HEADER OXIDOREDUCTASE 21-JAN-04 1V97
TITLE CRYSTAL STRUCTURE OF BOVINE MILK XANTHINE DEHYDROGENASE FYX-051 BOUND
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: XANTHINE DEHYDROGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: XD;
COMPND 5 EC: 1.1.1.204
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS XANTHINE DEHYDROGENASE, MOLYBDOPTERIN, FYX-051, REACTION
KEYWDS 2 INTERMEDIATE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.OKAMOTO,K.MATSUMOTO,R.HILLE,B.T.EGER,E.F.PAI,T.NISHINO
REVDAT 4 27-DEC-23 1V97 1 REMARK LINK
REVDAT 3 13-JUL-11 1V97 1 VERSN
REVDAT 2 24-FEB-09 1V97 1 VERSN
REVDAT 1 22-JUN-04 1V97 0
JRNL AUTH K.OKAMOTO,K.MATSUMOTO,R.HILLE,B.T.EGER,E.F.PAI,T.NISHINO
JRNL TITL THE CRYSTAL STRUCTURE OF XANTHINE OXIDOREDUCTASE DURING
JRNL TITL 2 CATALYSIS: IMPLICATIONS FOR REACTION MECHANISM AND ENZYME
JRNL TITL 3 INHIBITION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 7931 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 15148401
JRNL DOI 10.1073/PNAS.0400973101
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 214439
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6405
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 20125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 274
REMARK 3 SOLVENT ATOMS : 2082
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1V97 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-JAN-04.
REMARK 100 THE DEPOSITION ID IS D_1000006364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAY-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
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 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 214439
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.940
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : 0.07900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1530
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.39600
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: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5
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 83.99350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.30600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.99350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.30600
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: 14990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 86980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -148.0 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 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 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 NZ LYS A 340 O HOH A 6066 1.60
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 GLU B 5 N - CA - C ANGL. DEV. = 18.3 DEGREES
REMARK 500 ASP B1191 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 ILE B1192 N - CA - CB ANGL. DEV. = -22.5 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 -75.52 -7.66
REMARK 500 CYS A 43 -29.75 -155.44
REMARK 500 LEU A 61 -23.27 -167.67
REMARK 500 THR A 96 -91.57 -108.85
REMARK 500 GLN A 112 -85.89 -108.76
REMARK 500 TYR A 153 -33.20 63.95
REMARK 500 VAL A 259 -82.65 -118.17
REMARK 500 TRP A 336 55.14 -117.48
REMARK 500 ALA A 338 171.18 53.04
REMARK 500 LEU A 397 48.73 -82.37
REMARK 500 ALA A 424 -163.91 -114.30
REMARK 500 ASP A 429 83.56 19.77
REMARK 500 LYS A 433 -79.35 -79.29
REMARK 500 PRO A 444 119.20 -39.08
REMARK 500 ALA A 460 -177.71 -170.60
REMARK 500 SER A 475 -7.10 85.99
REMARK 500 LYS A 529 -89.11 64.42
REMARK 500 ASP A 539 73.06 169.58
REMARK 500 PRO A 540 176.33 -58.33
REMARK 500 THR A 541 -24.25 69.05
REMARK 500 HIS A 614 116.75 -162.48
REMARK 500 ASP A 658 -45.38 72.68
REMARK 500 THR A 803 -41.17 -142.60
REMARK 500 ASP A 872 -129.92 48.64
REMARK 500 ASN A 887 -117.75 51.89
REMARK 500 THR A 909 -156.73 -143.63
REMARK 500 ARG A 912 108.13 -15.28
REMARK 500 SER A1008 160.04 131.62
REMARK 500 CYS A1247 53.49 -145.46
REMARK 500 THR A1286 -95.21 -85.78
REMARK 500 ASN A1287 -163.36 -103.90
REMARK 500 VAL A1318 147.21 -34.25
REMARK 500 THR A1319 86.05 -59.95
REMARK 500 ALA A1321 76.70 52.13
REMARK 500 PRO A1322 -102.92 -82.60
REMARK 500 CYS A1325 25.08 -157.35
REMARK 500 ASP B 4 159.91 49.15
REMARK 500 GLU B 5 87.31 -52.72
REMARK 500 ASN B 19 -114.05 -108.14
REMARK 500 ALA B 20 112.70 93.45
REMARK 500 CYS B 43 -29.36 -160.79
REMARK 500 THR B 96 -88.18 -117.45
REMARK 500 GLN B 112 -87.86 -110.74
REMARK 500 TYR B 153 -32.37 64.13
REMARK 500 VAL B 259 -81.76 -118.95
REMARK 500 TRP B 336 54.97 -114.24
REMARK 500 ALA B 338 -159.48 53.35
REMARK 500 ALA B 424 -149.71 -121.13
REMARK 500 ASP B 429 80.17 27.37
REMARK 500 SER B 475 -5.44 82.98
REMARK 500
REMARK 500 THIS ENTRY HAS 70 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A3002 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 43 SG
REMARK 620 2 FES A3002 S1 98.0
REMARK 620 3 FES A3002 S2 117.2 104.2
REMARK 620 4 CYS A 48 SG 107.9 119.0 110.5
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 112.1
REMARK 620 3 FES A3002 S2 118.7 102.8
REMARK 620 4 CYS A 73 SG 100.9 115.1 107.8
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 121.5
REMARK 620 3 FES A3001 S2 113.0 102.9
REMARK 620 4 CYS A 150 SG 98.1 107.6 114.3
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 115.6
REMARK 620 3 FES A3001 S2 115.6 105.9
REMARK 620 4 CYS A 148 SG 102.7 107.3 109.4
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 85.6
REMARK 620 3 ARG A 871 O 145.8 74.7
REMARK 620 4 SER A 874 OG 97.1 110.3 65.4
REMARK 620 5 SER A 907 OG 90.2 71.9 109.2 172.5
REMARK 620 6 ASN A 908 O 97.5 155.4 112.1 93.6 83.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS A3004 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE A3003 S1'
REMARK 620 2 MOS A3004 S 88.0
REMARK 620 3 MOS A3004 O1 155.6 84.1
REMARK 620 4 MOS A3004 O2 113.7 105.5 90.6
REMARK 620 5 MTE A3003 S2' 83.8 141.2 88.1 112.6
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 98.5
REMARK 620 3 FES B4002 S2 115.7 104.1
REMARK 620 4 CYS B 48 SG 107.0 119.3 111.9
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 110.8
REMARK 620 3 FES B4002 S2 118.1 102.5
REMARK 620 4 CYS B 73 SG 101.0 115.8 109.3
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 122.6
REMARK 620 3 FES B4001 S2 113.6 102.8
REMARK 620 4 CYS B 150 SG 97.8 108.9 111.1
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 112.9
REMARK 620 3 FES B4001 S2 116.7 105.6
REMARK 620 4 CYS B 148 SG 103.6 107.9 109.9
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 85.2
REMARK 620 3 ARG B 871 O 145.1 76.0
REMARK 620 4 SER B 874 OG 98.6 110.7 62.5
REMARK 620 5 SER B 907 OG 91.5 71.3 109.4 169.8
REMARK 620 6 ASN B 908 O 99.3 155.6 110.0 92.4 84.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MOS B4004 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MTE B4003 S2'
REMARK 620 2 MOS B4004 S 142.3
REMARK 620 3 MOS B4004 O1 89.1 83.0
REMARK 620 4 MOS B4004 O2 108.4 108.6 92.2
REMARK 620 5 MTE B4003 S1' 85.1 90.2 160.3 107.5
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 CA A 3008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 4008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE A 3003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS A 3004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 3005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FYX A 3006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 4001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTE B 4003
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOS B 4004
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 FYX B 4006
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 3007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 4007
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5001
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5002
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5003
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5004
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5005
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5006
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 5007
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 5008
DBREF 1V97 A 1 1332 UNP P80457 XDH_BOVIN 0 1331
DBREF 1V97 B 1 1332 UNP P80457 XDH_BOVIN 0 1331
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 CA A3008 1
HET FES A3001 4
HET FES A3002 4
HET MTE A3003 24
HET MOS A3004 4
HET FAD A3005 53
HET FYX A3006 19
HET ACY A3007 4
HET GOL A5001 6
HET GOL A5003 6
HET GOL A5005 6
HET GOL A5007 6
HET CA B4008 1
HET FES B4001 4
HET FES B4002 4
HET MTE B4003 24
HET MOS B4004 4
HET FAD B4005 53
HET FYX B4006 19
HET ACY B4007 4
HET GOL B5002 6
HET GOL B5004 6
HET GOL B5006 6
HET GOL B5008 6
HETNAM CA CALCIUM ION
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
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 FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FYX 4-(5-PYRIDIN-4-YL-1H-1,2,4-TRIAZOL-3-YL)PYRIDINE-2-
HETNAM 2 FYX CARBONITRILE
HETNAM ACY ACETIC ACID
HETNAM GOL GLYCEROL
HETSYN FYX 4-[5-PYRIDIN-4-YL-1H-[1,2,4]TRIAZOL-3-YL]-PYRIDINE-2-
HETSYN 2 FYX CARBONITRILE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CA 2(CA 2+)
FORMUL 4 FES 4(FE2 S2)
FORMUL 6 MTE 2(C10 H14 N5 O6 P S2)
FORMUL 7 MOS 2(H MO O2 S)
FORMUL 8 FAD 2(C27 H33 N9 O15 P2)
FORMUL 9 FYX 2(C13 H8 N6)
FORMUL 10 ACY 2(C2 H4 O2)
FORMUL 11 GOL 8(C3 H8 O3)
FORMUL 27 HOH *2082(H2 O)
HELIX 1 1 THR A 25 LYS A 33 1 9
HELIX 2 2 PRO A 76 LEU A 80 5 5
HELIX 3 3 THR A 87 ILE A 91 5 5
HELIX 4 4 HIS A 99 SER A 108 1 10
HELIX 5 5 CYS A 116 GLN A 131 1 16
HELIX 6 6 THR A 135 ALA A 142 1 8
HELIX 7 7 TYR A 153 ARG A 161 1 9
HELIX 8 8 THR A 162 ALA A 164 5 3
HELIX 9 9 ASN A 197 PHE A 201 5 5
HELIX 10 10 ASP A 205 GLU A 209 5 5
HELIX 11 11 PRO A 213 LYS A 220 1 8
HELIX 12 12 THR A 241 HIS A 252 1 12
HELIX 13 13 GLU A 263 LYS A 271 1 9
HELIX 14 14 ILE A 284 ASN A 288 5 5
HELIX 15 15 ALA A 304 LEU A 319 1 16
HELIX 16 16 PRO A 320 LYS A 323 5 4
HELIX 17 17 THR A 324 TRP A 336 1 13
HELIX 18 18 GLY A 339 SER A 344 1 6
HELIX 19 19 SER A 347 ALA A 355 1 9
HELIX 20 20 LEU A 361 SER A 368 1 8
HELIX 21 21 ASP A 386 PHE A 390 5 5
HELIX 22 22 ALA A 466 LYS A 472 1 7
HELIX 23 23 ASN A 479 LEU A 494 1 16
HELIX 24 24 MET A 504 LEU A 527 1 24
HELIX 25 25 TYR A 542 THR A 546 5 5
HELIX 26 26 ALA A 581 SER A 587 1 7
HELIX 27 27 TYR A 592 ILE A 596 5 5
HELIX 28 28 GLU A 624 VAL A 628 5 5
HELIX 29 29 SER A 636 ILE A 640 5 5
HELIX 30 30 THR A 674 VAL A 684 1 11
HELIX 31 31 THR A 697 ASN A 704 1 8
HELIX 32 32 ASP A 718 ALA A 726 1 9
HELIX 33 33 ASN A 768 GLY A 781 1 14
HELIX 34 34 PRO A 783 ASN A 785 5 3
HELIX 35 35 SER A 805 GLY A 820 1 16
HELIX 36 36 ASP A 828 THR A 836 1 9
HELIX 37 37 LEU A 873 HIS A 884 1 12
HELIX 38 38 GLY A 915 GLY A 935 1 21
HELIX 39 39 PRO A 937 MET A 946 1 10
HELIX 40 40 SER A 963 SER A 975 1 13
HELIX 41 41 GLN A 976 ASN A 991 1 16
HELIX 42 42 VAL A 1011 LEU A 1014 5 4
HELIX 43 43 GLY A 1041 LYS A 1055 1 15
HELIX 44 44 PRO A 1057 SER A 1059 5 3
HELIX 45 45 VAL A 1081 ASN A 1108 1 28
HELIX 46 46 SER A 1112 ASP A 1123 1 12
HELIX 47 47 ASN A 1187 LEU A 1208 1 22
HELIX 48 48 ALA A 1231 ILE A 1235 5 5
HELIX 49 49 ALA A 1252 SER A 1256 5 5
HELIX 50 50 PRO A 1263 LEU A 1266 5 4
HELIX 51 51 GLY A 1267 THR A 1286 1 20
HELIX 52 52 THR A 1301 CYS A 1309 1 9
HELIX 53 53 THR B 25 LYS B 33 1 9
HELIX 54 54 PRO B 76 LEU B 80 5 5
HELIX 55 55 THR B 87 ILE B 91 5 5
HELIX 56 56 HIS B 99 SER B 108 1 10
HELIX 57 57 CYS B 116 GLN B 131 1 16
HELIX 58 58 THR B 135 ALA B 142 1 8
HELIX 59 59 TYR B 153 ARG B 161 1 9
HELIX 60 60 THR B 162 ALA B 164 5 3
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 ASN B 288 5 5
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 THR B 546 5 5
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 GLN B 976 1 14
HELIX 93 93 GLN B 976 ASN B 991 1 16
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 TYR A 58 -1 N SER A 56 O ALA A 84
SHEET 5 A 5 ILE A 65 ASN A 71 -1 O PHE A 68 N LEU A 55
SHEET 1 B 4 LEU 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 THR A 235
SHEET 4 B 4 LYS A 256 LEU A 257 1 N LYS A 256 O ILE A 279
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 407 N PHE A 299
SHEET 4 C 5 LYS A 371 SER A 376 -1 N THR A 373 O SER A 406
SHEET 5 C 5 THR A 379 PRO A 384 -1 O ARG A 381 N ILE A 374
SHEET 1 D 4 GLU A 416 ALA A 424 0
SHEET 2 D 4 ALA A 432 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 VAL A1241 N LEU A 559
SHEET 3 E 5 HIS A1171 ASP A1181 1 N THR A1176 O ARG A1240
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 LEU A 635 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 PHE A 604 O ALA A 672
SHEET 4 F 8 VAL A 823 MET A 826 1 O ARG A 824 N LEU A 603
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 LEU A 788 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 LYS A 902 -1 O ILE A 894 N LYS A 716
SHEET 3 I 5 ILE A 856 GLY A 868 1 N HIS A 863 O THR A 897
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 TYR A1062 0
SHEET 2 J 4 VAL A1029 HIS A1033 1 N VAL A1029 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 SER B 56 O ALA B 84
SHEET 5 K 5 LYS B 64 ASN B 71 -1 O PHE B 68 N LEU B 55
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 407 N PHE B 299
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 ARG B 381 N ILE B 374
SHEET 1 N 4 GLU B 416 GLN B 423 0
SHEET 2 N 4 VAL B 434 PHE B 442 -1 O MET B 438 N SER B 419
SHEET 3 N 4 VAL B 449 GLY B 457 -1 O LYS B 450 N LEU B 441
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 TYR B1155 O ASP B1181
SHEET 5 O 5 LYS B 994 ILE B1007 -1 N ILE B1007 O TYR B1152
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 ARG B 606 O VAL B 670
SHEET 4 P 8 VAL B 823 MET B 826 1 O ARG B 824 N LEU B 603
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 ASN B 893 LYS B 902 -1 O ILE B 894 N LYS B 716
SHEET 3 S 5 ILE B 856 GLY B 868 1 N HIS B 863 O THR B 897
SHEET 4 S 5 PHE B 842 PHE B 850 -1 N GLY B 849 O ALA B 858
SHEET 5 S 5 ASN B 728 ILE B 736 -1 N LEU B 734 O ALA B 844
SHEET 1 T 4 ILE B1061 TYR B1062 0
SHEET 2 T 4 VAL B1029 HIS B1033 1 N VAL B1029 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 OD1 ASP A 594 O3 GOL A5003 1555 1555 2.01
LINK NE2 GLN A1088 O3 GOL A5007 1555 1555 1.86
LINK O1 MOS A3004 CPR FYX A3006 1555 1555 1.32
LINK NE2 GLN B1088 O3 GOL B5008 1555 1555 1.50
LINK O1 MOS B4004 CPR FYX B4006 1555 1555 1.29
LINK SG CYS A 43 FE2 FES A3002 1555 1555 2.40
LINK SG CYS A 48 FE2 FES A3002 1555 1555 2.39
LINK SG CYS A 51 FE1 FES A3002 1555 1555 2.38
LINK SG CYS A 73 FE1 FES A3002 1555 1555 2.37
LINK SG CYS A 113 FE1 FES A3001 1555 1555 2.37
LINK SG CYS A 116 FE2 FES A3001 1555 1555 2.36
LINK SG CYS A 148 FE2 FES A3001 1555 1555 2.40
LINK SG CYS A 150 FE1 FES A3001 1555 1555 2.38
LINK O ALA A 867 CA CA A3008 1555 1555 2.67
LINK O SER A 870 CA CA A3008 1555 1555 2.70
LINK O ARG A 871 CA CA A3008 1555 1555 2.94
LINK OG SER A 874 CA CA A3008 1555 1555 2.62
LINK OG SER A 907 CA CA A3008 1555 1555 2.67
LINK O ASN A 908 CA CA A3008 1555 1555 2.74
LINK S1' MTE A3003 MO MOS A3004 1555 1555 2.43
LINK S2' MTE A3003 MO MOS A3004 1555 1555 2.40
LINK SG CYS B 43 FE2 FES B4002 1555 1555 2.39
LINK SG CYS B 48 FE2 FES B4002 1555 1555 2.38
LINK SG CYS B 51 FE1 FES B4002 1555 1555 2.37
LINK SG CYS B 73 FE1 FES B4002 1555 1555 2.37
LINK SG CYS B 113 FE1 FES B4001 1555 1555 2.36
LINK SG CYS B 116 FE2 FES B4001 1555 1555 2.35
LINK SG CYS B 148 FE2 FES B4001 1555 1555 2.38
LINK SG CYS B 150 FE1 FES B4001 1555 1555 2.39
LINK O ALA B 867 CA CA B4008 1555 1555 2.63
LINK O SER B 870 CA CA B4008 1555 1555 2.63
LINK O ARG B 871 CA CA B4008 1555 1555 2.96
LINK OG SER B 874 CA CA B4008 1555 1555 2.63
LINK OG SER B 907 CA CA B4008 1555 1555 2.67
LINK O ASN B 908 CA CA B4008 1555 1555 2.72
LINK S2' MTE B4003 MO MOS B4004 1555 1555 2.39
LINK S1' MTE B4003 MO MOS B4004 1555 1555 2.41
CISPEP 1 SER A 1298 PRO A 1299 0 0.02
CISPEP 2 SER B 1298 PRO B 1299 0 0.14
SITE 1 AC1 6 ALA A 867 SER A 870 ARG A 871 SER A 874
SITE 2 AC1 6 SER A 907 ASN A 908
SITE 1 AC2 6 ALA B 867 SER B 870 ARG B 871 SER B 874
SITE 2 AC2 6 SER B 907 ASN B 908
SITE 1 AC3 7 GLN A 112 CYS A 113 GLY A 114 CYS A 116
SITE 2 AC3 7 CYS A 148 ARG A 149 CYS A 150
SITE 1 AC4 10 GLY A 42 CYS A 43 GLY A 44 GLY A 46
SITE 2 AC4 10 GLY A 47 CYS A 48 GLY A 49 CYS A 51
SITE 3 AC4 10 ASN A 71 CYS A 73
SITE 1 AC5 22 GLN A 112 CYS A 150 GLY A 796 GLY A 797
SITE 2 AC5 22 PHE A 798 GLY A 799 ARG A 912 MET A1038
SITE 3 AC5 22 GLY A1039 GLN A1040 ALA A1078 ALA A1079
SITE 4 AC5 22 SER A1080 VAL A1081 SER A1082 GLN A1194
SITE 5 AC5 22 GLU A1261 MOS A3004 HOH A5020 HOH A5028
SITE 6 AC5 22 HOH A5052 HOH A5111
SITE 1 AC6 9 GLN A 767 GLY A 799 PHE A 911 ARG A 912
SITE 2 AC6 9 ALA A1078 ALA A1079 GLU A1261 MTE A3003
SITE 3 AC6 9 FYX A3006
SITE 1 AC7 34 GLU A 45 GLY A 46 LYS A 256 LEU A 257
SITE 2 AC7 34 VAL A 258 VAL A 259 GLY A 260 ASN A 261
SITE 3 AC7 34 THR A 262 GLU A 263 ILE A 264 ALA A 301
SITE 4 AC7 34 PHE A 337 ALA A 338 ALA A 346 SER A 347
SITE 5 AC7 34 GLY A 350 ASN A 351 ILE A 353 THR A 354
SITE 6 AC7 34 SER A 359 ASP A 360 ILE A 403 LEU A 404
SITE 7 AC7 34 LYS A 422 ASP A 429 HOH A5200 HOH A5235
SITE 8 AC7 34 HOH A5241 HOH A5364 HOH A5379 HOH A5584
SITE 9 AC7 34 HOH A6010 HOH A6062
SITE 1 AC8 13 ASN A 768 LYS A 771 GLU A 802 LEU A 873
SITE 2 AC8 13 ARG A 880 PHE A 914 PHE A1009 LEU A1014
SITE 3 AC8 13 ALA A1079 GLU A1261 MOS A3004 HOH A5593
SITE 4 AC8 13 HOH A5936
SITE 1 AC9 8 GLN B 112 CYS B 113 GLY B 114 CYS B 116
SITE 2 AC9 8 CYS B 148 ARG B 149 CYS B 150 LEU B 744
SITE 1 BC1 10 GLY B 42 CYS B 43 GLY B 44 GLY B 46
SITE 2 BC1 10 GLY B 47 CYS B 48 GLY B 49 CYS B 51
SITE 3 BC1 10 ASN B 71 CYS B 73
SITE 1 BC2 21 GLN B 112 CYS B 150 GLY B 796 GLY B 797
SITE 2 BC2 21 PHE B 798 GLY B 799 ARG B 912 MET B1038
SITE 3 BC2 21 GLY B1039 GLN B1040 ALA B1078 ALA B1079
SITE 4 BC2 21 SER B1080 VAL B1081 SER B1082 GLN B1194
SITE 5 BC2 21 GLU B1261 MOS B4004 HOH B5063 HOH B5065
SITE 6 BC2 21 HOH B5104
SITE 1 BC3 9 GLN B 767 GLY B 799 PHE B 911 ARG B 912
SITE 2 BC3 9 ALA B1078 ALA B1079 GLU B1261 MTE B4003
SITE 3 BC3 9 FYX B4006
SITE 1 BC4 33 GLU B 45 GLY B 46 LYS B 256 LEU B 257
SITE 2 BC4 33 VAL B 258 VAL B 259 GLY B 260 ASN B 261
SITE 3 BC4 33 THR B 262 GLU B 263 ILE B 264 ALA B 301
SITE 4 BC4 33 PHE B 337 ALA B 338 ALA B 346 SER B 347
SITE 5 BC4 33 GLY B 350 ASN B 351 ILE B 353 THR B 354
SITE 6 BC4 33 SER B 359 ASP B 360 LEU B 404 LYS B 422
SITE 7 BC4 33 ASP B 429 ASP B 430 HOH B5126 HOH B5191
SITE 8 BC4 33 HOH B5240 HOH B5252 HOH B5273 HOH B5474
SITE 9 BC4 33 HOH B5732
SITE 1 BC5 15 ASN B 768 GLU B 802 LEU B 873 SER B 876
SITE 2 BC5 15 ARG B 880 PHE B 914 PHE B1009 LEU B1014
SITE 3 BC5 15 PRO B1076 ALA B1078 ALA B1079 GLU B1261
SITE 4 BC5 15 MOS B4004 HOH B5486 HOH B5497
SITE 1 BC6 9 ARG A 839 HIS A 840 ILE A 877 THR A 909
SITE 2 BC6 9 ALA A 910 PHE A 911 PHE A 914 GLY A 915
SITE 3 BC6 9 GLN A 918
SITE 1 BC7 9 ARG B 839 HIS B 840 ILE B 877 THR B 909
SITE 2 BC7 9 ALA B 910 PHE B 911 PHE B 914 GLY B 915
SITE 3 BC7 9 GLN B 918
SITE 1 BC8 9 GLY A 664 HIS A 665 ILE A 666 ARG A 804
SITE 2 BC8 9 ASN A 869 SER A 906 SER A 907 HOH A5069
SITE 3 BC8 9 HOH A5801
SITE 1 BC9 9 GLY B 664 HIS B 665 ILE B 666 ARG B 804
SITE 2 BC9 9 ASN B 869 SER B 906 SER B 907 HOH B5048
SITE 3 BC9 9 HOH B5889
SITE 1 CC1 6 ASP A 594 ARG A 824 MET A 826 HOH A5160
SITE 2 CC1 6 HOH A5646 HOH A5885
SITE 1 CC2 6 ASP B 594 PHE B 604 ARG B 824 MET B 826
SITE 2 CC2 6 HOH B5185 HOH B5510
SITE 1 CC3 6 GLN A 561 GLY A 574 SER A1184 SER A1185
SITE 2 CC3 6 HOH A5327 HOH A5694
SITE 1 CC4 6 GLN B 561 GLY B 574 SER B1184 SER B1185
SITE 2 CC4 6 HOH B5222 HOH B5288
SITE 1 CC5 3 GLN A1088 TYR A1091 TYR A1254
SITE 1 CC6 5 GLN B1088 TYR B1091 ILE B1253 TYR B1254
SITE 2 CC6 5 HOH B5394
CRYST1 167.987 124.612 146.926 90.00 90.99 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 0.005953 0.000000 0.000103 0.00000
SCALE2 0.000000 0.008025 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006807 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
