HEADER OXIDOREDUCTASE 01-JUL-10 3NS1
TITLE CRYSTAL STRUCTURE OF BOVINE XANTHINE OXIDASE IN COMPLEX WITH 6-
TITLE 2 MERCAPTOPURINE
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 XANTHINE OXIDASE, HYPOXANTHINE, SUBSTRATE ORIENTATION, HYDROXYLASE,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CAO,J.M.PAUFF,R.HILLE
REVDAT 4 27-DEC-23 3NS1 1 REMARK LINK
REVDAT 3 15-SEP-10 3NS1 1 JRNL
REVDAT 2 28-JUL-10 3NS1 1 JRNL
REVDAT 1 14-JUL-10 3NS1 0
JRNL AUTH H.CAO,J.M.PAUFF,R.HILLE
JRNL TITL SUBSTRATE ORIENTATION AND CATALYTIC SPECIFICITY IN THE
JRNL TITL 2 ACTION OF XANTHINE OXIDASE: THE SEQUENTIAL HYDROXYLATION OF
JRNL TITL 3 HYPOXANTHINE TO URIC ACID.
JRNL REF J.BIOL.CHEM. V. 285 28044 2010
JRNL REFN ISSN 0021-9258
JRNL PMID 20615869
JRNL DOI 10.1074/JBC.M110.128561
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 3 NUMBER OF REFLECTIONS : 78350
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3922
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5410
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.14
REMARK 3 BIN R VALUE (WORKING SET) : 0.3120
REMARK 3 BIN FREE R VALUE SET COUNT : 285
REMARK 3 BIN FREE R VALUE : 0.3780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 18872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 198
REMARK 3 SOLVENT ATOMS : 287
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72000
REMARK 3 B22 (A**2) : 0.25000
REMARK 3 B33 (A**2) : 1.42000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.19000
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): 0.373
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.243
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.285
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.875
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19481 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26371 ; 1.682 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2432 ; 6.708 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 815 ;37.493 ;23.791
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3337 ;17.837 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 118 ;21.578 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2953 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14536 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7350 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13012 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 532 ; 0.156 ; 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): 66 ; 0.385 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.146 ; 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): 12500 ; 0.711 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19520 ; 1.174 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8070 ; 1.827 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6843 ; 2.936 ; 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 : 3
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A J
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 165 1
REMARK 3 1 J 2 J 165 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1255 ; 0.060 ; 0.050
REMARK 3 TIGHT THERMAL 1 A (A**2): 1255 ; 0.150 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 224 B 528 1
REMARK 3 1 K 224 K 528 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 2389 ; 0.070 ; 0.050
REMARK 3 TIGHT THERMAL 2 B (A**2): 2389 ; 0.130 ; 0.500
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 571 C 1315 1
REMARK 3 1 L 571 L 1315 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 5761 ; 0.070 ; 0.050
REMARK 3 TIGHT THERMAL 3 C (A**2): 5761 ; 0.150 ; 0.500
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 3NS1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1000060208.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.0
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 : 78350
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
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: MOLREP CCP4
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, PH 7.0, 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 36.96400
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: 30360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 83560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -213.0 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 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 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 O SER L 610 O VAL L 663 2.02
REMARK 500 O SER C 610 O VAL C 663 2.08
REMARK 500 OD2 ASP L 1191 O HOH L 168 2.17
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 CYS L 992 CB CYS L 992 SG -0.096
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 A 104 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLU B 286 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 LEU B 398 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ARG C 839 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 VAL C 848 CB - CA - C ANGL. DEV. = -13.3 DEGREES
REMARK 500 LEU C1203 CA - CB - CG ANGL. DEV. = 14.7 DEGREES
REMARK 500 LEU K 398 CA - CB - CG ANGL. DEV. = 14.5 DEGREES
REMARK 500 ARG L 839 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG L 839 NE - CZ - NH2 ANGL. DEV. = -3.9 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 -28.18 -151.88
REMARK 500 LEU A 61 -81.66 -69.99
REMARK 500 GLN A 62 -33.02 -38.95
REMARK 500 ASP A 63 -16.77 86.81
REMARK 500 THR A 96 -87.08 -121.69
REMARK 500 GLN A 112 -85.05 -110.94
REMARK 500 TYR A 153 -39.58 68.79
REMARK 500 VAL B 259 -81.32 -111.61
REMARK 500 ASN B 272 3.34 87.34
REMARK 500 GLU B 286 142.02 78.18
REMARK 500 LEU B 287 -25.68 71.65
REMARK 500 HIS B 292 77.71 -105.92
REMARK 500 ARG B 335 -71.76 -58.47
REMARK 500 TRP B 336 56.35 -101.45
REMARK 500 ALA B 338 176.13 51.60
REMARK 500 ARG B 377 109.36 -59.34
REMARK 500 TYR B 393 117.44 -37.16
REMARK 500 ALA B 424 -80.63 -63.47
REMARK 500 SER B 425 -137.63 -79.95
REMARK 500 ARG B 426 137.70 166.44
REMARK 500 ARG B 427 -32.68 -136.34
REMARK 500 SER B 475 -17.10 95.88
REMARK 500 LEU B 527 -117.91 -111.03
REMARK 500 LYS C 657 -73.56 -91.00
REMARK 500 LYS C 721 -57.32 105.54
REMARK 500 CYS C 748 124.71 -171.72
REMARK 500 PHE C 798 15.04 50.14
REMARK 500 THR C 803 -40.43 -142.22
REMARK 500 VAL C 857 -20.86 -141.65
REMARK 500 ASP C 872 -128.89 47.73
REMARK 500 ASN C 887 -112.71 36.75
REMARK 500 ARG C 912 104.50 -25.24
REMARK 500 SER C1008 149.72 140.94
REMARK 500 MET C1038 20.20 -141.02
REMARK 500 THR C1144 -34.33 70.61
REMARK 500 ASN C1187 93.78 -160.62
REMARK 500 THR C1207 -42.29 -138.64
REMARK 500 THR C1286 -60.03 -104.43
REMARK 500 LYS C1291 24.95 -78.77
REMARK 500 CYS J 43 -29.75 -150.43
REMARK 500 LEU J 61 -83.53 -71.29
REMARK 500 ASP J 63 -14.94 85.94
REMARK 500 THR J 96 -88.01 -120.02
REMARK 500 GLN J 112 -86.93 -116.24
REMARK 500 TYR J 153 -39.79 70.94
REMARK 500 VAL K 259 -75.98 -112.37
REMARK 500 ASN K 272 3.00 92.41
REMARK 500 GLU K 286 132.69 81.53
REMARK 500 LEU K 287 -25.14 78.12
REMARK 500 LYS K 318 -32.36 -134.37
REMARK 500
REMARK 500 THIS ENTRY HAS 81 RAMACHANDRAN OUTLIERS.
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 ASN C 1324 CYS C 1325 54.70
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 99.9
REMARK 620 3 FES A 602 S2 114.8 89.3
REMARK 620 4 CYS A 48 SG 116.3 119.1 113.9
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 117.4
REMARK 620 3 FES A 602 S2 117.9 90.0
REMARK 620 4 CYS A 73 SG 109.1 110.0 111.3
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 115.3
REMARK 620 3 FES A 601 S2 115.3 95.1
REMARK 620 4 CYS A 150 SG 98.1 106.2 127.6
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 125.0
REMARK 620 3 FES A 601 S2 110.6 96.7
REMARK 620 4 CYS A 148 SG 105.8 107.6 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS C1327 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE C1326 S1'
REMARK 620 2 MOS C1327 S 88.4
REMARK 620 3 MOS C1327 O1 148.6 90.8
REMARK 620 4 MOS C1327 O2 115.4 91.6 96.0
REMARK 620 5 MTE C1326 S2' 81.0 155.3 86.9 113.2
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 103.8
REMARK 620 3 FES J 602 S2 118.5 92.3
REMARK 620 4 CYS J 48 SG 117.5 111.8 109.8
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 115.7
REMARK 620 3 FES J 602 S2 118.5 93.9
REMARK 620 4 CYS J 73 SG 105.7 113.9 109.1
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 116.0
REMARK 620 3 FES J 601 S2 112.6 98.8
REMARK 620 4 CYS J 150 SG 101.2 103.5 125.2
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 120.2
REMARK 620 3 FES J 601 S2 108.8 97.5
REMARK 620 4 CYS J 148 SG 108.5 110.4 110.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS L1327 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE L1326 S1'
REMARK 620 2 MOS L1327 S 87.9
REMARK 620 3 MOS L1327 O1 150.1 88.0
REMARK 620 4 MOS L1327 O2 116.9 91.6 92.8
REMARK 620 5 MTE L1326 S2' 76.4 144.1 90.0 124.4
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 1326
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS C 1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PM6 C 1
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 1326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS L 1327
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PM6 L 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3EUB RELATED DB: PDB
REMARK 900 RELATED ID: 3ETR RELATED DB: PDB
REMARK 900 RELATED ID: 3B9J RELATED DB: PDB
REMARK 900 RELATED ID: 3NRZ RELATED DB: PDB
DBREF 3NS1 A 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NS1 B 224 528 UNP P80457 XDH_BOVIN 224 528
DBREF 3NS1 C 571 1325 UNP P80457 XDH_BOVIN 571 1325
DBREF 3NS1 J 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NS1 K 224 528 UNP P80457 XDH_BOVIN 224 528
DBREF 3NS1 L 571 1325 UNP P80457 XDH_BOVIN 571 1325
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 305 PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL THR TRP
SEQRES 2 B 305 ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP LEU LYS
SEQRES 3 B 305 ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL GLY ASN THR
SEQRES 4 B 305 GLU ILE GLY ILE GLU MET LYS PHE LYS ASN GLN LEU PHE
SEQRES 5 B 305 PRO MET ILE ILE CYS PRO ALA TRP ILE PRO GLU LEU ASN
SEQRES 6 B 305 ALA VAL GLU HIS GLY PRO GLU GLY ILE SER PHE GLY ALA
SEQRES 7 B 305 ALA CYS ALA LEU SER SER VAL GLU LYS THR LEU LEU GLU
SEQRES 8 B 305 ALA VAL ALA LYS LEU PRO THR GLN LYS THR GLU VAL PHE
SEQRES 9 B 305 ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA GLY LYS
SEQRES 10 B 305 GLN VAL LYS SER VAL ALA SER LEU GLY GLY ASN ILE ILE
SEQRES 11 B 305 THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL PHE MET
SEQRES 12 B 305 ALA SER GLY THR LYS LEU THR ILE VAL SER ARG GLY THR
SEQRES 13 B 305 ARG ARG THR VAL PRO MET ASP HIS THR PHE PHE PRO SER
SEQRES 14 B 305 TYR ARG LYS THR LEU LEU GLY PRO GLU GLU ILE LEU LEU
SEQRES 15 B 305 SER ILE GLU ILE PRO TYR SER ARG GLU ASP GLU PHE PHE
SEQRES 16 B 305 SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP ASP ILE
SEQRES 17 B 305 ALA LYS VAL THR CYS GLY MET ARG VAL LEU PHE GLN PRO
SEQRES 18 B 305 GLY SER MET GLN VAL LYS GLU LEU ALA LEU CYS TYR GLY
SEQRES 19 B 305 GLY MET ALA ASP ARG THR ILE SER ALA LEU LYS THR THR
SEQRES 20 B 305 GLN LYS GLN LEU SER LYS PHE TRP ASN GLU LYS LEU LEU
SEQRES 21 B 305 GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU SER LEU
SEQRES 22 B 305 SER PRO ASP ALA PRO GLY GLY MET ILE GLU PHE ARG ARG
SEQRES 23 B 305 THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR LEU THR
SEQRES 24 B 305 VAL LEU LYS LYS LEU GLY
SEQRES 1 C 755 ASP THR VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA
SEQRES 2 C 755 MET GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE
SEQRES 3 C 755 PRO ARG TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR
SEQRES 4 C 755 SER THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL
SEQRES 5 C 755 SER GLU ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU
SEQRES 6 C 755 SER ALA ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU
SEQRES 7 C 755 PHE ASN ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR
SEQRES 8 C 755 CYS VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR
SEQRES 9 C 755 PRO GLU HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL
SEQRES 10 C 755 THR TYR GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP
SEQRES 11 C 755 ALA ILE LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS
SEQRES 12 C 755 ILE GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA
SEQRES 13 C 755 ASP ASN VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN
SEQRES 14 C 755 ASP HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE
SEQRES 15 C 755 PRO LYS GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER
SEQRES 16 C 755 THR GLN ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS
SEQRES 17 C 755 MET LEU GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL
SEQRES 18 C 755 LYS ARG MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG
SEQRES 19 C 755 SER THR LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR
SEQRES 20 C 755 LYS THR GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN
SEQRES 21 C 755 GLU ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU
SEQRES 22 C 755 ALA ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE
SEQRES 23 C 755 VAL ALA LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN
SEQRES 24 C 755 SER ARG ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU
SEQRES 25 C 755 PHE HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG
SEQRES 26 C 755 GLY THR GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN
SEQRES 27 C 755 THR ALA PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE
SEQRES 28 C 755 ILE ALA GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS
SEQRES 29 C 755 GLY LEU PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR
SEQRES 30 C 755 LYS GLU GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU
SEQRES 31 C 755 GLY PHE SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS
SEQRES 32 C 755 SER SER GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS
SEQRES 33 C 755 PHE ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS
SEQRES 34 C 755 ILE ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO
SEQRES 35 C 755 PHE LEU ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR
SEQRES 36 C 755 ASP GLY SER VAL LEU VAL SER HIS GLY GLY THR GLU MET
SEQRES 37 C 755 GLY GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER
SEQRES 38 C 755 LYS ALA LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER
SEQRES 39 C 755 GLU THR SER THR ASN THR VAL PRO ASN SER SER PRO THR
SEQRES 40 C 755 ALA ALA SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL
SEQRES 41 C 755 TYR GLU ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO
SEQRES 42 C 755 PHE LYS LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP
SEQRES 43 C 755 VAL MET ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR
SEQRES 44 C 755 THR GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE
SEQRES 45 C 755 GLU THR ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR
SEQRES 46 C 755 GLY VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR
SEQRES 47 C 755 GLY ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP
SEQRES 48 C 755 VAL GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN
SEQRES 49 C 755 VAL GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR
SEQRES 50 C 755 LEU GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS
SEQRES 51 C 755 THR ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY
SEQRES 52 C 755 SER ILE PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP
SEQRES 53 C 755 CYS PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL
SEQRES 54 C 755 GLY GLU PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE
SEQRES 55 C 755 ALA ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS
SEQRES 56 C 755 THR ASN ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER
SEQRES 57 C 755 PRO ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP
SEQRES 58 C 755 LYS PHE THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN
SEQRES 59 C 755 CYS
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 305 PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL THR TRP
SEQRES 2 K 305 ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP LEU LYS
SEQRES 3 K 305 ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL GLY ASN THR
SEQRES 4 K 305 GLU ILE GLY ILE GLU MET LYS PHE LYS ASN GLN LEU PHE
SEQRES 5 K 305 PRO MET ILE ILE CYS PRO ALA TRP ILE PRO GLU LEU ASN
SEQRES 6 K 305 ALA VAL GLU HIS GLY PRO GLU GLY ILE SER PHE GLY ALA
SEQRES 7 K 305 ALA CYS ALA LEU SER SER VAL GLU LYS THR LEU LEU GLU
SEQRES 8 K 305 ALA VAL ALA LYS LEU PRO THR GLN LYS THR GLU VAL PHE
SEQRES 9 K 305 ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA GLY LYS
SEQRES 10 K 305 GLN VAL LYS SER VAL ALA SER LEU GLY GLY ASN ILE ILE
SEQRES 11 K 305 THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL PHE MET
SEQRES 12 K 305 ALA SER GLY THR LYS LEU THR ILE VAL SER ARG GLY THR
SEQRES 13 K 305 ARG ARG THR VAL PRO MET ASP HIS THR PHE PHE PRO SER
SEQRES 14 K 305 TYR ARG LYS THR LEU LEU GLY PRO GLU GLU ILE LEU LEU
SEQRES 15 K 305 SER ILE GLU ILE PRO TYR SER ARG GLU ASP GLU PHE PHE
SEQRES 16 K 305 SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP ASP ILE
SEQRES 17 K 305 ALA LYS VAL THR CYS GLY MET ARG VAL LEU PHE GLN PRO
SEQRES 18 K 305 GLY SER MET GLN VAL LYS GLU LEU ALA LEU CYS TYR GLY
SEQRES 19 K 305 GLY MET ALA ASP ARG THR ILE SER ALA LEU LYS THR THR
SEQRES 20 K 305 GLN LYS GLN LEU SER LYS PHE TRP ASN GLU LYS LEU LEU
SEQRES 21 K 305 GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU SER LEU
SEQRES 22 K 305 SER PRO ASP ALA PRO GLY GLY MET ILE GLU PHE ARG ARG
SEQRES 23 K 305 THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR LEU THR
SEQRES 24 K 305 VAL LEU LYS LYS LEU GLY
SEQRES 1 L 755 ASP THR VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA
SEQRES 2 L 755 MET GLN ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE
SEQRES 3 L 755 PRO ARG TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR
SEQRES 4 L 755 SER THR ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL
SEQRES 5 L 755 SER GLU ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU
SEQRES 6 L 755 SER ALA ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU
SEQRES 7 L 755 PHE ASN ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR
SEQRES 8 L 755 CYS VAL GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR
SEQRES 9 L 755 PRO GLU HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL
SEQRES 10 L 755 THR TYR GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP
SEQRES 11 L 755 ALA ILE LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS
SEQRES 12 L 755 ILE GLU LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA
SEQRES 13 L 755 ASP ASN VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN
SEQRES 14 L 755 ASP HIS PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE
SEQRES 15 L 755 PRO LYS GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER
SEQRES 16 L 755 THR GLN ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS
SEQRES 17 L 755 MET LEU GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL
SEQRES 18 L 755 LYS ARG MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG
SEQRES 19 L 755 SER THR LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR
SEQRES 20 L 755 LYS THR GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN
SEQRES 21 L 755 GLU ASP MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU
SEQRES 22 L 755 ALA ARG TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE
SEQRES 23 L 755 VAL ALA LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN
SEQRES 24 L 755 SER ARG ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU
SEQRES 25 L 755 PHE HIS MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG
SEQRES 26 L 755 GLY THR GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN
SEQRES 27 L 755 THR ALA PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE
SEQRES 28 L 755 ILE ALA GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS
SEQRES 29 L 755 GLY LEU PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR
SEQRES 30 L 755 LYS GLU GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU
SEQRES 31 L 755 GLY PHE SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS
SEQRES 32 L 755 SER SER GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS
SEQRES 33 L 755 PHE ASN LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS
SEQRES 34 L 755 ILE ILE PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO
SEQRES 35 L 755 PHE LEU ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR
SEQRES 36 L 755 ASP GLY SER VAL LEU VAL SER HIS GLY GLY THR GLU MET
SEQRES 37 L 755 GLY GLN GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER
SEQRES 38 L 755 LYS ALA LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER
SEQRES 39 L 755 GLU THR SER THR ASN THR VAL PRO ASN SER SER PRO THR
SEQRES 40 L 755 ALA ALA SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL
SEQRES 41 L 755 TYR GLU ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO
SEQRES 42 L 755 PHE LYS LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP
SEQRES 43 L 755 VAL MET ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR
SEQRES 44 L 755 THR GLY PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE
SEQRES 45 L 755 GLU THR ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR
SEQRES 46 L 755 GLY VAL ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR
SEQRES 47 L 755 GLY ASP HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP
SEQRES 48 L 755 VAL GLY SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN
SEQRES 49 L 755 VAL GLU GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR
SEQRES 50 L 755 LEU GLU GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS
SEQRES 51 L 755 THR ARG GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY
SEQRES 52 L 755 SER ILE PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP
SEQRES 53 L 755 CYS PRO ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL
SEQRES 54 L 755 GLY GLU PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE
SEQRES 55 L 755 ALA ILE LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS
SEQRES 56 L 755 THR ASN ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER
SEQRES 57 L 755 PRO ALA THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP
SEQRES 58 L 755 LYS PHE THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN
SEQRES 59 L 755 CYS
HET FES A 601 4
HET FES A 602 4
HET FAD B 606 53
HET MTE C1326 24
HET MOS C1327 4
HET PM6 C 1 10
HET FES J 601 4
HET FES J 602 4
HET FAD K 606 53
HET MTE L1326 24
HET MOS L1327 4
HET PM6 L 1 10
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 PM6 9H-PURINE-6-THIOL
HETSYN PM6 6-MERCAPTOPURINE
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 PM6 2(C5 H4 N4 S)
FORMUL 19 HOH *287(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 ARG A 161 1 9
HELIX 8 8 THR A 162 ALA A 164 5 3
HELIX 9 9 THR B 241 HIS B 252 1 12
HELIX 10 10 GLU B 263 PHE B 270 1 8
HELIX 11 11 ALA B 304 ALA B 317 1 14
HELIX 12 12 PRO B 320 LYS B 323 5 4
HELIX 13 13 THR B 324 LEU B 334 1 11
HELIX 14 14 GLY B 339 SER B 344 1 6
HELIX 15 15 SER B 347 ALA B 355 1 9
HELIX 16 16 LEU B 361 SER B 368 1 8
HELIX 17 17 ASP B 386 PHE B 390 5 5
HELIX 18 18 ALA B 466 LYS B 472 1 7
HELIX 19 19 ASN B 479 LEU B 494 1 16
HELIX 20 20 MET B 504 LYS B 526 1 23
HELIX 21 21 ALA C 581 SER C 587 1 7
HELIX 22 22 TYR C 592 ILE C 596 5 5
HELIX 23 23 GLU C 624 VAL C 628 5 5
HELIX 24 24 ASP C 638 ILE C 640 5 3
HELIX 25 25 THR C 674 VAL C 684 1 11
HELIX 26 26 THR C 697 ASN C 705 1 9
HELIX 27 27 ASP C 718 ALA C 726 1 9
HELIX 28 28 ASN C 768 GLY C 781 1 14
HELIX 29 29 PRO C 783 ASN C 785 5 3
HELIX 30 30 SER C 805 GLY C 820 1 16
HELIX 31 31 ASP C 828 THR C 836 1 9
HELIX 32 32 LEU C 873 PHE C 883 1 11
HELIX 33 33 GLY C 915 GLY C 935 1 21
HELIX 34 34 PRO C 937 ASN C 945 1 9
HELIX 35 35 SER C 963 SER C 975 1 13
HELIX 36 36 GLN C 976 ASN C 991 1 16
HELIX 37 37 VAL C 1011 LEU C 1014 5 4
HELIX 38 38 GLY C 1041 LYS C 1055 1 15
HELIX 39 39 PRO C 1057 SER C 1059 5 3
HELIX 40 40 VAL C 1081 ASN C 1108 1 28
HELIX 41 41 SER C 1112 ASP C 1123 1 12
HELIX 42 42 ASN C 1187 LEU C 1208 1 22
HELIX 43 43 ALA C 1231 ILE C 1235 5 5
HELIX 44 44 ALA C 1252 SER C 1256 5 5
HELIX 45 45 PRO C 1263 LEU C 1266 5 4
HELIX 46 46 GLY C 1267 THR C 1286 1 20
HELIX 47 47 THR C 1301 CYS C 1309 1 9
HELIX 48 48 LEU C 1316 GLY C 1320 5 5
HELIX 49 49 THR J 25 LYS J 33 1 9
HELIX 50 50 PRO J 76 LEU J 80 5 5
HELIX 51 51 THR J 87 ILE J 91 5 5
HELIX 52 52 HIS J 99 SER J 108 1 10
HELIX 53 53 CYS J 116 GLN J 131 1 16
HELIX 54 54 THR J 135 ALA J 142 1 8
HELIX 55 55 TYR J 153 ARG J 161 1 9
HELIX 56 56 THR J 162 ALA J 164 5 3
HELIX 57 57 THR K 241 HIS K 252 1 12
HELIX 58 58 GLU K 263 PHE K 270 1 8
HELIX 59 59 ALA K 304 ALA K 317 1 14
HELIX 60 60 PRO K 320 LYS K 323 5 4
HELIX 61 61 THR K 324 LEU K 334 1 11
HELIX 62 62 GLY K 339 SER K 344 1 6
HELIX 63 63 SER K 347 ALA K 355 1 9
HELIX 64 64 LEU K 361 SER K 368 1 8
HELIX 65 65 ASP K 386 PHE K 390 5 5
HELIX 66 66 ALA K 466 LYS K 472 1 7
HELIX 67 67 ASN K 479 LEU K 494 1 16
HELIX 68 68 MET K 504 LEU K 527 1 24
HELIX 69 69 ALA L 581 SER L 587 1 7
HELIX 70 70 TYR L 592 ILE L 596 5 5
HELIX 71 71 GLU L 624 VAL L 628 5 5
HELIX 72 72 ASP L 638 ILE L 640 5 3
HELIX 73 73 THR L 674 VAL L 684 1 11
HELIX 74 74 THR L 697 ASN L 704 1 8
HELIX 75 75 ASP L 718 ALA L 726 1 9
HELIX 76 76 ASN L 768 GLY L 781 1 14
HELIX 77 77 PRO L 783 ASN L 785 5 3
HELIX 78 78 SER L 805 GLY L 820 1 16
HELIX 79 79 ASP L 828 THR L 836 1 9
HELIX 80 80 LEU L 873 PHE L 883 1 11
HELIX 81 81 GLY L 915 GLY L 935 1 21
HELIX 82 82 PRO L 937 ASN L 945 1 9
HELIX 83 83 SER L 963 SER L 975 1 13
HELIX 84 84 GLN L 976 ASN L 991 1 16
HELIX 85 85 VAL L 1011 LEU L 1014 5 4
HELIX 86 86 GLY L 1041 LYS L 1055 1 15
HELIX 87 87 PRO L 1057 SER L 1059 5 3
HELIX 88 88 VAL L 1081 ASN L 1108 1 28
HELIX 89 89 SER L 1112 ASP L 1123 1 12
HELIX 90 90 ASN L 1187 THR L 1207 1 21
HELIX 91 91 ALA L 1231 ILE L 1235 5 5
HELIX 92 92 ALA L 1252 SER L 1256 5 5
HELIX 93 93 PRO L 1263 LEU L 1266 5 4
HELIX 94 94 GLY L 1267 THR L 1286 1 20
HELIX 95 95 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 LEU A 6 O GLU A 17
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 TYR A 58 -1 N SER A 56 O ALA A 84
SHEET 5 A 5 ILE A 65 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 TRP B 236 N PHE B 229
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 THR B 373 O SER B 406
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 CYS B 436 N PHE B 421
SHEET 3 D 4 VAL B 449 GLY B 457 -1 O LYS B 450 N LEU B 441
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 SER C 636 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 GLY C 668
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 PHE C 763 N ILE C 750
SHEET 7 E 8 ILE C 787 VAL C 791 1 O LEU C 788 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 5 LEU C 712 LYS C 716 0
SHEET 2 G 5 ILE C 894 LYS C 902 -1 O ILE C 894 N LYS C 716
SHEET 3 G 5 ILE C 856 GLY C 868 1 N VAL C 861 O THR C 897
SHEET 4 G 5 PHE C 842 PHE C 850 -1 N GLY C 849 O VAL C 857
SHEET 5 G 5 ASN C 728 ILE C 736 -1 N LEU C 734 O ALA C 844
SHEET 1 H 4 LYS C 994 ILE C1007 0
SHEET 2 H 4 TYR C1152 ASP C1165 -1 O ALA C1158 N ILE C1001
SHEET 3 H 4 HIS C1171 ASP C1181 -1 O ASP C1181 N TYR C1155
SHEET 4 H 4 GLU C1238 LEU C1243 1 O GLU C1238 N THR C1176
SHEET 1 I 4 ILE C1061 TYR C1062 0
SHEET 2 I 4 VAL C1029 HIS C1033 1 N VAL C1031 O TYR C1062
SHEET 3 I 4 GLN C1016 VAL C1023 -1 N LEU C1020 O SER C1032
SHEET 4 I 4 SER C1128 ARG C1134 -1 O THR C1129 N ILE C1021
SHEET 1 J 5 LYS J 13 GLU J 17 0
SHEET 2 J 5 LEU J 6 VAL J 10 -1 N LEU J 6 O GLU J 17
SHEET 3 J 5 ALA J 84 THR J 86 1 O VAL J 85 N PHE J 9
SHEET 4 J 5 THR J 52 TYR J 58 -1 N SER J 56 O ALA J 84
SHEET 5 J 5 ILE J 65 ASN J 71 -1 O PHE J 68 N LEU J 55
SHEET 1 K 4 LEU K 227 GLU K 230 0
SHEET 2 K 4 THR K 235 GLN K 238 -1 O TRP K 236 N PHE K 229
SHEET 3 K 4 MET K 277 CYS K 280 1 O CYS K 280 N ILE K 237
SHEET 4 K 4 LYS K 256 LEU K 257 1 N LYS K 256 O ILE K 279
SHEET 1 L 5 VAL K 290 HIS K 292 0
SHEET 2 L 5 GLY K 296 GLY K 300 -1 O SER K 298 N GLU K 291
SHEET 3 L 5 ILE K 403 PRO K 410 -1 O ILE K 409 N ILE K 297
SHEET 4 L 5 LYS K 371 VAL K 375 -1 N THR K 373 O SER K 406
SHEET 5 L 5 ARG K 380 PRO K 384 -1 O VAL K 383 N LEU K 372
SHEET 1 M 4 GLU K 416 LYS K 422 0
SHEET 2 M 4 THR K 435 PHE K 442 -1 O CYS K 436 N PHE K 421
SHEET 3 M 4 VAL K 449 GLY K 457 -1 O GLY K 457 N THR K 435
SHEET 4 M 4 ILE K 464 SER K 465 -1 O ILE K 464 N TYR K 456
SHEET 1 N 8 PHE L 631 SER L 636 0
SHEET 2 N 8 ILE L 666 ALA L 672 -1 O ALA L 669 N LEU L 635
SHEET 3 N 8 LEU L 603 THR L 609 -1 N ARG L 606 O VAL L 670
SHEET 4 N 8 VAL L 823 MET L 826 1 O ARG L 824 N LEU L 605
SHEET 5 N 8 CYS L 748 PRO L 753 -1 N ALA L 751 O VAL L 823
SHEET 6 N 8 MET L 760 VAL L 764 -1 O GLU L 761 N ILE L 752
SHEET 7 N 8 ILE L 787 VAL L 791 1 O ARG L 790 N LEU L 762
SHEET 8 N 8 THR L1066 SER L1067 -1 O THR L1066 N VAL L 791
SHEET 1 O 3 THR L 659 VAL L 660 0
SHEET 2 O 3 ALA L 615 ASP L 621 -1 N ALA L 615 O VAL L 660
SHEET 3 O 3 LYS L 686 ASP L 691 -1 O LYS L 686 N ASP L 621
SHEET 1 P 2 GLU L 645 THR L 646 0
SHEET 2 P 2 GLU L 652 THR L 653 -1 O GLU L 652 N THR L 646
SHEET 1 Q 5 LEU L 712 LYS L 716 0
SHEET 2 Q 5 ILE L 894 LYS L 902 -1 O GLY L 896 N ILE L 714
SHEET 3 Q 5 ILE L 856 GLY L 868 1 N VAL L 861 O THR L 897
SHEET 4 Q 5 PHE L 842 PHE L 850 -1 N GLY L 849 O ALA L 858
SHEET 5 Q 5 ASN L 728 ILE L 736 -1 N ILE L 736 O PHE L 842
SHEET 1 R 4 LYS L 994 GLY L1006 0
SHEET 2 R 4 PHE L1153 ASP L1165 -1 O ILE L1164 N LYS L 995
SHEET 3 R 4 HIS L1171 ASP L1181 -1 O ASP L1181 N TYR L1155
SHEET 4 R 4 GLU L1238 LEU L1243 1 O ARG L1240 N ILE L1178
SHEET 1 S 4 ILE L1061 TYR L1062 0
SHEET 2 S 4 VAL L1029 HIS L1033 1 N VAL L1029 O TYR L1062
SHEET 3 S 4 GLN L1016 VAL L1023 -1 N LEU L1020 O SER L1032
SHEET 4 S 4 SER L1128 ARG L1134 -1 O GLY L1131 N ALA L1019
LINK SG CYS A 43 FE2 FES A 602 1555 1555 2.45
LINK SG CYS A 48 FE2 FES A 602 1555 1555 2.18
LINK SG CYS A 51 FE1 FES A 602 1555 1555 2.25
LINK SG CYS A 73 FE1 FES A 602 1555 1555 2.26
LINK SG CYS A 113 FE1 FES A 601 1555 1555 2.41
LINK SG CYS A 116 FE2 FES A 601 1555 1555 2.23
LINK SG CYS A 148 FE2 FES A 601 1555 1555 2.42
LINK SG CYS A 150 FE1 FES A 601 1555 1555 2.39
LINK S1' MTE C1326 MO MOS C1327 1555 1555 2.46
LINK S2' MTE C1326 MO MOS C1327 1555 1555 2.60
LINK SG CYS J 43 FE2 FES J 602 1555 1555 2.42
LINK SG CYS J 48 FE2 FES J 602 1555 1555 2.24
LINK SG CYS J 51 FE1 FES J 602 1555 1555 2.24
LINK SG CYS J 73 FE1 FES J 602 1555 1555 2.32
LINK SG CYS J 113 FE1 FES J 601 1555 1555 2.33
LINK SG CYS J 116 FE2 FES J 601 1555 1555 2.41
LINK SG CYS J 148 FE2 FES J 601 1555 1555 2.48
LINK SG CYS J 150 FE1 FES J 601 1555 1555 2.35
LINK S1' MTE L1326 MO MOS L1327 1555 1555 2.53
LINK S2' MTE L1326 MO MOS L1327 1555 1555 2.58
CISPEP 1 SER C 1298 PRO C 1299 0 -1.57
CISPEP 2 SER L 1298 PRO L 1299 0 0.90
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 9 GLY A 42 CYS A 43 GLY A 44 GLY A 46
SITE 2 AC2 9 GLY A 47 CYS A 48 GLY A 49 CYS A 51
SITE 3 AC2 9 CYS A 73
SITE 1 AC3 23 GLY A 46 HOH B 133 LYS B 256 LEU B 257
SITE 2 AC3 23 VAL B 258 VAL B 259 GLY B 260 ASN B 261
SITE 3 AC3 23 THR B 262 GLU B 263 ILE B 264 ALA B 301
SITE 4 AC3 23 PHE B 337 ALA B 338 ALA B 346 SER B 347
SITE 5 AC3 23 GLY B 350 ASN B 351 ILE B 353 THR B 354
SITE 6 AC3 23 SER B 359 ASP B 360 LEU B 404
SITE 1 AC4 16 GLN A 112 CYS A 150 HOH C 58 GLY C 796
SITE 2 AC4 16 GLY C 797 PHE C 798 ARG C 912 MET C1038
SITE 3 AC4 16 GLY C1039 GLN C1040 ALA C1079 SER C1080
SITE 4 AC4 16 VAL C1081 SER C1082 GLN C1194 MOS C1327
SITE 1 AC5 10 PM6 C 1 GLN C 767 PHE C 798 GLY C 799
SITE 2 AC5 10 PHE C 911 ARG C 912 ALA C1078 ALA C1079
SITE 3 AC5 10 GLU C1261 MTE C1326
SITE 1 AC6 7 GLU C 802 ARG C 880 PHE C 914 PHE C1009
SITE 2 AC6 7 THR C1010 ALA C1079 MOS C1327
SITE 1 AC7 7 GLN J 112 CYS J 113 GLY J 114 CYS J 116
SITE 2 AC7 7 CYS J 148 ARG J 149 CYS J 150
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 21 GLY J 46 HOH K 136 LEU K 257 VAL K 258
SITE 2 AC9 21 VAL K 259 GLY K 260 ASN K 261 THR K 262
SITE 3 AC9 21 GLU K 263 ILE K 264 ALA K 301 PHE K 337
SITE 4 AC9 21 ALA K 338 SER K 347 GLY K 350 ASN K 351
SITE 5 AC9 21 ILE K 353 THR K 354 SER K 359 ASP K 360
SITE 6 AC9 21 LEU K 404
SITE 1 BC1 14 GLN J 112 CYS J 150 GLY L 797 PHE L 798
SITE 2 BC1 14 ARG L 912 MET L1038 GLY L1039 GLN L1040
SITE 3 BC1 14 ALA L1079 SER L1080 VAL L1081 SER L1082
SITE 4 BC1 14 GLN L1194 MOS L1327
SITE 1 BC2 10 PM6 L 1 GLN L 767 GLY L 799 GLU L 802
SITE 2 BC2 10 PHE L 911 ARG L 912 ALA L1078 ALA L1079
SITE 3 BC2 10 GLU L1261 MTE L1326
SITE 1 BC3 7 GLU L 802 ARG L 880 PHE L 914 PHE L1009
SITE 2 BC3 7 THR L1010 ALA L1079 MOS L1327
CRYST1 134.636 73.928 140.353 90.00 97.01 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 0.007427 0.000000 0.000914 0.00000
SCALE2 0.000000 0.013527 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007179 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
