HEADER OXIDOREDUCTASE 08-JUL-10 3NVV
TITLE CRYSTAL STRUCTURE OF BOVINE XANTHINE OXIDASE IN COMPLEX WITH ARSENITE
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, ARSENITE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.CAO,R.HILLE
REVDAT 2 09-MAY-12 3NVV 1 JRNL VERSN
REVDAT 1 19-JAN-11 3NVV 0
JRNL AUTH H.CAO,J.HALL,R.HILLE
JRNL TITL X-RAY CRYSTAL STRUCTURE OF ARSENITE-INHIBITED XANTHINE
JRNL TITL 2 OXIDASE: MU-SULFIDO,MU-OXO DOUBLE BRIDGE BETWEEN MOLYBDENUM
JRNL TITL 3 AND ARSENIC IN THE ACTIVE SITE.
JRNL REF J.AM.CHEM.SOC. V. 133 12414 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 21761899
JRNL DOI 10.1021/JA2050265
REMARK 2
REMARK 2 RESOLUTION. 1.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 131.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 228736
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) : 0.193
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11464
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) : 1.82
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15654
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 755
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19113
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 184
REMARK 3 SOLVENT ATOMS : 1374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.59
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.96000
REMARK 3 B22 (A**2) : 0.65000
REMARK 3 B33 (A**2) : 1.24000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.27000
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): 0.132
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.027
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 19715 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 26692 ; 1.399 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2461 ; 6.104 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 827 ;37.669 ;23.821
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3377 ;14.541 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 119 ;17.307 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2990 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 14722 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 9700 ; 0.204 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 13518 ; 0.307 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1440 ; 0.139 ; 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): 53 ; 0.227 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.296 ; 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): 12609 ; 0.774 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 19777 ; 1.204 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8103 ; 1.976 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6907 ; 3.084 ; 4.500
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 3NVV 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 RCSB ID CODE IS RCSB060343.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-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 : 228736
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.820
REMARK 200 RESOLUTION RANGE LOW (A) : 131.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
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) : 1.82
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
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 : 16.900
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 (%): 49.06
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 36.70900
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: 33510 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 80670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -234.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, L, J, K
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 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 AS AST L 1 O1 MOS L 1327 1.94
REMARK 500 O1 MOS C 1327 AS AST C 1 1.97
REMARK 500 OE1 GLU C 924 NH1 ARG C 942 1.97
REMARK 500 NH2 ARG K 439 OE1 GLU K 451 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 NH2 ARG C 958 O HOH L 1506 2655 1.88
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 C 829 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG C 829 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 LEU C1203 CA - CB - CG ANGL. DEV. = 18.2 DEGREES
REMARK 500 ARG L 829 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG L 829 NE - CZ - NH2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 LEU L1203 CA - CB - CG ANGL. DEV. = 15.1 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 -28.39 -160.76
REMARK 500 THR A 96 -92.40 -115.71
REMARK 500 GLN A 112 -88.31 -108.12
REMARK 500 TYR A 153 -35.99 70.90
REMARK 500 PRO B 210 129.02 -38.99
REMARK 500 VAL B 259 -80.85 -113.90
REMARK 500 TRP B 336 69.30 -115.98
REMARK 500 ALA B 338 -147.93 55.69
REMARK 500 ARG B 377 109.75 -58.90
REMARK 500 ALA B 424 46.78 -101.51
REMARK 500 ASP B 430 28.16 -144.84
REMARK 500 ALA B 460 -172.84 -173.17
REMARK 500 SER B 475 -9.27 75.32
REMARK 500 VAL C 632 -62.20 -105.34
REMARK 500 LYS C 657 -66.00 -101.32
REMARK 500 THR C 803 -34.04 -137.10
REMARK 500 ASP C 872 -133.26 50.32
REMARK 500 ASN C 887 -115.77 37.40
REMARK 500 ARG C 912 104.89 -9.11
REMARK 500 SER C1008 156.26 150.22
REMARK 500 SER C1080 9.81 56.59
REMARK 500 ASN C1187 95.52 -163.38
REMARK 500 ASN C1287 -167.73 -160.05
REMARK 500 CYS J 43 -27.57 -162.80
REMARK 500 THR J 96 -86.86 -116.94
REMARK 500 HIS J 109 32.03 70.46
REMARK 500 GLN J 112 -86.01 -106.57
REMARK 500 TYR J 153 -36.29 69.59
REMARK 500 VAL K 259 -78.35 -113.75
REMARK 500 TRP K 336 67.33 -108.97
REMARK 500 ALA K 338 -167.69 57.47
REMARK 500 ARG K 394 19.77 59.18
REMARK 500 ALA K 424 55.85 -105.56
REMARK 500 ASP K 430 32.41 -140.84
REMARK 500 HIS L 614 113.96 -164.06
REMARK 500 VAL L 632 -61.39 -103.56
REMARK 500 LYS L 657 -65.86 -97.52
REMARK 500 THR L 803 -34.98 -136.96
REMARK 500 ASP L 872 -130.02 45.78
REMARK 500 ASN L 887 -118.20 38.17
REMARK 500 ARG L 912 103.30 -10.22
REMARK 500 TYR L 947 157.98 -49.76
REMARK 500 SER L1008 152.85 151.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1237 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH B2166 DISTANCE = 5.18 ANGSTROMS
REMARK 525 HOH C2105 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH C2118 DISTANCE = 5.58 ANGSTROMS
REMARK 525 HOH C2167 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH J2060 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH K2084 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH L1637 DISTANCE = 6.47 ANGSTROMS
REMARK 525 HOH L2145 DISTANCE = 5.68 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 AST C 1
REMARK 610 AST L 1
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 J 601 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 116 SG
REMARK 620 2 FES J 601 S1 114.5
REMARK 620 3 FES J 601 S2 115.3 107.3
REMARK 620 4 CYS J 148 SG 101.9 107.7 109.7
REMARK 620 N 1 2 3
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 48 SG
REMARK 620 2 FES A 602 S1 116.9
REMARK 620 3 FES A 602 S2 111.0 101.2
REMARK 620 4 CYS A 43 SG 108.8 101.3 117.4
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 73 SG
REMARK 620 2 FES J 602 S1 111.2
REMARK 620 3 FES J 602 S2 111.4 100.1
REMARK 620 4 CYS J 51 SG 106.6 109.3 118.3
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 150 SG
REMARK 620 2 FES J 601 S1 112.5
REMARK 620 3 FES J 601 S2 116.4 106.0
REMARK 620 4 CYS J 113 SG 97.4 118.3 106.5
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 114.1
REMARK 620 3 FES A 601 S2 113.9 105.2
REMARK 620 4 CYS A 148 SG 101.8 109.1 112.9
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 109.9
REMARK 620 3 FES A 602 S2 113.4 102.3
REMARK 620 4 CYS A 73 SG 109.1 112.9 109.1
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 S2'
REMARK 620 2 MOS C1327 S 139.2
REMARK 620 3 MOS C1327 O1 80.6 88.4
REMARK 620 4 MOS C1327 O2 122.2 97.9 96.6
REMARK 620 5 MTE C1326 S1' 80.5 93.2 152.8 110.1
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 103.0
REMARK 620 3 FES J 602 S2 115.0 100.3
REMARK 620 4 CYS J 48 SG 109.5 115.7 112.8
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 150 SG
REMARK 620 2 FES A 601 S1 110.6
REMARK 620 3 FES A 601 S2 116.4 102.8
REMARK 620 4 CYS A 113 SG 98.3 119.8 109.8
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 94.7
REMARK 620 3 MOS L1327 O1 157.4 87.2
REMARK 620 4 MOS L1327 O2 104.9 103.1 96.5
REMARK 620 5 MTE L1326 S2' 83.2 141.0 81.3 115.1
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 AST 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 AST L 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE L 1326
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS L 1327
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NVW RELATED DB: PDB
REMARK 900 RELATED ID: 3NVY RELATED DB: PDB
REMARK 900 RELATED ID: 3NVZ RELATED DB: PDB
DBREF 3NVV A 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NVV B 195 528 UNP P80457 XDH_BOVIN 195 528
DBREF 3NVV C 571 1325 UNP P80457 XDH_BOVIN 571 1325
DBREF 3NVV J 2 165 UNP P80457 XDH_BOVIN 2 165
DBREF 3NVV K 195 528 UNP P80457 XDH_BOVIN 195 528
DBREF 3NVV 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 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 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 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 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 AST C 1 3
HET FES J 601 4
HET FES J 602 4
HET FAD K 606 53
HET AST L 1 3
HET MTE L1326 24
HET MOS L1327 4
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 AST ARSENITE
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 AST 2(AS O3 3-)
FORMUL 19 HOH *1374(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 ARG B 335 1 12
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 MET C 885 1 13
HELIX 36 36 GLY C 915 GLY C 935 1 21
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 ALA J 142 1 8
HELIX 58 58 TYR J 153 ARG J 161 1 9
HELIX 59 59 THR J 162 ALA J 164 5 3
HELIX 60 60 THR K 241 HIS K 252 1 12
HELIX 61 61 GLU K 263 LYS K 271 1 9
HELIX 62 62 ILE K 284 ASN K 288 5 5
HELIX 63 63 ALA K 304 LEU K 319 1 16
HELIX 64 64 PRO K 320 LYS K 323 5 4
HELIX 65 65 THR K 324 ARG K 335 1 12
HELIX 66 66 GLY K 339 ALA K 346 1 8
HELIX 67 67 SER K 347 ALA K 355 1 9
HELIX 68 68 LEU K 361 GLY K 369 1 9
HELIX 69 69 ASP K 386 PHE K 390 5 5
HELIX 70 70 ALA K 466 LYS K 472 1 7
HELIX 71 71 ASN K 479 LEU K 494 1 16
HELIX 72 72 MET K 504 GLY K 528 1 25
HELIX 73 73 ALA L 581 SER L 587 1 7
HELIX 74 74 TYR L 592 ILE L 596 5 5
HELIX 75 75 GLU L 624 VAL L 628 5 5
HELIX 76 76 SER L 636 ILE L 640 5 5
HELIX 77 77 THR L 674 VAL L 684 1 11
HELIX 78 78 THR L 697 ASN L 704 1 8
HELIX 79 79 ASP L 718 ALA L 726 1 9
HELIX 80 80 ASN L 768 GLY L 781 1 14
HELIX 81 81 PRO L 783 ASN L 785 5 3
HELIX 82 82 SER L 805 GLY L 820 1 16
HELIX 83 83 ASP L 828 THR L 836 1 9
HELIX 84 84 LEU L 873 HIS L 884 1 12
HELIX 85 85 GLY L 915 GLY L 935 1 21
HELIX 86 86 PRO L 937 MET L 946 1 10
HELIX 87 87 SER L 963 GLN L 976 1 14
HELIX 88 88 GLN L 976 ASN L 991 1 16
HELIX 89 89 VAL L 1011 LEU L 1014 5 4
HELIX 90 90 GLY L 1041 LYS L 1055 1 15
HELIX 91 91 PRO L 1057 SER L 1059 5 3
HELIX 92 92 VAL L 1081 ASN L 1108 1 28
HELIX 93 93 SER L 1112 ASP L 1123 1 12
HELIX 94 94 ASN L 1187 LEU L 1208 1 22
HELIX 95 95 ALA L 1231 ILE L 1235 5 5
HELIX 96 96 ALA L 1252 SER L 1256 5 5
HELIX 97 97 PRO L 1263 LEU L 1266 5 4
HELIX 98 98 GLY L 1267 THR L 1286 1 20
HELIX 99 99 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 ASP A 59 -1 N SER A 56 O ALA A 84
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 TRP B 236 N PHE B 229
SHEET 3 B 4 MET B 277 CYS B 280 1 O ILE B 278 N THR B 235
SHEET 4 B 4 LYS B 256 LEU B 257 1 N LYS B 256 O MET B 277
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 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 THR C 688 N LYS C 618
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 896 N ILE C 714
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 ASN C 728 O PHE C 850
SHEET 1 I 4 LYS C 994 ILE C1007 0
SHEET 2 I 4 TYR C1152 ASP C1165 -1 O ILE C1164 N LYS C 995
SHEET 3 I 4 HIS C1171 ASP C1181 -1 O ASP C1181 N TYR C1155
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 ASP J 59 -1 N SER J 56 O ALA J 84
SHEET 5 K 5 LYS J 64 ASN J 71 -1 O LYS J 64 N ASP J 59
SHEET 1 L 4 LEU K 227 GLU K 230 0
SHEET 2 L 4 THR K 235 GLN K 238 -1 O TRP K 236 N PHE K 229
SHEET 3 L 4 MET K 277 CYS K 280 1 O ILE K 278 N THR K 235
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 407 N PHE K 299
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 LYS K 450 N LEU K 441
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 VAL L 608 O GLY L 668
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 ILE L 894 N LYS L 716
SHEET 3 R 5 ILE L 856 GLY L 868 1 N SER L 865 O CYS L 901
SHEET 4 R 5 PHE L 842 PHE L 850 -1 N GLY L 849 O ALA L 858
SHEET 5 R 5 ASN L 728 ILE L 736 -1 N LEU L 734 O ALA L 844
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 ASP L1181 N TYR L1155
SHEET 4 S 4 GLU L1238 LEU L1243 1 O ARG L1240 N ILE L1178
SHEET 1 T 4 ILE L1061 TYR L1062 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
SSBOND 1 CYS C 1317 CYS C 1325 1555 1555 2.02
LINK SG CYS J 116 FE2 FES J 601 1555 1555 2.22
LINK SG CYS A 48 FE2 FES A 602 1555 1555 2.24
LINK SG CYS J 73 FE1 FES J 602 1555 1555 2.24
LINK SG CYS J 51 FE1 FES J 602 1555 1555 2.24
LINK SG CYS J 150 FE1 FES J 601 1555 1555 2.25
LINK SG CYS A 116 FE2 FES A 601 1555 1555 2.26
LINK SG CYS A 51 FE1 FES A 602 1555 1555 2.26
LINK SG CYS A 73 FE1 FES A 602 1555 1555 2.29
LINK S2' MTE C1326 MO MOS C1327 1555 1555 2.32
LINK SG CYS J 43 FE2 FES J 602 1555 1555 2.32
LINK SG CYS J 48 FE2 FES J 602 1555 1555 2.33
LINK SG CYS A 150 FE1 FES A 601 1555 1555 2.35
LINK S1' MTE C1326 MO MOS C1327 1555 1555 2.36
LINK S1' MTE L1326 MO MOS L1327 1555 1555 2.36
LINK SG CYS A 113 FE1 FES A 601 1555 1555 2.39
LINK SG CYS J 113 FE1 FES J 601 1555 1555 2.39
LINK SG CYS J 148 FE2 FES J 601 1555 1555 2.41
LINK S2' MTE L1326 MO MOS L1327 1555 1555 2.41
LINK SG CYS A 43 FE2 FES A 602 1555 1555 2.44
LINK SG CYS A 148 FE2 FES A 601 1555 1555 2.48
CISPEP 1 SER C 1298 PRO C 1299 0 0.40
CISPEP 2 ALA J 164 LYS J 165 0 -1.27
CISPEP 3 SER L 1298 PRO L 1299 0 2.59
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 540
SITE 7 AC3 29 HOH B 546 HOH B 559 HOH B 672 HOH B1281
SITE 8 AC3 29 HOH B1345
SITE 1 AC4 16 GLN A 112 CYS A 150 HOH C 247 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 9 AST C 1 GLN C 767 GLY C 799 PHE C 911
SITE 2 AC5 9 ARG C 912 ALA C1078 ALA C1079 GLU C1261
SITE 3 AC5 9 MTE C1326
SITE 1 AC6 7 HOH C 306 GLU C 802 PHE C 914 ALA C1078
SITE 2 AC6 7 ALA C1079 GLU C1261 MOS C1327
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 541 HOH K 719
SITE 7 AC9 26 HOH K1176 HOH K1514
SITE 1 BC1 6 GLU L 802 PHE L 914 ALA L1079 GLU L1261
SITE 2 BC1 6 MOS L1327 HOH L1499
SITE 1 BC2 19 GLN J 112 CYS J 150 HOH L 154 GLY L 796
SITE 2 BC2 19 GLY L 797 PHE L 798 GLY L 799 ARG L 912
SITE 3 BC2 19 MET L1038 GLY L1039 GLN L1040 ALA L1079
SITE 4 BC2 19 SER L1080 VAL L1081 SER L1082 GLN L1194
SITE 5 BC2 19 MOS L1327 HOH L1340 HOH L1408
SITE 1 BC3 9 AST L 1 GLN L 767 GLY L 799 PHE L 911
SITE 2 BC3 9 ARG L 912 ALA L1078 ALA L1079 GLU L1261
SITE 3 BC3 9 MTE L1326
CRYST1 132.766 73.418 138.158 90.00 96.93 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 0.007532 0.000000 0.000916 0.00000
SCALE2 0.000000 0.013621 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007291 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
