HEADER OXIDOREDUCTASE 06-APR-09 3GYX
TITLE CRYSTAL STRUCTURE OF ADENYLYLSULFATE REDUCTASE FROM DESULFOVIBRIO
TITLE 2 GIGAS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENYLYLSULFATE REDUCTASE;
COMPND 3 CHAIN: A, C, E, G, I, K;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: ADENYLYLSULFATE REDUCTASE;
COMPND 6 CHAIN: B, D, F, H, J, L
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO GIGAS;
SOURCE 3 ORGANISM_TAXID: 879;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DESULFOVIBRIO GIGAS;
SOURCE 6 ORGANISM_TAXID: 879
KEYWDS ADENYLYLSULFATE REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.-L.CHIANG,Y.-C.HSIEH,E.-H.LIU,M.-Y.LIU,C.-J.CHEN
REVDAT 2 01-NOV-23 3GYX 1 REMARK
REVDAT 1 15-DEC-09 3GYX 0
JRNL AUTH Y.-L.CHIANG,Y.-C.HSIEH,J.-Y.FANG,E.-H.LIU,Y.-C.HUANG,
JRNL AUTH 2 P.CHUANKHAYAN,J.JEYAKANTHAN,M.-Y.LIU,S.I.CHAN,C.-J.CHEN
JRNL TITL CRYSTAL STRUCTURE OF ADENYLYLSULFATE REDUCTASE FROM
JRNL TITL 2 DESULFOVIBRIO GIGAS SUGGESTS A POTENTIAL SELF-REGULATION
JRNL TITL 3 MECHANISM INVOLVING THE C TERMINUS OF THE BETA-SUBUNIT
JRNL REF J.BACTERIOL. V. 191 7597 2009
JRNL REFN ISSN 0021-9193
JRNL PMID 19820092
JRNL DOI 10.1128/JB.00583-09
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 105084
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) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5561
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7755
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.2750
REMARK 3 BIN FREE R VALUE SET COUNT : 398
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 39054
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 414
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.28000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : -0.42000
REMARK 3 B12 (A**2) : 0.14000
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): 0.504
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.338
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.909
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.921
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 40580 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 54996 ; 1.048 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 4956 ; 5.230 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1836 ;34.913 ;23.725
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 6768 ;18.123 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 270 ;15.580 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 5724 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 30936 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 20208 ; 0.186 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 27466 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1322 ; 0.127 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 86 ; 0.156 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.078 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 25351 ; 0.224 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 39480 ; 0.406 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 17981 ; 0.394 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15372 ; 0.623 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3GYX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052480.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUL-07
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 : NSRRC
REMARK 200 BEAMLINE : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 122146
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.640
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.41000
REMARK 200 R SYM FOR SHELL (I) : 0.44600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.640
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1JNR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.27
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M TRIS, 1M
REMARK 280 GUANIDINE HYDROCHLORIDE, 0.2M SODIUM CHLORIDE, PH7.4, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 105.80733
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 211.61467
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 211.61467
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 105.80733
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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: 8790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 8920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
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: 8870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 350
REMARK 350 BIOMOLECULE: 4
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: 8860 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 350
REMARK 350 BIOMOLECULE: 5
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: 8970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -35.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
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 350
REMARK 350 BIOMOLECULE: 6
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: 8910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 NH1 ARG G 102 O ALA G 426 1.99
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 PRO B 161 C - N - CA ANGL. DEV. = 13.2 DEGREES
REMARK 500 PRO D 161 C - N - CA ANGL. DEV. = 12.4 DEGREES
REMARK 500 PRO F 161 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO K 10 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500 PRO L 161 C - N - CA ANGL. DEV. = 11.4 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 ARG A 11 -15.04 72.87
REMARK 500 ALA A 14 -66.80 -176.77
REMARK 500 ILE A 15 117.27 63.13
REMARK 500 ILE A 20 105.23 77.30
REMARK 500 ALA A 62 -156.06 -108.45
REMARK 500 TYR A 80 110.96 -161.43
REMARK 500 LEU A 81 -72.81 -71.20
REMARK 500 ASP A 83 -24.33 94.81
REMARK 500 ALA A 86 1.97 -66.28
REMARK 500 GLU A 132 -35.10 171.85
REMARK 500 LYS A 154 114.31 57.04
REMARK 500 ARG A 157 113.45 65.46
REMARK 500 ASP A 185 -21.73 -150.89
REMARK 500 LYS A 195 -68.83 -109.94
REMARK 500 LEU A 196 114.20 77.17
REMARK 500 ASN A 201 -82.67 -92.10
REMARK 500 ASP A 285 -40.97 69.06
REMARK 500 LYS A 327 116.49 -12.88
REMARK 500 HIS A 329 38.53 27.18
REMARK 500 ARG A 348 30.43 -91.18
REMARK 500 CYS A 386 83.64 -155.93
REMARK 500 CYS A 398 48.93 -109.46
REMARK 500 HIS A 418 -150.56 -81.90
REMARK 500 SER A 419 20.98 -71.72
REMARK 500 CYS A 421 18.93 -158.60
REMARK 500 ASP A 430 78.64 84.24
REMARK 500 ARG A 441 117.13 52.24
REMARK 500 ALA A 461 95.01 56.77
REMARK 500 ASP A 462 -28.64 81.16
REMARK 500 ALA A 466 11.12 59.12
REMARK 500 PHE A 471 -167.28 58.70
REMARK 500 ASP A 495 78.06 -107.97
REMARK 500 LYS A 497 92.14 55.63
REMARK 500 GLU A 615 50.18 -91.22
REMARK 500 SER A 617 79.26 -103.54
REMARK 500 CYS A 638 170.46 175.11
REMARK 500 PRO A 663 -170.73 -65.18
REMARK 500 CYS B 13 78.18 52.50
REMARK 500 GLU B 17 39.68 -54.87
REMARK 500 TYR B 67 113.43 -28.91
REMARK 500 PHE B 70 -20.41 -155.83
REMARK 500 THR B 133 -32.00 -131.33
REMARK 500 GLN B 147 122.87 67.47
REMARK 500 ASP B 150 -54.04 72.30
REMARK 500 ASP B 159 -31.23 96.52
REMARK 500 PRO B 161 -20.31 -17.58
REMARK 500 PRO C 10 -14.95 -43.66
REMARK 500 ARG C 11 -7.70 59.90
REMARK 500 VAL C 13 -75.11 -71.39
REMARK 500 ALA C 14 -69.74 -160.33
REMARK 500
REMARK 500 THIS ENTRY HAS 262 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 SF4 B2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 10 SG
REMARK 620 2 SF4 B2000 S1 112.3
REMARK 620 3 SF4 B2000 S2 119.1 104.7
REMARK 620 4 SF4 B2000 S3 109.8 105.6 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 21 SG
REMARK 620 2 SF4 B2000 S1 111.3
REMARK 620 3 SF4 B2000 S2 121.7 104.5
REMARK 620 4 SF4 B2000 S4 107.7 105.7 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 25 SG
REMARK 620 2 SF4 B1000 S1 109.5
REMARK 620 3 SF4 B1000 S2 120.2 105.9
REMARK 620 4 SF4 B1000 S3 110.2 104.5 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 47 SG
REMARK 620 2 SF4 B1000 S2 131.0
REMARK 620 3 SF4 B1000 S3 109.9 105.4
REMARK 620 4 SF4 B1000 S4 98.1 104.2 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 50 SG
REMARK 620 2 SF4 B1000 S1 111.8
REMARK 620 3 SF4 B1000 S2 105.8 105.9
REMARK 620 4 SF4 B1000 S4 122.6 105.4 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 53 SG
REMARK 620 2 SF4 B1000 S1 97.5
REMARK 620 3 SF4 B1000 S3 122.6 104.6
REMARK 620 4 SF4 B1000 S4 118.6 105.7 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 57 SG
REMARK 620 2 SF4 B2000 S2 118.2
REMARK 620 3 SF4 B2000 S3 113.1 103.9
REMARK 620 4 SF4 B2000 S4 109.5 104.6 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 10 SG
REMARK 620 2 SF4 D2000 S1 116.6
REMARK 620 3 SF4 D2000 S2 109.4 106.3
REMARK 620 4 SF4 D2000 S3 115.3 104.4 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D2000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 13 SG
REMARK 620 2 SF4 D2000 S1 121.5
REMARK 620 3 SF4 D2000 S3 114.6 104.4
REMARK 620 4 SF4 D2000 S4 103.9 105.3 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 21 SG
REMARK 620 2 SF4 D2000 S1 113.4
REMARK 620 3 SF4 D2000 S2 126.6 105.9
REMARK 620 4 SF4 D2000 S4 97.5 104.6 106.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 25 SG
REMARK 620 2 SF4 D1000 S1 99.7
REMARK 620 3 SF4 D1000 S2 115.2 106.3
REMARK 620 4 SF4 D1000 S3 124.6 105.5 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 47 SG
REMARK 620 2 SF4 D1000 S2 123.1
REMARK 620 3 SF4 D1000 S3 108.6 104.4
REMARK 620 4 SF4 D1000 S4 109.9 104.5 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 50 SG
REMARK 620 2 SF4 D1000 S1 108.6
REMARK 620 3 SF4 D1000 S2 118.7 105.9
REMARK 620 4 SF4 D1000 S4 112.7 105.8 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 53 SG
REMARK 620 2 SF4 D1000 S1 108.8
REMARK 620 3 SF4 D1000 S3 113.0 105.3
REMARK 620 4 SF4 D1000 S4 118.6 106.0 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 D2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 57 SG
REMARK 620 2 SF4 D2000 S2 118.7
REMARK 620 3 SF4 D2000 S3 106.8 103.2
REMARK 620 4 SF4 D2000 S4 114.4 106.4 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 10 SG
REMARK 620 2 SF4 F2000 S1 119.4
REMARK 620 3 SF4 F2000 S2 106.9 106.3
REMARK 620 4 SF4 F2000 S3 114.2 105.1 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F2000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 13 SG
REMARK 620 2 SF4 F2000 S1 117.7
REMARK 620 3 SF4 F2000 S3 114.3 105.1
REMARK 620 4 SF4 F2000 S4 107.1 106.6 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 21 SG
REMARK 620 2 SF4 F2000 S1 109.1
REMARK 620 3 SF4 F2000 S2 126.8 106.0
REMARK 620 4 SF4 F2000 S4 103.0 106.4 103.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 25 SG
REMARK 620 2 SF4 F1000 S1 120.8
REMARK 620 3 SF4 F1000 S2 129.5 104.8
REMARK 620 4 SF4 F1000 S3 83.9 105.2 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 47 SG
REMARK 620 2 SF4 F1000 S2 115.0
REMARK 620 3 SF4 F1000 S3 131.6 104.6
REMARK 620 4 SF4 F1000 S4 89.1 104.8 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 50 SG
REMARK 620 2 SF4 F1000 S1 85.9
REMARK 620 3 SF4 F1000 S2 112.0 104.5
REMARK 620 4 SF4 F1000 S4 137.2 104.7 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 53 SG
REMARK 620 2 SF4 F1000 S1 117.8
REMARK 620 3 SF4 F1000 S3 117.0 104.9
REMARK 620 4 SF4 F1000 S4 104.8 104.1 107.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 57 SG
REMARK 620 2 SF4 F2000 S2 119.5
REMARK 620 3 SF4 F2000 S3 110.9 103.7
REMARK 620 4 SF4 F2000 S4 111.2 104.5 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 10 SG
REMARK 620 2 SF4 H2000 S1 113.6
REMARK 620 3 SF4 H2000 S2 111.8 105.9
REMARK 620 4 SF4 H2000 S3 115.9 105.6 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H2000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 13 SG
REMARK 620 2 SF4 H2000 S1 115.8
REMARK 620 3 SF4 H2000 S3 122.8 105.1
REMARK 620 4 SF4 H2000 S4 100.0 106.5 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 21 SG
REMARK 620 2 SF4 H2000 S1 109.1
REMARK 620 3 SF4 H2000 S2 123.4 105.6
REMARK 620 4 SF4 H2000 S4 106.7 106.4 104.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 25 SG
REMARK 620 2 SF4 H1000 S1 105.0
REMARK 620 3 SF4 H1000 S2 127.7 105.2
REMARK 620 4 SF4 H1000 S3 106.3 106.0 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 47 SG
REMARK 620 2 SF4 H1000 S2 129.0
REMARK 620 3 SF4 H1000 S3 109.7 105.3
REMARK 620 4 SF4 H1000 S4 100.3 104.0 106.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 50 SG
REMARK 620 2 SF4 H1000 S1 112.6
REMARK 620 3 SF4 H1000 S2 105.2 105.4
REMARK 620 4 SF4 H1000 S4 122.7 105.2 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 53 SG
REMARK 620 2 SF4 H1000 S1 108.6
REMARK 620 3 SF4 H1000 S3 121.5 105.9
REMARK 620 4 SF4 H1000 S4 109.0 104.8 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 H2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 57 SG
REMARK 620 2 SF4 H2000 S2 117.0
REMARK 620 3 SF4 H2000 S3 111.8 103.1
REMARK 620 4 SF4 H2000 S4 113.1 105.2 105.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 10 SG
REMARK 620 2 SF4 J2000 S1 114.0
REMARK 620 3 SF4 J2000 S2 114.2 105.7
REMARK 620 4 SF4 J2000 S3 112.6 105.5 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J2000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 13 SG
REMARK 620 2 SF4 J2000 S1 128.6
REMARK 620 3 SF4 J2000 S3 113.9 105.1
REMARK 620 4 SF4 J2000 S4 94.5 106.7 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 21 SG
REMARK 620 2 SF4 J2000 S1 107.1
REMARK 620 3 SF4 J2000 S2 128.8 105.4
REMARK 620 4 SF4 J2000 S4 102.1 106.7 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 25 SG
REMARK 620 2 SF4 J1000 S1 111.2
REMARK 620 3 SF4 J1000 S2 124.3 103.9
REMARK 620 4 SF4 J1000 S3 105.2 106.0 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 47 SG
REMARK 620 2 SF4 J1000 S2 128.2
REMARK 620 3 SF4 J1000 S3 111.9 105.0
REMARK 620 4 SF4 J1000 S4 99.8 105.0 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 50 SG
REMARK 620 2 SF4 J1000 S1 108.7
REMARK 620 3 SF4 J1000 S2 99.2 103.7
REMARK 620 4 SF4 J1000 S4 131.2 105.9 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 53 SG
REMARK 620 2 SF4 J1000 S1 112.4
REMARK 620 3 SF4 J1000 S3 126.9 105.8
REMARK 620 4 SF4 J1000 S4 99.5 105.7 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 57 SG
REMARK 620 2 SF4 J2000 S2 118.1
REMARK 620 3 SF4 J2000 S3 110.1 103.7
REMARK 620 4 SF4 J2000 S4 112.5 105.6 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L2000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 10 SG
REMARK 620 2 SF4 L2000 S1 116.8
REMARK 620 3 SF4 L2000 S2 110.5 104.7
REMARK 620 4 SF4 L2000 S3 113.8 105.3 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L2000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 13 SG
REMARK 620 2 SF4 L2000 S1 113.9
REMARK 620 3 SF4 L2000 S3 117.6 104.9
REMARK 620 4 SF4 L2000 S4 108.1 106.6 105.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L2000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 21 SG
REMARK 620 2 SF4 L2000 S1 107.0
REMARK 620 3 SF4 L2000 S2 126.1 104.6
REMARK 620 4 SF4 L2000 S4 107.1 106.6 104.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L1000 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 25 SG
REMARK 620 2 SF4 L1000 S1 112.9
REMARK 620 3 SF4 L1000 S2 114.0 106.3
REMARK 620 4 SF4 L1000 S3 113.9 105.1 103.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L1000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 47 SG
REMARK 620 2 SF4 L1000 S2 142.2
REMARK 620 3 SF4 L1000 S3 99.0 103.6
REMARK 620 4 SF4 L1000 S4 97.0 104.9 106.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L1000 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 50 SG
REMARK 620 2 SF4 L1000 S1 122.9
REMARK 620 3 SF4 L1000 S2 102.7 106.1
REMARK 620 4 SF4 L1000 S4 113.1 106.0 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L1000 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 53 SG
REMARK 620 2 SF4 L1000 S1 96.6
REMARK 620 3 SF4 L1000 S3 121.4 104.7
REMARK 620 4 SF4 L1000 S4 119.4 106.1 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 L2000 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L 57 SG
REMARK 620 2 SF4 L2000 S2 129.2
REMARK 620 3 SF4 L2000 S3 110.2 104.5
REMARK 620 4 SF4 L2000 S4 100.5 104.6 105.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 D 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD G 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 H 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 H 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 2000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD K 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 L 1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 L 2000
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN
REMARK 999 DOES NOT CURRENTLY EXIST.
REMARK 999 THIS SEQUENCE WILL BE DEPOSITED IN THE SEQUENCE DATABASE.
DBREF 3GYX A 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX B 2 167 PDB 3GYX 3GYX 2 167
DBREF 3GYX C 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX D 2 167 PDB 3GYX 3GYX 2 167
DBREF 3GYX E 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX F 2 167 PDB 3GYX 3GYX 2 167
DBREF 3GYX G 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX H 2 167 PDB 3GYX 3GYX 2 167
DBREF 3GYX I 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX J 2 167 PDB 3GYX 3GYX 2 167
DBREF 3GYX K 3 664 PDB 3GYX 3GYX 3 664
DBREF 3GYX L 2 167 PDB 3GYX 3GYX 2 167
SEQRES 1 A 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 A 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 A 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 A 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 A 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 A 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 A 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 A 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 A 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 A 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 A 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 A 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 A 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 A 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 A 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 A 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 A 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 A 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 A 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 A 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 A 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 A 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 A 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 A 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 A 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 A 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 A 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 A 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 A 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 A 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 A 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 A 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 A 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 A 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 A 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 A 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 A 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 A 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 A 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 A 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 A 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 A 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 A 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 A 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 A 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 A 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 A 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 A 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 A 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 A 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 A 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 B 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 B 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 B 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 B 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 B 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 B 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 B 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 B 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 B 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 B 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 B 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 B 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 B 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
SEQRES 1 C 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 C 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 C 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 C 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 C 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 C 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 C 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 C 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 C 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 C 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 C 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 C 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 C 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 C 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 C 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 C 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 C 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 C 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 C 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 C 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 C 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 C 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 C 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 C 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 C 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 C 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 C 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 C 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 C 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 C 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 C 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 C 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 C 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 C 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 C 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 C 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 C 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 C 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 C 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 C 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 C 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 C 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 C 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 C 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 C 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 C 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 C 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 C 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 C 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 C 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 C 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 D 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 D 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 D 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 D 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 D 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 D 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 D 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 D 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 D 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 D 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 D 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 D 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 D 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
SEQRES 1 E 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 E 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 E 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 E 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 E 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 E 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 E 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 E 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 E 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 E 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 E 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 E 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 E 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 E 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 E 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 E 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 E 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 E 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 E 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 E 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 E 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 E 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 E 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 E 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 E 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 E 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 E 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 E 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 E 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 E 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 E 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 E 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 E 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 E 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 E 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 E 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 E 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 E 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 E 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 E 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 E 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 E 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 E 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 E 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 E 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 E 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 E 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 E 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 E 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 E 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 E 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 F 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 F 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 F 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 F 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 F 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 F 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 F 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 F 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 F 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 F 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 F 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 F 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 F 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
SEQRES 1 G 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 G 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 G 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 G 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 G 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 G 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 G 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 G 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 G 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 G 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 G 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 G 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 G 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 G 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 G 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 G 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 G 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 G 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 G 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 G 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 G 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 G 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 G 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 G 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 G 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 G 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 G 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 G 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 G 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 G 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 G 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 G 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 G 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 G 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 G 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 G 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 G 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 G 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 G 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 G 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 G 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 G 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 G 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 G 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 G 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 G 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 G 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 G 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 G 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 G 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 G 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 H 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 H 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 H 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 H 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 H 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 H 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 H 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 H 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 H 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 H 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 H 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 H 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 H 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
SEQRES 1 I 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 I 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 I 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 I 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 I 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 I 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 I 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 I 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 I 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 I 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 I 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 I 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 I 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 I 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 I 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 I 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 I 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 I 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 I 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 I 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 I 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 I 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 I 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 I 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 I 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 I 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 I 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 I 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 I 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 I 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 I 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 I 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 I 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 I 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 I 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 I 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 I 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 I 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 I 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 I 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 I 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 I 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 I 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 I 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 I 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 I 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 I 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 I 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 I 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 I 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 I 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 J 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 J 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 J 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 J 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 J 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 J 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 J 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 J 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 J 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 J 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 J 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 J 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 J 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
SEQRES 1 K 662 LYS ILE PRO SER LYS GLU THR PRO ARG GLY VAL ALA ILE
SEQRES 2 K 662 ALA GLU PRO ILE ILE VAL GLU HIS SER VAL ASP LEU LEU
SEQRES 3 K 662 MET VAL GLY GLY GLY MET GLY ASN CYS GLY ALA ALA PHE
SEQRES 4 K 662 GLU ALA VAL ARG TRP ALA ASP LYS TYR ALA PRO GLU ALA
SEQRES 5 K 662 LYS ILE LEU LEU VAL ASP LYS ALA SER LEU GLU ARG SER
SEQRES 6 K 662 GLY ALA VAL ALA GLN GLY LEU SER ALA ILE ASN THR TYR
SEQRES 7 K 662 LEU GLY ASP ASN ASN ALA ASP ASP TYR VAL ARG MET VAL
SEQRES 8 K 662 ARG THR ASP LEU MET GLY LEU VAL ARG GLU ASP LEU ILE
SEQRES 9 K 662 TYR ASP LEU GLY ARG HIS VAL ASP ASP SER VAL HIS LEU
SEQRES 10 K 662 PHE GLU GLU TRP GLY LEU PRO VAL TRP ILE LYS ASP GLU
SEQRES 11 K 662 HIS GLY HIS ASN LEU ASP GLY ALA GLN ALA LYS ALA ALA
SEQRES 12 K 662 GLY LYS SER LEU ARG ASN GLY ASP LYS PRO VAL ARG SER
SEQRES 13 K 662 GLY ARG TRP GLN ILE MET ILE ASN GLY GLU SER TYR LYS
SEQRES 14 K 662 VAL ILE VAL ALA GLU ALA ALA LYS ASN ALA LEU GLY GLN
SEQRES 15 K 662 ASP ARG ILE ILE GLU ARG ILE PHE ILE VAL LYS LEU LEU
SEQRES 16 K 662 LEU ASP LYS ASN THR PRO ASN ARG ILE ALA GLY ALA VAL
SEQRES 17 K 662 GLY PHE ASN LEU ARG ALA ASN GLU VAL HIS ILE PHE LYS
SEQRES 18 K 662 ALA ASN ALA MET VAL VAL ALA CYS GLY GLY ALA VAL ASN
SEQRES 19 K 662 VAL TYR ARG PRO ARG SER VAL GLY GLU GLY MET GLY ARG
SEQRES 20 K 662 ALA TRP TYR PRO VAL TRP ASN ALA GLY SER THR TYR THR
SEQRES 21 K 662 MET CYS ALA GLN VAL GLY ALA GLU MET THR MET MET GLU
SEQRES 22 K 662 ASN ARG PHE VAL PRO ALA ARG PHE LYS ASP GLY TYR GLY
SEQRES 23 K 662 PRO VAL GLY ALA TRP PHE LEU LEU PHE LYS ALA LYS ALA
SEQRES 24 K 662 THR ASN CYS LYS GLY GLU ASP TYR CYS ALA THR ASN ARG
SEQRES 25 K 662 ALA MET LEU LYS PRO TYR GLU GLU ARG GLY TYR ALA LYS
SEQRES 26 K 662 GLY HIS VAL ILE PRO THR CYS LEU ARG ASN HIS MET MET
SEQRES 27 K 662 LEU ARG GLU MET ARG GLU GLY ARG GLY PRO ILE TYR MET
SEQRES 28 K 662 ASP THR LYS THR ALA LEU GLN THR SER PHE ALA THR MET
SEQRES 29 K 662 SER PRO ALA GLN GLN LYS HIS LEU GLU ALA GLU ALA TRP
SEQRES 30 K 662 GLU ASP PHE LEU ASP MET CYS VAL GLY GLN ALA ASN LEU
SEQRES 31 K 662 TRP ALA ALA THR ASN CYS ALA PRO GLU GLU ARG GLY SER
SEQRES 32 K 662 GLU ILE MET PRO THR GLU PRO TYR LEU LEU GLY SER HIS
SEQRES 33 K 662 SER GLY CYS CYS GLY ILE TRP ALA SER GLY PRO ASP GLU
SEQRES 34 K 662 ALA TRP VAL PRO GLU ASP TYR LYS VAL ARG ALA ALA ASN
SEQRES 35 K 662 GLY LYS VAL TYR ASN ARG MET THR THR VAL GLU GLY LEU
SEQRES 36 K 662 TRP THR CYS ALA ASP GLY VAL GLY ALA SER GLY HIS LYS
SEQRES 37 K 662 PHE SER SER GLY SER HIS ALA GLU GLY ARG ILE VAL GLY
SEQRES 38 K 662 LYS GLN MET VAL ARG TRP TYR LEU ASP HIS LYS ASP PHE
SEQRES 39 K 662 LYS PRO GLU PHE VAL GLU THR ALA GLU GLU LEU LYS THR
SEQRES 40 K 662 LEU ILE TYR ARG PRO TYR TYR ASN TYR GLU LYS GLY LYS
SEQRES 41 K 662 GLY ALA SER THR CYS PRO VAL VAL ASN PRO GLU TYR ILE
SEQRES 42 K 662 SER PRO LYS ASN PHE MET MET ARG LEU ILE LYS CYS THR
SEQRES 43 K 662 ASP GLU TYR GLY GLY GLY VAL GLY THR TYR TYR ASN THR
SEQRES 44 K 662 SER LYS ALA LEU LEU ASP THR GLY PHE TRP LEU MET GLU
SEQRES 45 K 662 MET LEU GLU GLU ASP SER LEU LYS LEU ALA ALA ARG ASP
SEQRES 46 K 662 LEU HIS GLU LEU LEU ARG CYS TRP GLU ASN TYR HIS ARG
SEQRES 47 K 662 LEU TRP THR VAL ARG LEU HIS MET GLN HIS ILE ALA PHE
SEQRES 48 K 662 ARG GLU GLU SER ARG TYR PRO GLY PHE TYR TYR ARG ALA
SEQRES 49 K 662 ASP PHE LEU GLY LEU ASP ASP SER LYS TRP LYS CYS PHE
SEQRES 50 K 662 VAL ASN SER LYS TYR ASP PRO ALA LYS LYS GLU THR LYS
SEQRES 51 K 662 ILE PHE LYS LYS PRO TYR TYR GLN ILE ILE PRO ASP
SEQRES 1 L 166 PRO THR TYR VAL ASP PRO SER LYS CYS ASP GLY CYS LYS
SEQRES 2 L 166 GLY GLY GLU LYS THR ALA CYS MET TYR ILE CYS PRO ASN
SEQRES 3 L 166 ASP LEU MET ILE LEU ASP PRO GLU GLU MET LYS ALA PHE
SEQRES 4 L 166 ASN GLN GLU PRO GLU ALA CYS TRP GLU CYS TYR SER CYS
SEQRES 5 L 166 ILE LYS ILE CYS PRO GLN GLY ALA ILE THR ALA ARG PRO
SEQRES 6 L 166 TYR ALA ASP PHE ALA PRO MET GLY GLY THR CYS ILE PRO
SEQRES 7 L 166 LEU ARG GLY SER GLU ASP ILE MET TRP THR ILE LYS PHE
SEQRES 8 L 166 ARG ASN GLY SER VAL LYS ARG PHE LYS PHE PRO ILE ARG
SEQRES 9 L 166 THR THR PRO GLU GLY SER ILE LYS PRO PHE GLU GLY LYS
SEQRES 10 L 166 PRO GLU ALA GLY ASP LEU GLU ASN GLU LEU LEU PHE THR
SEQRES 11 L 166 GLU THR ALA LEU THR VAL PRO GLN VAL ALA LEU GLY GLN
SEQRES 12 L 166 LYS ALA GLN ILE ALA ASP ALA GLU THR SER GLN CYS TRP
SEQRES 13 L 166 PHE ASP LEU PRO CYS GLU GLY GLY ASN ARG
HET FAD A1000 53
HET SF4 B1000 8
HET SF4 B2000 8
HET FAD C1000 53
HET SF4 D1000 8
HET SF4 D2000 8
HET FAD E1000 53
HET SF4 F1000 8
HET SF4 F2000 8
HET FAD G1000 53
HET SF4 H1000 8
HET SF4 H2000 8
HET FAD I1000 53
HET SF4 J1000 8
HET SF4 J2000 8
HET FAD K1000 53
HET SF4 L1000 8
HET SF4 L2000 8
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SF4 IRON/SULFUR CLUSTER
FORMUL 13 FAD 6(C27 H33 N9 O15 P2)
FORMUL 14 SF4 12(FE4 S4)
FORMUL 31 HOH *69(H2 O)
HELIX 1 1 ILE A 4 GLU A 8 5 5
HELIX 2 2 GLY A 33 ALA A 51 1 19
HELIX 3 3 ASN A 85 LEU A 97 1 13
HELIX 4 4 ARG A 102 GLY A 124 1 23
HELIX 5 5 ASP A 138 GLY A 146 1 9
HELIX 6 6 SER A 169 GLY A 183 1 15
HELIX 7 7 GLY A 244 ARG A 249 5 6
HELIX 8 8 GLY A 258 GLN A 266 1 9
HELIX 9 9 VAL A 290 LYS A 298 1 9
HELIX 10 10 ASP A 308 ASN A 313 1 6
HELIX 11 11 ARG A 314 MET A 316 5 3
HELIX 12 12 LEU A 317 GLU A 322 1 6
HELIX 13 13 PRO A 332 ASN A 337 1 6
HELIX 14 14 ASN A 337 GLU A 346 1 10
HELIX 15 15 ASP A 354 PHE A 363 1 10
HELIX 16 16 SER A 367 ASP A 384 1 18
HELIX 17 17 CYS A 386 THR A 396 1 11
HELIX 18 18 PRO A 435 LYS A 439 5 5
HELIX 19 19 LYS A 470 HIS A 493 1 24
HELIX 20 20 THR A 503 TYR A 512 1 10
HELIX 21 21 TYR A 512 LYS A 522 1 11
HELIX 22 22 GLY A 523 SER A 525 5 3
HELIX 23 23 SER A 536 GLY A 552 1 17
HELIX 24 24 SER A 562 SER A 580 1 19
HELIX 25 25 LEU A 581 LEU A 583 5 3
HELIX 26 26 ASP A 587 ARG A 614 1 28
HELIX 27 27 THR B 19 CYS B 25 1 7
HELIX 28 28 GLU B 43 CYS B 47 5 5
HELIX 29 29 TYR B 51 CYS B 57 1 7
HELIX 30 30 ILE C 4 GLU C 8 5 5
HELIX 31 31 GLY C 33 ALA C 51 1 19
HELIX 32 32 ASN C 85 LEU C 97 1 13
HELIX 33 33 ARG C 102 GLY C 124 1 23
HELIX 34 34 ASP C 138 ALA C 144 1 7
HELIX 35 35 SER C 169 GLY C 183 1 15
HELIX 36 36 GLY C 244 ARG C 249 5 6
HELIX 37 37 GLY C 258 GLN C 266 1 9
HELIX 38 38 VAL C 290 LYS C 298 1 9
HELIX 39 39 ASP C 308 ASN C 313 1 6
HELIX 40 40 ARG C 314 MET C 316 5 3
HELIX 41 41 LEU C 317 GLU C 322 1 6
HELIX 42 42 PRO C 332 GLU C 346 1 15
HELIX 43 43 ASP C 354 ALA C 364 1 11
HELIX 44 44 SER C 367 ASP C 384 1 18
HELIX 45 45 CYS C 386 ASN C 397 1 12
HELIX 46 46 PRO C 435 LYS C 439 5 5
HELIX 47 47 LYS C 470 HIS C 493 1 24
HELIX 48 48 THR C 503 TYR C 512 1 10
HELIX 49 49 TYR C 512 LYS C 522 1 11
HELIX 50 50 GLY C 523 SER C 525 5 3
HELIX 51 51 SER C 536 GLY C 552 1 17
HELIX 52 52 GLY C 554 TYR C 558 5 5
HELIX 53 53 SER C 562 LEU C 581 1 20
HELIX 54 54 ASP C 587 ARG C 614 1 28
HELIX 55 55 ASP C 632 LYS C 637 1 6
HELIX 56 56 THR D 19 CYS D 25 1 7
HELIX 57 57 GLU D 43 CYS D 47 5 5
HELIX 58 58 TYR D 51 CYS D 57 1 7
HELIX 59 59 ILE E 4 GLU E 8 5 5
HELIX 60 60 GLY E 33 LYS E 49 1 17
HELIX 61 61 ASN E 85 LEU E 97 1 13
HELIX 62 62 ARG E 102 ARG E 111 1 10
HELIX 63 63 HIS E 112 GLY E 124 1 13
HELIX 64 64 ASP E 138 ALA E 145 1 8
HELIX 65 65 SER E 148 GLY E 152 5 5
HELIX 66 66 SER E 169 GLY E 183 1 15
HELIX 67 67 GLY E 244 ARG E 249 5 6
HELIX 68 68 GLY E 258 GLN E 266 1 9
HELIX 69 69 GLY E 291 PHE E 297 1 7
HELIX 70 70 ASP E 308 ASN E 313 1 6
HELIX 71 71 ARG E 314 MET E 316 5 3
HELIX 72 72 LEU E 317 ARG E 323 1 7
HELIX 73 73 PRO E 332 GLY E 347 1 16
HELIX 74 74 ASP E 354 PHE E 363 1 10
HELIX 75 75 MET E 366 CYS E 386 1 21
HELIX 76 76 CYS E 386 ASN E 397 1 12
HELIX 77 77 PRO E 435 LYS E 439 5 5
HELIX 78 78 LYS E 470 HIS E 493 1 24
HELIX 79 79 LEU E 507 TYR E 512 1 6
HELIX 80 80 TYR E 512 LYS E 522 1 11
HELIX 81 81 GLY E 523 SER E 525 5 3
HELIX 82 82 SER E 536 GLY E 552 1 17
HELIX 83 83 GLY E 554 TYR E 558 5 5
HELIX 84 84 SER E 562 LEU E 581 1 20
HELIX 85 85 ASP E 587 ARG E 614 1 28
HELIX 86 86 ASP E 632 LYS E 637 1 6
HELIX 87 87 THR F 19 CYS F 25 1 7
HELIX 88 88 GLU F 43 CYS F 47 5 5
HELIX 89 89 TYR F 51 CYS F 57 1 7
HELIX 90 90 ILE G 4 GLU G 8 5 5
HELIX 91 91 GLY G 33 ALA G 51 1 19
HELIX 92 92 ASN G 85 LEU G 97 1 13
HELIX 93 93 ARG G 102 ARG G 111 1 10
HELIX 94 94 HIS G 112 GLY G 124 1 13
HELIX 95 95 SER G 169 GLY G 183 1 15
HELIX 96 96 GLY G 244 ARG G 249 5 6
HELIX 97 97 GLY G 258 GLN G 266 1 9
HELIX 98 98 VAL G 290 LYS G 298 1 9
HELIX 99 99 ASP G 308 ASN G 313 1 6
HELIX 100 100 ARG G 314 MET G 316 5 3
HELIX 101 101 LEU G 317 GLU G 322 1 6
HELIX 102 102 PRO G 332 GLU G 346 1 15
HELIX 103 103 ASP G 354 PHE G 363 1 10
HELIX 104 104 SER G 367 TRP G 379 1 13
HELIX 105 105 TRP G 379 ASP G 384 1 6
HELIX 106 106 CYS G 386 THR G 396 1 11
HELIX 107 107 LYS G 470 HIS G 493 1 24
HELIX 108 108 GLU G 505 TYR G 512 1 8
HELIX 109 109 TYR G 512 LYS G 522 1 11
HELIX 110 110 GLY G 523 SER G 525 5 3
HELIX 111 111 SER G 536 GLY G 552 1 17
HELIX 112 112 GLY G 554 TYR G 558 5 5
HELIX 113 113 SER G 562 LEU G 581 1 20
HELIX 114 114 ASP G 587 ARG G 614 1 28
HELIX 115 115 ASP G 632 LYS G 637 1 6
HELIX 116 116 THR H 19 CYS H 25 1 7
HELIX 117 117 GLU H 43 CYS H 47 5 5
HELIX 118 118 TYR H 51 CYS H 57 1 7
HELIX 119 119 ILE I 4 GLU I 8 5 5
HELIX 120 120 GLY I 33 ALA I 51 1 19
HELIX 121 121 ASN I 85 LEU I 97 1 13
HELIX 122 122 ARG I 102 ARG I 111 1 10
HELIX 123 123 HIS I 112 GLY I 124 1 13
HELIX 124 124 ASP I 138 ALA I 144 1 7
HELIX 125 125 SER I 169 GLY I 183 1 15
HELIX 126 126 GLY I 244 ARG I 249 5 6
HELIX 127 127 GLY I 258 GLN I 266 1 9
HELIX 128 128 VAL I 290 LYS I 298 1 9
HELIX 129 129 ASP I 308 ASN I 313 1 6
HELIX 130 130 ARG I 314 MET I 316 5 3
HELIX 131 131 LEU I 317 ARG I 323 1 7
HELIX 132 132 PRO I 332 GLU I 346 1 15
HELIX 133 133 ASP I 354 THR I 365 1 12
HELIX 134 134 SER I 367 ASP I 384 1 18
HELIX 135 135 CYS I 386 THR I 396 1 11
HELIX 136 136 ALA I 461 VAL I 464 5 4
HELIX 137 137 LYS I 470 HIS I 493 1 24
HELIX 138 138 GLU I 505 TYR I 512 1 8
HELIX 139 139 TYR I 512 LYS I 522 1 11
HELIX 140 140 GLY I 523 SER I 525 5 3
HELIX 141 141 SER I 536 GLY I 552 1 17
HELIX 142 142 SER I 562 LEU I 581 1 20
HELIX 143 143 ASP I 587 ARG I 614 1 28
HELIX 144 144 ASP I 632 LYS I 637 1 6
HELIX 145 145 THR J 19 CYS J 25 1 7
HELIX 146 146 GLU J 43 CYS J 47 5 5
HELIX 147 147 TYR J 51 CYS J 57 1 7
HELIX 148 148 ILE K 4 GLU K 8 5 5
HELIX 149 149 GLY K 35 ALA K 51 1 17
HELIX 150 150 ASN K 85 LEU K 97 1 13
HELIX 151 151 ARG K 102 GLY K 124 1 23
HELIX 152 152 ASP K 138 ALA K 145 1 8
HELIX 153 153 SER K 169 GLY K 183 1 15
HELIX 154 154 GLY K 244 ARG K 249 5 6
HELIX 155 155 GLY K 258 GLN K 266 1 9
HELIX 156 156 VAL K 290 LYS K 298 1 9
HELIX 157 157 ASP K 308 ASN K 313 1 6
HELIX 158 158 ARG K 314 MET K 316 5 3
HELIX 159 159 LEU K 317 GLU K 322 1 6
HELIX 160 160 PRO K 332 GLU K 346 1 15
HELIX 161 161 THR K 355 ALA K 364 1 10
HELIX 162 162 SER K 367 ASP K 384 1 18
HELIX 163 163 CYS K 386 THR K 396 1 11
HELIX 164 164 PRO K 435 LYS K 439 5 5
HELIX 165 165 LYS K 470 HIS K 493 1 24
HELIX 166 166 THR K 503 TYR K 512 1 10
HELIX 167 167 TYR K 512 LYS K 522 1 11
HELIX 168 168 GLY K 523 SER K 525 5 3
HELIX 169 169 SER K 536 GLY K 552 1 17
HELIX 170 170 GLY K 554 TYR K 558 5 5
HELIX 171 171 SER K 562 SER K 580 1 19
HELIX 172 172 LEU K 581 LEU K 583 5 3
HELIX 173 173 ASP K 587 ARG K 614 1 28
HELIX 174 174 ASP K 632 LYS K 637 1 6
HELIX 175 175 THR L 19 CYS L 25 1 7
HELIX 176 176 GLU L 43 CYS L 47 5 5
HELIX 177 177 TYR L 51 CYS L 57 1 7
SHEET 1 A 4 VAL A 21 SER A 24 0
SHEET 2 A 4 VAL A 219 LYS A 223 1 O LYS A 223 N HIS A 23
SHEET 3 A 4 ILE A 206 ASN A 213 -1 N ALA A 209 O PHE A 222
SHEET 4 A 4 ILE A 191 ILE A 193 -1 N PHE A 192 O PHE A 212
SHEET 1 B 4 VAL A 21 SER A 24 0
SHEET 2 B 4 VAL A 219 LYS A 223 1 O LYS A 223 N HIS A 23
SHEET 3 B 4 ILE A 206 ASN A 213 -1 N ALA A 209 O PHE A 222
SHEET 4 B 4 LEU A 197 LEU A 198 -1 N LEU A 197 O GLY A 208
SHEET 1 C 5 ILE A 187 ILE A 188 0
SHEET 2 C 5 ILE A 56 VAL A 59 1 N LEU A 58 O ILE A 188
SHEET 3 C 5 LEU A 27 VAL A 30 1 N MET A 29 O VAL A 59
SHEET 4 C 5 ALA A 226 VAL A 229 1 O VAL A 228 N VAL A 30
SHEET 5 C 5 LEU A 457 TRP A 458 1 O TRP A 458 N MET A 227
SHEET 1 D 2 LEU A 74 ILE A 77 0
SHEET 2 D 2 ILE A 163 GLY A 167 -1 O GLY A 167 N LEU A 74
SHEET 1 E 2 ILE A 129 LYS A 130 0
SHEET 2 E 2 ASN A 136 LEU A 137 -1 O LEU A 137 N ILE A 129
SHEET 1 F 4 GLY A 423 ILE A 424 0
SHEET 2 F 4 GLU A 270 THR A 272 -1 N THR A 272 O GLY A 423
SHEET 3 F 4 PHE A 639 ASP A 645 -1 O SER A 642 N MET A 271
SHEET 4 F 4 GLU A 650 LYS A 656 -1 O LYS A 656 N PHE A 639
SHEET 1 G 4 ALA A 281 PHE A 283 0
SHEET 2 G 4 SER A 405 PRO A 409 -1 O MET A 408 N ARG A 282
SHEET 3 G 4 TYR A 352 MET A 353 -1 N MET A 353 O SER A 405
SHEET 4 G 4 ALA A 301 THR A 302 -1 N THR A 302 O TYR A 352
SHEET 1 H 2 ASN A 560 THR A 561 0
SHEET 2 H 2 TYR A 624 ARG A 625 1 O TYR A 624 N THR A 561
SHEET 1 I 2 TYR A 659 GLN A 660 0
SHEET 2 I 2 GLN B 144 LYS B 145 -1 O GLN B 144 N GLN A 660
SHEET 1 J 2 THR B 3 VAL B 5 0
SHEET 2 J 2 ILE B 62 ALA B 64 -1 O THR B 63 N TYR B 4
SHEET 1 K 2 MET B 30 ASP B 33 0
SHEET 2 K 2 LYS B 38 ASN B 41 -1 O LYS B 38 N ASP B 33
SHEET 1 L 3 THR B 76 ARG B 81 0
SHEET 2 L 3 ASP B 85 LYS B 91 -1 O LYS B 91 N THR B 76
SHEET 3 L 3 VAL B 97 PRO B 103 -1 O LYS B 98 N ILE B 90
SHEET 1 M 4 VAL C 21 SER C 24 0
SHEET 2 M 4 VAL C 219 LYS C 223 1 O LYS C 223 N HIS C 23
SHEET 3 M 4 ILE C 206 ASN C 213 -1 N GLY C 211 O HIS C 220
SHEET 4 M 4 ILE C 191 LEU C 198 -1 N LEU C 197 O GLY C 208
SHEET 1 N 5 ILE C 187 ILE C 188 0
SHEET 2 N 5 ILE C 56 VAL C 59 1 N LEU C 58 O ILE C 188
SHEET 3 N 5 LEU C 27 VAL C 30 1 N MET C 29 O VAL C 59
SHEET 4 N 5 ALA C 226 VAL C 229 1 O VAL C 228 N VAL C 30
SHEET 5 N 5 LEU C 457 TRP C 458 1 O TRP C 458 N MET C 227
SHEET 1 O 2 LEU C 74 ILE C 77 0
SHEET 2 O 2 ILE C 163 GLY C 167 -1 O ILE C 163 N ILE C 77
SHEET 1 P 2 ILE C 129 LYS C 130 0
SHEET 2 P 2 ASN C 136 LEU C 137 -1 O LEU C 137 N ILE C 129
SHEET 1 Q 4 GLY C 423 ILE C 424 0
SHEET 2 Q 4 MET C 271 THR C 272 -1 N THR C 272 O GLY C 423
SHEET 3 Q 4 PHE C 639 ASP C 645 -1 O SER C 642 N MET C 271
SHEET 4 Q 4 GLU C 650 LYS C 656 -1 O LYS C 656 N PHE C 639
SHEET 1 R 4 ALA C 281 PHE C 283 0
SHEET 2 R 4 SER C 405 PRO C 409 -1 O MET C 408 N ARG C 282
SHEET 3 R 4 TYR C 352 MET C 353 -1 N MET C 353 O SER C 405
SHEET 4 R 4 ALA C 301 THR C 302 -1 N THR C 302 O TYR C 352
SHEET 1 S 2 ASN C 560 THR C 561 0
SHEET 2 S 2 TYR C 624 ARG C 625 1 O TYR C 624 N THR C 561
SHEET 1 T 2 TYR C 659 GLN C 660 0
SHEET 2 T 2 GLN D 144 LYS D 145 -1 O GLN D 144 N GLN C 660
SHEET 1 U 2 THR D 3 VAL D 5 0
SHEET 2 U 2 ILE D 62 ALA D 64 -1 O THR D 63 N TYR D 4
SHEET 1 V 2 MET D 30 ASP D 33 0
SHEET 2 V 2 LYS D 38 ASN D 41 -1 O LYS D 38 N ASP D 33
SHEET 1 W 3 THR D 76 ARG D 81 0
SHEET 2 W 3 ASP D 85 LYS D 91 -1 O THR D 89 N ILE D 78
SHEET 3 W 3 VAL D 97 PRO D 103 -1 O LYS D 98 N ILE D 90
SHEET 1 X 4 VAL E 21 SER E 24 0
SHEET 2 X 4 VAL E 219 LYS E 223 1 O VAL E 219 N VAL E 21
SHEET 3 X 4 ILE E 206 ASN E 213 -1 N ALA E 209 O PHE E 222
SHEET 4 X 4 ILE E 191 LEU E 198 -1 N VAL E 194 O VAL E 210
SHEET 1 Y 5 ILE E 187 ILE E 188 0
SHEET 2 Y 5 ILE E 56 VAL E 59 1 N LEU E 58 O ILE E 188
SHEET 3 Y 5 LEU E 27 VAL E 30 1 N MET E 29 O VAL E 59
SHEET 4 Y 5 ALA E 226 VAL E 229 1 O VAL E 228 N VAL E 30
SHEET 5 Y 5 LEU E 457 TRP E 458 1 O TRP E 458 N MET E 227
SHEET 1 Z 2 LEU E 74 ILE E 77 0
SHEET 2 Z 2 ILE E 163 GLY E 167 -1 O ILE E 163 N ILE E 77
SHEET 1 AA 2 ILE E 129 LYS E 130 0
SHEET 2 AA 2 ASN E 136 LEU E 137 -1 O LEU E 137 N ILE E 129
SHEET 1 AB 4 GLY E 423 ILE E 424 0
SHEET 2 AB 4 MET E 271 THR E 272 -1 N THR E 272 O GLY E 423
SHEET 3 AB 4 CYS E 638 ASP E 645 -1 O SER E 642 N MET E 271
SHEET 4 AB 4 GLU E 650 PRO E 657 -1 O PHE E 654 N ASN E 641
SHEET 1 AC 4 ALA E 281 PHE E 283 0
SHEET 2 AC 4 SER E 405 PRO E 409 -1 O MET E 408 N ARG E 282
SHEET 3 AC 4 TYR E 352 MET E 353 -1 N MET E 353 O SER E 405
SHEET 4 AC 4 ALA E 301 THR E 302 -1 N THR E 302 O TYR E 352
SHEET 1 AD 2 ASN E 560 THR E 561 0
SHEET 2 AD 2 TYR E 624 ARG E 625 1 O TYR E 624 N THR E 561
SHEET 1 AE 2 TYR E 659 GLN E 660 0
SHEET 2 AE 2 GLN F 144 LYS F 145 -1 O GLN F 144 N GLN E 660
SHEET 1 AF 2 THR F 3 VAL F 5 0
SHEET 2 AF 2 ILE F 62 ALA F 64 -1 O THR F 63 N TYR F 4
SHEET 1 AG 2 MET F 30 ASP F 33 0
SHEET 2 AG 2 LYS F 38 ASN F 41 -1 O LYS F 38 N ASP F 33
SHEET 1 AH 3 THR F 76 ARG F 81 0
SHEET 2 AH 3 ASP F 85 LYS F 91 -1 O MET F 87 N LEU F 80
SHEET 3 AH 3 VAL F 97 PRO F 103 -1 O PHE F 102 N ILE F 86
SHEET 1 AI 4 VAL G 21 SER G 24 0
SHEET 2 AI 4 VAL G 219 LYS G 223 1 O VAL G 219 N VAL G 21
SHEET 3 AI 4 ILE G 206 ASN G 213 -1 N GLY G 211 O HIS G 220
SHEET 4 AI 4 ILE G 191 ILE G 193 -1 N PHE G 192 O PHE G 212
SHEET 1 AJ 4 VAL G 21 SER G 24 0
SHEET 2 AJ 4 VAL G 219 LYS G 223 1 O VAL G 219 N VAL G 21
SHEET 3 AJ 4 ILE G 206 ASN G 213 -1 N GLY G 211 O HIS G 220
SHEET 4 AJ 4 LEU G 197 LEU G 198 -1 N LEU G 197 O GLY G 208
SHEET 1 AK 5 ILE G 187 ILE G 188 0
SHEET 2 AK 5 ILE G 56 VAL G 59 1 N LEU G 58 O ILE G 188
SHEET 3 AK 5 LEU G 27 VAL G 30 1 N MET G 29 O VAL G 59
SHEET 4 AK 5 ALA G 226 VAL G 229 1 O ALA G 226 N LEU G 28
SHEET 5 AK 5 LEU G 457 TRP G 458 1 O TRP G 458 N MET G 227
SHEET 1 AL 2 ALA G 76 ILE G 77 0
SHEET 2 AL 2 ILE G 163 MET G 164 -1 O ILE G 163 N ILE G 77
SHEET 1 AM 4 GLY G 423 ILE G 424 0
SHEET 2 AM 4 GLU G 270 THR G 272 -1 N THR G 272 O GLY G 423
SHEET 3 AM 4 CYS G 638 ASP G 645 -1 O SER G 642 N MET G 271
SHEET 4 AM 4 GLU G 650 PRO G 657 -1 O LYS G 656 N PHE G 639
SHEET 1 AN 4 ALA G 281 PHE G 283 0
SHEET 2 AN 4 SER G 405 PRO G 409 -1 O MET G 408 N ARG G 282
SHEET 3 AN 4 ILE G 351 MET G 353 -1 N ILE G 351 O ILE G 407
SHEET 4 AN 4 ALA G 301 THR G 302 -1 N THR G 302 O TYR G 352
SHEET 1 AO 2 ASN G 560 THR G 561 0
SHEET 2 AO 2 TYR G 624 ARG G 625 1 O TYR G 624 N THR G 561
SHEET 1 AP 2 THR H 3 VAL H 5 0
SHEET 2 AP 2 ILE H 62 ALA H 64 -1 O THR H 63 N TYR H 4
SHEET 1 AQ 2 MET H 30 ASP H 33 0
SHEET 2 AQ 2 LYS H 38 ASN H 41 -1 O LYS H 38 N ASP H 33
SHEET 1 AR 3 THR H 76 ARG H 81 0
SHEET 2 AR 3 ASP H 85 LYS H 91 -1 O LYS H 91 N THR H 76
SHEET 3 AR 3 VAL H 97 PRO H 103 -1 O PHE H 100 N TRP H 88
SHEET 1 AS 4 VAL I 21 SER I 24 0
SHEET 2 AS 4 VAL I 219 LYS I 223 1 O LYS I 223 N HIS I 23
SHEET 3 AS 4 ILE I 206 ASN I 213 -1 N GLY I 211 O HIS I 220
SHEET 4 AS 4 ILE I 191 LEU I 198 -1 N LYS I 195 O VAL I 210
SHEET 1 AT 5 ILE I 187 GLU I 189 0
SHEET 2 AT 5 ILE I 56 ASP I 60 1 N LEU I 58 O ILE I 188
SHEET 3 AT 5 LEU I 27 VAL I 30 1 N LEU I 27 O LEU I 57
SHEET 4 AT 5 ALA I 226 VAL I 229 1 O VAL I 228 N VAL I 30
SHEET 5 AT 5 LEU I 457 THR I 459 1 O TRP I 458 N MET I 227
SHEET 1 AU 2 LEU I 74 ILE I 77 0
SHEET 2 AU 2 ILE I 163 GLY I 167 -1 O ILE I 165 N SER I 75
SHEET 1 AV 2 ILE I 129 LYS I 130 0
SHEET 2 AV 2 ASN I 136 LEU I 137 -1 O LEU I 137 N ILE I 129
SHEET 1 AW 4 GLY I 423 ILE I 424 0
SHEET 2 AW 4 MET I 271 THR I 272 -1 N THR I 272 O GLY I 423
SHEET 3 AW 4 CYS I 638 ASP I 645 -1 O SER I 642 N MET I 271
SHEET 4 AW 4 GLU I 650 PRO I 657 -1 O GLU I 650 N ASP I 645
SHEET 1 AX 4 ALA I 281 PHE I 283 0
SHEET 2 AX 4 SER I 405 PRO I 409 -1 O MET I 408 N ARG I 282
SHEET 3 AX 4 TYR I 352 MET I 353 -1 N MET I 353 O SER I 405
SHEET 4 AX 4 ALA I 301 THR I 302 -1 N THR I 302 O TYR I 352
SHEET 1 AY 2 ASN I 560 THR I 561 0
SHEET 2 AY 2 TYR I 624 ARG I 625 1 O TYR I 624 N THR I 561
SHEET 1 AZ 2 TYR I 659 GLN I 660 0
SHEET 2 AZ 2 GLN J 144 LYS J 145 -1 O GLN J 144 N GLN I 660
SHEET 1 BA 2 THR J 3 VAL J 5 0
SHEET 2 BA 2 ILE J 62 ALA J 64 -1 O THR J 63 N TYR J 4
SHEET 1 BB 2 MET J 30 ASP J 33 0
SHEET 2 BB 2 LYS J 38 ASN J 41 -1 O LYS J 38 N ASP J 33
SHEET 1 BC 3 THR J 76 ARG J 81 0
SHEET 2 BC 3 ASP J 85 LYS J 91 -1 O LYS J 91 N THR J 76
SHEET 3 BC 3 VAL J 97 PRO J 103 -1 O LYS J 98 N ILE J 90
SHEET 1 BD 4 VAL K 21 SER K 24 0
SHEET 2 BD 4 VAL K 219 LYS K 223 1 O ILE K 221 N HIS K 23
SHEET 3 BD 4 ILE K 206 ASN K 213 -1 N ALA K 209 O PHE K 222
SHEET 4 BD 4 ILE K 191 LEU K 198 -1 N LEU K 197 O GLY K 208
SHEET 1 BE 5 ILE K 187 ILE K 188 0
SHEET 2 BE 5 ILE K 56 VAL K 59 1 N LEU K 58 O ILE K 188
SHEET 3 BE 5 LEU K 27 VAL K 30 1 N MET K 29 O VAL K 59
SHEET 4 BE 5 ALA K 226 VAL K 229 1 O VAL K 228 N VAL K 30
SHEET 5 BE 5 LEU K 457 THR K 459 1 O TRP K 458 N MET K 227
SHEET 1 BF 2 LEU K 74 ILE K 77 0
SHEET 2 BF 2 ILE K 163 GLY K 167 -1 O ILE K 163 N ILE K 77
SHEET 1 BG 4 GLY K 423 ILE K 424 0
SHEET 2 BG 4 MET K 271 THR K 272 -1 N THR K 272 O GLY K 423
SHEET 3 BG 4 CYS K 638 ASP K 645 -1 O SER K 642 N MET K 271
SHEET 4 BG 4 GLU K 650 PRO K 657 -1 O PHE K 654 N ASN K 641
SHEET 1 BH 4 ALA K 281 PHE K 283 0
SHEET 2 BH 4 SER K 405 PRO K 409 -1 O MET K 408 N ARG K 282
SHEET 3 BH 4 ILE K 351 MET K 353 -1 N ILE K 351 O ILE K 407
SHEET 4 BH 4 ALA K 301 THR K 302 -1 N THR K 302 O TYR K 352
SHEET 1 BI 2 ASN K 560 THR K 561 0
SHEET 2 BI 2 TYR K 624 ARG K 625 1 O TYR K 624 N THR K 561
SHEET 1 BJ 2 TYR K 659 GLN K 660 0
SHEET 2 BJ 2 GLN L 144 LYS L 145 -1 O GLN L 144 N GLN K 660
SHEET 1 BK 2 THR L 3 VAL L 5 0
SHEET 2 BK 2 ILE L 62 ALA L 64 -1 O THR L 63 N TYR L 4
SHEET 1 BL 2 MET L 30 ASP L 33 0
SHEET 2 BL 2 LYS L 38 ASN L 41 -1 O LYS L 38 N ASP L 33
SHEET 1 BM 3 THR L 76 ARG L 81 0
SHEET 2 BM 3 ASP L 85 LYS L 91 -1 O THR L 89 N ILE L 78
SHEET 3 BM 3 VAL L 97 PRO L 103 -1 O LYS L 98 N ILE L 90
SSBOND 1 CYS B 156 CYS B 162 1555 1555 2.04
SSBOND 2 CYS D 156 CYS D 162 1555 1555 2.04
SSBOND 3 CYS F 156 CYS F 162 1555 1555 2.04
SSBOND 4 CYS H 156 CYS H 162 1555 1555 2.04
SSBOND 5 CYS J 156 CYS J 162 1555 1555 2.04
SSBOND 6 CYS L 156 CYS L 162 1555 1555 2.04
LINK SG CYS B 10 FE4 SF4 B2000 1555 1555 2.28
LINK SG CYS B 21 FE3 SF4 B2000 1555 1555 2.30
LINK SG CYS B 25 FE4 SF4 B1000 1555 1555 2.30
LINK SG CYS B 47 FE1 SF4 B1000 1555 1555 2.30
LINK SG CYS B 50 FE3 SF4 B1000 1555 1555 2.31
LINK SG CYS B 53 FE2 SF4 B1000 1555 1555 2.30
LINK SG CYS B 57 FE1 SF4 B2000 1555 1555 2.37
LINK SG CYS D 10 FE4 SF4 D2000 1555 1555 2.30
LINK SG CYS D 13 FE2 SF4 D2000 1555 1555 2.32
LINK SG CYS D 21 FE3 SF4 D2000 1555 1555 2.31
LINK SG CYS D 25 FE4 SF4 D1000 1555 1555 2.30
LINK SG CYS D 47 FE1 SF4 D1000 1555 1555 2.28
LINK SG CYS D 50 FE3 SF4 D1000 1555 1555 2.30
LINK SG CYS D 53 FE2 SF4 D1000 1555 1555 2.29
LINK SG CYS D 57 FE1 SF4 D2000 1555 1555 2.30
LINK SG CYS F 10 FE4 SF4 F2000 1555 1555 2.31
LINK SG CYS F 13 FE2 SF4 F2000 1555 1555 2.32
LINK SG CYS F 21 FE3 SF4 F2000 1555 1555 2.30
LINK SG CYS F 25 FE4 SF4 F1000 1555 1555 2.28
LINK SG CYS F 47 FE1 SF4 F1000 1555 1555 2.31
LINK SG CYS F 50 FE3 SF4 F1000 1555 1555 2.29
LINK SG CYS F 53 FE2 SF4 F1000 1555 1555 2.29
LINK SG CYS F 57 FE1 SF4 F2000 1555 1555 2.30
LINK SG CYS H 10 FE4 SF4 H2000 1555 1555 2.30
LINK SG CYS H 13 FE2 SF4 H2000 1555 1555 2.33
LINK SG CYS H 21 FE3 SF4 H2000 1555 1555 2.30
LINK SG CYS H 25 FE4 SF4 H1000 1555 1555 2.30
LINK SG CYS H 47 FE1 SF4 H1000 1555 1555 2.32
LINK SG CYS H 50 FE3 SF4 H1000 1555 1555 2.30
LINK SG CYS H 53 FE2 SF4 H1000 1555 1555 2.30
LINK SG CYS H 57 FE1 SF4 H2000 1555 1555 2.31
LINK SG CYS J 10 FE4 SF4 J2000 1555 1555 2.30
LINK SG CYS J 13 FE2 SF4 J2000 1555 1555 2.32
LINK SG CYS J 21 FE3 SF4 J2000 1555 1555 2.31
LINK SG CYS J 25 FE4 SF4 J1000 1555 1555 2.28
LINK SG CYS J 47 FE1 SF4 J1000 1555 1555 2.32
LINK SG CYS J 50 FE3 SF4 J1000 1555 1555 2.28
LINK SG CYS J 53 FE2 SF4 J1000 1555 1555 2.28
LINK SG CYS J 57 FE1 SF4 J2000 1555 1555 2.29
LINK SG CYS L 10 FE4 SF4 L2000 1555 1555 2.30
LINK SG CYS L 13 FE2 SF4 L2000 1555 1555 2.31
LINK SG CYS L 21 FE3 SF4 L2000 1555 1555 2.30
LINK SG CYS L 25 FE4 SF4 L1000 1555 1555 2.30
LINK SG CYS L 47 FE1 SF4 L1000 1555 1555 2.31
LINK SG CYS L 50 FE3 SF4 L1000 1555 1555 2.30
LINK SG CYS L 53 FE2 SF4 L1000 1555 1555 2.29
LINK SG CYS L 57 FE1 SF4 L2000 1555 1555 2.30
CISPEP 1 GLY A 349 PRO A 350 0 0.86
CISPEP 2 GLY C 349 PRO C 350 0 1.32
CISPEP 3 GLY E 349 PRO E 350 0 2.01
CISPEP 4 GLY G 349 PRO G 350 0 0.54
CISPEP 5 GLY I 349 PRO I 350 0 4.05
CISPEP 6 GLY K 349 PRO K 350 0 1.49
SITE 1 AC1 31 GLY A 31 GLY A 32 GLY A 33 MET A 34
SITE 2 AC1 31 GLY A 35 ASP A 60 LYS A 61 SER A 67
SITE 3 AC1 31 GLY A 68 ALA A 69 VAL A 70 LEU A 74
SITE 4 AC1 31 ALA A 76 ASN A 78 PHE A 192 ILE A 193
SITE 5 AC1 31 ALA A 230 CYS A 231 GLY A 232 TRP A 251
SITE 6 AC1 31 TYR A 252 PRO A 253 SER A 259 MET A 385
SITE 7 AC1 31 SER A 417 HIS A 418 ALA A 461 ASP A 462
SITE 8 AC1 31 PHE A 471 SER A 472 SER A 475
SITE 1 AC2 8 THR B 3 CYS B 25 ASN B 41 CYS B 47
SITE 2 AC2 8 GLU B 49 CYS B 50 TYR B 51 CYS B 53
SITE 1 AC3 9 CYS B 10 ASP B 11 GLY B 12 CYS B 13
SITE 2 AC3 9 THR B 19 CYS B 21 ALA B 39 CYS B 57
SITE 3 AC3 9 ILE B 62
SITE 1 AC4 27 GLY C 32 GLY C 33 MET C 34 GLY C 35
SITE 2 AC4 27 ASP C 60 LYS C 61 SER C 67 GLY C 68
SITE 3 AC4 27 ALA C 69 LEU C 74 ALA C 76 ASN C 78
SITE 4 AC4 27 PHE C 192 ILE C 193 ALA C 230 CYS C 231
SITE 5 AC4 27 TRP C 251 TYR C 252 PRO C 253 SER C 259
SITE 6 AC4 27 SER C 417 HIS C 418 ALA C 461 ASP C 462
SITE 7 AC4 27 PHE C 471 SER C 472 SER C 475
SITE 1 AC5 10 THR D 3 CYS D 25 PRO D 26 ASN D 41
SITE 2 AC5 10 CYS D 47 TRP D 48 GLU D 49 CYS D 50
SITE 3 AC5 10 TYR D 51 CYS D 53
SITE 1 AC6 9 CYS D 10 ASP D 11 GLY D 12 CYS D 13
SITE 2 AC6 9 ALA D 20 CYS D 21 ALA D 39 CYS D 57
SITE 3 AC6 9 ILE D 62
SITE 1 AC7 31 GLY E 31 GLY E 32 GLY E 33 MET E 34
SITE 2 AC7 31 GLY E 35 ASP E 60 LYS E 61 SER E 67
SITE 3 AC7 31 GLY E 68 ALA E 69 VAL E 70 LEU E 74
SITE 4 AC7 31 ALA E 76 ILE E 77 ASN E 78 PHE E 192
SITE 5 AC7 31 ILE E 193 ALA E 230 CYS E 231 GLY E 232
SITE 6 AC7 31 TRP E 251 TYR E 252 PRO E 253 SER E 259
SITE 7 AC7 31 SER E 417 HIS E 418 ALA E 461 ASP E 462
SITE 8 AC7 31 PHE E 471 SER E 472 SER E 475
SITE 1 AC8 9 THR F 3 CYS F 25 PRO F 26 MET F 30
SITE 2 AC8 9 CYS F 47 TRP F 48 CYS F 50 SER F 52
SITE 3 AC8 9 CYS F 53
SITE 1 AC9 7 CYS F 10 CYS F 13 CYS F 21 ALA F 39
SITE 2 AC9 7 CYS F 57 PRO F 58 ILE F 62
SITE 1 BC1 33 GLY G 31 GLY G 32 GLY G 33 MET G 34
SITE 2 BC1 33 GLY G 35 ASP G 60 LYS G 61 SER G 67
SITE 3 BC1 33 GLY G 68 ALA G 69 VAL G 70 LEU G 74
SITE 4 BC1 33 ALA G 76 ILE G 77 ASN G 78 ILE G 191
SITE 5 BC1 33 PHE G 192 ILE G 193 ALA G 230 CYS G 231
SITE 6 BC1 33 GLY G 232 TRP G 251 TYR G 252 PRO G 253
SITE 7 BC1 33 SER G 259 MET G 385 SER G 417 HIS G 418
SITE 8 BC1 33 ALA G 461 ASP G 462 PHE G 471 SER G 472
SITE 9 BC1 33 SER G 475
SITE 1 BC2 9 TRP G 255 THR H 3 CYS H 25 PRO H 26
SITE 2 BC2 9 ASN H 41 CYS H 47 CYS H 50 TYR H 51
SITE 3 BC2 9 CYS H 53
SITE 1 BC3 11 CYS H 10 ASP H 11 GLY H 12 CYS H 13
SITE 2 BC3 11 THR H 19 ALA H 20 CYS H 21 CYS H 57
SITE 3 BC3 11 PRO H 58 GLN H 59 ILE H 62
SITE 1 BC4 31 GLY I 31 GLY I 32 GLY I 33 MET I 34
SITE 2 BC4 31 GLY I 35 ASP I 60 LYS I 61 SER I 67
SITE 3 BC4 31 GLY I 68 ALA I 69 VAL I 70 LEU I 74
SITE 4 BC4 31 ALA I 76 ASN I 78 ILE I 191 PHE I 192
SITE 5 BC4 31 ILE I 193 ALA I 230 CYS I 231 GLY I 232
SITE 6 BC4 31 TRP I 251 TYR I 252 PRO I 253 SER I 259
SITE 7 BC4 31 MET I 385 SER I 417 ALA I 461 ASP I 462
SITE 8 BC4 31 PHE I 471 SER I 472 SER I 475
SITE 1 BC5 8 THR J 3 CYS J 25 PRO J 26 ASN J 41
SITE 2 BC5 8 CYS J 47 CYS J 50 TYR J 51 CYS J 53
SITE 1 BC6 9 CYS J 10 ASP J 11 GLY J 12 CYS J 13
SITE 2 BC6 9 THR J 19 CYS J 21 CYS J 57 GLN J 59
SITE 3 BC6 9 ILE J 62
SITE 1 BC7 28 GLY K 31 GLY K 32 GLY K 33 MET K 34
SITE 2 BC7 28 GLY K 35 ASP K 60 LYS K 61 SER K 67
SITE 3 BC7 28 GLY K 68 ALA K 69 VAL K 70 LEU K 74
SITE 4 BC7 28 ALA K 76 ASN K 78 PHE K 192 ILE K 193
SITE 5 BC7 28 ALA K 230 CYS K 231 GLY K 232 TRP K 251
SITE 6 BC7 28 PRO K 253 SER K 259 SER K 417 ALA K 461
SITE 7 BC7 28 ASP K 462 PHE K 471 SER K 472 SER K 475
SITE 1 BC8 7 THR L 3 CYS L 25 ASN L 41 CYS L 47
SITE 2 BC8 7 CYS L 50 TYR L 51 CYS L 53
SITE 1 BC9 10 VAL L 5 CYS L 10 GLY L 12 CYS L 13
SITE 2 BC9 10 THR L 19 ALA L 20 CYS L 21 CYS L 57
SITE 3 BC9 10 GLN L 59 ILE L 62
CRYST1 199.629 199.629 317.422 90.00 90.00 120.00 P 31 2 1 36
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 0.005009 0.002892 0.000000 0.00000
SCALE2 0.000000 0.005784 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003150 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
