HEADER OXIDOREDUCTASE 22-JUL-93 2SBL
TITLE THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID 15-LIPOXYGENASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOXYGENASE-1;
COMPND 3 CHAIN: B, A;
COMPND 4 EC: 1.13.11.12;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GLYCINE MAX;
SOURCE 3 ORGANISM_COMMON: SOYBEAN;
SOURCE 4 ORGANISM_TAXID: 3847
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.AMZEL,J.C.BOYINGTON
REVDAT 4 21-FEB-24 2SBL 1 REMARK LINK
REVDAT 3 24-FEB-09 2SBL 1 VERSN
REVDAT 2 03-MAR-95 2SBL 3 REMARK FTNOTE HET FORMUL
REVDAT 2 2 3 HELIX MTRIX ATOM HETATM
REVDAT 2 3 3 TER CONECT
REVDAT 1 27-FEB-95 2SBL 0
JRNL AUTH J.C.BOYINGTON,B.J.GAFFNEY,L.M.AMZEL
JRNL TITL THE THREE-DIMENSIONAL STRUCTURE OF AN ARACHIDONIC ACID
JRNL TITL 2 15-LIPOXYGENASE.
JRNL REF SCIENCE V. 260 1482 1993
JRNL REFN ISSN 0036-8075
JRNL PMID 8502991
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.C.BOYINGTON,B.J.GAFFNEY,L.M.AMZEL
REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY ANALYSIS OF SOYBEAN
REMARK 1 TITL 2 LIPOXYGENASE-1, A NON-HEME IRON-CONTAINING DIOXYGENASE
REMARK 1 REF J.BIOL.CHEM. V. 265 12771 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : NULL
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) : 0.173
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 : 12890
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 63
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) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 2.700
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: NULL
REMARK 4
REMARK 4 2SBL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178613.
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 : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : NULL
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
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: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 92.25000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 92.25000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.80000
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
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: 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 350
REMARK 350 BIOMOLECULE: 2
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 B 1
REMARK 465 PHE B 2
REMARK 465 SER B 3
REMARK 465 ALA B 4
REMARK 465 GLY B 5
REMARK 465 HIS B 6
REMARK 465 VAL B 22
REMARK 465 ASN B 23
REMARK 465 PRO B 24
REMARK 465 ASP B 25
REMARK 465 GLY B 26
REMARK 465 SER B 27
REMARK 465 ALA B 28
REMARK 465 VAL B 29
REMARK 465 ASP B 30
REMARK 465 ASN B 31
REMARK 465 THR B 69
REMARK 465 SER B 70
REMARK 465 LEU B 71
REMARK 465 PRO B 72
REMARK 465 THR B 73
REMARK 465 SER B 118
REMARK 465 ASN B 119
REMARK 465 GLN B 120
REMARK 465 GLY B 121
REMARK 465 HIS B 454
REMARK 465 SER B 455
REMARK 465 ALA B 456
REMARK 465 GLY B 457
REMARK 465 ASP B 458
REMARK 465 LEU B 459
REMARK 465 SER B 460
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 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 ASN A 31
REMARK 465 THR A 69
REMARK 465 SER A 70
REMARK 465 LEU A 71
REMARK 465 PRO A 72
REMARK 465 THR A 73
REMARK 465 SER A 118
REMARK 465 ASN A 119
REMARK 465 GLN A 120
REMARK 465 GLY A 121
REMARK 465 HIS A 454
REMARK 465 SER A 455
REMARK 465 ALA A 456
REMARK 465 GLY A 457
REMARK 465 ASP A 458
REMARK 465 LEU A 459
REMARK 465 SER A 460
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 NE ARG B 767 O HOH B 902 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O PRO B 415 CG PRO A 595 4546 1.91
REMARK 500 CB PRO B 415 CB PRO A 595 4546 2.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS B 53 NE2 HIS B 53 CD2 -0.068
REMARK 500 HIS B 84 NE2 HIS B 84 CD2 -0.071
REMARK 500 HIS B 147 NE2 HIS B 147 CD2 -0.072
REMARK 500 HIS B 248 NE2 HIS B 248 CD2 -0.070
REMARK 500 HIS B 284 NE2 HIS B 284 CD2 -0.075
REMARK 500 HIS B 323 NE2 HIS B 323 CD2 -0.070
REMARK 500 HIS B 410 NE2 HIS B 410 CD2 -0.069
REMARK 500 HIS B 494 NE2 HIS B 494 CD2 -0.066
REMARK 500 HIS B 504 NE2 HIS B 504 CD2 -0.068
REMARK 500 HIS B 515 NE2 HIS B 515 CD2 -0.072
REMARK 500 HIS B 522 NE2 HIS B 522 CD2 -0.072
REMARK 500 HIS B 531 NE2 HIS B 531 CD2 -0.077
REMARK 500 HIS B 647 NE2 HIS B 647 CD2 -0.076
REMARK 500 HIS B 730 NE2 HIS B 730 CD2 -0.072
REMARK 500 HIS B 757 NE2 HIS B 757 CD2 -0.076
REMARK 500 HIS B 771 NE2 HIS B 771 CD2 -0.066
REMARK 500 HIS A 53 NE2 HIS A 53 CD2 -0.067
REMARK 500 HIS A 84 NE2 HIS A 84 CD2 -0.071
REMARK 500 HIS A 147 NE2 HIS A 147 CD2 -0.071
REMARK 500 HIS A 248 NE2 HIS A 248 CD2 -0.070
REMARK 500 HIS A 284 NE2 HIS A 284 CD2 -0.075
REMARK 500 HIS A 323 NE2 HIS A 323 CD2 -0.070
REMARK 500 HIS A 410 NE2 HIS A 410 CD2 -0.069
REMARK 500 HIS A 494 NE2 HIS A 494 CD2 -0.066
REMARK 500 HIS A 504 NE2 HIS A 504 CD2 -0.067
REMARK 500 HIS A 515 NE2 HIS A 515 CD2 -0.073
REMARK 500 HIS A 522 NE2 HIS A 522 CD2 -0.071
REMARK 500 HIS A 531 NE2 HIS A 531 CD2 -0.076
REMARK 500 HIS A 599 NE2 HIS A 599 CD2 -0.066
REMARK 500 HIS A 647 NE2 HIS A 647 CD2 -0.076
REMARK 500 HIS A 730 NE2 HIS A 730 CD2 -0.072
REMARK 500 HIS A 757 NE2 HIS A 757 CD2 -0.077
REMARK 500 HIS A 771 NE2 HIS A 771 CD2 -0.066
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 B 38 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TRP B 87 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP B 87 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 87 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP B 130 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP B 130 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG B 141 NE - CZ - NH1 ANGL. DEV. = 5.2 DEGREES
REMARK 500 ARG B 141 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG B 177 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 177 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 VAL B 188 N - CA - CB ANGL. DEV. = -15.2 DEGREES
REMARK 500 ARG B 217 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 TRP B 340 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 340 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP B 479 CD1 - CG - CD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 TRP B 479 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 TRP B 479 CG - CD2 - CE3 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TRP B 500 CD1 - CG - CD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 TRP B 500 CB - CG - CD1 ANGL. DEV. = -8.5 DEGREES
REMARK 500 TRP B 500 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 MET B 507 CG - SD - CE ANGL. DEV. = -13.5 DEGREES
REMARK 500 TRP B 574 CD1 - CG - CD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 TRP B 574 CE2 - CD2 - CG ANGL. DEV. = -6.2 DEGREES
REMARK 500 ILE B 605 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 TYR B 608 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP B 618 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP B 618 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP B 618 CG - CD2 - CE3 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP B 624 CD1 - CG - CD2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 TRP B 624 CB - CG - CD1 ANGL. DEV. = -8.4 DEGREES
REMARK 500 TRP B 624 CE2 - CD2 - CG ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP B 624 CG - CD2 - CE3 ANGL. DEV. = 5.8 DEGREES
REMARK 500 TRP B 648 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP B 648 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 649 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP B 649 CE2 - CD2 - CG ANGL. DEV. = -5.9 DEGREES
REMARK 500 TRP B 665 CD1 - CG - CD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 TRP B 665 CE2 - CD2 - CG ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP B 665 CG - CD2 - CE3 ANGL. DEV. = 5.4 DEGREES
REMARK 500 TRP B 666 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP B 666 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 684 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP B 684 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP B 772 CD1 - CG - CD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 TRP B 772 CE2 - CD2 - CG ANGL. DEV. = -6.4 DEGREES
REMARK 500 TRP A 87 CD1 - CG - CD2 ANGL. DEV. = 6.5 DEGREES
REMARK 500 TRP A 87 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 TRP A 87 CG - CD2 - CE3 ANGL. DEV. = 5.7 DEGREES
REMARK 500 TRP A 130 CD1 - CG - CD2 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TRP A 130 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 90 ANGLE DEVIATIONS.
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 ARG B 38 45.14 -98.62
REMARK 500 ALA B 52 10.91 -64.18
REMARK 500 GLU B 115 40.50 -80.95
REMARK 500 ASN B 146 33.88 -73.44
REMARK 500 SER B 198 143.45 -171.93
REMARK 500 PRO B 229 -9.49 -57.22
REMARK 500 ILE B 265 -56.34 -121.79
REMARK 500 GLU B 294 -95.01 -92.54
REMARK 500 HIS B 323 -21.79 -170.16
REMARK 500 VAL B 335 -50.32 -120.43
REMARK 500 ALA B 352 15.45 -143.13
REMARK 500 LEU B 390 50.35 -92.06
REMARK 500 SER B 560 -122.30 47.51
REMARK 500 ASP B 607 75.98 -108.44
REMARK 500 SER B 687 -82.68 -100.91
REMARK 500 ASN B 729 55.69 -161.79
REMARK 500 THR B 739 119.61 -39.81
REMARK 500 LEU B 810 -47.65 -130.13
REMARK 500 TYR B 817 94.57 -64.02
REMARK 500 ARG A 38 45.18 -98.60
REMARK 500 ALA A 52 10.92 -64.22
REMARK 500 GLU A 115 40.53 -80.94
REMARK 500 ASN A 146 33.86 -73.43
REMARK 500 SER A 198 143.48 -171.91
REMARK 500 PRO A 229 -9.45 -57.23
REMARK 500 ILE A 265 -56.39 -121.78
REMARK 500 GLU A 294 -95.05 -92.50
REMARK 500 HIS A 323 -21.81 -170.13
REMARK 500 VAL A 335 -50.36 -120.41
REMARK 500 ALA A 352 15.43 -143.14
REMARK 500 LEU A 390 50.38 -92.08
REMARK 500 SER A 560 -122.27 47.47
REMARK 500 ASP A 607 76.01 -108.52
REMARK 500 SER A 687 -82.67 -100.88
REMARK 500 ASN A 729 55.68 -161.78
REMARK 500 THR A 739 119.57 -39.77
REMARK 500 LEU A 810 -47.66 -130.14
REMARK 500 TYR A 817 94.55 -63.98
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 B 840 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 499 NE2
REMARK 620 2 HIS B 504 NE2 91.7
REMARK 620 3 HIS B 690 NE2 105.3 100.4
REMARK 620 4 ILE B 839 OXT 158.5 107.0 82.1
REMARK 620 N 1 2 3
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 91.7
REMARK 620 3 HIS A 690 NE2 105.3 100.4
REMARK 620 4 ILE A 839 OXT 158.5 107.1 82.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 840
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 840
DBREF 2SBL B 1 839 UNP P08170 LOX1_SOYBN 1 839
DBREF 2SBL A 1 839 UNP P08170 LOX1_SOYBN 1 839
SEQRES 1 B 839 MET PHE SER ALA GLY HIS LYS ILE LYS GLY THR VAL VAL
SEQRES 2 B 839 LEU MET PRO LYS ASN GLU LEU GLU VAL ASN PRO ASP GLY
SEQRES 3 B 839 SER ALA VAL ASP ASN LEU ASN ALA PHE LEU GLY ARG SER
SEQRES 4 B 839 VAL SER LEU GLN LEU ILE SER ALA THR LYS ALA ASP ALA
SEQRES 5 B 839 HIS GLY LYS GLY LYS VAL GLY LYS ASP THR PHE LEU GLU
SEQRES 6 B 839 GLY ILE ASN THR SER LEU PRO THR LEU GLY ALA GLY GLU
SEQRES 7 B 839 SER ALA PHE ASN ILE HIS PHE GLU TRP ASP GLY SER MET
SEQRES 8 B 839 GLY ILE PRO GLY ALA PHE TYR ILE LYS ASN TYR MET GLN
SEQRES 9 B 839 VAL GLU PHE PHE LEU LYS SER LEU THR LEU GLU ALA ILE
SEQRES 10 B 839 SER ASN GLN GLY THR ILE ARG PHE VAL CYS ASN SER TRP
SEQRES 11 B 839 VAL TYR ASN THR LYS LEU TYR LYS SER VAL ARG ILE PHE
SEQRES 12 B 839 PHE ALA ASN HIS THR TYR VAL PRO SER GLU THR PRO ALA
SEQRES 13 B 839 PRO LEU VAL SER TYR ARG GLU GLU GLU LEU LYS SER LEU
SEQRES 14 B 839 ARG GLY ASN GLY THR GLY GLU ARG LYS GLU TYR ASP ARG
SEQRES 15 B 839 ILE TYR ASP TYR ASP VAL TYR ASN ASP LEU GLY ASN PRO
SEQRES 16 B 839 ASP LYS SER GLU LYS LEU ALA ARG PRO VAL LEU GLY GLY
SEQRES 17 B 839 SER SER THR PHE PRO TYR PRO ARG ARG GLY ARG THR GLY
SEQRES 18 B 839 ARG GLY PRO THR VAL THR ASP PRO ASN THR GLU LYS GLN
SEQRES 19 B 839 GLY GLU VAL PHE TYR VAL PRO ARG ASP GLU ASN LEU GLY
SEQRES 20 B 839 HIS LEU LYS SER LYS ASP ALA LEU GLU ILE GLY THR LYS
SEQRES 21 B 839 SER LEU SER GLN ILE VAL GLN PRO ALA PHE GLU SER ALA
SEQRES 22 B 839 PHE ASP LEU LYS SER THR PRO ILE GLU PHE HIS SER PHE
SEQRES 23 B 839 GLN ASP VAL HIS ASP LEU TYR GLU GLY GLY ILE LYS LEU
SEQRES 24 B 839 PRO ARG ASP VAL ILE SER THR ILE ILE PRO LEU PRO VAL
SEQRES 25 B 839 ILE LYS GLU LEU TYR ARG THR ASP GLY GLN HIS ILE LEU
SEQRES 26 B 839 LYS PHE PRO GLN PRO HIS VAL VAL GLN VAL SER GLN SER
SEQRES 27 B 839 ALA TRP MET THR ASP GLU GLU PHE ALA ARG GLU MET ILE
SEQRES 28 B 839 ALA GLY VAL ASN PRO CYS VAL ILE ARG GLY LEU GLU GLU
SEQRES 29 B 839 PHE PRO PRO LYS SER ASN LEU ASP PRO ALA ILE TYR GLY
SEQRES 30 B 839 ASP GLN SER SER LYS ILE THR ALA ASP SER LEU ASP LEU
SEQRES 31 B 839 ASP GLY TYR THR MET ASP GLU ALA LEU GLY SER ARG ARG
SEQRES 32 B 839 LEU PHE MET LEU ASP TYR HIS ASP ILE PHE MET PRO TYR
SEQRES 33 B 839 VAL ARG GLN ILE ASN GLN LEU ASN SER ALA LYS THR TYR
SEQRES 34 B 839 ALA THR ARG THR ILE LEU PHE LEU ARG GLU ASP GLY THR
SEQRES 35 B 839 LEU LYS PRO VAL ALA ILE GLU LEU SER LEU PRO HIS SER
SEQRES 36 B 839 ALA GLY ASP LEU SER ALA ALA VAL SER GLN VAL VAL LEU
SEQRES 37 B 839 PRO ALA LYS GLU GLY VAL GLU SER THR ILE TRP LEU LEU
SEQRES 38 B 839 ALA LYS ALA TYR VAL ILE VAL ASN ASP SER CYS TYR HIS
SEQRES 39 B 839 GLN LEU MET SER HIS TRP LEU ASN THR HIS ALA ALA MET
SEQRES 40 B 839 GLU PRO PHE VAL ILE ALA THR HIS ARG HIS LEU SER VAL
SEQRES 41 B 839 LEU HIS PRO ILE TYR LYS LEU LEU THR PRO HIS TYR ARG
SEQRES 42 B 839 ASN ASN MET ASN ILE ASN ALA LEU ALA ARG GLN SER LEU
SEQRES 43 B 839 ILE ASN ALA ASN GLY ILE ILE GLU THR THR PHE LEU PRO
SEQRES 44 B 839 SER LYS TYR SER VAL GLU MET SER SER ALA VAL TYR LYS
SEQRES 45 B 839 ASN TRP VAL PHE THR ASP GLN ALA LEU PRO ALA ASP LEU
SEQRES 46 B 839 ILE LYS ARG GLY VAL ALA ILE LYS ASP PRO SER THR PRO
SEQRES 47 B 839 HIS GLY VAL ARG LEU LEU ILE GLU ASP TYR PRO TYR ALA
SEQRES 48 B 839 ALA ASP GLY LEU GLU ILE TRP ALA ALA ILE LYS THR TRP
SEQRES 49 B 839 VAL GLN GLU TYR VAL PRO LEU TYR TYR ALA ARG ASP ASP
SEQRES 50 B 839 ASP VAL LYS ASN ASP SER GLU LEU GLN HIS TRP TRP LYS
SEQRES 51 B 839 GLU ALA VAL GLU LYS GLY HIS GLY ASP LEU LYS ASP LYS
SEQRES 52 B 839 PRO TRP TRP PRO LYS LEU GLN THR LEU GLU ASP LEU VAL
SEQRES 53 B 839 GLU VAL CYS LEU ILE ILE ILE TRP ILE ALA SER ALA LEU
SEQRES 54 B 839 HIS ALA ALA VAL ASN PHE GLY GLN TYR PRO TYR GLY GLY
SEQRES 55 B 839 LEU ILE MET ASN ARG PRO THR ALA SER ARG ARG LEU LEU
SEQRES 56 B 839 PRO GLU LYS GLY THR PRO GLU TYR GLU GLU MET ILE ASN
SEQRES 57 B 839 ASN HIS GLU LYS ALA TYR LEU ARG THR ILE THR SER LYS
SEQRES 58 B 839 LEU PRO THR LEU ILE SER LEU SER VAL ILE GLU ILE LEU
SEQRES 59 B 839 SER THR HIS ALA SER ASP GLU VAL TYR LEU GLY GLN ARG
SEQRES 60 B 839 ASP ASN PRO HIS TRP THR SER ASP SER LYS ALA LEU GLN
SEQRES 61 B 839 ALA PHE GLN LYS PHE GLY ASN LYS LEU LYS GLU ILE GLU
SEQRES 62 B 839 GLU LYS LEU VAL ARG ARG ASN ASN ASP PRO SER LEU GLN
SEQRES 63 B 839 GLY ASN ARG LEU GLY PRO VAL GLN LEU PRO TYR THR LEU
SEQRES 64 B 839 LEU TYR PRO SER SER GLU GLU GLY LEU THR PHE ARG GLY
SEQRES 65 B 839 ILE PRO ASN SER ILE SER ILE
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 ASN 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 B 840 1
HET FE A 840 1
HETNAM FE FE (III) ION
FORMUL 3 FE 2(FE 3+)
FORMUL 5 HOH *63(H2 O)
HELIX 1 B1 ALA B 156 ARG B 170 1 15
HELIX 2 B2 LEU B 255 LEU B 276 1 22
HELIX 3 B3 PHE B 286 GLY B 295 1 10
HELIX 4 B4 ARG B 301 ILE B 308 1 8
HELIX 5 B5 VAL B 312 LEU B 316 1 5
HELIX 6 B6 THR B 342 ALA B 352 1 11
HELIX 7 B7 MET B 395 SER B 401 1 7
HELIX 8 B8 HIS B 410 LEU B 423 1 14
HELIX 9 B9 VAL B 474 ARG B 516 1INTERNAL PI-HELIX 494 - 506 43
HELIX 10 B10 PRO B 523 HIS B 531 1 9
HELIX 11 B11 ASN B 534 LEU B 546 1 13
HELIX 12 B12 ILE B 552 THR B 556 1 5
HELIX 13 B13 SER B 560 ASN B 573 1 14
HELIX 14 B14 LEU B 581 ARG B 588 1 8
HELIX 15 B15 TYR B 610 TYR B 633 1 24
HELIX 16 B16 ASP B 636 ASN B 641 1 6
HELIX 17 B17 SER B 643 GLY B 656 1 14
HELIX 18 B18 LEU B 672 GLY B 701 1INTERNAL PI-HELIX 685 - 690 30
HELIX 19 B19 PRO B 721 ASN B 728 1 8
HELIX 20 B20 HIS B 730 THR B 737 1 8
HELIX 21 B21 LYS B 741 SER B 755 1 15
HELIX 22 B22 SER B 776 ASN B 800 1 25
HELIX 23 B23 SER B 804 ASN B 808 1 5
HELIX 24 A1 ALA A 156 ARG A 170 1 15
HELIX 25 A2 LEU A 255 LEU A 276 1 22
HELIX 26 A3 PHE A 286 GLY A 295 1 10
HELIX 27 A4 ARG A 301 ILE A 308 1 8
HELIX 28 A5 VAL A 312 LEU A 316 1 5
HELIX 29 A6 THR A 342 ALA A 352 1 11
HELIX 30 A7 MET A 395 SER A 401 1 7
HELIX 31 A8 HIS A 410 LEU A 423 1 14
HELIX 32 A9 VAL A 474 ARG A 516 1INTERNAL PI-HELIX 494 - 506 43
HELIX 33 A10 PRO A 523 HIS A 531 1 9
HELIX 34 A11 ASN A 534 LEU A 546 1 13
HELIX 35 A12 ILE A 552 THR A 556 1 5
HELIX 36 A13 SER A 560 ASN A 573 1 14
HELIX 37 A14 LEU A 581 ARG A 588 1 8
HELIX 38 A15 TYR A 610 TYR A 633 1 24
HELIX 39 A16 ASP A 636 ASN A 641 1 6
HELIX 40 A17 SER A 643 GLY A 656 1 14
HELIX 41 A18 LEU A 672 GLY A 701 1INTERNAL PI-HELIX 685 - 690 30
HELIX 42 A19 PRO A 721 ASN A 728 1 8
HELIX 43 A20 HIS A 730 THR A 737 1 8
HELIX 44 A21 LYS A 741 SER A 755 1 15
HELIX 45 A22 SER A 776 ASN A 800 1 25
HELIX 46 A23 SER A 804 ASN A 808 1 5
SHEET 1 B1B 8 LYS B 7 MET B 15 0
SHEET 2 B1B 8 VAL B 40 THR B 48 -1
SHEET 3 B1B 8 LYS B 57 GLU B 65 -1
SHEET 4 B1B 8 GLU B 78 PHE B 85 -1
SHEET 5 B1B 8 GLY B 95 TYR B 102 -1
SHEET 6 B1B 8 GLU B 106 LEU B 114 -1
SHEET 7 B1B 8 ILE B 123 VAL B 131 -1
SHEET 8 B1B 8 ARG B 141 ALA B 145 -1
SHEET 1 B2B 3 GLY B 296 LEU B 299 0
SHEET 2 B2B 3 TYR B 317 ASP B 320 -1
SHEET 3 B2B 3 HIS B 323 PHE B 327 -1
SHEET 1 B3B 5 ILE B 359 LEU B 362 0
SHEET 2 B3B 5 ARG B 403 ASP B 408 -1
SHEET 3 B3B 5 ALA B 430 LEU B 437 -1
SHEET 4 B3B 5 THR B 442 PRO B 453 -1
SHEET 5 B3B 5 ALA B 461 LEU B 468 -1
SHEET 1 B1A 8 LYS A 7 MET A 15 0
SHEET 2 B1A 8 VAL A 40 THR A 48 -1
SHEET 3 B1A 8 LYS A 57 GLU A 65 -1
SHEET 4 B1A 8 GLU A 78 PHE A 85 -1
SHEET 5 B1A 8 GLY A 95 TYR A 102 -1
SHEET 6 B1A 8 GLU A 106 LEU A 114 -1
SHEET 7 B1A 8 ILE A 123 VAL A 131 -1
SHEET 8 B1A 8 ARG A 141 ALA A 145 -1
SHEET 1 B2A 3 GLY A 296 LEU A 299 0
SHEET 2 B2A 3 TYR A 317 ASP A 320 -1
SHEET 3 B2A 3 HIS A 323 PHE A 327 -1
SHEET 1 B3A 5 ILE A 359 LEU A 362 0
SHEET 2 B3A 5 ARG A 403 ASP A 408 -1
SHEET 3 B3A 5 ALA A 430 LEU A 437 -1
SHEET 4 B3A 5 THR A 442 PRO A 453 -1
SHEET 5 B3A 5 ALA A 461 LEU A 468 -1
LINK NE2 HIS B 499 FE FE B 840 1555 1555 2.27
LINK NE2 HIS B 504 FE FE B 840 1555 1555 2.22
LINK NE2 HIS B 690 FE FE B 840 1555 1555 2.25
LINK OXT ILE B 839 FE FE B 840 1555 1555 2.16
LINK NE2 HIS A 499 FE FE A 840 1555 1555 2.27
LINK NE2 HIS A 504 FE FE A 840 1555 1555 2.22
LINK NE2 HIS A 690 FE FE A 840 1555 1555 2.25
LINK OXT ILE A 839 FE FE A 840 1555 1555 2.16
CISPEP 1 PHE B 365 PRO B 366 0 -5.70
CISPEP 2 PHE A 365 PRO A 366 0 -5.71
SITE 1 AC1 5 HIS B 499 HIS B 504 HIS B 690 ASN B 694
SITE 2 AC1 5 ILE B 839
SITE 1 AC2 5 HIS A 499 HIS A 504 HIS A 690 ASN A 694
SITE 2 AC2 5 ILE A 839
CRYST1 184.500 125.600 94.700 90.00 102.90 90.00 C 1 2 1 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 0.005420 0.000000 0.001241 0.00000
SCALE2 0.000000 0.007962 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010833 0.00000
MTRIX1 1 -0.761029 -0.489822 -0.425334 103.85080 1
MTRIX2 1 0.633847 -0.421869 -0.648278 36.31530 1
MTRIX3 1 0.138106 -0.762955 0.631527 46.71780 1
(ATOM LINES ARE NOT SHOWN.)
END
