HEADER OXIDOREDUCTASE 28-JUL-00 1FGM
TITLE LIPOXYGENASE-1 (SOYBEAN) AT 100K, N694H MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEED LIPOXYGENASE-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: L-1;
COMPND 5 EC: 1.13.11.12;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DIOXYGENASE, LIPOXYGENASE, METALLOPROTEIN, FATTY ACIDS,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.TOMCHICK,W.MINOR,T.R.HOLMAN
REVDAT 6 09-AUG-23 1FGM 1 REMARK
REVDAT 5 13-APR-22 1FGM 1 AUTHOR JRNL
REVDAT 4 03-NOV-21 1FGM 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1FGM 1 VERSN
REVDAT 2 01-APR-03 1FGM 1 JRNL
REVDAT 1 24-OCT-01 1FGM 0
JRNL AUTH D.R.TOMCHICK,P.PHAN,M.CYMBOROWSKI,W.MINOR,T.R.HOLMAN
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF
JRNL TITL 2 SECOND-COORDINATION SPHERE MUTANTS OF SOYBEAN
JRNL TITL 3 LIPOXYGENASE-1.
JRNL REF BIOCHEMISTRY V. 40 7509 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11412104
JRNL DOI 10.1021/BI002893D
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.MINOR,J.STECZKO,B.STEC,Z.OTWINOWSKI,J.T.BOLIN,R.WALTER,
REMARK 1 AUTH 2 B.AXELROD
REMARK 1 TITL CRYSTAL STRUCTURE OF SOYBEAN LIPOXYGENASE L-1 AT 1.4 A
REMARK 1 TITL 2 RESOLUTION
REMARK 1 REF BIOCHEMISTRY V. 35 10687 1996
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI960576U
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.J.NELSON,S.P.SEITZ
REMARK 1 TITL THE STRUCTURE AND FUNCTION OF LIPOXYGENASE
REMARK 1 REF CURR.OPIN.STRUCT.BIOL. V. 4 878 1994
REMARK 1 REFN ISSN 0959-440X
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.JONSSON,M.H.GLICKMAN,S.SUN,J.P.KLINMAN
REMARK 1 TITL EXPERIMENTAL EVIDENCE FOR EXTENSIVE TUNNELING OF HYDROGEN IN
REMARK 1 TITL 2 THE LIPOXYGENASE REACTION: IMPLICATIONS FOR ENZYME CATALYSIS
REMARK 1 REF J.AM.CHEM.SOC. V. 118 10319 1996
REMARK 1 REFN ISSN 0002-7863
REMARK 1 DOI 10.1021/JA961827P
REMARK 1 REFERENCE 4
REMARK 1 AUTH M.H.GLICKMAN,J.P.KLINMAN
REMARK 1 TITL NATURE OF THE RATE-LIMITING STEPS IN THE SOYBEAN
REMARK 1 TITL 2 LIPOXYGENASE-1 REACTION
REMARK 1 REF BIOCHEMISTRY V. 34 14077 1995
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 5
REMARK 1 AUTH J.C.BOYINGTON,B.J.GAFFNEY,L.M.AMZEL
REMARK 1 TITL THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID
REMARK 1 TITL 2 15-LIPOXYGENASE
REMARK 1 REF SCIENCE V. 260 1482 1993
REMARK 1 REFN ISSN 0036-8075
REMARK 1 REFERENCE 6
REMARK 1 AUTH W.MINOR,J.STECZKO,J.T.BOLIN,Z.OTWINOWSKI,B.AXELROD
REMARK 1 TITL CRYSTALLOGRAPHIC DETERMINATION OF THE ACTIVE SITE IRON AND
REMARK 1 TITL 2 ITS LIGANDS IN SOYBEAN LIPOXYGENASE L-1
REMARK 1 REF BIOCHEMISTRY V. 32 6320 1993
REMARK 1 REFN ISSN 0006-2960
REMARK 1 REFERENCE 7
REMARK 1 AUTH J.STECZKO,C.R.MUCHMORE,J.L.SMITH,B.AXELROD
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION OF
REMARK 1 TITL 2 LIPOXYGENASE 1 FROM SOYBEANS
REMARK 1 REF J.BIOL.CHEM. V. 265 11352 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
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) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 65373
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) : 0.178
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3314
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.96
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4562
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE : 0.3370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.44
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 231
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 : 6519
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 681
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.57
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 2.04300
REMARK 3 B33 (A**2) : -2.13300
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.35100
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.24
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.471
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.83
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.948
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) : 1.456 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.014 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.198 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.983 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : ANISOTROPIC
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 47.41
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 1FGM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011569.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-97
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : 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 : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 65373
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 3.070
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.31200
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: IR
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: 1F8N
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, SODIUM ACETATE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 46.38500
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 A 1
REMARK 465 PHE A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 GLY A 5
REMARK 465 HIS A 6
REMARK 465 GLU A 21
REMARK 465 VAL A 22
REMARK 465 ASN A 23
REMARK 465 PRO A 24
REMARK 465 ASP A 25
REMARK 465 GLY A 26
REMARK 465 SER A 27
REMARK 465 ALA A 28
REMARK 465 VAL A 29
REMARK 465 ASP A 30
REMARK 465 ILE A 117
REMARK 465 SER A 118
REMARK 465 ASN A 119
REMARK 465 GLN A 120
REMARK 465 GLY A 121
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 ALA A 116 CB
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 -54.83 -22.77
REMARK 500 LEU A 36 -160.71 -79.54
REMARK 500 ASP A 51 -166.29 -75.99
REMARK 500 SER A 70 -75.20 -116.09
REMARK 500 THR A 73 90.62 -56.71
REMARK 500 LEU A 74 82.14 -176.92
REMARK 500 ALA A 76 55.70 38.88
REMARK 500 ASN A 146 18.76 -67.58
REMARK 500 TYR A 214 147.99 -172.60
REMARK 500 GLU A 294 -97.95 -110.74
REMARK 500 VAL A 312 -57.16 74.28
REMARK 500 GLN A 322 -59.33 -123.00
REMARK 500 ALA A 352 17.35 -145.52
REMARK 500 LEU A 390 41.40 -105.47
REMARK 500 MET A 497 -62.19 -107.87
REMARK 500 HIS A 499 -73.70 -95.36
REMARK 500 THR A 503 -80.40 -117.76
REMARK 500 SER A 560 -128.08 53.08
REMARK 500 SER A 687 -86.68 -102.97
REMARK 500 THR A 739 132.04 -38.75
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 FE A 840 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 499 NE2
REMARK 620 2 HIS A 504 NE2 96.7
REMARK 620 3 HIS A 690 NE2 109.1 101.8
REMARK 620 4 HIS A 694 ND1 85.4 167.3 89.3
REMARK 620 5 ILE A 839 OXT 164.1 87.1 85.1 87.7
REMARK 620 6 HOH A1522 O 87.2 79.3 163.2 88.3 78.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 840
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1YGE RELATED DB: PDB
REMARK 900 1YGE IS LIPOXYGENASE-1 (SOYBEAN)
REMARK 900 RELATED ID: 1F8N RELATED DB: PDB
REMARK 900 1F8N IS LIPOXYGENASE-1 (SOYBEAN), NEW REFINEMENT
REMARK 900 RELATED ID: 1FGO RELATED DB: PDB
REMARK 900 1FGO IS LIPOXYGENASE-1 (SOYBEAN), Q495A MUTANT
REMARK 900 RELATED ID: 1FGQ RELATED DB: PDB
REMARK 900 1FGQ IS LIPOXYGENASE-1 (SOYBEAN), Q495E MUTANT
REMARK 900 RELATED ID: 1FGR RELATED DB: PDB
REMARK 900 1FGR IS LIPOXYGENASE-1 (SOYBEAN), Q697E MUTANT
REMARK 900 RELATED ID: 1FGT RELATED DB: PDB
REMARK 900 1FGT IS LIPOXYGENASE-1 (SOYBEAN), Q697N MUTANT
DBREF 1FGM A 1 839 UNP P08170 LOX1_SOYBN 1 839
SEQADV 1FGM HIS A 694 UNP P08170 ASN 694 ENGINEERED MUTATION
SEQRES 1 A 839 MET PHE SER ALA GLY HIS LYS ILE LYS GLY THR VAL VAL
SEQRES 2 A 839 LEU MET PRO LYS ASN GLU LEU GLU VAL ASN PRO ASP GLY
SEQRES 3 A 839 SER ALA VAL ASP ASN LEU ASN ALA PHE LEU GLY ARG SER
SEQRES 4 A 839 VAL SER LEU GLN LEU ILE SER ALA THR LYS ALA ASP ALA
SEQRES 5 A 839 HIS GLY LYS GLY LYS VAL GLY LYS ASP THR PHE LEU GLU
SEQRES 6 A 839 GLY ILE ASN THR SER LEU PRO THR LEU GLY ALA GLY GLU
SEQRES 7 A 839 SER ALA PHE ASN ILE HIS PHE GLU TRP ASP GLY SER MET
SEQRES 8 A 839 GLY ILE PRO GLY ALA PHE TYR ILE LYS ASN TYR MET GLN
SEQRES 9 A 839 VAL GLU PHE PHE LEU LYS SER LEU THR LEU GLU ALA ILE
SEQRES 10 A 839 SER ASN GLN GLY THR ILE ARG PHE VAL CYS ASN SER TRP
SEQRES 11 A 839 VAL TYR ASN THR LYS LEU TYR LYS SER VAL ARG ILE PHE
SEQRES 12 A 839 PHE ALA ASN HIS THR TYR VAL PRO SER GLU THR PRO ALA
SEQRES 13 A 839 PRO LEU VAL SER TYR ARG GLU GLU GLU LEU LYS SER LEU
SEQRES 14 A 839 ARG GLY ASN GLY THR GLY GLU ARG LYS GLU TYR ASP ARG
SEQRES 15 A 839 ILE TYR ASP TYR ASP VAL TYR ASN ASP LEU GLY ASN PRO
SEQRES 16 A 839 ASP LYS SER GLU LYS LEU ALA ARG PRO VAL LEU GLY GLY
SEQRES 17 A 839 SER SER THR PHE PRO TYR PRO ARG ARG GLY ARG THR GLY
SEQRES 18 A 839 ARG GLY PRO THR VAL THR ASP PRO ASN THR GLU LYS GLN
SEQRES 19 A 839 GLY GLU VAL PHE TYR VAL PRO ARG ASP GLU ASN LEU GLY
SEQRES 20 A 839 HIS LEU LYS SER LYS ASP ALA LEU GLU ILE GLY THR LYS
SEQRES 21 A 839 SER LEU SER GLN ILE VAL GLN PRO ALA PHE GLU SER ALA
SEQRES 22 A 839 PHE ASP LEU LYS SER THR PRO ILE GLU PHE HIS SER PHE
SEQRES 23 A 839 GLN ASP VAL HIS ASP LEU TYR GLU GLY GLY ILE LYS LEU
SEQRES 24 A 839 PRO ARG ASP VAL ILE SER THR ILE ILE PRO LEU PRO VAL
SEQRES 25 A 839 ILE LYS GLU LEU TYR ARG THR ASP GLY GLN HIS ILE LEU
SEQRES 26 A 839 LYS PHE PRO GLN PRO HIS VAL VAL GLN VAL SER GLN SER
SEQRES 27 A 839 ALA TRP MET THR ASP GLU GLU PHE ALA ARG GLU MET ILE
SEQRES 28 A 839 ALA GLY VAL ASN PRO CYS VAL ILE ARG GLY LEU GLU GLU
SEQRES 29 A 839 PHE PRO PRO LYS SER ASN LEU ASP PRO ALA ILE TYR GLY
SEQRES 30 A 839 ASP GLN SER SER LYS ILE THR ALA ASP SER LEU ASP LEU
SEQRES 31 A 839 ASP GLY TYR THR MET ASP GLU ALA LEU GLY SER ARG ARG
SEQRES 32 A 839 LEU PHE MET LEU ASP TYR HIS ASP ILE PHE MET PRO TYR
SEQRES 33 A 839 VAL ARG GLN ILE ASN GLN LEU ASN SER ALA LYS THR TYR
SEQRES 34 A 839 ALA THR ARG THR ILE LEU PHE LEU ARG GLU ASP GLY THR
SEQRES 35 A 839 LEU LYS PRO VAL ALA ILE GLU LEU SER LEU PRO HIS SER
SEQRES 36 A 839 ALA GLY ASP LEU SER ALA ALA VAL SER GLN VAL VAL LEU
SEQRES 37 A 839 PRO ALA LYS GLU GLY VAL GLU SER THR ILE TRP LEU LEU
SEQRES 38 A 839 ALA LYS ALA TYR VAL ILE VAL ASN ASP SER CYS TYR HIS
SEQRES 39 A 839 GLN LEU MET SER HIS TRP LEU ASN THR HIS ALA ALA MET
SEQRES 40 A 839 GLU PRO PHE VAL ILE ALA THR HIS ARG HIS LEU SER VAL
SEQRES 41 A 839 LEU HIS PRO ILE TYR LYS LEU LEU THR PRO HIS TYR ARG
SEQRES 42 A 839 ASN ASN MET ASN ILE ASN ALA LEU ALA ARG GLN SER LEU
SEQRES 43 A 839 ILE ASN ALA ASN GLY ILE ILE GLU THR THR PHE LEU PRO
SEQRES 44 A 839 SER LYS TYR SER VAL GLU MET SER SER ALA VAL TYR LYS
SEQRES 45 A 839 ASN TRP VAL PHE THR ASP GLN ALA LEU PRO ALA ASP LEU
SEQRES 46 A 839 ILE LYS ARG GLY VAL ALA ILE LYS ASP PRO SER THR PRO
SEQRES 47 A 839 HIS GLY VAL ARG LEU LEU ILE GLU ASP TYR PRO TYR ALA
SEQRES 48 A 839 ALA ASP GLY LEU GLU ILE TRP ALA ALA ILE LYS THR TRP
SEQRES 49 A 839 VAL GLN GLU TYR VAL PRO LEU TYR TYR ALA ARG ASP ASP
SEQRES 50 A 839 ASP VAL LYS ASN ASP SER GLU LEU GLN HIS TRP TRP LYS
SEQRES 51 A 839 GLU ALA VAL GLU LYS GLY HIS GLY ASP LEU LYS ASP LYS
SEQRES 52 A 839 PRO TRP TRP PRO LYS LEU GLN THR LEU GLU ASP LEU VAL
SEQRES 53 A 839 GLU VAL CYS LEU ILE ILE ILE TRP ILE ALA SER ALA LEU
SEQRES 54 A 839 HIS ALA ALA VAL HIS PHE GLY GLN TYR PRO TYR GLY GLY
SEQRES 55 A 839 LEU ILE MET ASN ARG PRO THR ALA SER ARG ARG LEU LEU
SEQRES 56 A 839 PRO GLU LYS GLY THR PRO GLU TYR GLU GLU MET ILE ASN
SEQRES 57 A 839 ASN HIS GLU LYS ALA TYR LEU ARG THR ILE THR SER LYS
SEQRES 58 A 839 LEU PRO THR LEU ILE SER LEU SER VAL ILE GLU ILE LEU
SEQRES 59 A 839 SER THR HIS ALA SER ASP GLU VAL TYR LEU GLY GLN ARG
SEQRES 60 A 839 ASP ASN PRO HIS TRP THR SER ASP SER LYS ALA LEU GLN
SEQRES 61 A 839 ALA PHE GLN LYS PHE GLY ASN LYS LEU LYS GLU ILE GLU
SEQRES 62 A 839 GLU LYS LEU VAL ARG ARG ASN ASN ASP PRO SER LEU GLN
SEQRES 63 A 839 GLY ASN ARG LEU GLY PRO VAL GLN LEU PRO TYR THR LEU
SEQRES 64 A 839 LEU TYR PRO SER SER GLU GLU GLY LEU THR PHE ARG GLY
SEQRES 65 A 839 ILE PRO ASN SER ILE SER ILE
HET FE A 840 1
HETNAM FE FE (III) ION
FORMUL 2 FE FE 3+
FORMUL 3 HOH *681(H2 O)
HELIX 1 1 ASN A 18 LEU A 20 5 3
HELIX 2 2 ASN A 31 LEU A 36 5 6
HELIX 3 3 ASP A 88 GLY A 92 5 5
HELIX 4 4 THR A 134 TYR A 137 5 4
HELIX 5 5 VAL A 150 THR A 154 5 5
HELIX 6 6 LEU A 158 GLY A 171 1 14
HELIX 7 7 SER A 198 ALA A 202 5 5
HELIX 8 8 PRO A 241 ASN A 245 5 5
HELIX 9 9 LYS A 250 ASP A 253 5 4
HELIX 10 10 ALA A 254 ILE A 265 1 12
HELIX 11 11 ILE A 265 LEU A 276 1 12
HELIX 12 12 SER A 285 ASP A 291 1 7
HELIX 13 13 LEU A 292 GLU A 294 5 3
HELIX 14 14 PRO A 300 ILE A 308 1 9
HELIX 15 15 VAL A 312 LEU A 316 5 5
HELIX 16 16 PRO A 330 GLN A 334 5 5
HELIX 17 17 SER A 338 MET A 341 5 4
HELIX 18 18 THR A 342 GLY A 353 1 12
HELIX 19 19 ASP A 372 GLY A 377 1 6
HELIX 20 20 THR A 384 LEU A 388 5 5
HELIX 21 21 THR A 394 SER A 401 1 8
HELIX 22 22 TYR A 409 GLN A 422 1 14
HELIX 23 23 GLU A 472 MET A 497 1 26
HELIX 24 24 THR A 503 LEU A 518 1 16
HELIX 25 25 HIS A 522 THR A 529 1 8
HELIX 26 26 PRO A 530 ARG A 533 5 4
HELIX 27 27 ASN A 534 LEU A 546 1 13
HELIX 28 28 GLY A 551 PHE A 557 1 7
HELIX 29 29 PRO A 559 LYS A 561 5 3
HELIX 30 30 TYR A 562 LYS A 572 1 11
HELIX 31 31 ASN A 573 TRP A 574 5 2
HELIX 32 32 VAL A 575 GLN A 579 5 5
HELIX 33 33 ALA A 580 ARG A 588 1 9
HELIX 34 34 TYR A 608 VAL A 629 1 22
HELIX 35 35 PRO A 630 TYR A 632 5 3
HELIX 36 36 ARG A 635 ASN A 641 1 7
HELIX 37 37 ASP A 642 LYS A 655 1 14
HELIX 38 38 HIS A 657 LYS A 661 5 5
HELIX 39 39 THR A 671 SER A 687 1 17
HELIX 40 40 SER A 687 PHE A 695 1 9
HELIX 41 41 GLY A 696 GLY A 702 1 7
HELIX 42 42 THR A 720 ASN A 729 1 10
HELIX 43 43 ASN A 729 ILE A 738 1 10
HELIX 44 44 SER A 740 SER A 755 1 16
HELIX 45 45 ASP A 775 ASP A 802 1 28
HELIX 46 46 LEU A 805 LEU A 810 1 6
SHEET 1 A 5 GLY A 66 ASN A 68 0
SHEET 2 A 5 SER A 79 PHE A 85 -1 O ALA A 80 N ASN A 68
SHEET 3 A 5 ILE A 8 PRO A 16 -1 N ILE A 8 O PHE A 85
SHEET 4 A 5 PHE A 107 GLU A 115 -1 N PHE A 108 O MET A 15
SHEET 5 A 5 ILE A 123 VAL A 131 -1 O ILE A 123 N LEU A 114
SHEET 1 B 4 ARG A 141 PHE A 144 0
SHEET 2 B 4 PRO A 94 ASN A 101 -1 N PHE A 97 O PHE A 143
SHEET 3 B 4 VAL A 40 ALA A 50 -1 O SER A 41 N LYS A 100
SHEET 4 B 4 GLY A 56 VAL A 58 -1 N LYS A 57 O LYS A 49
SHEET 1 C 4 ARG A 141 PHE A 144 0
SHEET 2 C 4 PRO A 94 ASN A 101 -1 N PHE A 97 O PHE A 143
SHEET 3 C 4 VAL A 40 ALA A 50 -1 O SER A 41 N LYS A 100
SHEET 4 C 4 THR A 62 PHE A 63 -1 O THR A 62 N LEU A 42
SHEET 1 D 2 TYR A 186 ASP A 187 0
SHEET 2 D 2 ARG A 217 GLY A 218 -1 N ARG A 217 O ASP A 187
SHEET 1 E 2 ILE A 297 LYS A 298 0
SHEET 2 E 2 ILE A 324 LEU A 325 -1 O LEU A 325 N ILE A 297
SHEET 1 F 5 ARG A 360 GLY A 361 0
SHEET 2 F 5 LEU A 404 ASP A 408 -1 O MET A 406 N ARG A 360
SHEET 3 F 5 ALA A 430 LEU A 437 -1 N THR A 433 O LEU A 407
SHEET 4 F 5 LEU A 443 SER A 451 -1 O LYS A 444 N PHE A 436
SHEET 5 F 5 GLN A 465 VAL A 467 -1 O GLN A 465 N LEU A 450
SHEET 1 G 2 ALA A 591 LYS A 593 0
SHEET 2 G 2 VAL A 601 LEU A 603 -1 N ARG A 602 O ILE A 592
LINK NE2 HIS A 499 FE FE A 840 1555 1555 2.11
LINK NE2 HIS A 504 FE FE A 840 1555 1555 2.14
LINK NE2 HIS A 690 FE FE A 840 1555 1555 2.21
LINK ND1 HIS A 694 FE FE A 840 1555 1555 2.38
LINK OXT ILE A 839 FE FE A 840 1555 1555 2.46
LINK FE FE A 840 O HOH A1522 1555 1555 2.54
CISPEP 1 PHE A 365 PRO A 366 0 -0.27
SITE 1 AC1 6 HIS A 499 HIS A 504 HIS A 690 HIS A 694
SITE 2 AC1 6 ILE A 839 HOH A1522
CRYST1 94.260 92.770 49.230 90.00 90.22 90.00 P 1 21 1 2
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 0.010609 0.000000 0.000041 0.00000
SCALE2 0.000000 0.010779 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020313 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
