HEADER OXIDOREDUCTASE 18-AUG-10 3AM9
TITLE COMPLEX OF BOVINE XANTHINE DEHYDROGENASE AND TRIHYDROXY FYX-051
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XANTHINE DEHYDROGENASE/OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: XANTHINE OXIDOREDUCTASE, XANTHINE DEHYDROGENASE, XD,
COMPND 5 XANTHINE OXIDASE, XO;
COMPND 6 EC: 1.17.1.4, 1.17.3.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS XANTHINE OXIDOREDUCTASE, XANTHINE DEHYDROGENASE, FYX-051,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.MATSUMOTO,K.OKAMOTO,N.ASHIZAWA,T.MATSUMURA,T.KUSANO,T.NISHINO
REVDAT 3 01-NOV-23 3AM9 1 REMARK LINK
REVDAT 2 29-DEC-10 3AM9 1 JRNL
REVDAT 1 03-NOV-10 3AM9 0
JRNL AUTH K.MATSUMOTO,K.OKAMOTO,N.ASHIZAWA,T.NISHINO
JRNL TITL FYX-051: A NOVEL AND POTENT HYBRID-TYPE INHIBITOR OF
JRNL TITL 2 XANTHINE OXIDOREDUCTASE
JRNL REF J.PHARMACOL.EXP.THER. V. 336 95 2011
JRNL REFN ISSN 0022-3565
JRNL PMID 20952484
JRNL DOI 10.1124/JPET.110.174540
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.5
REMARK 3 NUMBER OF REFLECTIONS : 144234
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7582
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) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8866
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 437
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20068
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 244
REMARK 3 SOLVENT ATOMS : 1914
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
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): 0.214
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.502
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20764 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 28140 ; 2.099 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16 ; 1.973 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2576 ; 6.951 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 870 ;37.611 ;23.908
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3546 ;16.459 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 122 ;18.760 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3136 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 15556 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 12861 ; 1.051 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 20774 ; 1.831 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7903 ; 3.136 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 7358 ; 4.787 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3AM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000029424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 144234
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 33.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.31000
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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1FO4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30%(WT/VOL) GLYCEROL, 50MM POTASSIUM
REMARK 280 PHOSPHATE BUFFER (PH 6.5) CONTAINING 8.0-9.5% POLYETHYLENE
REMARK 280 GLYCOL 4000, 30% (WT/VOL) GLYCEROL, 0.2MM EDTA, 5MM DTT , VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K, PH 7.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 84.45800
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.36100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.45800
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.36100
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 88790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 ASN A 166
REMARK 465 GLY A 167
REMARK 465 GLY A 168
REMARK 465 CYS A 169
REMARK 465 CYS A 170
REMARK 465 GLY A 171
REMARK 465 GLY A 172
REMARK 465 ASN A 173
REMARK 465 GLY A 174
REMARK 465 ASN A 175
REMARK 465 ASN A 176
REMARK 465 PRO A 177
REMARK 465 ASN A 178
REMARK 465 CYS A 179
REMARK 465 CYS A 180
REMARK 465 MET A 181
REMARK 465 ASN A 182
REMARK 465 GLN A 183
REMARK 465 LYS A 184
REMARK 465 LYS A 185
REMARK 465 ASP A 186
REMARK 465 HIS A 187
REMARK 465 THR A 188
REMARK 465 VAL A 189
REMARK 465 THR A 190
REMARK 465 LEU A 191
REMARK 465 SER A 531
REMARK 465 LYS A 532
REMARK 465 ASP A 533
REMARK 465 LYS A 534
REMARK 465 CYS A 535
REMARK 465 GLY A 536
REMARK 465 ALA A 1321
REMARK 465 PRO A 1322
REMARK 465 GLY A 1323
REMARK 465 ASN A 1324
REMARK 465 CYS A 1325
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 166
REMARK 465 GLY B 167
REMARK 465 GLY B 168
REMARK 465 CYS B 169
REMARK 465 CYS B 170
REMARK 465 GLY B 171
REMARK 465 GLY B 172
REMARK 465 ASN B 173
REMARK 465 GLY B 174
REMARK 465 ASN B 175
REMARK 465 ASN B 176
REMARK 465 PRO B 177
REMARK 465 ASN B 178
REMARK 465 CYS B 179
REMARK 465 CYS B 180
REMARK 465 MET B 181
REMARK 465 ASN B 182
REMARK 465 GLN B 183
REMARK 465 LYS B 184
REMARK 465 LYS B 185
REMARK 465 ASP B 186
REMARK 465 HIS B 187
REMARK 465 THR B 188
REMARK 465 VAL B 189
REMARK 465 THR B 190
REMARK 465 LEU B 191
REMARK 465 LYS B 529
REMARK 465 ASP B 530
REMARK 465 SER B 531
REMARK 465 LYS B 532
REMARK 465 ASP B 533
REMARK 465 LYS B 534
REMARK 465 CYS B 535
REMARK 465 GLY B 536
REMARK 465 THR B 1319
REMARK 465 GLY B 1320
REMARK 465 ALA B 1321
REMARK 465 PRO B 1322
REMARK 465 GLY B 1323
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 SD MET A 504 O HOH A 1779 2.09
REMARK 500 NH1 ARG B 129 O HOH B 1669 2.09
REMARK 500 OH TYR A 58 OD1 ASP A 63 2.16
REMARK 500 O HOH A 1821 O HOH A 1952 2.16
REMARK 500 OE1 GLU A 802 NAN FYO A 1335 2.19
REMARK 500 O HOH A 1465 O HOH A 2261 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 137 CG GLU A 137 CD 0.098
REMARK 500 GLU A 506 CG GLU A 506 CD 0.094
REMARK 500 SER A 774 CB SER A 774 OG -0.079
REMARK 500 GLU A 983 CG GLU A 983 CD 0.109
REMARK 500 CYS A 992 CB CYS A 992 SG -0.152
REMARK 500 GLU B 45 CB GLU B 45 CG -0.125
REMARK 500 TYR B1227 CD1 TYR B1227 CE1 -0.092
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 LEU A 61 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 154 NE - CZ - NH2 ANGL. DEV. = -7.5 DEGREES
REMARK 500 SER A 412 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 ASP A 651 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 651 CB - CG - OD2 ANGL. DEV. = -8.0 DEGREES
REMARK 500 LEU A 719 CB - CG - CD1 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ARG A 793 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 793 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 829 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 829 NE - CZ - NH2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 LEU A1203 CA - CB - CG ANGL. DEV. = 19.2 DEGREES
REMARK 500 ASP B 4 CB - CG - OD1 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ASP B 4 N - CA - C ANGL. DEV. = 23.6 DEGREES
REMARK 500 ARG B 154 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 154 NE - CZ - NH2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG B 427 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 427 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 LEU B 719 CB - CG - CD1 ANGL. DEV. = -11.2 DEGREES
REMARK 500 ARG B 845 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 980 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG B 980 NE - CZ - NH2 ANGL. DEV. = -3.6 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 ASP A 4 -41.80 -26.63
REMARK 500 CYS A 43 -32.46 -157.86
REMARK 500 LEU A 61 -34.20 177.92
REMARK 500 THR A 96 -92.49 -117.36
REMARK 500 GLN A 112 -86.01 -113.41
REMARK 500 TYR A 153 -41.55 78.07
REMARK 500 VAL A 259 -79.37 -115.04
REMARK 500 ALA A 338 -143.44 47.37
REMARK 500 TYR A 393 108.43 -42.47
REMARK 500 LEU A 397 47.32 -79.72
REMARK 500 ALA A 424 -151.78 -123.18
REMARK 500 ASP A 429 60.25 36.47
REMARK 500 ALA A 460 -177.10 -174.73
REMARK 500 SER A 475 -14.94 71.57
REMARK 500 LEU A 494 59.80 -104.66
REMARK 500 LYS A 529 -111.66 64.71
REMARK 500 ASP A 539 73.80 -164.55
REMARK 500 THR A 541 -39.53 95.30
REMARK 500 ASN A 565 -48.40 -18.18
REMARK 500 HIS A 579 130.42 -37.39
REMARK 500 HIS A 614 109.58 -160.96
REMARK 500 ASP A 658 -55.62 76.82
REMARK 500 PHE A 742 45.01 38.49
REMARK 500 THR A 803 -29.62 -140.13
REMARK 500 ASP A 872 -130.38 46.15
REMARK 500 ASN A 887 -116.79 40.18
REMARK 500 ARG A 912 111.92 -19.43
REMARK 500 TYR A 947 159.22 -44.57
REMARK 500 GLU A 949 108.83 -33.66
REMARK 500 SER A1008 161.98 162.12
REMARK 500 GLU A1065 -176.03 -174.09
REMARK 500 SER A1080 12.66 57.48
REMARK 500 ASN A1145 60.83 30.24
REMARK 500 THR A1207 -14.25 -143.31
REMARK 500 TYR A1254 27.76 48.57
REMARK 500 THR A1319 97.47 5.86
REMARK 500 SER A1329 42.68 137.60
REMARK 500 ASP B 4 162.91 25.81
REMARK 500 ASN B 19 -113.45 -103.18
REMARK 500 ALA B 20 106.77 111.76
REMARK 500 CYS B 43 -25.49 -151.92
REMARK 500 LEU B 61 28.26 -72.75
REMARK 500 GLN B 62 -8.90 -171.21
REMARK 500 THR B 96 -92.73 -116.10
REMARK 500 GLN B 112 -84.01 -113.08
REMARK 500 TYR B 153 -38.92 74.32
REMARK 500 VAL B 259 -75.20 -117.74
REMARK 500 ALA B 338 -147.18 61.95
REMARK 500 ARG B 380 114.37 -161.47
REMARK 500 LEU B 397 15.78 -66.14
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 THE LIGAND FYO(TRIHYDROXY FYX-051) IS METAL-COORDINATED TO MO
REMARK 600 COMPOUND MOS, MOLYBDPOTERIN. IT WAS CHEMICALLY SYNTHESIZED.
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 A3002 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 FES A3002 S1 103.1
REMARK 620 3 FES A3002 S2 119.4 99.4
REMARK 620 4 CYS A 48 SG 105.9 116.6 112.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3002 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 51 SG
REMARK 620 2 FES A3002 S1 110.9
REMARK 620 3 FES A3002 S2 111.8 103.7
REMARK 620 4 CYS A 73 SG 99.4 120.3 111.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3001 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 113 SG
REMARK 620 2 FES A3001 S1 120.5
REMARK 620 3 FES A3001 S2 108.2 102.7
REMARK 620 4 CYS A 150 SG 96.1 112.0 118.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3001 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 116 SG
REMARK 620 2 FES A3001 S1 109.9
REMARK 620 3 FES A3001 S2 114.1 105.3
REMARK 620 4 CYS A 148 SG 106.7 106.4 114.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1336 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR A 743 OH
REMARK 620 2 THR A 836 OG1 76.8
REMARK 620 3 GLY A 837 O 173.2 98.4
REMARK 620 4 HOH A2311 O 86.2 83.4 88.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A3008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA A 867 O
REMARK 620 2 SER A 870 O 83.0
REMARK 620 3 ARG A 871 O 142.7 76.5
REMARK 620 4 SER A 874 OG 104.2 108.7 55.5
REMARK 620 5 SER A 907 OG 89.0 68.9 111.5 166.3
REMARK 620 6 ASN A 908 O 100.3 154.7 111.5 94.9 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS A1334 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE A1333 S2'
REMARK 620 2 MOS A1334 S 138.1
REMARK 620 3 MOS A1334 O1 115.6 106.3
REMARK 620 4 MTE A1333 S1' 83.2 87.4 102.8
REMARK 620 5 FYO A1335 NAA 83.9 80.4 112.6 144.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B4002 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 43 SG
REMARK 620 2 FES B4002 S1 102.3
REMARK 620 3 FES B4002 S2 121.0 99.9
REMARK 620 4 CYS B 48 SG 105.5 117.1 111.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B4002 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 51 SG
REMARK 620 2 FES B4002 S1 111.2
REMARK 620 3 FES B4002 S2 113.8 104.8
REMARK 620 4 CYS B 73 SG 102.6 114.1 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B4001 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 113 SG
REMARK 620 2 FES B4001 S1 118.7
REMARK 620 3 FES B4001 S2 109.6 103.3
REMARK 620 4 CYS B 150 SG 100.2 110.2 115.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B4001 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 116 SG
REMARK 620 2 FES B4001 S1 114.6
REMARK 620 3 FES B4001 S2 115.8 104.4
REMARK 620 4 CYS B 148 SG 103.3 108.9 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1337 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TYR B 743 OH
REMARK 620 2 THR B 836 OG1 78.5
REMARK 620 3 GLY B 837 O 170.7 95.5
REMARK 620 4 HOH B2257 O 87.2 79.7 84.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B4008 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ALA B 867 O
REMARK 620 2 SER B 870 O 82.8
REMARK 620 3 ARG B 871 O 146.1 76.9
REMARK 620 4 SER B 874 OG 101.6 114.1 63.9
REMARK 620 5 SER B 907 OG 88.0 66.0 107.4 170.3
REMARK 620 6 ASN B 908 O 99.5 151.7 111.3 93.2 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS B1334 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE B1333 S2'
REMARK 620 2 MOS B1334 S 142.7
REMARK 620 3 MOS B1334 O1 108.6 108.7
REMARK 620 4 MTE B1333 S1' 81.8 90.8 102.8
REMARK 620 5 FYO B1335 NAA 88.7 78.3 109.5 147.6
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 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE A 1333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS A 1334
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FYO A 1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1336
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4008
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 4005
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT B 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE B 1333
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS B 1334
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FYO B 1335
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1336
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1337
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1338
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AMZ RELATED DB: PDB
REMARK 900 BOVINE XANTHINE OXIDOREDUCTASE URATE BOUND FORM
REMARK 900 RELATED ID: 3AN1 RELATED DB: PDB
REMARK 900 RAT D428A MUTANT, URATE BOUND FORM
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS A SEQUENCE CONFLICT AT THIS POSITION. THE USING DATABASE
REMARK 999 REFERENCE SEQUENCE REFERS REF 1 OF P80457.
DBREF 3AM9 A 1 1332 UNP P80457 XDH_BOVIN 1 1332
DBREF 3AM9 B 1 1332 UNP P80457 XDH_BOVIN 1 1332
SEQRES 1 A 1332 MET THR ALA ASP GLU LEU VAL PHE PHE VAL ASN GLY LYS
SEQRES 2 A 1332 LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU
SEQRES 3 A 1332 LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU ARG GLY THR
SEQRES 4 A 1332 LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR
SEQRES 5 A 1332 VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASP LYS ILE
SEQRES 6 A 1332 ILE HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS
SEQRES 7 A 1332 THR LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE
SEQRES 8 A 1332 GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG
SEQRES 9 A 1332 ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR
SEQRES 10 A 1332 PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN
SEQRES 11 A 1332 GLN PRO GLU PRO THR VAL GLU GLU ILE GLU ASP ALA PHE
SEQRES 12 A 1332 GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE
SEQRES 13 A 1332 LEU GLN GLY PHE ARG THR PHE ALA LYS ASN GLY GLY CYS
SEQRES 14 A 1332 CYS GLY GLY ASN GLY ASN ASN PRO ASN CYS CYS MET ASN
SEQRES 15 A 1332 GLN LYS LYS ASP HIS THR VAL THR LEU SER PRO SER LEU
SEQRES 16 A 1332 PHE ASN PRO GLU GLU PHE MET PRO LEU ASP PRO THR GLN
SEQRES 17 A 1332 GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP
SEQRES 18 A 1332 VAL PRO PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL
SEQRES 19 A 1332 THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP
SEQRES 20 A 1332 LEU LYS ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL GLY
SEQRES 21 A 1332 ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN GLN
SEQRES 22 A 1332 LEU PHE PRO MET ILE ILE CYS PRO ALA TRP ILE PRO GLU
SEQRES 23 A 1332 LEU ASN ALA VAL GLU HIS GLY PRO GLU GLY ILE SER PHE
SEQRES 24 A 1332 GLY ALA ALA CYS ALA LEU SER SER VAL GLU LYS THR LEU
SEQRES 25 A 1332 LEU GLU ALA VAL ALA LYS LEU PRO THR GLN LYS THR GLU
SEQRES 26 A 1332 VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA
SEQRES 27 A 1332 GLY LYS GLN VAL LYS SER VAL ALA SER LEU GLY GLY ASN
SEQRES 28 A 1332 ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL
SEQRES 29 A 1332 PHE MET ALA SER GLY THR LYS LEU THR ILE VAL SER ARG
SEQRES 30 A 1332 GLY THR ARG ARG THR VAL PRO MET ASP HIS THR PHE PHE
SEQRES 31 A 1332 PRO SER TYR ARG LYS THR LEU LEU GLY PRO GLU GLU ILE
SEQRES 32 A 1332 LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU ASP GLU
SEQRES 33 A 1332 PHE PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP
SEQRES 34 A 1332 ASP ILE ALA LYS VAL THR CYS GLY MET ARG VAL LEU PHE
SEQRES 35 A 1332 GLN PRO GLY SER MET GLN VAL LYS GLU LEU ALA LEU CYS
SEQRES 36 A 1332 TYR GLY GLY MET ALA ASP ARG THR ILE SER ALA LEU LYS
SEQRES 37 A 1332 THR THR GLN LYS GLN LEU SER LYS PHE TRP ASN GLU LYS
SEQRES 38 A 1332 LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU
SEQRES 39 A 1332 SER LEU SER PRO ASP ALA PRO GLY GLY MET ILE GLU PHE
SEQRES 40 A 1332 ARG ARG THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR
SEQRES 41 A 1332 LEU THR VAL LEU LYS LYS LEU GLY LYS ASP SER LYS ASP
SEQRES 42 A 1332 LYS CYS GLY LYS LEU ASP PRO THR TYR THR SER ALA THR
SEQRES 43 A 1332 LEU LEU PHE GLN LYS HIS PRO PRO ALA ASN ILE GLN LEU
SEQRES 44 A 1332 PHE GLN GLU VAL PRO ASN GLY GLN SER LYS GLU ASP THR
SEQRES 45 A 1332 VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA MET GLN
SEQRES 46 A 1332 ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO ARG
SEQRES 47 A 1332 TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR SER THR
SEQRES 48 A 1332 ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL SER GLU
SEQRES 49 A 1332 ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU SER ALA
SEQRES 50 A 1332 ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU PHE ASN
SEQRES 51 A 1332 ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR CYS VAL
SEQRES 52 A 1332 GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO GLU
SEQRES 53 A 1332 HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL THR TYR
SEQRES 54 A 1332 GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP ALA ILE
SEQRES 55 A 1332 LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS ILE GLU
SEQRES 56 A 1332 LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP ASN
SEQRES 57 A 1332 VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN ASP HIS
SEQRES 58 A 1332 PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE PRO LYS
SEQRES 59 A 1332 GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER THR GLN
SEQRES 60 A 1332 ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS MET LEU
SEQRES 61 A 1332 GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL LYS ARG
SEQRES 62 A 1332 MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG SER THR
SEQRES 63 A 1332 LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR LYS THR
SEQRES 64 A 1332 GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN GLU ASP
SEQRES 65 A 1332 MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA ARG
SEQRES 66 A 1332 TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE VAL ALA
SEQRES 67 A 1332 LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN SER ARG
SEQRES 68 A 1332 ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU PHE HIS
SEQRES 69 A 1332 MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY THR
SEQRES 70 A 1332 GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN THR ALA
SEQRES 71 A 1332 PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE ILE ALA
SEQRES 72 A 1332 GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS GLY LEU
SEQRES 73 A 1332 PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR LYS GLU
SEQRES 74 A 1332 GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU GLY PHE
SEQRES 75 A 1332 SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS SER SER
SEQRES 76 A 1332 GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS PHE ASN
SEQRES 77 A 1332 LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE ILE
SEQRES 78 A 1332 PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE LEU
SEQRES 79 A 1332 ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR ASP GLY
SEQRES 80 A 1332 SER VAL LEU VAL SER HIS GLY GLY THR GLU MET GLY GLN
SEQRES 81 A 1332 GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER LYS ALA
SEQRES 82 A 1332 LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER GLU THR
SEQRES 83 A 1332 SER THR ASN THR VAL PRO ASN SER SER PRO THR ALA ALA
SEQRES 84 A 1332 SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL TYR GLU
SEQRES 85 A 1332 ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO PHE LYS
SEQRES 86 A 1332 LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP VAL MET
SEQRES 87 A 1332 ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR THR GLY
SEQRES 88 A 1332 PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU THR
SEQRES 89 A 1332 ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR GLY VAL
SEQRES 90 A 1332 ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY ASP
SEQRES 91 A 1332 HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL GLY
SEQRES 92 A 1332 SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL GLU
SEQRES 93 A 1332 GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU GLU
SEQRES 94 A 1332 GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR ARG
SEQRES 95 A 1332 GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER ILE
SEQRES 96 A 1332 PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP CYS PRO
SEQRES 97 A 1332 ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY GLU
SEQRES 98 A 1332 PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE ALA ILE
SEQRES 99 A 1332 LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR ASN
SEQRES 100 A 1332 ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER PRO ALA
SEQRES 101 A 1332 THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS PHE
SEQRES 102 A 1332 THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN CYS LYS
SEQRES 103 A 1332 PRO TRP SER LEU ARG VAL
SEQRES 1 B 1332 MET THR ALA ASP GLU LEU VAL PHE PHE VAL ASN GLY LYS
SEQRES 2 B 1332 LYS VAL VAL GLU LYS ASN ALA ASP PRO GLU THR THR LEU
SEQRES 3 B 1332 LEU ALA TYR LEU ARG ARG LYS LEU GLY LEU ARG GLY THR
SEQRES 4 B 1332 LYS LEU GLY CYS GLY GLU GLY GLY CYS GLY ALA CYS THR
SEQRES 5 B 1332 VAL MET LEU SER LYS TYR ASP ARG LEU GLN ASP LYS ILE
SEQRES 6 B 1332 ILE HIS PHE SER ALA ASN ALA CYS LEU ALA PRO ILE CYS
SEQRES 7 B 1332 THR LEU HIS HIS VAL ALA VAL THR THR VAL GLU GLY ILE
SEQRES 8 B 1332 GLY SER THR LYS THR ARG LEU HIS PRO VAL GLN GLU ARG
SEQRES 9 B 1332 ILE ALA LYS SER HIS GLY SER GLN CYS GLY PHE CYS THR
SEQRES 10 B 1332 PRO GLY ILE VAL MET SER MET TYR THR LEU LEU ARG ASN
SEQRES 11 B 1332 GLN PRO GLU PRO THR VAL GLU GLU ILE GLU ASP ALA PHE
SEQRES 12 B 1332 GLN GLY ASN LEU CYS ARG CYS THR GLY TYR ARG PRO ILE
SEQRES 13 B 1332 LEU GLN GLY PHE ARG THR PHE ALA LYS ASN GLY GLY CYS
SEQRES 14 B 1332 CYS GLY GLY ASN GLY ASN ASN PRO ASN CYS CYS MET ASN
SEQRES 15 B 1332 GLN LYS LYS ASP HIS THR VAL THR LEU SER PRO SER LEU
SEQRES 16 B 1332 PHE ASN PRO GLU GLU PHE MET PRO LEU ASP PRO THR GLN
SEQRES 17 B 1332 GLU PRO ILE PHE PRO PRO GLU LEU LEU ARG LEU LYS ASP
SEQRES 18 B 1332 VAL PRO PRO LYS GLN LEU ARG PHE GLU GLY GLU ARG VAL
SEQRES 19 B 1332 THR TRP ILE GLN ALA SER THR LEU LYS GLU LEU LEU ASP
SEQRES 20 B 1332 LEU LYS ALA GLN HIS PRO GLU ALA LYS LEU VAL VAL GLY
SEQRES 21 B 1332 ASN THR GLU ILE GLY ILE GLU MET LYS PHE LYS ASN GLN
SEQRES 22 B 1332 LEU PHE PRO MET ILE ILE CYS PRO ALA TRP ILE PRO GLU
SEQRES 23 B 1332 LEU ASN ALA VAL GLU HIS GLY PRO GLU GLY ILE SER PHE
SEQRES 24 B 1332 GLY ALA ALA CYS ALA LEU SER SER VAL GLU LYS THR LEU
SEQRES 25 B 1332 LEU GLU ALA VAL ALA LYS LEU PRO THR GLN LYS THR GLU
SEQRES 26 B 1332 VAL PHE ARG GLY VAL LEU GLU GLN LEU ARG TRP PHE ALA
SEQRES 27 B 1332 GLY LYS GLN VAL LYS SER VAL ALA SER LEU GLY GLY ASN
SEQRES 28 B 1332 ILE ILE THR ALA SER PRO ILE SER ASP LEU ASN PRO VAL
SEQRES 29 B 1332 PHE MET ALA SER GLY THR LYS LEU THR ILE VAL SER ARG
SEQRES 30 B 1332 GLY THR ARG ARG THR VAL PRO MET ASP HIS THR PHE PHE
SEQRES 31 B 1332 PRO SER TYR ARG LYS THR LEU LEU GLY PRO GLU GLU ILE
SEQRES 32 B 1332 LEU LEU SER ILE GLU ILE PRO TYR SER ARG GLU ASP GLU
SEQRES 33 B 1332 PHE PHE SER ALA PHE LYS GLN ALA SER ARG ARG GLU ASP
SEQRES 34 B 1332 ASP ILE ALA LYS VAL THR CYS GLY MET ARG VAL LEU PHE
SEQRES 35 B 1332 GLN PRO GLY SER MET GLN VAL LYS GLU LEU ALA LEU CYS
SEQRES 36 B 1332 TYR GLY GLY MET ALA ASP ARG THR ILE SER ALA LEU LYS
SEQRES 37 B 1332 THR THR GLN LYS GLN LEU SER LYS PHE TRP ASN GLU LYS
SEQRES 38 B 1332 LEU LEU GLN ASP VAL CYS ALA GLY LEU ALA GLU GLU LEU
SEQRES 39 B 1332 SER LEU SER PRO ASP ALA PRO GLY GLY MET ILE GLU PHE
SEQRES 40 B 1332 ARG ARG THR LEU THR LEU SER PHE PHE PHE LYS PHE TYR
SEQRES 41 B 1332 LEU THR VAL LEU LYS LYS LEU GLY LYS ASP SER LYS ASP
SEQRES 42 B 1332 LYS CYS GLY LYS LEU ASP PRO THR TYR THR SER ALA THR
SEQRES 43 B 1332 LEU LEU PHE GLN LYS HIS PRO PRO ALA ASN ILE GLN LEU
SEQRES 44 B 1332 PHE GLN GLU VAL PRO ASN GLY GLN SER LYS GLU ASP THR
SEQRES 45 B 1332 VAL GLY ARG PRO LEU PRO HIS LEU ALA ALA ALA MET GLN
SEQRES 46 B 1332 ALA SER GLY GLU ALA VAL TYR CYS ASP ASP ILE PRO ARG
SEQRES 47 B 1332 TYR GLU ASN GLU LEU PHE LEU ARG LEU VAL THR SER THR
SEQRES 48 B 1332 ARG ALA HIS ALA LYS ILE LYS SER ILE ASP VAL SER GLU
SEQRES 49 B 1332 ALA GLN LYS VAL PRO GLY PHE VAL CYS PHE LEU SER ALA
SEQRES 50 B 1332 ASP ASP ILE PRO GLY SER ASN GLU THR GLY LEU PHE ASN
SEQRES 51 B 1332 ASP GLU THR VAL PHE ALA LYS ASP THR VAL THR CYS VAL
SEQRES 52 B 1332 GLY HIS ILE ILE GLY ALA VAL VAL ALA ASP THR PRO GLU
SEQRES 53 B 1332 HIS ALA GLU ARG ALA ALA HIS VAL VAL LYS VAL THR TYR
SEQRES 54 B 1332 GLU ASP LEU PRO ALA ILE ILE THR ILE GLU ASP ALA ILE
SEQRES 55 B 1332 LYS ASN ASN SER PHE TYR GLY SER GLU LEU LYS ILE GLU
SEQRES 56 B 1332 LYS GLY ASP LEU LYS LYS GLY PHE SER GLU ALA ASP ASN
SEQRES 57 B 1332 VAL VAL SER GLY GLU LEU TYR ILE GLY GLY GLN ASP HIS
SEQRES 58 B 1332 PHE TYR LEU GLU THR HIS CYS THR ILE ALA ILE PRO LYS
SEQRES 59 B 1332 GLY GLU GLU GLY GLU MET GLU LEU PHE VAL SER THR GLN
SEQRES 60 B 1332 ASN ALA MET LYS THR GLN SER PHE VAL ALA LYS MET LEU
SEQRES 61 B 1332 GLY VAL PRO VAL ASN ARG ILE LEU VAL ARG VAL LYS ARG
SEQRES 62 B 1332 MET GLY GLY GLY PHE GLY GLY LYS GLU THR ARG SER THR
SEQRES 63 B 1332 LEU VAL SER VAL ALA VAL ALA LEU ALA ALA TYR LYS THR
SEQRES 64 B 1332 GLY HIS PRO VAL ARG CYS MET LEU ASP ARG ASN GLU ASP
SEQRES 65 B 1332 MET LEU ILE THR GLY GLY ARG HIS PRO PHE LEU ALA ARG
SEQRES 66 B 1332 TYR LYS VAL GLY PHE MET LYS THR GLY THR ILE VAL ALA
SEQRES 67 B 1332 LEU GLU VAL ASP HIS TYR SER ASN ALA GLY ASN SER ARG
SEQRES 68 B 1332 ASP LEU SER HIS SER ILE MET GLU ARG ALA LEU PHE HIS
SEQRES 69 B 1332 MET ASP ASN CYS TYR LYS ILE PRO ASN ILE ARG GLY THR
SEQRES 70 B 1332 GLY ARG LEU CYS LYS THR ASN LEU SER SER ASN THR ALA
SEQRES 71 B 1332 PHE ARG GLY PHE GLY GLY PRO GLN ALA LEU PHE ILE ALA
SEQRES 72 B 1332 GLU ASN TRP MET SER GLU VAL ALA VAL THR CYS GLY LEU
SEQRES 73 B 1332 PRO ALA GLU GLU VAL ARG TRP LYS ASN MET TYR LYS GLU
SEQRES 74 B 1332 GLY ASP LEU THR HIS PHE ASN GLN ARG LEU GLU GLY PHE
SEQRES 75 B 1332 SER VAL PRO ARG CYS TRP ASP GLU CYS LEU LYS SER SER
SEQRES 76 B 1332 GLN TYR TYR ALA ARG LYS SER GLU VAL ASP LYS PHE ASN
SEQRES 77 B 1332 LYS GLU ASN CYS TRP LYS LYS ARG GLY LEU CYS ILE ILE
SEQRES 78 B 1332 PRO THR LYS PHE GLY ILE SER PHE THR VAL PRO PHE LEU
SEQRES 79 B 1332 ASN GLN ALA GLY ALA LEU ILE HIS VAL TYR THR ASP GLY
SEQRES 80 B 1332 SER VAL LEU VAL SER HIS GLY GLY THR GLU MET GLY GLN
SEQRES 81 B 1332 GLY LEU HIS THR LYS MET VAL GLN VAL ALA SER LYS ALA
SEQRES 82 B 1332 LEU LYS ILE PRO ILE SER LYS ILE TYR ILE SER GLU THR
SEQRES 83 B 1332 SER THR ASN THR VAL PRO ASN SER SER PRO THR ALA ALA
SEQRES 84 B 1332 SER VAL SER THR ASP ILE TYR GLY GLN ALA VAL TYR GLU
SEQRES 85 B 1332 ALA CYS GLN THR ILE LEU LYS ARG LEU GLU PRO PHE LYS
SEQRES 86 B 1332 LYS LYS ASN PRO ASP GLY SER TRP GLU ASP TRP VAL MET
SEQRES 87 B 1332 ALA ALA TYR GLN ASP ARG VAL SER LEU SER THR THR GLY
SEQRES 88 B 1332 PHE TYR ARG THR PRO ASN LEU GLY TYR SER PHE GLU THR
SEQRES 89 B 1332 ASN SER GLY ASN ALA PHE HIS TYR PHE THR TYR GLY VAL
SEQRES 90 B 1332 ALA CYS SER GLU VAL GLU ILE ASP CYS LEU THR GLY ASP
SEQRES 91 B 1332 HIS LYS ASN LEU ARG THR ASP ILE VAL MET ASP VAL GLY
SEQRES 92 B 1332 SER SER LEU ASN PRO ALA ILE ASP ILE GLY GLN VAL GLU
SEQRES 93 B 1332 GLY ALA PHE VAL GLN GLY LEU GLY LEU PHE THR LEU GLU
SEQRES 94 B 1332 GLU LEU HIS TYR SER PRO GLU GLY SER LEU HIS THR ARG
SEQRES 95 B 1332 GLY PRO SER THR TYR LYS ILE PRO ALA PHE GLY SER ILE
SEQRES 96 B 1332 PRO THR GLU PHE ARG VAL SER LEU LEU ARG ASP CYS PRO
SEQRES 97 B 1332 ASN LYS LYS ALA ILE TYR ALA SER LYS ALA VAL GLY GLU
SEQRES 98 B 1332 PRO PRO LEU PHE LEU GLY ALA SER VAL PHE PHE ALA ILE
SEQRES 99 B 1332 LYS ASP ALA ILE ARG ALA ALA ARG ALA GLN HIS THR ASN
SEQRES 100 B 1332 ASN ASN THR LYS GLU LEU PHE ARG LEU ASP SER PRO ALA
SEQRES 101 B 1332 THR PRO GLU LYS ILE ARG ASN ALA CYS VAL ASP LYS PHE
SEQRES 102 B 1332 THR THR LEU CYS VAL THR GLY ALA PRO GLY ASN CYS LYS
SEQRES 103 B 1332 PRO TRP SER LEU ARG VAL
HET FES A3001 4
HET FES A3002 4
HET CA A3008 1
HET FAD A3005 53
HET BCT A1904 4
HET MTE A1333 24
HET MOS A1334 3
HET FYO A1335 22
HET CA A1336 1
HET FES B4001 4
HET FES B4002 4
HET CA B4008 1
HET FAD B4005 53
HET BCT B1904 4
HET MTE B1333 24
HET MOS B1334 3
HET FYO B1335 22
HET GOL B1336 6
HET CA B1337 1
HET GOL B1338 6
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM CA CALCIUM ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM BCT BICARBONATE ION
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 FYO 4-[5-(2,6-DIOXO-1,2,3,6-TETRAHYDROPYRIDIN-4-YL)-1H-1,2,
HETNAM 2 FYO 4-TRIAZOL-3-YL]-6-OXO-1,6-DIHYDROPYRIDINE-2-
HETNAM 3 FYO CARBONITRILE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FES 4(FE2 S2)
FORMUL 5 CA 4(CA 2+)
FORMUL 6 FAD 2(C27 H33 N9 O15 P2)
FORMUL 7 BCT 2(C H O3 1-)
FORMUL 8 MTE 2(C10 H14 N5 O6 P S2)
FORMUL 9 MOS 2(H MO O2 S)
FORMUL 10 FYO 2(C13 H8 N6 O3)
FORMUL 20 GOL 2(C3 H8 O3)
FORMUL 23 HOH *1914(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 A 197 PHE A 201 5 5
HELIX 9 9 ASP A 205 GLU A 209 5 5
HELIX 10 10 PRO A 213 LYS A 220 1 8
HELIX 11 11 THR A 241 HIS A 252 1 12
HELIX 12 12 GLU A 263 LYS A 271 1 9
HELIX 13 13 ILE A 284 ASN A 288 5 5
HELIX 14 14 ALA A 304 LEU A 319 1 16
HELIX 15 15 PRO A 320 LYS A 323 5 4
HELIX 16 16 THR A 324 ARG A 335 1 12
HELIX 17 17 GLY A 339 SER A 344 1 6
HELIX 18 18 SER A 347 ALA A 355 1 9
HELIX 19 19 LEU A 361 SER A 368 1 8
HELIX 20 20 ASP A 386 PHE A 390 5 5
HELIX 21 21 ALA A 466 LYS A 472 1 7
HELIX 22 22 ASN A 479 LEU A 494 1 16
HELIX 23 23 MET A 504 GLY A 528 1 25
HELIX 24 24 TYR A 542 LEU A 547 5 6
HELIX 25 25 ALA A 581 SER A 587 1 7
HELIX 26 26 TYR A 592 ILE A 596 5 5
HELIX 27 27 GLU A 624 VAL A 628 5 5
HELIX 28 28 ASP A 638 ILE A 640 5 3
HELIX 29 29 THR A 674 VAL A 684 1 11
HELIX 30 30 THR A 697 ASN A 704 1 8
HELIX 31 31 ASP A 718 ALA A 726 1 9
HELIX 32 32 ASN A 768 GLY A 781 1 14
HELIX 33 33 PRO A 783 ASN A 785 5 3
HELIX 34 34 SER A 805 GLY A 820 1 16
HELIX 35 35 ASP A 828 THR A 836 1 9
HELIX 36 36 LEU A 873 MET A 885 1 13
HELIX 37 37 GLY A 915 GLY A 935 1 21
HELIX 38 38 PRO A 937 MET A 946 1 10
HELIX 39 39 SER A 963 SER A 975 1 13
HELIX 40 40 GLN A 976 ASN A 991 1 16
HELIX 41 41 VAL A 1011 LEU A 1014 5 4
HELIX 42 42 GLY A 1041 LYS A 1055 1 15
HELIX 43 43 PRO A 1057 SER A 1059 5 3
HELIX 44 44 VAL A 1081 ASN A 1108 1 28
HELIX 45 45 SER A 1112 ASP A 1123 1 12
HELIX 46 46 ASN A 1187 LEU A 1208 1 22
HELIX 47 47 ALA A 1231 ILE A 1235 5 5
HELIX 48 48 ALA A 1252 SER A 1256 5 5
HELIX 49 49 GLU A 1261 LEU A 1266 5 6
HELIX 50 50 GLY A 1267 THR A 1286 1 20
HELIX 51 51 THR A 1301 CYS A 1309 1 9
HELIX 52 52 ASP A 1311 VAL A 1318 1 8
HELIX 53 53 THR B 25 LYS B 33 1 9
HELIX 54 54 ARG B 60 ASP B 63 5 4
HELIX 55 55 PRO B 76 LEU B 80 5 5
HELIX 56 56 THR B 87 GLY B 92 1 6
HELIX 57 57 HIS B 99 SER B 108 1 10
HELIX 58 58 CYS B 116 GLN B 131 1 16
HELIX 59 59 THR B 135 ALA B 142 1 8
HELIX 60 60 TYR B 153 THR B 162 1 10
HELIX 61 61 ASN B 197 PHE B 201 5 5
HELIX 62 62 ASP B 205 GLU B 209 5 5
HELIX 63 63 PRO B 213 LYS B 220 1 8
HELIX 64 64 THR B 241 HIS B 252 1 12
HELIX 65 65 GLU B 263 LYS B 271 1 9
HELIX 66 66 ILE B 284 ALA B 289 1 6
HELIX 67 67 ALA B 304 LEU B 319 1 16
HELIX 68 68 PRO B 320 LYS B 323 5 4
HELIX 69 69 THR B 324 TRP B 336 1 13
HELIX 70 70 GLY B 339 SER B 344 1 6
HELIX 71 71 SER B 347 ALA B 355 1 9
HELIX 72 72 LEU B 361 SER B 368 1 8
HELIX 73 73 ASP B 386 PHE B 390 5 5
HELIX 74 74 ALA B 466 LYS B 472 1 7
HELIX 75 75 ASN B 479 LEU B 494 1 16
HELIX 76 76 MET B 504 LEU B 527 1 24
HELIX 77 77 TYR B 542 LEU B 547 5 6
HELIX 78 78 ALA B 581 SER B 587 1 7
HELIX 79 79 TYR B 592 ILE B 596 5 5
HELIX 80 80 GLU B 624 VAL B 628 5 5
HELIX 81 81 SER B 636 ILE B 640 5 5
HELIX 82 82 THR B 674 VAL B 684 1 11
HELIX 83 83 THR B 697 ASN B 704 1 8
HELIX 84 84 ASP B 718 ALA B 726 1 9
HELIX 85 85 ASN B 768 GLY B 781 1 14
HELIX 86 86 PRO B 783 ASN B 785 5 3
HELIX 87 87 SER B 805 GLY B 820 1 16
HELIX 88 88 ASP B 828 THR B 836 1 9
HELIX 89 89 LEU B 873 HIS B 884 1 12
HELIX 90 90 GLY B 915 GLY B 935 1 21
HELIX 91 91 PRO B 937 MET B 946 1 10
HELIX 92 92 SER B 963 SER B 975 1 13
HELIX 93 93 GLN B 976 GLU B 990 1 15
HELIX 94 94 VAL B 1011 LEU B 1014 5 4
HELIX 95 95 GLY B 1041 LYS B 1055 1 15
HELIX 96 96 PRO B 1057 SER B 1059 5 3
HELIX 97 97 VAL B 1081 ASN B 1108 1 28
HELIX 98 98 SER B 1112 ASP B 1123 1 12
HELIX 99 99 ASN B 1187 LEU B 1208 1 22
HELIX 100 100 ALA B 1231 ILE B 1235 5 5
HELIX 101 101 ALA B 1252 SER B 1256 5 5
HELIX 102 102 PRO B 1263 LEU B 1266 5 4
HELIX 103 103 GLY B 1267 THR B 1286 1 20
HELIX 104 104 THR B 1301 CYS B 1309 1 9
HELIX 105 105 PHE B 1313 CYS B 1317 5 5
SHEET 1 A 5 LYS A 13 GLU A 17 0
SHEET 2 A 5 LEU A 6 VAL A 10 -1 N PHE A 8 O VAL A 15
SHEET 3 A 5 ALA A 84 THR A 86 1 O VAL A 85 N PHE A 9
SHEET 4 A 5 THR A 52 ASP A 59 -1 N SER A 56 O ALA A 84
SHEET 5 A 5 LYS A 64 ASN A 71 -1 O LYS A 64 N ASP A 59
SHEET 1 B 4 LEU A 227 GLU A 230 0
SHEET 2 B 4 THR A 235 GLN A 238 -1 O TRP A 236 N PHE A 229
SHEET 3 B 4 MET A 277 CYS A 280 1 O ILE A 278 N ILE A 237
SHEET 4 B 4 LYS A 256 LEU A 257 1 N LYS A 256 O MET A 277
SHEET 1 C 5 VAL A 290 HIS A 292 0
SHEET 2 C 5 GLY A 296 GLY A 300 -1 O SER A 298 N GLU A 291
SHEET 3 C 5 ILE A 403 PRO A 410 -1 O ILE A 409 N ILE A 297
SHEET 4 C 5 LYS A 371 SER A 376 -1 N VAL A 375 O ILE A 403
SHEET 5 C 5 THR A 379 PRO A 384 -1 O VAL A 383 N LEU A 372
SHEET 1 D 4 GLU A 416 GLN A 423 0
SHEET 2 D 4 VAL A 434 PHE A 442 -1 O MET A 438 N SER A 419
SHEET 3 D 4 VAL A 449 GLY A 457 -1 O LYS A 450 N LEU A 441
SHEET 4 D 4 ILE A 464 SER A 465 -1 O ILE A 464 N TYR A 456
SHEET 1 E 5 ALA A 555 LEU A 559 0
SHEET 2 E 5 GLU A1238 LEU A1243 1 O LEU A1243 N LEU A 559
SHEET 3 E 5 HIS A1171 ASP A1181 1 N MET A1180 O SER A1242
SHEET 4 E 5 TYR A1152 ASP A1165 -1 N TYR A1155 O ASP A1181
SHEET 5 E 5 LYS A 994 ILE A1007 -1 N LYS A 995 O ILE A1164
SHEET 1 F 8 PHE A 631 SER A 636 0
SHEET 2 F 8 ILE A 666 ALA A 672 -1 O ALA A 669 N LEU A 635
SHEET 3 F 8 LEU A 603 THR A 609 -1 N ARG A 606 O VAL A 670
SHEET 4 F 8 VAL A 823 MET A 826 1 O ARG A 824 N LEU A 605
SHEET 5 F 8 CYS A 748 PRO A 753 -1 N ALA A 751 O VAL A 823
SHEET 6 F 8 MET A 760 VAL A 764 -1 O GLU A 761 N ILE A 752
SHEET 7 F 8 ILE A 787 VAL A 791 1 O ARG A 790 N LEU A 762
SHEET 8 F 8 THR A1066 SER A1067 -1 O THR A1066 N VAL A 791
SHEET 1 G 3 THR A 659 VAL A 660 0
SHEET 2 G 3 ALA A 615 ASP A 621 -1 N ALA A 615 O VAL A 660
SHEET 3 G 3 LYS A 686 ASP A 691 -1 O LYS A 686 N ASP A 621
SHEET 1 H 2 GLU A 645 THR A 646 0
SHEET 2 H 2 GLU A 652 THR A 653 -1 O GLU A 652 N THR A 646
SHEET 1 I 5 PHE A 707 LYS A 716 0
SHEET 2 I 5 ILE A 894 CYS A 901 -1 O ILE A 894 N LYS A 716
SHEET 3 I 5 ILE A 856 ASN A 866 1 N SER A 865 O CYS A 901
SHEET 4 I 5 PHE A 842 PHE A 850 -1 N GLY A 849 O VAL A 857
SHEET 5 I 5 ASN A 728 ILE A 736 -1 N LEU A 734 O ALA A 844
SHEET 1 J 4 ILE A1061 ILE A1063 0
SHEET 2 J 4 VAL A1029 HIS A1033 1 N VAL A1031 O TYR A1062
SHEET 3 J 4 GLN A1016 VAL A1023 -1 N LEU A1020 O SER A1032
SHEET 4 J 4 SER A1128 ARG A1134 -1 O THR A1129 N ILE A1021
SHEET 1 K 5 LYS B 13 GLU B 17 0
SHEET 2 K 5 LEU B 6 VAL B 10 -1 N PHE B 8 O VAL B 15
SHEET 3 K 5 ALA B 84 THR B 86 1 O VAL B 85 N PHE B 9
SHEET 4 K 5 THR B 52 ASP B 59 -1 N MET B 54 O THR B 86
SHEET 5 K 5 LYS B 64 ASN B 71 -1 O ILE B 66 N LYS B 57
SHEET 1 L 4 LEU B 227 GLU B 230 0
SHEET 2 L 4 THR B 235 GLN B 238 -1 O TRP B 236 N PHE B 229
SHEET 3 L 4 MET B 277 CYS B 280 1 O ILE B 278 N THR B 235
SHEET 4 L 4 LYS B 256 LEU B 257 1 N LYS B 256 O ILE B 279
SHEET 1 M 5 VAL B 290 HIS B 292 0
SHEET 2 M 5 GLY B 296 GLY B 300 -1 O SER B 298 N GLU B 291
SHEET 3 M 5 ILE B 403 PRO B 410 -1 O ILE B 409 N ILE B 297
SHEET 4 M 5 LYS B 371 SER B 376 -1 N VAL B 375 O ILE B 403
SHEET 5 M 5 THR B 379 PRO B 384 -1 O VAL B 383 N LEU B 372
SHEET 1 N 4 GLU B 416 GLN B 423 0
SHEET 2 N 4 VAL B 434 PHE B 442 -1 O CYS B 436 N PHE B 421
SHEET 3 N 4 VAL B 449 GLY B 457 -1 O GLY B 457 N THR B 435
SHEET 4 N 4 ILE B 464 SER B 465 -1 O ILE B 464 N TYR B 456
SHEET 1 O 5 ALA B 555 LEU B 559 0
SHEET 2 O 5 GLU B1238 LEU B1243 1 O VAL B1241 N LEU B 559
SHEET 3 O 5 HIS B1171 ASP B1181 1 N MET B1180 O SER B1242
SHEET 4 O 5 TYR B1152 ASP B1165 -1 N CYS B1159 O ASP B1177
SHEET 5 O 5 LYS B 994 ILE B1007 -1 N LYS B 995 O ILE B1164
SHEET 1 P 8 PHE B 631 LEU B 635 0
SHEET 2 P 8 ILE B 666 ALA B 672 -1 O ALA B 669 N LEU B 635
SHEET 3 P 8 LEU B 603 THR B 609 -1 N VAL B 608 O ILE B 667
SHEET 4 P 8 VAL B 823 MET B 826 1 O ARG B 824 N LEU B 605
SHEET 5 P 8 CYS B 748 PRO B 753 -1 N ALA B 751 O VAL B 823
SHEET 6 P 8 MET B 760 VAL B 764 -1 O GLU B 761 N ILE B 752
SHEET 7 P 8 ILE B 787 VAL B 791 1 O LEU B 788 N LEU B 762
SHEET 8 P 8 THR B1066 SER B1067 -1 O THR B1066 N VAL B 791
SHEET 1 Q 3 THR B 659 VAL B 660 0
SHEET 2 Q 3 ALA B 615 ASP B 621 -1 N ALA B 615 O VAL B 660
SHEET 3 Q 3 LYS B 686 ASP B 691 -1 O LYS B 686 N ASP B 621
SHEET 1 R 2 GLU B 645 THR B 646 0
SHEET 2 R 2 GLU B 652 THR B 653 -1 O GLU B 652 N THR B 646
SHEET 1 S 5 PHE B 707 LYS B 716 0
SHEET 2 S 5 ILE B 894 LYS B 902 -1 O GLY B 898 N LEU B 712
SHEET 3 S 5 ILE B 856 GLY B 868 1 N SER B 865 O CYS B 901
SHEET 4 S 5 PHE B 842 PHE B 850 -1 N GLY B 849 O VAL B 857
SHEET 5 S 5 ASN B 728 ILE B 736 -1 N VAL B 730 O VAL B 848
SHEET 1 T 4 ILE B1061 TYR B1062 0
SHEET 2 T 4 VAL B1029 HIS B1033 1 N VAL B1031 O TYR B1062
SHEET 3 T 4 GLN B1016 VAL B1023 -1 N LEU B1020 O SER B1032
SHEET 4 T 4 SER B1128 ARG B1134 -1 O THR B1129 N ILE B1021
LINK SG CYS A 43 FE2 FES A3002 1555 1555 2.29
LINK SG CYS A 48 FE2 FES A3002 1555 1555 2.32
LINK SG CYS A 51 FE1 FES A3002 1555 1555 2.33
LINK SG CYS A 73 FE1 FES A3002 1555 1555 2.27
LINK SG CYS A 113 FE1 FES A3001 1555 1555 2.21
LINK SG CYS A 116 FE2 FES A3001 1555 1555 2.28
LINK SG CYS A 148 FE2 FES A3001 1555 1555 2.31
LINK SG CYS A 150 FE1 FES A3001 1555 1555 2.34
LINK OH TYR A 743 CA CA A1336 1555 1555 2.80
LINK OG1 THR A 836 CA CA A1336 1555 1555 2.68
LINK O GLY A 837 CA CA A1336 1555 1555 2.52
LINK O ALA A 867 CA CA A3008 1555 1555 2.74
LINK O SER A 870 CA CA A3008 1555 1555 2.86
LINK O ARG A 871 CA CA A3008 1555 1555 3.07
LINK OG SER A 874 CA CA A3008 1555 1555 2.57
LINK OG SER A 907 CA CA A3008 1555 1555 2.76
LINK O ASN A 908 CA CA A3008 1555 1555 2.71
LINK S2' MTE A1333 MO MOS A1334 1555 1555 2.29
LINK S1' MTE A1333 MO MOS A1334 1555 1555 2.37
LINK MO MOS A1334 NAA FYO A1335 1555 1555 2.34
LINK CA CA A1336 O HOH A2311 1555 1555 2.63
LINK SG CYS B 43 FE2 FES B4002 1555 1555 2.32
LINK SG CYS B 48 FE2 FES B4002 1555 1555 2.24
LINK SG CYS B 51 FE1 FES B4002 1555 1555 2.28
LINK SG CYS B 73 FE1 FES B4002 1555 1555 2.34
LINK SG CYS B 113 FE1 FES B4001 1555 1555 2.25
LINK SG CYS B 116 FE2 FES B4001 1555 1555 2.27
LINK SG CYS B 148 FE2 FES B4001 1555 1555 2.36
LINK SG CYS B 150 FE1 FES B4001 1555 1555 2.38
LINK OH TYR B 743 CA CA B1337 1555 1555 2.68
LINK OG1 THR B 836 CA CA B1337 1555 1555 2.52
LINK O GLY B 837 CA CA B1337 1555 1555 2.60
LINK O ALA B 867 CA CA B4008 1555 1555 2.69
LINK O SER B 870 CA CA B4008 1555 1555 2.70
LINK O ARG B 871 CA CA B4008 1555 1555 2.84
LINK OG SER B 874 CA CA B4008 1555 1555 2.57
LINK OG SER B 907 CA CA B4008 1555 1555 2.80
LINK O ASN B 908 CA CA B4008 1555 1555 2.78
LINK S2' MTE B1333 MO MOS B1334 1555 1555 2.33
LINK S1' MTE B1333 MO MOS B1334 1555 1555 2.35
LINK MO MOS B1334 NAA FYO B1335 1555 1555 2.34
LINK CA CA B1337 O HOH B2257 1555 1555 2.58
CISPEP 1 SER A 1298 PRO A 1299 0 2.23
CISPEP 2 TRP A 1328 SER A 1329 0 -12.54
CISPEP 3 SER B 1298 PRO B 1299 0 2.58
CISPEP 4 CYS B 1325 LYS B 1326 0 16.59
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 6 ALA A 867 SER A 870 ARG A 871 SER A 874
SITE 2 AC3 6 SER A 907 ASN A 908
SITE 1 AC4 31 GLU A 45 GLY A 46 LYS A 256 LEU A 257
SITE 2 AC4 31 VAL A 259 GLY A 260 ASN A 261 THR A 262
SITE 3 AC4 31 GLU A 263 ILE A 264 ALA A 301 PHE A 337
SITE 4 AC4 31 ALA A 338 VAL A 342 ALA A 346 SER A 347
SITE 5 AC4 31 GLY A 350 ASN A 351 ILE A 353 THR A 354
SITE 6 AC4 31 SER A 359 ASP A 360 LEU A 404 LYS A 422
SITE 7 AC4 31 ASP A 429 ASP A 430 HOH A1483 HOH A1582
SITE 8 AC4 31 HOH A1609 HOH A1895 HOH A2074
SITE 1 AC5 9 ARG A 839 HIS A 840 ILE A 877 THR A 909
SITE 2 AC5 9 ALA A 910 PHE A 911 PHE A 914 GLY A 915
SITE 3 AC5 9 GLN A 918
SITE 1 AC6 21 GLN A 112 CYS A 150 GLY A 796 GLY A 797
SITE 2 AC6 21 PHE A 798 GLY A 799 ARG A 912 MET A1038
SITE 3 AC6 21 GLY A1039 GLN A1040 ALA A1079 SER A1080
SITE 4 AC6 21 VAL A1081 SER A1082 GLN A1194 GLU A1261
SITE 5 AC6 21 MOS A1334 FYO A1335 HOH A1677 HOH A2293
SITE 6 AC6 21 HOH A2294
SITE 1 AC7 8 GLN A 767 GLY A 799 GLU A 802 PHE A 911
SITE 2 AC7 8 ARG A 912 GLU A1261 MTE A1333 FYO A1335
SITE 1 AC8 14 LEU A 648 GLU A 802 LEU A 873 SER A 876
SITE 2 AC8 14 ARG A 880 PHE A 914 PHE A1009 LEU A1014
SITE 3 AC8 14 ALA A1079 GLU A1261 MTE A1333 MOS A1334
SITE 4 AC8 14 HOH A2289 HOH A2291
SITE 1 AC9 5 HIS A 741 TYR A 743 THR A 836 GLY A 837
SITE 2 AC9 5 HOH A2311
SITE 1 BC1 7 GLN B 112 CYS B 113 GLY B 114 CYS B 116
SITE 2 BC1 7 CYS B 148 ARG B 149 CYS B 150
SITE 1 BC2 10 GLY B 42 CYS B 43 GLY B 44 GLY B 46
SITE 2 BC2 10 GLY B 47 CYS B 48 GLY B 49 CYS B 51
SITE 3 BC2 10 ASN B 71 CYS B 73
SITE 1 BC3 6 ALA B 867 SER B 870 ARG B 871 SER B 874
SITE 2 BC3 6 SER B 907 ASN B 908
SITE 1 BC4 29 GLU B 45 GLY B 46 LYS B 256 LEU B 257
SITE 2 BC4 29 VAL B 258 VAL B 259 GLY B 260 ASN B 261
SITE 3 BC4 29 THR B 262 GLU B 263 ILE B 264 ALA B 301
SITE 4 BC4 29 PHE B 337 ALA B 338 SER B 347 GLY B 350
SITE 5 BC4 29 ASN B 351 ILE B 353 THR B 354 SER B 359
SITE 6 BC4 29 ASP B 360 ILE B 403 LEU B 404 LYS B 422
SITE 7 BC4 29 ASP B 429 ASP B 430 HOH B1713 HOH B1867
SITE 8 BC4 29 HOH B2068
SITE 1 BC5 9 ARG B 839 HIS B 840 ILE B 877 THR B 909
SITE 2 BC5 9 ALA B 910 PHE B 911 PHE B 914 GLY B 915
SITE 3 BC5 9 GLN B 918
SITE 1 BC6 22 GLN B 112 CYS B 150 GLY B 796 GLY B 797
SITE 2 BC6 22 PHE B 798 GLY B 799 ARG B 912 MET B1038
SITE 3 BC6 22 GLY B1039 GLN B1040 ALA B1078 ALA B1079
SITE 4 BC6 22 SER B1080 VAL B1081 SER B1082 GLN B1194
SITE 5 BC6 22 GLU B1261 MOS B1334 FYO B1335 HOH B1386
SITE 6 BC6 22 HOH B2248 HOH B2249
SITE 1 BC7 7 GLN B 767 GLY B 799 PHE B 911 ARG B 912
SITE 2 BC7 7 GLU B1261 MTE B1333 FYO B1335
SITE 1 BC8 16 LEU B 648 GLU B 802 LEU B 873 SER B 876
SITE 2 BC8 16 ARG B 880 PHE B 914 PHE B1009 VAL B1011
SITE 3 BC8 16 LEU B1014 ALA B1078 ALA B1079 GLU B1261
SITE 4 BC8 16 MTE B1333 MOS B1334 HOH B1848 HOH B2247
SITE 1 BC9 9 HIS B 665 ILE B 666 ARG B 804 ILE B 835
SITE 2 BC9 9 ASN B 869 SER B 906 SER B 907 HOH B1557
SITE 3 BC9 9 HOH B1602
SITE 1 CC1 5 HIS B 741 TYR B 743 THR B 836 GLY B 837
SITE 2 CC1 5 HOH B2257
SITE 1 CC2 5 ASP B 594 PHE B 604 ARG B 824 MET B 826
SITE 2 CC2 5 HOH B1352
CRYST1 168.916 124.722 146.195 90.00 91.04 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005920 0.000000 0.000107 0.00000
SCALE2 0.000000 0.008018 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006841 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
