HEADER OXIDOREDUCTASE 08-JUL-10 3NVY
TITLE CRYSTAL STRUCTURE OF BOVINE XANTHINE OXIDASE IN COMPLEX WITH QUERCETIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XANTHINE DEHYDROGENASE/OXIDASE;
COMPND 3 CHAIN: A, J;
COMPND 4 FRAGMENT: IRON-SULFUR BINDING DOMAIN;
COMPND 5 SYNONYM: XANTHINE DEHYDROGENASE, XD, XANTHINE OXIDASE, XO, XANTHINE
COMPND 6 OXIDOREDUCTASE;
COMPND 7 EC: 1.17.1.4, 1.17.3.2;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: XANTHINE DEHYDROGENASE/OXIDASE;
COMPND 10 CHAIN: B, K;
COMPND 11 FRAGMENT: FLAVIN BINDING DOMAIN;
COMPND 12 SYNONYM: XANTHINE DEHYDROGENASE, XD, XANTHINE OXIDASE, XO, XANTHINE
COMPND 13 OXIDOREDUCTASE;
COMPND 14 EC: 1.17.1.4, 1.17.3.2;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: XANTHINE DEHYDROGENASE/OXIDASE;
COMPND 17 CHAIN: C, L;
COMPND 18 FRAGMENT: MOLYBDENUM BINDING DOMAIN;
COMPND 19 SYNONYM: XANTHINE DEHYDROGENASE, XD, XANTHINE OXIDASE, XO, XANTHINE
COMPND 20 OXIDOREDUCTASE;
COMPND 21 EC: 1.17.1.4, 1.17.3.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 OTHER_DETAILS: MILK;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 OTHER_DETAILS: MILK;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;
SOURCE 14 ORGANISM_TAXID: 9913;
SOURCE 15 OTHER_DETAILS: MILK
KEYWDS HYDROXYLASE, HOMODIMER, XANTHINE OXIDASE, QUERCETIN, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CAO,R.HILLE
REVDAT 3 21-FEB-24 3NVY 1 REMARK LINK
REVDAT 2 03-SEP-14 3NVY 1 JRNL VERSN
REVDAT 1 19-JAN-11 3NVY 0
JRNL AUTH H.CAO,J.M.PAUFF,R.HILLE
JRNL TITL X-RAY CRYSTAL STRUCTURE OF A XANTHINE OXIDASE COMPLEX WITH
JRNL TITL 2 THE FLAVONOID INHIBITOR QUERCETIN.
JRNL REF J NAT PROD V. 77 1693 2014
JRNL REFN ISSN 0163-3864
JRNL PMID 25060641
JRNL DOI 10.1021/NP500320G
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 101.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 175239
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 + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8835
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12280
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2150
REMARK 3 BIN FREE R VALUE SET COUNT : 658
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19122
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 222
REMARK 3 SOLVENT ATOMS : 1057
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.67000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : 1.98000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.41000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.170
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.368
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19767 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26771 ; 1.554 ; 1.977
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2462 ; 6.327 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 827 ;38.437 ;23.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3381 ;15.988 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;17.684 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2991 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14772 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9321 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13555 ; 0.308 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1318 ; 0.153 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 61 ; 0.284 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.255 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 12620 ; 0.908 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19785 ; 1.426 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8237 ; 2.366 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6978 ; 3.630 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3NVY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060346.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 31-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178392
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 101.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
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) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4 MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 7.2, SITTING BATCH,
REMARK 280 TEMPERATURE 298K
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 36.69900
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -244.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, J, K, 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 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 LEU K 195
REMARK 465 PHE K 196
REMARK 465 ASN K 197
REMARK 465 PRO K 198
REMARK 465 GLU K 199
REMARK 465 GLU K 200
REMARK 465 PHE K 201
REMARK 465 MET K 202
REMARK 465 PRO K 203
REMARK 465 LEU K 204
REMARK 465 ASP K 205
REMARK 465 PRO K 206
REMARK 465 THR K 207
REMARK 465 GLN K 208
REMARK 465 GLU K 209
REMARK 465 PRO K 210
REMARK 465 ILE K 211
REMARK 465 PHE K 212
REMARK 465 PRO K 213
REMARK 465 PRO K 214
REMARK 465 GLU K 215
REMARK 465 LEU K 216
REMARK 465 LEU K 217
REMARK 465 ARG K 218
REMARK 465 LEU K 219
REMARK 465 LYS K 220
REMARK 465 ASP K 221
REMARK 465 VAL K 222
REMARK 465 PRO K 223
REMARK 465 LEU L 1316
REMARK 465 CYS L 1317
REMARK 465 VAL L 1318
REMARK 465 THR L 1319
REMARK 465 GLY L 1320
REMARK 465 ALA L 1321
REMARK 465 PRO L 1322
REMARK 465 GLY L 1323
REMARK 465 ASN L 1324
REMARK 465 CYS L 1325
REMARK 465 LYS L 1326
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 OE1 GLU C 924 NH1 ARG C 942 1.96
REMARK 500 OE1 GLU C 802 O27 QUE C 1356 2.05
REMARK 500 OE1 GLU L 802 O27 QUE L 1356 2.07
REMARK 500 OD1 ASN B 288 O HOH B 903 2.15
REMARK 500 OD1 ASN C 705 O HOH C 395 2.18
REMARK 500 O SER C 610 O VAL C 663 2.19
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 OD2 ASP A 63 NH1 ARG C 871 1545 2.06
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 GLU L 699 CG GLU L 699 CD 0.099
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 439 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 GLY C 664 C - N - CA ANGL. DEV. = -17.0 DEGREES
REMARK 500 ARG C 829 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG C 829 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 VAL C 848 CB - CA - C ANGL. DEV. = -13.7 DEGREES
REMARK 500 ARG C 942 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG C 942 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 980 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG C 980 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 LEU C1203 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 VAL L 848 CB - CA - C ANGL. DEV. = -12.2 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 CYS A 43 -27.39 -155.84
REMARK 500 THR A 96 -87.57 -125.62
REMARK 500 GLN A 112 -88.23 -107.73
REMARK 500 TYR A 153 -37.34 73.29
REMARK 500 VAL B 222 118.76 -38.39
REMARK 500 VAL B 259 -81.08 -115.32
REMARK 500 ASN B 272 16.22 55.69
REMARK 500 TRP B 336 68.58 -109.15
REMARK 500 ALA B 338 -138.91 50.09
REMARK 500 ARG B 377 106.49 -56.96
REMARK 500 ASP B 430 28.25 -140.79
REMARK 500 SER B 475 -7.28 73.74
REMARK 500 LEU B 527 -72.85 -67.39
REMARK 500 HIS C 579 126.53 -37.03
REMARK 500 HIS C 614 110.04 -162.94
REMARK 500 VAL C 632 -61.44 -109.84
REMARK 500 LYS C 657 -64.08 -103.58
REMARK 500 PHE C 798 19.17 58.60
REMARK 500 ASP C 872 -134.04 48.59
REMARK 500 ASN C 887 -116.03 35.12
REMARK 500 ARG C 912 109.33 -14.69
REMARK 500 TYR C 947 159.60 -48.70
REMARK 500 SER C1008 161.45 156.56
REMARK 500 SER C1080 10.26 58.70
REMARK 500 ASN C1187 93.82 -162.70
REMARK 500 ASN C1287 -169.32 -166.84
REMARK 500 ASN C1324 50.93 -95.59
REMARK 500 CYS J 43 -31.53 -151.11
REMARK 500 ASP J 63 -53.29 76.97
REMARK 500 THR J 96 -80.61 -112.93
REMARK 500 GLN J 112 -89.48 -107.48
REMARK 500 TYR J 153 -36.53 70.93
REMARK 500 VAL K 259 -75.68 -122.38
REMARK 500 TRP K 336 58.51 -106.84
REMARK 500 ALA K 338 -137.34 56.36
REMARK 500 SER K 425 -103.81 -144.34
REMARK 500 ARG K 426 133.75 92.37
REMARK 500 ASP K 430 42.74 -147.90
REMARK 500 PRO K 444 113.25 -39.95
REMARK 500 LYS L 657 -69.02 -98.58
REMARK 500 LYS L 721 -49.14 -165.01
REMARK 500 THR L 803 -28.69 -144.02
REMARK 500 ASP L 872 -127.23 42.92
REMARK 500 ASN L 887 -121.92 39.17
REMARK 500 ARG L 912 110.15 -13.31
REMARK 500 SER L1008 155.36 157.11
REMARK 500 TYR L1152 -179.51 -171.00
REMARK 500 LEU L1208 -44.43 -143.32
REMARK 500 LYS L1291 36.04 -87.20
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA A 164 LYS A 165 140.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 602 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 FES A 602 S1 102.3
REMARK 620 3 FES A 602 S2 119.2 100.1
REMARK 620 4 CYS A 48 SG 111.0 112.8 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 602 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 FES A 602 S1 109.0
REMARK 620 3 FES A 602 S2 114.6 100.9
REMARK 620 4 CYS A 73 SG 107.2 113.1 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 601 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 113 SG
REMARK 620 2 FES A 601 S1 116.3
REMARK 620 3 FES A 601 S2 108.8 101.9
REMARK 620 4 CYS A 150 SG 99.7 112.4 118.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A 601 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 116 SG
REMARK 620 2 FES A 601 S1 111.9
REMARK 620 3 FES A 601 S2 115.7 103.5
REMARK 620 4 CYS A 148 SG 101.2 111.6 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS C1328 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE C1327 S2'
REMARK 620 2 MOS C1328 S 148.4
REMARK 620 3 MOS C1328 O1 89.0 86.0
REMARK 620 4 MOS C1328 O2 119.2 92.3 96.7
REMARK 620 5 MTE C1327 S1' 81.6 90.6 156.1 107.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 602 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 43 SG
REMARK 620 2 FES J 602 S1 102.5
REMARK 620 3 FES J 602 S2 117.3 98.8
REMARK 620 4 CYS J 48 SG 111.0 113.2 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 602 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 51 SG
REMARK 620 2 FES J 602 S1 106.7
REMARK 620 3 FES J 602 S2 120.2 99.6
REMARK 620 4 CYS J 73 SG 107.3 112.5 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 601 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 113 SG
REMARK 620 2 FES J 601 S1 116.5
REMARK 620 3 FES J 601 S2 107.5 106.3
REMARK 620 4 CYS J 150 SG 96.6 110.9 119.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 601 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 116 SG
REMARK 620 2 FES J 601 S1 113.7
REMARK 620 3 FES J 601 S2 119.4 107.7
REMARK 620 4 CYS J 148 SG 99.8 106.2 109.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS L1328 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE L1327 S1'
REMARK 620 2 MOS L1328 S 95.5
REMARK 620 3 MOS L1328 O1 156.3 82.4
REMARK 620 4 MOS L1328 O2 103.9 99.4 99.7
REMARK 620 5 MTE L1327 S2' 83.7 143.9 84.4 115.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE C 1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS C 1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUE C 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD K 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE L 1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS L 1328
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE QUE L 1356
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NVV RELATED DB: PDB
REMARK 900 RELATED ID: 3NVW RELATED DB: PDB
REMARK 900 RELATED ID: 3NVZ RELATED DB: PDB
DBREF 3NVY A 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NVY B 195 528 UNP P80457 XDH_BOVIN 195 528
DBREF 3NVY C 571 1326 UNP P80457 XDH_BOVIN 571 1326
DBREF 3NVY J 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NVY K 195 528 UNP P80457 XDH_BOVIN 195 528
DBREF 3NVY L 571 1326 UNP P80457 XDH_BOVIN 571 1326
SEQRES 1 A 164 THR ALA ASP GLU LEU VAL PHE PHE VAL ASN GLY LYS LYS
SEQRES 2 A 164 VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU LEU
SEQRES 3 A 164 ALA TYR LEU ARG ARG LYS LEU GLY LEU ARG GLY THR LYS
SEQRES 4 A 164 LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR VAL
SEQRES 5 A 164 MET LEU SER LYS TYR ASP ARG LEU GLN ASP LYS ILE ILE
SEQRES 6 A 164 HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS THR
SEQRES 7 A 164 LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE GLY
SEQRES 8 A 164 SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG ILE
SEQRES 9 A 164 ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR PRO
SEQRES 10 A 164 GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN GLN
SEQRES 11 A 164 PRO GLU PRO THR VAL GLU GLU ILE GLU ASP ALA PHE GLN
SEQRES 12 A 164 GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE LEU
SEQRES 13 A 164 GLN GLY PHE ARG THR PHE ALA LYS
SEQRES 1 B 334 LEU PHE ASN PRO GLU GLU PHE MET PRO LEU ASP PRO THR
SEQRES 2 B 334 GLN GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS
SEQRES 3 B 334 ASP VAL PRO PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG
SEQRES 4 B 334 VAL THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU
SEQRES 5 B 334 ASP LEU LYS ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL
SEQRES 6 B 334 GLY ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN
SEQRES 7 B 334 GLN LEU PHE PRO MET ILE ILE CYS PRO ALA TRP ILE PRO
SEQRES 8 B 334 GLU LEU ASN ALA VAL GLU HIS GLY PRO GLU GLY ILE SER
SEQRES 9 B 334 PHE GLY ALA ALA CYS ALA LEU SER SER VAL GLU LYS THR
SEQRES 10 B 334 LEU LEU GLU ALA VAL ALA LYS LEU PRO THR GLN LYS THR
SEQRES 11 B 334 GLU VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE
SEQRES 12 B 334 ALA GLY LYS GLN VAL LYS SER VAL ALA SER LEU GLY GLY
SEQRES 13 B 334 ASN ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO
SEQRES 14 B 334 VAL PHE MET ALA SER GLY THR LYS LEU THR ILE VAL SER
SEQRES 15 B 334 ARG GLY THR ARG ARG THR VAL PRO MET ASP HIS THR PHE
SEQRES 16 B 334 PHE PRO SER TYR ARG LYS THR LEU LEU GLY PRO GLU GLU
SEQRES 17 B 334 ILE LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU ASP
SEQRES 18 B 334 GLU PHE PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU
SEQRES 19 B 334 ASP ASP ILE ALA LYS VAL THR CYS GLY MET ARG VAL LEU
SEQRES 20 B 334 PHE GLN PRO GLY SER MET GLN VAL LYS GLU LEU ALA LEU
SEQRES 21 B 334 CYS TYR GLY GLY MET ALA ASP ARG THR ILE SER ALA LEU
SEQRES 22 B 334 LYS THR THR GLN LYS GLN LEU SER LYS PHE TRP ASN GLU
SEQRES 23 B 334 LYS LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU
SEQRES 24 B 334 LEU SER LEU SER PRO ASP ALA PRO GLY GLY MET ILE GLU
SEQRES 25 B 334 PHE ARG ARG THR LEU THR LEU SER PHE PHE PHE LYS PHE
SEQRES 26 B 334 TYR LEU THR VAL LEU LYS LYS LEU GLY
SEQRES 1 C 756 ASP THR VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA
SEQRES 2 C 756 MET GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE
SEQRES 3 C 756 PRO ARG TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR
SEQRES 4 C 756 SER THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL
SEQRES 5 C 756 SER GLU ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU
SEQRES 6 C 756 SER ALA ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU
SEQRES 7 C 756 PHE ASN ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR
SEQRES 8 C 756 CYS VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR
SEQRES 9 C 756 PRO GLU HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL
SEQRES 10 C 756 THR TYR GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP
SEQRES 11 C 756 ALA ILE LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS
SEQRES 12 C 756 ILE GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA
SEQRES 13 C 756 ASP ASN VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN
SEQRES 14 C 756 ASP HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE
SEQRES 15 C 756 PRO LYS GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER
SEQRES 16 C 756 THR GLN ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS
SEQRES 17 C 756 MET LEU GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL
SEQRES 18 C 756 LYS ARG MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG
SEQRES 19 C 756 SER THR LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR
SEQRES 20 C 756 LYS THR GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN
SEQRES 21 C 756 GLU ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU
SEQRES 22 C 756 ALA ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE
SEQRES 23 C 756 VAL ALA LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN
SEQRES 24 C 756 SER ARG ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU
SEQRES 25 C 756 PHE HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG
SEQRES 26 C 756 GLY THR GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN
SEQRES 27 C 756 THR ALA PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE
SEQRES 28 C 756 ILE ALA GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS
SEQRES 29 C 756 GLY LEU PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR
SEQRES 30 C 756 LYS GLU GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU
SEQRES 31 C 756 GLY PHE SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS
SEQRES 32 C 756 SER SER GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS
SEQRES 33 C 756 PHE ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS
SEQRES 34 C 756 ILE ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO
SEQRES 35 C 756 PHE LEU ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR
SEQRES 36 C 756 ASP GLY SER VAL LEU VAL SER HIS GLY GLY THR GLU MET
SEQRES 37 C 756 GLY GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER
SEQRES 38 C 756 LYS ALA LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER
SEQRES 39 C 756 GLU THR SER THR ASN THR VAL PRO ASN SER SER PRO THR
SEQRES 40 C 756 ALA ALA SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL
SEQRES 41 C 756 TYR GLU ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO
SEQRES 42 C 756 PHE LYS LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP
SEQRES 43 C 756 VAL MET ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR
SEQRES 44 C 756 THR GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE
SEQRES 45 C 756 GLU THR ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR
SEQRES 46 C 756 GLY VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR
SEQRES 47 C 756 GLY ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP
SEQRES 48 C 756 VAL GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN
SEQRES 49 C 756 VAL GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR
SEQRES 50 C 756 LEU GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS
SEQRES 51 C 756 THR ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY
SEQRES 52 C 756 SER ILE PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP
SEQRES 53 C 756 CYS PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL
SEQRES 54 C 756 GLY GLU PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE
SEQRES 55 C 756 ALA ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS
SEQRES 56 C 756 THR ASN ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER
SEQRES 57 C 756 PRO ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP
SEQRES 58 C 756 LYS PHE THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN
SEQRES 59 C 756 CYS LYS
SEQRES 1 J 164 THR ALA ASP GLU LEU VAL PHE PHE VAL ASN GLY LYS LYS
SEQRES 2 J 164 VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU LEU
SEQRES 3 J 164 ALA TYR LEU ARG ARG LYS LEU GLY LEU ARG GLY THR LYS
SEQRES 4 J 164 LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR VAL
SEQRES 5 J 164 MET LEU SER LYS TYR ASP ARG LEU GLN ASP LYS ILE ILE
SEQRES 6 J 164 HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS THR
SEQRES 7 J 164 LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE GLY
SEQRES 8 J 164 SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG ILE
SEQRES 9 J 164 ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR PRO
SEQRES 10 J 164 GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN GLN
SEQRES 11 J 164 PRO GLU PRO THR VAL GLU GLU ILE GLU ASP ALA PHE GLN
SEQRES 12 J 164 GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE LEU
SEQRES 13 J 164 GLN GLY PHE ARG THR PHE ALA LYS
SEQRES 1 K 334 LEU PHE ASN PRO GLU GLU PHE MET PRO LEU ASP PRO THR
SEQRES 2 K 334 GLN GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS
SEQRES 3 K 334 ASP VAL PRO PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG
SEQRES 4 K 334 VAL THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU
SEQRES 5 K 334 ASP LEU LYS ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL
SEQRES 6 K 334 GLY ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN
SEQRES 7 K 334 GLN LEU PHE PRO MET ILE ILE CYS PRO ALA TRP ILE PRO
SEQRES 8 K 334 GLU LEU ASN ALA VAL GLU HIS GLY PRO GLU GLY ILE SER
SEQRES 9 K 334 PHE GLY ALA ALA CYS ALA LEU SER SER VAL GLU LYS THR
SEQRES 10 K 334 LEU LEU GLU ALA VAL ALA LYS LEU PRO THR GLN LYS THR
SEQRES 11 K 334 GLU VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE
SEQRES 12 K 334 ALA GLY LYS GLN VAL LYS SER VAL ALA SER LEU GLY GLY
SEQRES 13 K 334 ASN ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO
SEQRES 14 K 334 VAL PHE MET ALA SER GLY THR LYS LEU THR ILE VAL SER
SEQRES 15 K 334 ARG GLY THR ARG ARG THR VAL PRO MET ASP HIS THR PHE
SEQRES 16 K 334 PHE PRO SER TYR ARG LYS THR LEU LEU GLY PRO GLU GLU
SEQRES 17 K 334 ILE LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU ASP
SEQRES 18 K 334 GLU PHE PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU
SEQRES 19 K 334 ASP ASP ILE ALA LYS VAL THR CYS GLY MET ARG VAL LEU
SEQRES 20 K 334 PHE GLN PRO GLY SER MET GLN VAL LYS GLU LEU ALA LEU
SEQRES 21 K 334 CYS TYR GLY GLY MET ALA ASP ARG THR ILE SER ALA LEU
SEQRES 22 K 334 LYS THR THR GLN LYS GLN LEU SER LYS PHE TRP ASN GLU
SEQRES 23 K 334 LYS LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU
SEQRES 24 K 334 LEU SER LEU SER PRO ASP ALA PRO GLY GLY MET ILE GLU
SEQRES 25 K 334 PHE ARG ARG THR LEU THR LEU SER PHE PHE PHE LYS PHE
SEQRES 26 K 334 TYR LEU THR VAL LEU LYS LYS LEU GLY
SEQRES 1 L 756 ASP THR VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA
SEQRES 2 L 756 MET GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE
SEQRES 3 L 756 PRO ARG TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR
SEQRES 4 L 756 SER THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL
SEQRES 5 L 756 SER GLU ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU
SEQRES 6 L 756 SER ALA ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU
SEQRES 7 L 756 PHE ASN ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR
SEQRES 8 L 756 CYS VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR
SEQRES 9 L 756 PRO GLU HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL
SEQRES 10 L 756 THR TYR GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP
SEQRES 11 L 756 ALA ILE LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS
SEQRES 12 L 756 ILE GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA
SEQRES 13 L 756 ASP ASN VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN
SEQRES 14 L 756 ASP HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE
SEQRES 15 L 756 PRO LYS GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER
SEQRES 16 L 756 THR GLN ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS
SEQRES 17 L 756 MET LEU GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL
SEQRES 18 L 756 LYS ARG MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG
SEQRES 19 L 756 SER THR LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR
SEQRES 20 L 756 LYS THR GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN
SEQRES 21 L 756 GLU ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU
SEQRES 22 L 756 ALA ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE
SEQRES 23 L 756 VAL ALA LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN
SEQRES 24 L 756 SER ARG ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU
SEQRES 25 L 756 PHE HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG
SEQRES 26 L 756 GLY THR GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN
SEQRES 27 L 756 THR ALA PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE
SEQRES 28 L 756 ILE ALA GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS
SEQRES 29 L 756 GLY LEU PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR
SEQRES 30 L 756 LYS GLU GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU
SEQRES 31 L 756 GLY PHE SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS
SEQRES 32 L 756 SER SER GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS
SEQRES 33 L 756 PHE ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS
SEQRES 34 L 756 ILE ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO
SEQRES 35 L 756 PHE LEU ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR
SEQRES 36 L 756 ASP GLY SER VAL LEU VAL SER HIS GLY GLY THR GLU MET
SEQRES 37 L 756 GLY GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER
SEQRES 38 L 756 LYS ALA LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER
SEQRES 39 L 756 GLU THR SER THR ASN THR VAL PRO ASN SER SER PRO THR
SEQRES 40 L 756 ALA ALA SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL
SEQRES 41 L 756 TYR GLU ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO
SEQRES 42 L 756 PHE LYS LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP
SEQRES 43 L 756 VAL MET ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR
SEQRES 44 L 756 THR GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE
SEQRES 45 L 756 GLU THR ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR
SEQRES 46 L 756 GLY VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR
SEQRES 47 L 756 GLY ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP
SEQRES 48 L 756 VAL GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN
SEQRES 49 L 756 VAL GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR
SEQRES 50 L 756 LEU GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS
SEQRES 51 L 756 THR ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY
SEQRES 52 L 756 SER ILE PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP
SEQRES 53 L 756 CYS PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL
SEQRES 54 L 756 GLY GLU PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE
SEQRES 55 L 756 ALA ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS
SEQRES 56 L 756 THR ASN ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER
SEQRES 57 L 756 PRO ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP
SEQRES 58 L 756 LYS PHE THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN
SEQRES 59 L 756 CYS LYS
HET FES A 601 4
HET FES A 602 4
HET FAD B 606 53
HET MTE C1327 24
HET MOS C1328 4
HET QUE C1356 22
HET FES J 601 4
HET FES J 602 4
HET FAD K 606 53
HET MTE L1327 24
HET MOS L1328 4
HET QUE L1356 22
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM MTE PHOSPHONIC ACIDMONO-(2-AMINO-5,6-DIMERCAPTO-4-OXO-3,7,
HETNAM 2 MTE 8A,9,10,10A-HEXAHYDRO-4H-8-OXA-1,3,9,10-TETRAAZA-
HETNAM 3 MTE ANTHRACEN-7-YLMETHYL)ESTER
HETNAM MOS DIOXOTHIOMOLYBDENUM(VI) ION
HETNAM QUE 3,5,7,3',4'-PENTAHYDROXYFLAVONE
HETSYN QUE QUERCETIN
FORMUL 7 FES 4(FE2 S2)
FORMUL 9 FAD 2(C27 H33 N9 O15 P2)
FORMUL 10 MTE 2(C10 H14 N5 O6 P S2)
FORMUL 11 MOS 2(H MO O2 S)
FORMUL 12 QUE 2(C15 H10 O7)
FORMUL 19 HOH *1057(H2 O)
HELIX 1 1 THR A 25 LYS A 33 1 9
HELIX 2 2 PRO A 76 LEU A 80 5 5
HELIX 3 3 THR A 87 ILE A 91 5 5
HELIX 4 4 HIS A 99 SER A 108 1 10
HELIX 5 5 CYS A 116 GLN A 131 1 16
HELIX 6 6 THR A 135 ALA A 142 1 8
HELIX 7 7 TYR A 153 THR A 162 1 10
HELIX 8 8 ASN B 197 PHE B 201 5 5
HELIX 9 9 ASP B 205 GLU B 209 5 5
HELIX 10 10 PRO B 213 LYS B 220 1 8
HELIX 11 11 THR B 241 HIS B 252 1 12
HELIX 12 12 GLU B 263 LYS B 271 1 9
HELIX 13 13 ILE B 284 ASN B 288 5 5
HELIX 14 14 ALA B 304 LEU B 319 1 16
HELIX 15 15 PRO B 320 LYS B 323 5 4
HELIX 16 16 THR B 324 TRP B 336 1 13
HELIX 17 17 GLY B 339 SER B 344 1 6
HELIX 18 18 SER B 347 ALA B 355 1 9
HELIX 19 19 LEU B 361 SER B 368 1 8
HELIX 20 20 ASP B 386 PHE B 390 5 5
HELIX 21 21 ALA B 466 LYS B 472 1 7
HELIX 22 22 ASN B 479 LEU B 494 1 16
HELIX 23 23 MET B 504 GLY B 528 1 25
HELIX 24 24 ALA C 581 SER C 587 1 7
HELIX 25 25 TYR C 592 ILE C 596 5 5
HELIX 26 26 GLU C 624 VAL C 628 5 5
HELIX 27 27 SER C 636 ILE C 640 5 5
HELIX 28 28 THR C 674 VAL C 684 1 11
HELIX 29 29 THR C 697 ASN C 704 1 8
HELIX 30 30 ASP C 718 ALA C 726 1 9
HELIX 31 31 ASN C 768 GLY C 781 1 14
HELIX 32 32 PRO C 783 ASN C 785 5 3
HELIX 33 33 SER C 805 GLY C 820 1 16
HELIX 34 34 ASP C 828 THR C 836 1 9
HELIX 35 35 LEU C 873 HIS C 884 1 12
HELIX 36 36 GLY C 915 CYS C 934 1 20
HELIX 37 37 PRO C 937 MET C 946 1 10
HELIX 38 38 SER C 963 SER C 975 1 13
HELIX 39 39 GLN C 976 ASN C 991 1 16
HELIX 40 40 VAL C 1011 LEU C 1014 5 4
HELIX 41 41 GLY C 1041 LYS C 1055 1 15
HELIX 42 42 PRO C 1057 SER C 1059 5 3
HELIX 43 43 VAL C 1081 ASN C 1108 1 28
HELIX 44 44 SER C 1112 ASP C 1123 1 12
HELIX 45 45 ASN C 1187 LEU C 1208 1 22
HELIX 46 46 ALA C 1231 ILE C 1235 5 5
HELIX 47 47 ALA C 1252 SER C 1256 5 5
HELIX 48 48 PRO C 1263 LEU C 1266 5 4
HELIX 49 49 GLY C 1267 THR C 1286 1 20
HELIX 50 50 THR C 1301 CYS C 1309 1 9
HELIX 51 51 LEU C 1316 GLY C 1320 5 5
HELIX 52 52 THR J 25 LYS J 33 1 9
HELIX 53 53 PRO J 76 LEU J 80 5 5
HELIX 54 54 THR J 87 ILE J 91 5 5
HELIX 55 55 HIS J 99 SER J 108 1 10
HELIX 56 56 CYS J 116 GLN J 131 1 16
HELIX 57 57 THR J 135 PHE J 143 1 9
HELIX 58 58 TYR J 153 THR J 162 1 10
HELIX 59 59 THR K 241 HIS K 252 1 12
HELIX 60 60 GLU K 263 LYS K 271 1 9
HELIX 61 61 ILE K 284 ASN K 288 5 5
HELIX 62 62 ALA K 304 LEU K 319 1 16
HELIX 63 63 PRO K 320 LYS K 323 5 4
HELIX 64 64 THR K 324 TRP K 336 1 13
HELIX 65 65 GLY K 339 SER K 344 1 6
HELIX 66 66 SER K 347 ALA K 355 1 9
HELIX 67 67 LEU K 361 GLY K 369 1 9
HELIX 68 68 ASP K 386 PHE K 390 5 5
HELIX 69 69 ALA K 466 GLN K 473 1 8
HELIX 70 70 ASN K 479 LEU K 494 1 16
HELIX 71 71 MET K 504 LYS K 526 1 23
HELIX 72 72 ALA L 581 SER L 587 1 7
HELIX 73 73 TYR L 592 ILE L 596 5 5
HELIX 74 74 GLU L 624 VAL L 628 5 5
HELIX 75 75 SER L 636 ILE L 640 5 5
HELIX 76 76 THR L 674 VAL L 684 1 11
HELIX 77 77 THR L 697 ASN L 704 1 8
HELIX 78 78 ASP L 718 ALA L 726 1 9
HELIX 79 79 ASN L 768 GLY L 781 1 14
HELIX 80 80 PRO L 783 ASN L 785 5 3
HELIX 81 81 SER L 805 GLY L 820 1 16
HELIX 82 82 ASP L 828 THR L 836 1 9
HELIX 83 83 LEU L 873 HIS L 884 1 12
HELIX 84 84 GLY L 915 GLY L 935 1 21
HELIX 85 85 PRO L 937 MET L 946 1 10
HELIX 86 86 SER L 963 GLN L 976 1 14
HELIX 87 87 GLN L 976 ASN L 991 1 16
HELIX 88 88 VAL L 1011 LEU L 1014 5 4
HELIX 89 89 GLY L 1041 LYS L 1055 1 15
HELIX 90 90 PRO L 1057 SER L 1059 5 3
HELIX 91 91 VAL L 1081 ASN L 1108 1 28
HELIX 92 92 SER L 1112 ASP L 1123 1 12
HELIX 93 93 ASN L 1187 LEU L 1208 1 22
HELIX 94 94 ALA L 1252 SER L 1256 5 5
HELIX 95 95 PRO L 1263 LEU L 1266 5 4
HELIX 96 96 GLY L 1267 THR L 1286 1 20
HELIX 97 97 THR L 1301 CYS L 1309 1 9
SHEET 1 A 5 LYS A 13 GLU A 17 0
SHEET 2 A 5 LEU A 6 VAL A 10 -1 N PHE A 8 O VAL A 15
SHEET 3 A 5 ALA A 84 THR A 86 1 O VAL A 85 N PHE A 9
SHEET 4 A 5 THR A 52 ASP A 59 -1 N MET A 54 O THR A 86
SHEET 5 A 5 LYS A 64 ASN A 71 -1 O PHE A 68 N LEU A 55
SHEET 1 B 4 LEU B 227 GLU B 230 0
SHEET 2 B 4 THR B 235 GLN B 238 -1 O GLN B 238 N LEU B 227
SHEET 3 B 4 MET B 277 CYS B 280 1 O CYS B 280 N ILE B 237
SHEET 4 B 4 LYS B 256 LEU B 257 1 N LYS B 256 O ILE B 279
SHEET 1 C 5 VAL B 290 HIS B 292 0
SHEET 2 C 5 GLY B 296 GLY B 300 -1 O SER B 298 N GLU B 291
SHEET 3 C 5 ILE B 403 PRO B 410 -1 O ILE B 409 N ILE B 297
SHEET 4 C 5 LYS B 371 VAL B 375 -1 N LYS B 371 O GLU B 408
SHEET 5 C 5 ARG B 380 PRO B 384 -1 O ARG B 381 N ILE B 374
SHEET 1 D 4 GLU B 416 LYS B 422 0
SHEET 2 D 4 THR B 435 PHE B 442 -1 O MET B 438 N SER B 419
SHEET 3 D 4 VAL B 449 GLY B 457 -1 O GLY B 457 N THR B 435
SHEET 4 D 4 ILE B 464 SER B 465 -1 O ILE B 464 N TYR B 456
SHEET 1 E 8 PHE C 631 LEU C 635 0
SHEET 2 E 8 ILE C 666 ALA C 672 -1 O ALA C 669 N LEU C 635
SHEET 3 E 8 LEU C 603 THR C 609 -1 N VAL C 608 O ILE C 667
SHEET 4 E 8 VAL C 823 MET C 826 1 O ARG C 824 N LEU C 605
SHEET 5 E 8 CYS C 748 PRO C 753 -1 N ALA C 751 O VAL C 823
SHEET 6 E 8 MET C 760 VAL C 764 -1 O GLU C 761 N ILE C 752
SHEET 7 E 8 ILE C 787 VAL C 791 1 O ARG C 790 N LEU C 762
SHEET 8 E 8 THR C1066 SER C1067 -1 O THR C1066 N VAL C 791
SHEET 1 F 3 THR C 659 VAL C 660 0
SHEET 2 F 3 ALA C 615 ASP C 621 -1 N ALA C 615 O VAL C 660
SHEET 3 F 3 LYS C 686 ASP C 691 -1 O LYS C 686 N ASP C 621
SHEET 1 G 2 GLU C 645 THR C 646 0
SHEET 2 G 2 GLU C 652 THR C 653 -1 O GLU C 652 N THR C 646
SHEET 1 H 5 PHE C 707 LYS C 716 0
SHEET 2 H 5 ILE C 894 LYS C 902 -1 O GLY C 898 N LEU C 712
SHEET 3 H 5 ILE C 856 GLY C 868 1 N HIS C 863 O THR C 897
SHEET 4 H 5 PHE C 842 PHE C 850 -1 N GLY C 849 O ALA C 858
SHEET 5 H 5 ASN C 728 ILE C 736 -1 N LEU C 734 O ALA C 844
SHEET 1 I 4 LYS C 994 ILE C1007 0
SHEET 2 I 4 TYR C1152 ASP C1165 -1 O TYR C1152 N ILE C1007
SHEET 3 I 4 HIS C1171 ASP C1181 -1 O LYS C1172 N GLU C1163
SHEET 4 I 4 GLU C1238 LEU C1243 1 O ARG C1240 N THR C1176
SHEET 1 J 4 ILE C1061 TYR C1062 0
SHEET 2 J 4 VAL C1029 HIS C1033 1 N VAL C1031 O TYR C1062
SHEET 3 J 4 GLN C1016 VAL C1023 -1 N LEU C1020 O SER C1032
SHEET 4 J 4 SER C1128 ARG C1134 -1 O THR C1129 N ILE C1021
SHEET 1 K 5 LYS J 13 GLU J 17 0
SHEET 2 K 5 LEU J 6 VAL J 10 -1 N PHE J 8 O VAL J 15
SHEET 3 K 5 ALA J 84 THR J 86 1 O VAL J 85 N PHE J 9
SHEET 4 K 5 THR J 52 TYR J 58 -1 N SER J 56 O ALA J 84
SHEET 5 K 5 ILE J 65 ASN J 71 -1 O PHE J 68 N LEU J 55
SHEET 1 L 4 LEU K 227 GLU K 230 0
SHEET 2 L 4 THR K 235 GLN K 238 -1 O GLN K 238 N LEU K 227
SHEET 3 L 4 MET K 277 CYS K 280 1 O CYS K 280 N ILE K 237
SHEET 4 L 4 LYS K 256 LEU K 257 1 N LYS K 256 O ILE K 279
SHEET 1 M 5 VAL K 290 HIS K 292 0
SHEET 2 M 5 GLY K 296 GLY K 300 -1 O SER K 298 N GLU K 291
SHEET 3 M 5 ILE K 403 PRO K 410 -1 O ILE K 409 N ILE K 297
SHEET 4 M 5 LYS K 371 VAL K 375 -1 N THR K 373 O LEU K 405
SHEET 5 M 5 ARG K 380 PRO K 384 -1 O VAL K 383 N LEU K 372
SHEET 1 N 4 GLU K 416 LYS K 422 0
SHEET 2 N 4 THR K 435 PHE K 442 -1 O CYS K 436 N PHE K 421
SHEET 3 N 4 VAL K 449 GLY K 457 -1 O GLY K 457 N THR K 435
SHEET 4 N 4 ILE K 464 SER K 465 -1 O ILE K 464 N TYR K 456
SHEET 1 O 8 PHE L 631 LEU L 635 0
SHEET 2 O 8 ILE L 666 ALA L 672 -1 O ALA L 669 N LEU L 635
SHEET 3 O 8 LEU L 603 THR L 609 -1 N PHE L 604 O ALA L 672
SHEET 4 O 8 VAL L 823 MET L 826 1 O ARG L 824 N LEU L 605
SHEET 5 O 8 CYS L 748 PRO L 753 -1 N ALA L 751 O VAL L 823
SHEET 6 O 8 MET L 760 VAL L 764 -1 O GLU L 761 N ILE L 752
SHEET 7 O 8 ILE L 787 VAL L 791 1 O ARG L 790 N LEU L 762
SHEET 8 O 8 THR L1066 SER L1067 -1 O THR L1066 N VAL L 791
SHEET 1 P 3 THR L 659 VAL L 660 0
SHEET 2 P 3 ALA L 615 ASP L 621 -1 N ALA L 615 O VAL L 660
SHEET 3 P 3 LYS L 686 ASP L 691 -1 O THR L 688 N LYS L 618
SHEET 1 Q 2 GLU L 645 THR L 646 0
SHEET 2 Q 2 GLU L 652 THR L 653 -1 O GLU L 652 N THR L 646
SHEET 1 R 5 PHE L 707 LYS L 716 0
SHEET 2 R 5 ILE L 894 LYS L 902 -1 O GLY L 896 N ILE L 714
SHEET 3 R 5 ILE L 856 GLY L 868 1 N HIS L 863 O THR L 897
SHEET 4 R 5 PHE L 842 PHE L 850 -1 N GLY L 849 O VAL L 857
SHEET 5 R 5 ASN L 728 ILE L 736 -1 N ILE L 736 O PHE L 842
SHEET 1 S 4 LYS L 994 ILE L1007 0
SHEET 2 S 4 TYR L1152 ASP L1165 -1 O ILE L1164 N LYS L 995
SHEET 3 S 4 HIS L1171 ASP L1181 -1 O ARG L1175 N GLU L1161
SHEET 4 S 4 GLU L1238 LEU L1243 1 O ARG L1240 N THR L1176
SHEET 1 T 4 ILE L1061 ILE L1063 0
SHEET 2 T 4 VAL L1029 HIS L1033 1 N VAL L1031 O TYR L1062
SHEET 3 T 4 GLN L1016 VAL L1023 -1 N LEU L1020 O SER L1032
SHEET 4 T 4 SER L1128 ARG L1134 -1 O THR L1129 N ILE L1021
LINK SG CYS A 43 FE2 FES A 602 1555 1555 2.39
LINK SG CYS A 48 FE2 FES A 602 1555 1555 2.18
LINK SG CYS A 51 FE1 FES A 602 1555 1555 2.27
LINK SG CYS A 73 FE1 FES A 602 1555 1555 2.30
LINK SG CYS A 113 FE1 FES A 601 1555 1555 2.34
LINK SG CYS A 116 FE2 FES A 601 1555 1555 2.25
LINK SG CYS A 148 FE2 FES A 601 1555 1555 2.44
LINK SG CYS A 150 FE1 FES A 601 1555 1555 2.33
LINK S2' MTE C1327 MO MOS C1328 1555 1555 2.33
LINK S1' MTE C1327 MO MOS C1328 1555 1555 2.36
LINK SG CYS J 43 FE2 FES J 602 1555 1555 2.25
LINK SG CYS J 48 FE2 FES J 602 1555 1555 2.25
LINK SG CYS J 51 FE1 FES J 602 1555 1555 2.28
LINK SG CYS J 73 FE1 FES J 602 1555 1555 2.21
LINK SG CYS J 113 FE1 FES J 601 1555 1555 2.44
LINK SG CYS J 116 FE2 FES J 601 1555 1555 2.26
LINK SG CYS J 148 FE2 FES J 601 1555 1555 2.43
LINK SG CYS J 150 FE1 FES J 601 1555 1555 2.34
LINK S1' MTE L1327 MO MOS L1328 1555 1555 2.32
LINK S2' MTE L1327 MO MOS L1328 1555 1555 2.36
CISPEP 1 SER C 1298 PRO C 1299 0 -1.39
CISPEP 2 SER L 1298 PRO L 1299 0 1.97
SITE 1 AC1 7 GLN A 112 CYS A 113 GLY A 114 CYS A 116
SITE 2 AC1 7 CYS A 148 ARG A 149 CYS A 150
SITE 1 AC2 10 GLY A 42 CYS A 43 GLY A 44 GLY A 46
SITE 2 AC2 10 GLY A 47 CYS A 48 GLY A 49 CYS A 51
SITE 3 AC2 10 ASN A 71 CYS A 73
SITE 1 AC3 29 GLY A 46 LYS B 256 LEU B 257 VAL B 258
SITE 2 AC3 29 VAL B 259 GLY B 260 ASN B 261 THR B 262
SITE 3 AC3 29 GLU B 263 ILE B 264 ALA B 301 PHE B 337
SITE 4 AC3 29 ALA B 338 ALA B 346 SER B 347 GLY B 350
SITE 5 AC3 29 ASN B 351 ILE B 353 THR B 354 SER B 359
SITE 6 AC3 29 ASP B 360 ILE B 403 LEU B 404 HOH B 560
SITE 7 AC3 29 HOH B 561 HOH B 628 HOH B 691 HOH B1231
SITE 8 AC3 29 HOH B1472
SITE 1 AC4 21 GLN A 112 CYS A 150 HOH C 96 HOH C 336
SITE 2 AC4 21 HOH C 356 GLY C 796 GLY C 797 PHE C 798
SITE 3 AC4 21 GLY C 799 ARG C 912 MET C1038 GLY C1039
SITE 4 AC4 21 GLN C1040 ALA C1078 ALA C1079 SER C1080
SITE 5 AC4 21 VAL C1081 SER C1082 GLN C1194 GLU C1261
SITE 6 AC4 21 MOS C1328
SITE 1 AC5 9 GLN C 767 GLY C 799 PHE C 911 ARG C 912
SITE 2 AC5 9 ALA C1078 ALA C1079 GLU C1261 MTE C1327
SITE 3 AC5 9 QUE C1356
SITE 1 AC6 14 LEU C 648 GLU C 802 LEU C 873 SER C 876
SITE 2 AC6 14 ARG C 880 PHE C 914 PHE C1009 THR C1010
SITE 3 AC6 14 VAL C1011 LEU C1014 PRO C1076 ALA C1078
SITE 4 AC6 14 ALA C1079 MOS C1328
SITE 1 AC7 8 GLN J 112 CYS J 113 GLY J 114 CYS J 116
SITE 2 AC7 8 CYS J 148 ARG J 149 CYS J 150 LEU L 744
SITE 1 AC8 9 GLY J 42 CYS J 43 GLY J 44 GLY J 46
SITE 2 AC8 9 GLY J 47 CYS J 48 GLY J 49 CYS J 51
SITE 3 AC8 9 CYS J 73
SITE 1 AC9 26 GLY J 46 LEU K 257 VAL K 258 VAL K 259
SITE 2 AC9 26 GLY K 260 ASN K 261 THR K 262 GLU K 263
SITE 3 AC9 26 ILE K 264 ALA K 301 PHE K 337 ALA K 338
SITE 4 AC9 26 ALA K 346 SER K 347 GLY K 350 ASN K 351
SITE 5 AC9 26 ILE K 353 THR K 354 SER K 359 ASP K 360
SITE 6 AC9 26 ILE K 403 LEU K 404 HOH K 531 HOH K 543
SITE 7 AC9 26 HOH K1147 HOH K1453
SITE 1 BC1 18 GLN J 112 CYS J 150 HOH L 338 GLY L 797
SITE 2 BC1 18 PHE L 798 GLY L 799 ARG L 912 MET L1038
SITE 3 BC1 18 GLY L1039 GLN L1040 ALA L1078 ALA L1079
SITE 4 BC1 18 SER L1080 VAL L1081 SER L1082 GLN L1194
SITE 5 BC1 18 GLU L1261 MOS L1328
SITE 1 BC2 9 GLN L 767 GLY L 799 PHE L 911 ARG L 912
SITE 2 BC2 9 ALA L1078 ALA L1079 GLU L1261 MTE L1327
SITE 3 BC2 9 QUE L1356
SITE 1 BC3 15 HOH L 452 LEU L 648 GLU L 802 LEU L 873
SITE 2 BC3 15 SER L 876 ARG L 880 PHE L 914 SER L1008
SITE 3 BC3 15 PHE L1009 THR L1010 VAL L1011 LEU L1014
SITE 4 BC3 15 ALA L1078 ALA L1079 MOS L1328
CRYST1 132.686 73.398 138.210 90.00 97.13 90.00 P 1 21 1 4
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 0.007537 0.000000 0.000943 0.00000
SCALE2 0.000000 0.013624 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007292 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
