GLU GLY PHE GLY ASP LYS LEU ALA GLU GLY SER
SEQRES 32 A 605 TYR ARG LEU ALA GLU SER TYR GLY HIS PRO GLU LEU SER
SEQRES 33 A 605 MET THR VAL LYS LYS LEU GLU LEU PRO ALA TYR ASP PRO
SEQRES 34 A 605 ARG GLY ALA GLU GLY HIS GLY LEU GLY TYR ALA THR ASN
SEQRES 35 A 605 ASN ARG GLY GLY CYS HIS ILE LYS ASN TYR MET ILE SER
SEQRES 36 A 605 PRO GLU ILE LEU GLY TYR PRO TYR LYS MET ASP PRO HIS
SEQRES 37 A 605 ASP VAL SER ASP ASP LYS ILE LYS MET LEU ILE LEU PHE
SEQRES 38 A 605 GLN ASP LEU THR ALA LEU ILE ASP SER ALA GLY LEU CYS
SEQRES 39 A 605 LEU PHE THR THR PHE GLY LEU GLY ALA ASP ASP TYR ARG
SEQRES 40 A 605 ASP LEU LEU ASN ALA ALA LEU GLY TRP ASP PHE THR THR
SEQRES 41 A 605 GLU ASP TYR LEU LYS ILE GLY GLU ARG ILE TRP ASN ALA
SEQRES 42 A 605 GLU ARG LEU PHE ASN LEU LYS ALA GLY LEU ASP PRO ALA
SEQRES 43 A 605 ARG ASP ASP THR LEU PRO LYS ARG PHE LEU GLU GLU PRO
SEQRES 44 A 605 MET PRO GLU GLY PRO ASN LYS GLY HIS THR VAL ARG LEU
SEQRES 45 A 605 LYS GLU MET LEU PRO ARG TYR TYR LYS LEU ARG GLY TRP
SEQRES 46 A 605 THR GLU ASP GLY LYS ILE PRO LYS GLU LYS LEU GLU GLU
SEQRES 47 A 605 LEU GLY ILE ALA GLU PHE TYR
SEQRES 1 B 605 MET TYR GLY ASN TRP GLY ARG PHE ILE ARG VAL ASN LEU
SEQRES 2 B 605 SER THR GLY ASP ILE LYS VAL GLU GLU TYR ASP GLU GLU
SEQRES 3 B 605 LEU ALA LYS LYS TRP LEU GLY SER ARG GLY LEU ALA ILE
SEQRES 4 B 605 TYR LEU LEU LEU LYS GLU MET ASP PRO THR VAL ASP PRO
SEQRES 5 B 605 LEU SER PRO GLU ASN LYS LEU ILE ILE ALA ALA GLY PRO
SEQRES 6 B 605 LEU THR GLY THR SER ALA PRO THR GLY GLY ARG TYR ASN
SEQRES 7 B 605 VAL VAL THR LYS SER PRO LEU THR GLY PHE ILE THR MET
SEQRES 8 B 605 ALA ASN SER GLY GLY TYR PHE GLY ALA GLU LEU LYS PHE
SEQRES 9 B 605 ALA GLY TYR ASP ALA ILE VAL VAL GLU GLY LYS ALA GLU
SEQRES 10 B 605 LYS PRO VAL TYR ILE TYR ILE LYS ASP GLU HIS ILE GLU
SEQRES 11 B 605 ILE ARG ASP ALA SER HIS ILE TRP GLY LYS LYS VAL SER
SEQRES 12 B 605 GLU THR GLU ALA THR ILE ARG LYS GLU VAL GLY SER GLU
SEQRES 13 B 605 LYS VAL LYS ILE ALA SER ILE GLY PRO ALA GLY GLU ASN
SEQRES 14 B 605 LEU VAL LYS PHE ALA ALA ILE MET ASN ASP GLY HIS ARG
SEQRES 15 B 605 ALA ALA GLY ARG GLY GLY VAL GLY ALA VAL MET GLY SER
SEQRES 16 B 605 LYS ASN LEU LYS ALA ILE ALA VAL GLU GLY SER LYS THR
SEQRES 17 B 605 VAL PRO ILE ALA ASP LYS GLN LYS PHE MET LEU VAL VAL
SEQRES 18 B 605 ARG GLU LYS VAL ASN LYS LEU ARG ASN ASP PRO VAL ALA
SEQRES 19 B 605 GLY GLY GLY LEU PRO LYS TYR GLY THR ALA VAL LEU VAL
SEQRES 20 B 605 ASN ILE ILE ASN GLU ASN GLY LEU TYR PRO VAL LYS ASN
SEQRES 21 B 605 PHE GLN THR GLY VAL TYR PRO TYR ALA TYR GLU GLN SER
SEQRES 22 B 605 GLY GLU ALA MET ALA ALA LYS TYR LEU VAL ARG ASN LYS
SEQRES 23 B 605 PRO CYS TYR ALA CYS PRO ILE GLY CYS GLY ARG VAL ASN
SEQRES 24 B 605 ARG LEU PRO THR VAL GLY GLU THR GLU GLY PRO GLU TYR
SEQRES 25 B 605 GLU SER VAL TRP ALA LEU GLY ALA ASN LEU GLY ILE ASN
SEQRES 26 B 605 ASP LEU ALA SER ILE ILE GLU ALA ASN HIS MET CYS ASP
SEQRES 27 B 605 GLU LEU GLY LEU ASP THR ILE SER THR GLY GLY THR LEU
SEQRES 28 B 605 ALA THR ALA MET GLU LEU TYR GLU LYS GLY HIS ILE LYS
SEQRES 29 B 605 ASP GLU GLU LEU GLY ASP ALA PRO PRO PHE ARG TRP GLY
SEQRES 30 B 605 ASN THR GLU VAL LEU HIS TYR TYR ILE GLU LYS ILE ALA
SEQRES 31 B 605 LYS ARG GLU GLY PHE GLY ASP LYS LEU ALA GLU GLY SER
SEQRES 32 B 605 TYR ARG LEU ALA GLU SER TYR GLY HIS PRO GLU LEU SER
SEQRES 33 B 605 MET THR VAL LYS LYS LEU GLU LEU PRO ALA TYR ASP PRO
SEQRES 34 B 605 ARG GLY ALA GLU GLY HIS GLY LEU GLY TYR ALA THR ASN
SEQRES 35 B 605 ASN ARG GLY GLY CYS HIS ILE LYS ASN TYR MET ILE SER
SEQRES 36 B 605 PRO GLU ILE LEU GLY TYR PRO TYR LYS MET ASP PRO HIS
SEQRES 37 B 605 ASP VAL SER ASP ASP LYS ILE LYS MET LEU ILE LEU PHE
SEQRES 38 B 605 GLN ASP LEU THR ALA LEU ILE ASP SER ALA GLY LEU CYS
SEQRES 39 B 605 LEU PHE THR THR PHE GLY LEU GLY ALA ASP ASP TYR ARG
SEQRES 40 B 605 ASP LEU LEU ASN ALA ALA LEU GLY TRP ASP PHE THR THR
SEQRES 41 B 605 GLU ASP TYR LEU LYS ILE GLY GLU ARG ILE TRP ASN ALA
SEQRES 42 B 605 GLU ARG LEU PHE ASN LEU LYS ALA GLY LEU ASP PRO ALA
SEQRES 43 B 605 ARG ASP ASP THR LEU PRO LYS ARG PHE LEU GLU GLU PRO
SEQRES 44 B 605 MET PRO GLU GLY PRO ASN LYS GLY HIS THR VAL ARG LEU
SEQRES 45 B 605 LYS GLU MET LEU PRO ARG TYR TYR LYS LEU ARG GLY TRP
SEQRES 46 B 605 THR GLU ASP GLY LYS ILE PRO LYS GLU LYS LEU GLU GLU
SEQRES 47 B 605 LEU GLY ILE ALA GLU PHE TYR
HET FE A 606 1
HET NA A 607 1
HET NA B 606 1
HET SF4 A 608 8
HET PTE A 609 52
HET SF4 B 607 8
HET PTE B 608 52
HETNAM FE FE (III) ION
HETNAM NA SODIUM ION
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM PTE TUNGSTOPTERIN COFACTOR
FORMUL 3 FE FE 3+
FORMUL 4 NA 2(NA 1+)
FORMUL 6 SF4 2(FE4 S4)
FORMUL 7 PTE 2(C20 H29 MG N10 O14 P2 S4 W)
FORMUL 10 HOH *379(H2 O)
HELIX 1 1 GLU A 25 TRP A 31 1 7
HELIX 2 2 SER A 34 GLU A 45 1 12
HELIX 3 3 PHE A 98 PHE A 104 1 7
HELIX 4 4 VAL A 142 VAL A 153 1 12
HELIX 5 5 PRO A 165 GLU A 168 1 4
HELIX 6 6 VAL A 189 LYS A 196 1 8
HELIX 7 7 LYS A 214 ASN A 230 1 17
HELIX 8 8 PRO A 232 GLY A 235 1 4
HELIX 9 9 GLY A 237 TYR A 241 1 5
HELIX 10 10 THR A 243 GLU A 252 5 10
HELIX 11 11 ALA A 269 GLN A 272 5 4
HELIX 12 12 GLY A 274 LYS A 280 1 7
HELIX 13 13 TYR A 312 LEU A 318 1 7
HELIX 14 14 ALA A 320 LEU A 322 5 3
HELIX 15 15 LEU A 327 LEU A 340 1 14
HELIX 16 16 THR A 344 GLU A 359 1 16
HELIX 17 17 ASP A 365 LEU A 368 1 4
HELIX 18 18 THR A 379 ALA A 390 5 12
HELIX 19 19 GLY A 394 GLU A 401 5 8
HELIX 20 20 SER A 403 TYR A 410 1 8
HELIX 21 21 PRO A 413 LEU A 415 5 3
HELIX 22 22 PRO A 429 GLY A 431 5 3
HELIX 23 23 GLU A 433 THR A 441 1 9
HELIX 24 24 ILE A 449 ASN A 451 5 3
HELIX 25 25 ILE A 454 GLU A 457 1 4
HELIX 26 26 ASP A 472 ALA A 491 1 20
HELIX 27 27 LEU A 495 THR A 498 5 4
HELIX 28 28 ALA A 503 LEU A 514 1 12
HELIX 29 29 THR A 520 ALA A 541 1 22
HELIX 30 30 PRO A 545 ASP A 548 1 4
HELIX 31 31 LYS A 553 GLU A 557 1 5
HELIX 32 32 LEU A 572 ARG A 583 1 12
HELIX 33 33 LYS A 593 LEU A 599 1 7
HELIX 34 34 ALA A 602 PHE A 604 5 3
HELIX 35 35 GLU B 25 TRP B 31 1 7
HELIX 36 36 SER B 34 GLU B 45 1 12
HELIX 37 37 PHE B 98 ALA B 105 1 8
HELIX 38 38 VAL B 142 GLU B 152 1 11
HELIX 39 39 PRO B 165 GLU B 168 1 4
HELIX 40 40 VAL B 189 LYS B 196 1 8
HELIX 41 41 LYS B 214 ASN B 230 1 17
HELIX 42 42 PRO B 232 GLY B 235 1 4
HELIX 43 43 GLY B 237 TYR B 241 1 5
HELIX 44 44 THR B 243 GLU B 252 5 10
HELIX 45 45 ALA B 269 GLN B 272 5 4
HELIX 46 46 GLY B 274 LYS B 280 1 7
HELIX 47 47 TYR B 312 ALA B 317 1 6
HELIX 48 48 ALA B 320 LEU B 322 5 3
HELIX 49 49 LEU B 327 LEU B 340 1 14
HELIX 50 50 THR B 344 GLU B 359 1 16
HELIX 51 51 ASP B 365 LEU B 368 1 4
HELIX 52 52 THR B 379 ALA B 390 5 12
HELIX 53 53 GLY B 394 GLU B 401 5 8
HELIX 54 54 SER B 403 TYR B 410 1 8
HELIX 55 55 PRO B 413 LEU B 415 5 3
HELIX 56 56 PRO B 429 GLY B 431 5 3
HELIX 57 57 GLU B 433 THR B 441 1 9
HELIX 58 58 ILE B 449 ASN B 451 5 3
HELIX 59 59 ILE B 454 GLU B 457 1 4
HELIX 60 60 ASP B 472 ALA B 491 1 20
HELIX 61 61 LEU B 495 THR B 498 5 4
HELIX 62 62 ALA B 503 LEU B 514 1 12
HELIX 63 63 THR B 520 ALA B 541 1 22
HELIX 64 64 PRO B 545 ASP B 548 1 4
HELIX 65 65 LYS B 553 GLU B 557 1 5
HELIX 66 66 LEU B 572 ARG B 583 1 12
HELIX 67 67 LYS B 593 GLU B 598 1 6
SHEET 1 A 6 ASP A 17 GLU A 22 0
SHEET 2 A 6 ARG A 7 ASN A 12 -1 N ASN A 12 O ASP A 17
SHEET 3 A 6 ALA A 109 GLU A 113 1 N ALA A 109 O ILE A 9
SHEET 4 A 6 LEU A 59 ALA A 63 -1 N ILE A 61 O ILE A 110
SHEET 5 A 6 TYR A 77 LYS A 82 -1 N VAL A 80 O ILE A 60
SHEET 6 A 6 ILE A 89 SER A 94 -1 N SER A 94 O TYR A 77
SHEET 1 B 4 HIS A 128 ASP A 133 0
SHEET 2 B 4 VAL A 120 LYS A 125 -1 N LYS A 125 O HIS A 128
SHEET 3 B 4 LEU A 198 GLU A 204 1 N LYS A 199 O VAL A 120
SHEET 4 B 4 LYS A 159 SER A 162 -1 N ALA A 161 O ILE A 201
SHEET 1 C 2 ILE A 176 ASN A 178 0
SHEET 2 C 2 ARG A 182 ALA A 184 -1 N ALA A 184 O ILE A 176
SHEET 1 D 3 GLY A 305 GLU A 308 0
SHEET 2 D 3 GLY A 296 LEU A 301 -1 N LEU A 301 O GLY A 305
SHEET 3 D 3 LEU A 282 LYS A 286 -1 N LYS A 286 O GLY A 296
SHEET 1 E 6 ASP B 17 GLU B 22 0
SHEET 2 E 6 ARG B 7 ASN B 12 -1 N ASN B 12 O ASP B 17
SHEET 3 E 6 ALA B 109 GLU B 113 1 N ALA B 109 O ILE B 9
SHEET 4 E 6 LEU B 59 ALA B 63 -1 N ILE B 61 O ILE B 110
SHEET 5 E 6 TYR B 77 LYS B 82 -1 N VAL B 80 O ILE B 60
SHEET 6 E 6 ILE B 89 SER B 94 -1 N SER B 94 O TYR B 77
SHEET 1 F 4 HIS B 128 ASP B 133 0
SHEET 2 F 4 VAL B 120 LYS B 125 -1 N LYS B 125 O HIS B 128
SHEET 3 F 4 LEU B 198 GLU B 204 1 N LYS B 199 O VAL B 120
SHEET 4 F 4 LYS B 159 SER B 162 -1 N ALA B 161 O ILE B 201
SHEET 1 G 2 ILE B 176 ASN B 178 0
SHEET 2 G 2 ARG B 182 ALA B 184 -1 N ALA B 184 O ILE B 176
SHEET 1 H 3 GLY B 305 GLU B 308 0
SHEET 2 H 3 GLY B 296 LEU B 301 -1 N LEU B 301 O GLY B 305
SHEET 3 H 3 LEU B 282 LYS B 286 -1 N LYS B 286 O GLY B 296
LINK O ASN A 93 MG1 PTE A 609 1555 1555 2.05
LINK O ALA A 183 MG1 PTE A 609 1555 1555 2.08
LINK SG CYS A 288 FE1 SF4 A 608 1555 1555 2.31
LINK SG CYS A 291 FE3 SF4 A 608 1555 1555 2.31
LINK SG CYS A 295 FE4 SF4 A 608 1555 1555 2.32
LINK OE1 GLU A 332 FE FE A 606 1555 1555 2.01
LINK NE2 HIS A 383 FE FE A 606 1555 1555 2.07
LINK SG CYS A 494 FE2 SF4 A 608 1555 1555 2.33
LINK O ASN B 93 MG1 PTE B 608 1555 1555 2.08
LINK O ALA B 183 MG1 PTE B 608 1555 1555 2.04
LINK SG CYS B 288 FE1 SF4 B 607 1555 1555 2.31
LINK SG CYS B 291 FE3 SF4 B 607 1555 1555 2.31
LINK SG CYS B 295 FE4 SF4 B 607 1555 1555 2.31
LINK OE1 GLU B 332 FE FE A 606 1555 1555 2.05
LINK NE2 HIS B 383 FE FE A 606 1555 1555 2.05
LINK SG CYS B 494 FE2 SF4 B 607 1555 1555 2.28
LINK O HIS A 181 NA NA A 607 1555 1555 2.14
LINK O HIS B 181 NA NA B 606 1555 1555 2.12
LINK NA NA A 607 O8 PTE A 609 1555 1555 2.46
LINK NA NA B 606 O8 PTE B 608 1555 1555 2.78
LINK NA NA A 607 O HOH A5011 1555 1555 2.13
LINK NA NA A 607 O HOH A5013 1555 1555 2.11
LINK NA NA A 607 O HOH A5012 1555 1555 2.09
LINK NA NA B 606 O HOH B5026 1555 1555 2.12
LINK NA NA B 606 O HOH B5024 1555 1555 2.11
LINK NA NA B 606 O HOH B5025 1555 1555 2.13
LINK FE FE A 606 OE2 GLU A 332 1555 1555 2.71
LINK FE FE A 606 OE2 GLU B 332 1555 1555 2.72
CISPEP 1 GLY A 309 PRO A 310 0 -0.02
CISPEP 2 TYR A 461 PRO A 462 0 0.12
CISPEP 3 GLY B 309 PRO B 310 0 0.51
CISPEP 4 TYR B 461 PRO B 462 0 0.29
SITE 1 PT1 1 PTE A 609
SITE 1 PT2 1 PTE B 608
SITE 1 AC1 4 GLU A 332 HIS A 383 GLU B 332 HIS B 383
SITE 1 AC2 5 HIS A 181 PTE A 609 HOH A5011 HOH A5012
SITE 2 AC2 5 HOH A5013
SITE 1 AC3 5 HIS B 181 PTE B 608 HOH B5024 HOH B5025
SITE 2 AC3 5 HOH B5026
SITE 1 AC4 9 THR A 73 ARG A 76 ARG A 182 CYS A 288
SITE 2 AC4 9 CYS A 291 CYS A 295 CYS A 494 PHE A 496
SITE 3 AC4 9 PTE A 609
SITE 1 AC5 28 ARG A 76 ALA A 92 ASN A 93 SER A 94
SITE 2 AC5 28 GLY A 95 ARG A 182 ALA A 183 GLY A 185
SITE 3 AC5 28 ARG A 186 GLU A 311 GLU A 313 ASP A 338
SITE 4 AC5 28 LEU A 342 ASP A 343 THR A 344 ARG A 444
SITE 5 AC5 28 HIS A 448 ILE A 449 LYS A 450 ASP A 489
SITE 6 AC5 28 LEU A 493 CYS A 494 LEU A 495 PHE A 496
SITE 7 AC5 28 NA A 607 SF4 A 608 HOH A5012 HOH A5115
SITE 1 AC6 6 ARG B 76 CYS B 288 CYS B 291 CYS B 295
SITE 2 AC6 6 CYS B 494 PHE B 496
SITE 1 AC7 27 ARG B 76 ALA B 92 ASN B 93 SER B 94
SITE 2 AC7 27 GLY B 95 ARG B 182 ALA B 183 ALA B 184
SITE 3 AC7 27 GLY B 185 ARG B 186 GLU B 311 GLU B 313
SITE 4 AC7 27 ASP B 338 LEU B 342 ASP B 343 THR B 344
SITE 5 AC7 27 ARG B 444 ILE B 449 LYS B 450 ASP B 489
SITE 6 AC7 27 LEU B 493 CYS B 494 LEU B 495 PHE B 496
SITE 7 AC7 27 NA B 606 HOH B5026 HOH B5032
CRYST1 80.939 108.332 159.792 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 0.012355 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009231 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006258 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
