HEADER OXIDOREDUCTASE 23-SEP-10 2XRX
TITLE CRYSTAL STRUCTURE OF BIPHENYL DIOXYGENASE IN COMPLEX WITH BIPHENYL
TITLE 2 FROM BURKHOLDERIA XENOVORANS LB400
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BIPHENYL DIOXYGENASE SUBUNIT ALPHA;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W;
COMPND 4 SYNONYM: BIPHENYL 2,3-DIOXYGENASE, SUBUNIT A;
COMPND 5 EC: 1.14.12.18;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BIPHENYL DIOXYGENASE SUBUNIT BETA;
COMPND 9 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X;
COMPND 10 SYNONYM: BIPHENYL 2,3-DIOXYGENASE, SUBUNIT B;
COMPND 11 EC: 1.14.12.18;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_TAXID: 266265;
SOURCE 4 STRAIN: LB400;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 9 ORGANISM_TAXID: 266265;
SOURCE 10 STRAIN: LB400;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, DEGRADATION, BPDO
EXPDTA X-RAY DIFFRACTION
AUTHOR P.KUMAR,J.T.BOLIN
REVDAT 3 20-DEC-23 2XRX 1 REMARK LINK
REVDAT 2 16-FEB-11 2XRX 1 JRNL
REVDAT 1 24-NOV-10 2XRX 0
JRNL AUTH P.KUMAR,M.MOHAMMADI,J.F.VIGER,D.BARRIAULT,L.GOMEZ-GIL,
JRNL AUTH 2 L.D.ELTIS,J.T.BOLIN,M.SYLVESTRE
JRNL TITL STRUCTURAL INSIGHT INTO THE EXPANDED PCB-DEGRADING ABILITIES
JRNL TITL 2 OF A BIPHENYL DIOXYGENASE OBTAINED BY DIRECTED EVOLUTION.
JRNL REF J.MOL.BIOL. V. 405 531 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21073881
JRNL DOI 10.1016/J.JMB.2010.11.009
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 119.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.1
REMARK 3 NUMBER OF REFLECTIONS : 291398
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) : 0.233
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3001
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.42
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.48
REMARK 3 REFLECTION IN BIN (WORKING SET) : 18989
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 193
REMARK 3 BIN FREE R VALUE : 0.3740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 59079
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 204
REMARK 3 SOLVENT ATOMS : 694
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43000
REMARK 3 B22 (A**2) : -0.64000
REMARK 3 B33 (A**2) : 1.53000
REMARK 3 B12 (A**2) : -0.05000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 1.09000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.619
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.302
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.264
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.661
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.904
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 60927 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 82587 ; 0.905 ; 1.936
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 7320 ; 5.168 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 3111 ;35.418 ;23.308
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 9771 ;14.553 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 501 ;13.899 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 8457 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 47865 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 28293 ; 0.162 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 40766 ; 0.297 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 2760 ; 0.113 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 6 ; 0.095 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 74 ; 0.123 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.215 ; 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): 37649 ; 0.301 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 58566 ; 0.448 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 27159 ; 0.486 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 23997 ; 0.705 ; 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 2XRX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1290045469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-FEB-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC SX-165
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 309885
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.0
REMARK 200 DATA REDUNDANCY IN SHELL : 1.20
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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 2XR8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 20% PEG
REMARK 280 5000MME, 50 MM PIPES, PH 6.5.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.9 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 34060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 55980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -176.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 57920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -172.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -177.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, U, V, W, X
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 SER A 2
REMARK 465 SER A 3
REMARK 465 ALA A 4
REMARK 465 ILE A 5
REMARK 465 LYS A 6
REMARK 465 GLU A 7
REMARK 465 VAL A 8
REMARK 465 GLN A 9
REMARK 465 GLY A 10
REMARK 465 ALA A 11
REMARK 465 PRO A 12
REMARK 465 VAL A 13
REMARK 465 LYS A 14
REMARK 465 TRP A 15
REMARK 465 VAL A 16
REMARK 465 THR A 17
REMARK 465 PHE A 143
REMARK 465 CYS A 144
REMARK 465 ASP A 145
REMARK 465 LYS A 146
REMARK 465 LYS A 147
REMARK 465 GLU A 148
REMARK 465 GLY A 149
REMARK 465 ASP A 150
REMARK 465 CYS A 151
REMARK 465 GLY A 152
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 ASN B 3
REMARK 465 PRO B 4
REMARK 465 SER B 5
REMARK 465 PRO B 6
REMARK 465 HIS B 7
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 SER C 3
REMARK 465 ALA C 4
REMARK 465 ILE C 5
REMARK 465 LYS C 6
REMARK 465 GLU C 7
REMARK 465 VAL C 8
REMARK 465 GLN C 9
REMARK 465 GLY C 10
REMARK 465 ALA C 11
REMARK 465 PRO C 12
REMARK 465 VAL C 13
REMARK 465 LYS C 14
REMARK 465 TRP C 15
REMARK 465 VAL C 16
REMARK 465 THR C 17
REMARK 465 PHE C 143
REMARK 465 CYS C 144
REMARK 465 ASP C 145
REMARK 465 LYS C 146
REMARK 465 LYS C 147
REMARK 465 GLU C 148
REMARK 465 GLY C 149
REMARK 465 ASP C 150
REMARK 465 CYS C 151
REMARK 465 GLY C 152
REMARK 465 MET D 1
REMARK 465 THR D 2
REMARK 465 ASN D 3
REMARK 465 PRO D 4
REMARK 465 SER D 5
REMARK 465 PRO D 6
REMARK 465 HIS D 7
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 SER E 3
REMARK 465 ALA E 4
REMARK 465 ILE E 5
REMARK 465 LYS E 6
REMARK 465 GLU E 7
REMARK 465 VAL E 8
REMARK 465 GLN E 9
REMARK 465 GLY E 10
REMARK 465 ALA E 11
REMARK 465 PRO E 12
REMARK 465 VAL E 13
REMARK 465 LYS E 14
REMARK 465 TRP E 15
REMARK 465 VAL E 16
REMARK 465 THR E 17
REMARK 465 PHE E 143
REMARK 465 CYS E 144
REMARK 465 ASP E 145
REMARK 465 LYS E 146
REMARK 465 LYS E 147
REMARK 465 GLU E 148
REMARK 465 GLY E 149
REMARK 465 ASP E 150
REMARK 465 CYS E 151
REMARK 465 GLY E 152
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 ASN F 3
REMARK 465 PRO F 4
REMARK 465 SER F 5
REMARK 465 PRO F 6
REMARK 465 HIS F 7
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 SER G 3
REMARK 465 ALA G 4
REMARK 465 ILE G 5
REMARK 465 LYS G 6
REMARK 465 GLU G 7
REMARK 465 VAL G 8
REMARK 465 GLN G 9
REMARK 465 GLY G 10
REMARK 465 ALA G 11
REMARK 465 PRO G 12
REMARK 465 VAL G 13
REMARK 465 LYS G 14
REMARK 465 TRP G 15
REMARK 465 VAL G 16
REMARK 465 THR G 17
REMARK 465 PHE G 143
REMARK 465 CYS G 144
REMARK 465 ASP G 145
REMARK 465 LYS G 146
REMARK 465 LYS G 147
REMARK 465 GLU G 148
REMARK 465 GLY G 149
REMARK 465 ASP G 150
REMARK 465 CYS G 151
REMARK 465 GLY G 152
REMARK 465 MET H 1
REMARK 465 THR H 2
REMARK 465 ASN H 3
REMARK 465 PRO H 4
REMARK 465 SER H 5
REMARK 465 PRO H 6
REMARK 465 HIS H 7
REMARK 465 MET I 1
REMARK 465 SER I 2
REMARK 465 SER I 3
REMARK 465 ALA I 4
REMARK 465 ILE I 5
REMARK 465 LYS I 6
REMARK 465 GLU I 7
REMARK 465 VAL I 8
REMARK 465 GLN I 9
REMARK 465 GLY I 10
REMARK 465 ALA I 11
REMARK 465 PRO I 12
REMARK 465 VAL I 13
REMARK 465 LYS I 14
REMARK 465 TRP I 15
REMARK 465 VAL I 16
REMARK 465 THR I 17
REMARK 465 PHE I 143
REMARK 465 CYS I 144
REMARK 465 ASP I 145
REMARK 465 LYS I 146
REMARK 465 LYS I 147
REMARK 465 GLU I 148
REMARK 465 GLY I 149
REMARK 465 ASP I 150
REMARK 465 CYS I 151
REMARK 465 GLY I 152
REMARK 465 MET J 1
REMARK 465 THR J 2
REMARK 465 ASN J 3
REMARK 465 PRO J 4
REMARK 465 SER J 5
REMARK 465 PRO J 6
REMARK 465 HIS J 7
REMARK 465 MET K 1
REMARK 465 SER K 2
REMARK 465 SER K 3
REMARK 465 ALA K 4
REMARK 465 ILE K 5
REMARK 465 LYS K 6
REMARK 465 GLU K 7
REMARK 465 VAL K 8
REMARK 465 GLN K 9
REMARK 465 GLY K 10
REMARK 465 ALA K 11
REMARK 465 PRO K 12
REMARK 465 VAL K 13
REMARK 465 LYS K 14
REMARK 465 TRP K 15
REMARK 465 VAL K 16
REMARK 465 THR K 17
REMARK 465 PHE K 143
REMARK 465 CYS K 144
REMARK 465 ASP K 145
REMARK 465 LYS K 146
REMARK 465 LYS K 147
REMARK 465 GLU K 148
REMARK 465 GLY K 149
REMARK 465 ASP K 150
REMARK 465 CYS K 151
REMARK 465 GLY K 152
REMARK 465 MET L 1
REMARK 465 THR L 2
REMARK 465 ASN L 3
REMARK 465 PRO L 4
REMARK 465 SER L 5
REMARK 465 PRO L 6
REMARK 465 HIS L 7
REMARK 465 MET M 1
REMARK 465 SER M 2
REMARK 465 SER M 3
REMARK 465 ALA M 4
REMARK 465 ILE M 5
REMARK 465 LYS M 6
REMARK 465 GLU M 7
REMARK 465 VAL M 8
REMARK 465 GLN M 9
REMARK 465 GLY M 10
REMARK 465 ALA M 11
REMARK 465 PRO M 12
REMARK 465 VAL M 13
REMARK 465 LYS M 14
REMARK 465 TRP M 15
REMARK 465 VAL M 16
REMARK 465 THR M 17
REMARK 465 PHE M 143
REMARK 465 CYS M 144
REMARK 465 ASP M 145
REMARK 465 LYS M 146
REMARK 465 LYS M 147
REMARK 465 GLU M 148
REMARK 465 GLY M 149
REMARK 465 ASP M 150
REMARK 465 CYS M 151
REMARK 465 GLY M 152
REMARK 465 MET N 1
REMARK 465 THR N 2
REMARK 465 ASN N 3
REMARK 465 PRO N 4
REMARK 465 SER N 5
REMARK 465 PRO N 6
REMARK 465 HIS N 7
REMARK 465 MET O 1
REMARK 465 SER O 2
REMARK 465 SER O 3
REMARK 465 ALA O 4
REMARK 465 ILE O 5
REMARK 465 LYS O 6
REMARK 465 GLU O 7
REMARK 465 VAL O 8
REMARK 465 GLN O 9
REMARK 465 GLY O 10
REMARK 465 ALA O 11
REMARK 465 PRO O 12
REMARK 465 VAL O 13
REMARK 465 LYS O 14
REMARK 465 TRP O 15
REMARK 465 VAL O 16
REMARK 465 THR O 17
REMARK 465 PHE O 143
REMARK 465 CYS O 144
REMARK 465 ASP O 145
REMARK 465 LYS O 146
REMARK 465 LYS O 147
REMARK 465 GLU O 148
REMARK 465 GLY O 149
REMARK 465 ASP O 150
REMARK 465 CYS O 151
REMARK 465 GLY O 152
REMARK 465 MET P 1
REMARK 465 THR P 2
REMARK 465 ASN P 3
REMARK 465 PRO P 4
REMARK 465 SER P 5
REMARK 465 PRO P 6
REMARK 465 HIS P 7
REMARK 465 MET Q 1
REMARK 465 SER Q 2
REMARK 465 SER Q 3
REMARK 465 ALA Q 4
REMARK 465 ILE Q 5
REMARK 465 LYS Q 6
REMARK 465 GLU Q 7
REMARK 465 VAL Q 8
REMARK 465 GLN Q 9
REMARK 465 GLY Q 10
REMARK 465 ALA Q 11
REMARK 465 PRO Q 12
REMARK 465 VAL Q 13
REMARK 465 LYS Q 14
REMARK 465 TRP Q 15
REMARK 465 VAL Q 16
REMARK 465 THR Q 17
REMARK 465 PHE Q 143
REMARK 465 CYS Q 144
REMARK 465 ASP Q 145
REMARK 465 LYS Q 146
REMARK 465 LYS Q 147
REMARK 465 GLU Q 148
REMARK 465 GLY Q 149
REMARK 465 ASP Q 150
REMARK 465 CYS Q 151
REMARK 465 GLY Q 152
REMARK 465 MET R 1
REMARK 465 THR R 2
REMARK 465 ASN R 3
REMARK 465 PRO R 4
REMARK 465 SER R 5
REMARK 465 PRO R 6
REMARK 465 HIS R 7
REMARK 465 MET S 1
REMARK 465 SER S 2
REMARK 465 SER S 3
REMARK 465 ALA S 4
REMARK 465 ILE S 5
REMARK 465 LYS S 6
REMARK 465 GLU S 7
REMARK 465 VAL S 8
REMARK 465 GLN S 9
REMARK 465 GLY S 10
REMARK 465 ALA S 11
REMARK 465 PRO S 12
REMARK 465 VAL S 13
REMARK 465 LYS S 14
REMARK 465 TRP S 15
REMARK 465 VAL S 16
REMARK 465 THR S 17
REMARK 465 PHE S 143
REMARK 465 CYS S 144
REMARK 465 ASP S 145
REMARK 465 LYS S 146
REMARK 465 LYS S 147
REMARK 465 GLU S 148
REMARK 465 GLY S 149
REMARK 465 ASP S 150
REMARK 465 CYS S 151
REMARK 465 GLY S 152
REMARK 465 MET T 1
REMARK 465 THR T 2
REMARK 465 ASN T 3
REMARK 465 PRO T 4
REMARK 465 SER T 5
REMARK 465 PRO T 6
REMARK 465 HIS T 7
REMARK 465 MET U 1
REMARK 465 SER U 2
REMARK 465 SER U 3
REMARK 465 ALA U 4
REMARK 465 ILE U 5
REMARK 465 LYS U 6
REMARK 465 GLU U 7
REMARK 465 VAL U 8
REMARK 465 GLN U 9
REMARK 465 GLY U 10
REMARK 465 ALA U 11
REMARK 465 PRO U 12
REMARK 465 VAL U 13
REMARK 465 LYS U 14
REMARK 465 TRP U 15
REMARK 465 VAL U 16
REMARK 465 THR U 17
REMARK 465 PHE U 143
REMARK 465 CYS U 144
REMARK 465 ASP U 145
REMARK 465 LYS U 146
REMARK 465 LYS U 147
REMARK 465 GLU U 148
REMARK 465 GLY U 149
REMARK 465 ASP U 150
REMARK 465 CYS U 151
REMARK 465 GLY U 152
REMARK 465 MET V 1
REMARK 465 THR V 2
REMARK 465 ASN V 3
REMARK 465 PRO V 4
REMARK 465 SER V 5
REMARK 465 PRO V 6
REMARK 465 HIS V 7
REMARK 465 MET W 1
REMARK 465 SER W 2
REMARK 465 SER W 3
REMARK 465 ALA W 4
REMARK 465 ILE W 5
REMARK 465 LYS W 6
REMARK 465 GLU W 7
REMARK 465 VAL W 8
REMARK 465 GLN W 9
REMARK 465 GLY W 10
REMARK 465 ALA W 11
REMARK 465 PRO W 12
REMARK 465 VAL W 13
REMARK 465 LYS W 14
REMARK 465 TRP W 15
REMARK 465 VAL W 16
REMARK 465 THR W 17
REMARK 465 PHE W 143
REMARK 465 CYS W 144
REMARK 465 ASP W 145
REMARK 465 LYS W 146
REMARK 465 LYS W 147
REMARK 465 GLU W 148
REMARK 465 GLY W 149
REMARK 465 ASP W 150
REMARK 465 CYS W 151
REMARK 465 GLY W 152
REMARK 465 MET X 1
REMARK 465 THR X 2
REMARK 465 ASN X 3
REMARK 465 PRO X 4
REMARK 465 SER X 5
REMARK 465 PRO X 6
REMARK 465 HIS X 7
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 ARG B 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 70 CG CD OE1 OE2
REMARK 470 LYS C 140 CG CD CE NZ
REMARK 470 ARG D 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 70 CG CD OE1 OE2
REMARK 470 LYS E 140 CG CD CE NZ
REMARK 470 ARG F 67 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 70 CG CD OE1 OE2
REMARK 470 LYS G 140 CG CD CE NZ
REMARK 470 GLN G 255 CB CG CD OE1 NE2
REMARK 470 LYS I 140 CG CD CE NZ
REMARK 470 GLN I 255 CB CG CD OE1 NE2
REMARK 470 LYS K 140 CG CD CE NZ
REMARK 470 GLN K 255 CB CG CD OE1 NE2
REMARK 470 LYS M 140 CG CD CE NZ
REMARK 470 LYS O 140 CG CD CE NZ
REMARK 470 LYS Q 140 CG CD CE NZ
REMARK 470 LYS S 132 CG CD CE NZ
REMARK 470 LYS S 140 CG CD CE NZ
REMARK 470 LYS U 132 CG CD CE NZ
REMARK 470 LYS U 140 CG CD CE NZ
REMARK 470 LYS W 132 CG CD CE NZ
REMARK 470 LYS W 140 CG CD CE NZ
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 VAL A 53 -64.20 -104.66
REMARK 500 LYS A 91 -0.48 72.88
REMARK 500 ASP A 199 63.84 -118.20
REMARK 500 THR A 236 -111.07 -115.43
REMARK 500 ASN A 428 96.22 -69.85
REMARK 500 LYS B 10 173.47 59.58
REMARK 500 LEU B 141 -135.92 54.41
REMARK 500 ASP B 160 43.24 -91.93
REMARK 500 ASN B 161 -158.88 -98.90
REMARK 500 SER B 177 -74.36 -107.33
REMARK 500 LEU B 184 67.73 -117.15
REMARK 500 VAL C 53 -71.66 -108.96
REMARK 500 ARG C 56 15.11 -144.72
REMARK 500 ASP C 90 20.74 -78.21
REMARK 500 ARG C 103 30.08 -140.66
REMARK 500 LEU C 133 99.48 -69.66
REMARK 500 SER C 229 -14.47 -145.67
REMARK 500 THR C 236 -96.62 -113.24
REMARK 500 PHE D 9 -51.36 -132.45
REMARK 500 LYS D 10 175.65 55.33
REMARK 500 GLU D 68 36.20 -92.42
REMARK 500 THR D 122 -158.57 -101.68
REMARK 500 LEU D 141 -127.39 55.58
REMARK 500 ASP D 160 47.77 -93.34
REMARK 500 SER D 177 -80.27 -93.20
REMARK 500 VAL E 53 -65.50 -102.19
REMARK 500 LYS E 91 -6.05 71.78
REMARK 500 SER E 229 -13.13 -146.51
REMARK 500 ASP E 230 78.51 -103.73
REMARK 500 THR E 236 -98.62 -115.32
REMARK 500 ARG E 345 57.74 -143.38
REMARK 500 TYR E 433 78.72 -100.86
REMARK 500 LYS F 10 -173.27 47.83
REMARK 500 THR F 122 -163.20 -105.09
REMARK 500 LEU F 141 -121.80 48.74
REMARK 500 SER F 177 -79.57 -105.92
REMARK 500 VAL G 53 -61.41 -94.74
REMARK 500 THR G 76 -157.02 -140.72
REMARK 500 LYS G 91 -14.28 70.40
REMARK 500 ARG G 103 23.61 -144.26
REMARK 500 THR G 236 -94.69 -111.04
REMARK 500 ASP G 252 -162.99 -113.09
REMARK 500 LEU G 253 6.48 -68.53
REMARK 500 ASN G 428 96.36 -68.77
REMARK 500 PHE H 9 -80.39 150.18
REMARK 500 LYS H 10 171.30 62.27
REMARK 500 ASP H 126 -1.58 66.65
REMARK 500 LEU H 141 -118.26 58.02
REMARK 500 GLU H 142 -63.27 -95.53
REMARK 500 SER H 177 -81.58 -89.37
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 A1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 100 SG
REMARK 620 2 FES A1460 S1 117.0
REMARK 620 3 FES A1460 S2 109.6 93.1
REMARK 620 4 CYS A 120 SG 123.6 103.1 105.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES A1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 102 ND1
REMARK 620 2 FES A1460 S1 126.3
REMARK 620 3 FES A1460 S2 98.9 92.6
REMARK 620 4 HIS A 123 ND1 94.8 121.0 124.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 A1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 233 NE2
REMARK 620 2 HIS A 239 NE2 83.2
REMARK 620 3 ASP A 388 OD2 142.2 101.6
REMARK 620 4 ASP A 388 OD1 88.7 89.7 54.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 100 SG
REMARK 620 2 FES C1460 S1 114.3
REMARK 620 3 FES C1460 S2 114.7 92.2
REMARK 620 4 CYS C 120 SG 128.2 101.8 99.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES C1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 102 ND1
REMARK 620 2 FES C1460 S1 117.6
REMARK 620 3 FES C1460 S2 112.1 91.8
REMARK 620 4 HIS C 123 ND1 93.0 122.0 122.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 C1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 233 NE2
REMARK 620 2 HIS C 239 NE2 95.0
REMARK 620 3 ASP C 388 OD1 106.2 94.2
REMARK 620 4 ASP C 388 OD2 157.8 92.0 52.2
REMARK 620 5 HOH C2027 O 134.5 96.9 116.4 65.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 100 SG
REMARK 620 2 FES E1460 S1 120.3
REMARK 620 3 FES E1460 S2 107.8 93.1
REMARK 620 4 CYS E 120 SG 122.0 110.2 95.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES E1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 102 ND1
REMARK 620 2 FES E1460 S1 122.1
REMARK 620 3 FES E1460 S2 117.8 92.7
REMARK 620 4 HIS E 123 ND1 93.5 110.7 122.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 E1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 233 NE2
REMARK 620 2 HIS E 239 NE2 87.6
REMARK 620 3 ASP E 388 OD1 97.9 106.4
REMARK 620 4 ASP E 388 OD2 151.6 96.5 53.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES G1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 100 SG
REMARK 620 2 FES G1460 S1 122.6
REMARK 620 3 FES G1460 S2 104.1 92.1
REMARK 620 4 CYS G 120 SG 117.9 110.7 103.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES G1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 102 ND1
REMARK 620 2 FES G1460 S1 120.9
REMARK 620 3 FES G1460 S2 113.7 92.1
REMARK 620 4 HIS G 123 ND1 93.1 120.4 118.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 G1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 233 NE2
REMARK 620 2 HIS G 239 NE2 93.9
REMARK 620 3 ASP G 388 OD1 110.7 99.1
REMARK 620 4 ASP G 388 OD2 163.2 88.3 52.6
REMARK 620 5 HOH G2013 O 87.6 78.8 161.8 109.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES I1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 100 SG
REMARK 620 2 FES I1460 S1 116.2
REMARK 620 3 FES I1460 S2 111.4 92.2
REMARK 620 4 CYS I 120 SG 119.1 106.7 107.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES I1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 102 ND1
REMARK 620 2 FES I1460 S1 128.8
REMARK 620 3 FES I1460 S2 102.4 91.7
REMARK 620 4 HIS I 123 ND1 96.2 123.4 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 I1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS I 233 NE2
REMARK 620 2 HIS I 239 NE2 89.3
REMARK 620 3 ASP I 388 OD1 100.8 90.4
REMARK 620 4 ASP I 388 OD2 153.2 91.7 52.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES K1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 100 SG
REMARK 620 2 FES K1460 S1 116.4
REMARK 620 3 FES K1460 S2 108.0 90.4
REMARK 620 4 CYS K 120 SG 129.7 106.3 96.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES K1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 102 ND1
REMARK 620 2 FES K1460 S1 114.5
REMARK 620 3 FES K1460 S2 131.2 90.4
REMARK 620 4 HIS K 123 ND1 90.1 113.2 118.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 K1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 233 NE2
REMARK 620 2 HIS K 239 NE2 86.6
REMARK 620 3 ASP K 388 OD2 143.1 89.7
REMARK 620 4 ASP K 388 OD1 91.3 85.8 51.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES M1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 100 SG
REMARK 620 2 FES M1460 S1 117.6
REMARK 620 3 FES M1460 S2 108.5 92.8
REMARK 620 4 CYS M 120 SG 119.4 109.2 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES M1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 102 ND1
REMARK 620 2 FES M1460 S1 126.2
REMARK 620 3 FES M1460 S2 107.6 92.3
REMARK 620 4 HIS M 123 ND1 96.7 120.5 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 M1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS M 233 NE2
REMARK 620 2 HIS M 239 NE2 90.4
REMARK 620 3 ASP M 388 OD1 102.2 90.8
REMARK 620 4 ASP M 388 OD2 157.0 94.1 55.2
REMARK 620 5 HOH M2034 O 128.8 98.7 127.6 72.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES O1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 100 SG
REMARK 620 2 FES O1460 S1 103.4
REMARK 620 3 FES O1460 S2 100.0 92.4
REMARK 620 4 CYS O 120 SG 125.9 119.5 108.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES O1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 102 ND1
REMARK 620 2 FES O1460 S1 124.4
REMARK 620 3 FES O1460 S2 116.5 92.2
REMARK 620 4 HIS O 123 ND1 97.5 111.7 116.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 O1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 233 NE2
REMARK 620 2 HIS O 239 NE2 97.0
REMARK 620 3 ASP O 388 OD1 101.3 104.5
REMARK 620 4 ASP O 388 OD2 156.2 95.3 55.7
REMARK 620 5 HOH O2053 O 115.4 124.0 111.6 73.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES Q1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Q 100 SG
REMARK 620 2 FES Q1460 S1 115.0
REMARK 620 3 FES Q1460 S2 110.5 93.0
REMARK 620 4 CYS Q 120 SG 119.2 106.1 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES Q1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 102 ND1
REMARK 620 2 FES Q1460 S1 120.8
REMARK 620 3 FES Q1460 S2 103.4 92.4
REMARK 620 4 HIS Q 123 ND1 100.0 119.4 121.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 Q1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS Q 233 NE2
REMARK 620 2 HIS Q 239 NE2 84.4
REMARK 620 3 ASP Q 388 OD1 96.8 105.0
REMARK 620 4 ASP Q 388 OD2 156.0 96.8 59.6
REMARK 620 5 HOH Q2048 O 73.7 76.2 170.4 129.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES S1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S 100 SG
REMARK 620 2 FES S1460 S1 111.8
REMARK 620 3 FES S1460 S2 107.3 90.7
REMARK 620 4 CYS S 120 SG 125.9 108.1 107.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES S1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 102 ND1
REMARK 620 2 FES S1460 S1 118.3
REMARK 620 3 FES S1460 S2 83.4 90.7
REMARK 620 4 HIS S 123 ND1 90.1 143.4 116.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 S1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS S 233 NE2
REMARK 620 2 HIS S 239 NE2 86.4
REMARK 620 3 ASP S 388 OD1 94.2 86.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES U1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS U 100 SG
REMARK 620 2 FES U1460 S1 101.0
REMARK 620 3 FES U1460 S2 92.8 91.8
REMARK 620 4 CYS U 120 SG 120.7 128.7 112.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES U1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS U 102 ND1
REMARK 620 2 FES U1460 S1 123.1
REMARK 620 3 FES U1460 S2 119.7 91.8
REMARK 620 4 HIS U 123 ND1 94.7 114.6 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 U1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS U 233 NE2
REMARK 620 2 HIS U 239 NE2 90.9
REMARK 620 3 ASP U 388 OD1 96.6 92.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES W1460 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS W 100 SG
REMARK 620 2 FES W1460 S1 112.6
REMARK 620 3 FES W1460 S2 110.8 91.2
REMARK 620 4 CYS W 120 SG 125.9 111.8 97.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES W1460 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS W 102 ND1
REMARK 620 2 FES W1460 S1 113.4
REMARK 620 3 FES W1460 S2 113.6 91.1
REMARK 620 4 HIS W 123 ND1 95.2 128.6 116.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE2 W1461 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS W 233 NE2
REMARK 620 2 HIS W 239 NE2 86.3
REMARK 620 3 ASP W 388 OD2 149.7 102.9
REMARK 620 4 ASP W 388 OD1 95.8 92.8 55.4
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 FES A 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL A 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES C 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 C 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL C 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 E 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL E 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES G 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 G 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL G 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES I 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 I 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL I 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES K 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 K 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL K 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES M 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 M 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL M 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES O 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 O 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL O 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES Q 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 Q 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL Q 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES S 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 S 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL S 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES U 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 U 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL U 1462
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES W 1460
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 W 1461
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BNL W 1462
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2XR8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BIPHENYL DIOXYGENASE FROM BURKHOLDERIA
REMARK 900 XENOVORANS LB400
DBREF 2XRX A 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX B 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX C 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX D 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX E 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX F 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX G 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX H 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX I 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX J 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX K 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX L 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX M 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX N 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX O 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX P 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX Q 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX R 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX S 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX T 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX U 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX V 1 188 UNP P37334 BPHE_BURXL 1 188
DBREF 2XRX W 1 459 UNP P37333 BPHA_BURXL 1 459
DBREF 2XRX X 1 188 UNP P37334 BPHE_BURXL 1 188
SEQRES 1 A 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 A 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 A 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 A 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 A 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 A 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 A 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 A 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 A 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 A 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 A 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 A 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 A 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 A 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 A 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 A 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 A 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 A 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 A 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 A 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 A 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 A 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 A 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 A 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 A 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 A 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 A 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 A 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 A 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 A 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 A 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 A 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 A 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 A 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 A 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 A 459 THR LEU LYS PRO
SEQRES 1 B 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 B 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 B 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 B 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 B 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 B 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 B 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 B 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 B 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 B 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 B 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 B 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 B 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 B 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 B 188 ASN LEU SER MET PHE PHE
SEQRES 1 C 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 C 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 C 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 C 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 C 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 C 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 C 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 C 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 C 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 C 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 C 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 C 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 C 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 C 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 C 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 C 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 C 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 C 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 C 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 C 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 C 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 C 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 C 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 C 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 C 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 C 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 C 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 C 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 C 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 C 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 C 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 C 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 C 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 C 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 C 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 C 459 THR LEU LYS PRO
SEQRES 1 D 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 D 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 D 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 D 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 D 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 D 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 D 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 D 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 D 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 D 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 D 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 D 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 D 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 D 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 D 188 ASN LEU SER MET PHE PHE
SEQRES 1 E 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 E 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 E 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 E 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 E 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 E 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 E 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 E 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 E 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 E 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 E 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 E 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 E 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 E 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 E 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 E 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 E 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 E 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 E 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 E 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 E 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 E 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 E 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 E 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 E 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 E 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 E 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 E 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 E 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 E 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 E 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 E 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 E 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 E 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 E 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 E 459 THR LEU LYS PRO
SEQRES 1 F 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 F 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 F 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 F 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 F 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 F 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 F 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 F 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 F 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 F 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 F 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 F 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 F 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 F 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 F 188 ASN LEU SER MET PHE PHE
SEQRES 1 G 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 G 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 G 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 G 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 G 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 G 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 G 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 G 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 G 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 G 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 G 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 G 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 G 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 G 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 G 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 G 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 G 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 G 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 G 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 G 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 G 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 G 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 G 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 G 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 G 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 G 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 G 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 G 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 G 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 G 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 G 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 G 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 G 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 G 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 G 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 G 459 THR LEU LYS PRO
SEQRES 1 H 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 H 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 H 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 H 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 H 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 H 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 H 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 H 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 H 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 H 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 H 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 H 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 H 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 H 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 H 188 ASN LEU SER MET PHE PHE
SEQRES 1 I 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 I 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 I 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 I 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 I 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 I 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 I 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 I 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 I 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 I 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 I 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 I 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 I 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 I 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 I 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 I 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 I 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 I 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 I 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 I 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 I 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 I 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 I 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 I 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 I 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 I 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 I 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 I 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 I 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 I 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 I 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 I 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 I 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 I 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 I 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 I 459 THR LEU LYS PRO
SEQRES 1 J 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 J 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 J 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 J 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 J 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 J 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 J 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 J 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 J 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 J 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 J 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 J 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 J 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 J 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 J 188 ASN LEU SER MET PHE PHE
SEQRES 1 K 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 K 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 K 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 K 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 K 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 K 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 K 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 K 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 K 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 K 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 K 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 K 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 K 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 K 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 K 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 K 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 K 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 K 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 K 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 K 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 K 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 K 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 K 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 K 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 K 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 K 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 K 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 K 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 K 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 K 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 K 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 K 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 K 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 K 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 K 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 K 459 THR LEU LYS PRO
SEQRES 1 L 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 L 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 L 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 L 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 L 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 L 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 L 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 L 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 L 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 L 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 L 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 L 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 L 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 L 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 L 188 ASN LEU SER MET PHE PHE
SEQRES 1 M 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 M 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 M 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 M 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 M 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 M 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 M 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 M 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 M 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 M 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 M 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 M 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 M 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 M 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 M 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 M 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 M 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 M 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 M 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 M 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 M 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 M 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 M 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 M 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 M 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 M 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 M 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 M 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 M 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 M 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 M 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 M 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 M 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 M 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 M 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 M 459 THR LEU LYS PRO
SEQRES 1 N 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 N 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 N 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 N 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 N 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 N 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 N 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 N 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 N 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 N 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 N 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 N 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 N 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 N 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 N 188 ASN LEU SER MET PHE PHE
SEQRES 1 O 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 O 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 O 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 O 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 O 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 O 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 O 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 O 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 O 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 O 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 O 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 O 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 O 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 O 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 O 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 O 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 O 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 O 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 O 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 O 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 O 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 O 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 O 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 O 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 O 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 O 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 O 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 O 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 O 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 O 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 O 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 O 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 O 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 O 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 O 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 O 459 THR LEU LYS PRO
SEQRES 1 P 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 P 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 P 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 P 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 P 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 P 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 P 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 P 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 P 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 P 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 P 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 P 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 P 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 P 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 P 188 ASN LEU SER MET PHE PHE
SEQRES 1 Q 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 Q 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 Q 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 Q 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 Q 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 Q 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 Q 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 Q 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 Q 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 Q 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 Q 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 Q 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 Q 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 Q 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 Q 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 Q 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 Q 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 Q 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 Q 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 Q 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 Q 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 Q 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 Q 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 Q 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 Q 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 Q 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 Q 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 Q 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 Q 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 Q 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 Q 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 Q 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 Q 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 Q 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 Q 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 Q 459 THR LEU LYS PRO
SEQRES 1 R 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 R 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 R 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 R 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 R 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 R 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 R 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 R 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 R 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 R 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 R 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 R 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 R 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 R 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 R 188 ASN LEU SER MET PHE PHE
SEQRES 1 S 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 S 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 S 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 S 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 S 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 S 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 S 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 S 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 S 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 S 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 S 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 S 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 S 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 S 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 S 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 S 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 S 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 S 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 S 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 S 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 S 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 S 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 S 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 S 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 S 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 S 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 S 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 S 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 S 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 S 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 S 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 S 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 S 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 S 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 S 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 S 459 THR LEU LYS PRO
SEQRES 1 T 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 T 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 T 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 T 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 T 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 T 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 T 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 T 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 T 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 T 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 T 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 T 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 T 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 T 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 T 188 ASN LEU SER MET PHE PHE
SEQRES 1 U 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 U 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 U 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 U 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 U 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 U 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 U 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 U 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 U 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 U 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 U 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 U 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 U 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 U 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 U 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 U 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 U 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 U 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 U 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 U 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 U 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 U 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 U 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 U 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 U 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 U 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 U 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 U 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 U 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 U 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 U 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 U 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 U 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 U 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 U 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 U 459 THR LEU LYS PRO
SEQRES 1 V 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 V 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 V 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 V 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 V 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 V 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 V 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 V 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 V 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 V 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 V 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 V 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 V 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 V 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 V 188 ASN LEU SER MET PHE PHE
SEQRES 1 W 459 MET SER SER ALA ILE LYS GLU VAL GLN GLY ALA PRO VAL
SEQRES 2 W 459 LYS TRP VAL THR ASN TRP THR PRO GLU ALA ILE ARG GLY
SEQRES 3 W 459 LEU VAL ASP GLN GLU LYS GLY LEU LEU ASP PRO ARG ILE
SEQRES 4 W 459 TYR ALA ASP GLN SER LEU TYR GLU LEU GLU LEU GLU ARG
SEQRES 5 W 459 VAL PHE GLY ARG SER TRP LEU LEU LEU GLY HIS GLU SER
SEQRES 6 W 459 HIS VAL PRO GLU THR GLY ASP PHE LEU ALA THR TYR MET
SEQRES 7 W 459 GLY GLU ASP PRO VAL VAL MET VAL ARG GLN LYS ASP LYS
SEQRES 8 W 459 SER ILE LYS VAL PHE LEU ASN GLN CYS ARG HIS ARG GLY
SEQRES 9 W 459 MET ARG ILE CYS ARG SER ASP ALA GLY ASN ALA LYS ALA
SEQRES 10 W 459 PHE THR CYS SER TYR HIS GLY TRP ALA TYR ASP ILE ALA
SEQRES 11 W 459 GLY LYS LEU VAL ASN VAL PRO PHE GLU LYS GLU ALA PHE
SEQRES 12 W 459 CYS ASP LYS LYS GLU GLY ASP CYS GLY PHE ASP LYS ALA
SEQRES 13 W 459 GLU TRP GLY PRO LEU GLN ALA ARG VAL ALA THR TYR LYS
SEQRES 14 W 459 GLY LEU VAL PHE ALA ASN TRP ASP VAL GLN ALA PRO ASP
SEQRES 15 W 459 LEU GLU THR TYR LEU GLY ASP ALA ARG PRO TYR MET ASP
SEQRES 16 W 459 VAL MET LEU ASP ARG THR PRO ALA GLY THR VAL ALA ILE
SEQRES 17 W 459 GLY GLY MET GLN LYS TRP VAL ILE PRO CYS ASN TRP LYS
SEQRES 18 W 459 PHE ALA ALA GLU GLN PHE CYS SER ASP MET TYR HIS ALA
SEQRES 19 W 459 GLY THR THR THR HIS LEU SER GLY ILE LEU ALA GLY ILE
SEQRES 20 W 459 PRO PRO GLU MET ASP LEU SER GLN ALA GLN ILE PRO THR
SEQRES 21 W 459 LYS GLY ASN GLN PHE ARG ALA ALA TRP GLY GLY HIS GLY
SEQRES 22 W 459 SER GLY TRP TYR VAL ASP GLU PRO GLY SER LEU LEU ALA
SEQRES 23 W 459 VAL MET GLY PRO LYS VAL THR GLN TYR TRP THR GLU GLY
SEQRES 24 W 459 PRO ALA ALA GLU LEU ALA GLU GLN ARG LEU GLY HIS THR
SEQRES 25 W 459 GLY MET PRO VAL ARG ARG MET VAL GLY GLN HIS MET THR
SEQRES 26 W 459 ILE PHE PRO THR CYS SER PHE LEU PRO THR PHE ASN ASN
SEQRES 27 W 459 ILE ARG ILE TRP HIS PRO ARG GLY PRO ASN GLU ILE GLU
SEQRES 28 W 459 VAL TRP ALA PHE THR LEU VAL ASP ALA ASP ALA PRO ALA
SEQRES 29 W 459 GLU ILE LYS GLU GLU TYR ARG ARG HIS ASN ILE ARG ASN
SEQRES 30 W 459 PHE SER ALA GLY GLY VAL PHE GLU GLN ASP ASP GLY GLU
SEQRES 31 W 459 ASN TRP VAL GLU ILE GLN LYS GLY LEU ARG GLY TYR LYS
SEQRES 32 W 459 ALA LYS SER GLN PRO LEU ASN ALA GLN MET GLY LEU GLY
SEQRES 33 W 459 ARG SER GLN THR GLY HIS PRO ASP PHE PRO GLY ASN VAL
SEQRES 34 W 459 GLY TYR VAL TYR ALA GLU GLU ALA ALA ARG GLY MET TYR
SEQRES 35 W 459 HIS HIS TRP MET ARG MET MET SER GLU PRO SER TRP ALA
SEQRES 36 W 459 THR LEU LYS PRO
SEQRES 1 X 188 MET THR ASN PRO SER PRO HIS PHE PHE LYS THR PHE GLU
SEQRES 2 X 188 TRP PRO SER LYS ALA ALA GLY LEU GLU LEU GLN ASN GLU
SEQRES 3 X 188 ILE GLU GLN PHE TYR TYR ARG GLU ALA GLN LEU LEU ASP
SEQRES 4 X 188 HIS ARG ALA TYR GLU ALA TRP PHE ALA LEU LEU ASP LYS
SEQRES 5 X 188 ASP ILE HIS TYR PHE MET PRO LEU ARG THR ASN ARG MET
SEQRES 6 X 188 ILE ARG GLU GLY GLU LEU GLU TYR SER GLY ASP GLN ASP
SEQRES 7 X 188 LEU ALA HIS PHE ASP GLU THR HIS GLU THR MET TYR GLY
SEQRES 8 X 188 ARG ILE ARG LYS VAL THR SER ASP VAL GLY TRP ALA GLU
SEQRES 9 X 188 ASN PRO PRO SER ARG THR ARG HIS LEU VAL SER ASN VAL
SEQRES 10 X 188 ILE VAL LYS GLU THR ALA THR PRO ASP THR PHE GLU VAL
SEQRES 11 X 188 ASN SER ALA PHE ILE LEU TYR ARG ASN ARG LEU GLU ARG
SEQRES 12 X 188 GLN VAL ASP ILE PHE ALA GLY GLU ARG ARG ASP VAL LEU
SEQRES 13 X 188 ARG ARG ALA ASP ASN ASN LEU GLY PHE SER ILE ALA LYS
SEQRES 14 X 188 ARG THR ILE LEU LEU ASP ALA SER THR LEU LEU SER ASN
SEQRES 15 X 188 ASN LEU SER MET PHE PHE
HET FES A1460 4
HET FE2 A1461 1
HET BNL A1462 12
HET FES C1460 4
HET FE2 C1461 1
HET BNL C1462 12
HET FES E1460 4
HET FE2 E1461 1
HET BNL E1462 12
HET FES G1460 4
HET FE2 G1461 1
HET BNL G1462 12
HET FES I1460 4
HET FE2 I1461 1
HET BNL I1462 12
HET FES K1460 4
HET FE2 K1461 1
HET BNL K1462 12
HET FES M1460 4
HET FE2 M1461 1
HET BNL M1462 12
HET FES O1460 4
HET FE2 O1461 1
HET BNL O1462 12
HET FES Q1460 4
HET FE2 Q1461 1
HET BNL Q1462 12
HET FES S1460 4
HET FE2 S1461 1
HET BNL S1462 12
HET FES U1460 4
HET FE2 U1461 1
HET BNL U1462 12
HET FES W1460 4
HET FE2 W1461 1
HET BNL W1462 12
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM FE2 FE (II) ION
HETNAM BNL BIPHENYL
FORMUL 25 FES 12(FE2 S2)
FORMUL 26 FE2 12(FE 2+)
FORMUL 27 BNL 12(C12 H10)
FORMUL 61 HOH *694(H2 O)
HELIX 1 1 THR A 20 GLY A 26 1 7
HELIX 2 2 PRO A 37 ALA A 41 5 5
HELIX 3 3 ASP A 42 VAL A 53 1 12
HELIX 4 4 ASP A 154 TRP A 158 5 5
HELIX 5 5 ASP A 182 GLY A 188 1 7
HELIX 6 6 ALA A 190 ASP A 199 1 10
HELIX 7 7 ASN A 219 ASP A 230 1 12
HELIX 8 8 MET A 231 THR A 236 1 6
HELIX 9 9 HIS A 239 GLY A 246 1 8
HELIX 10 10 ASP A 252 ALA A 256 5 5
HELIX 11 11 GLU A 280 GLU A 298 1 19
HELIX 12 12 GLY A 299 LEU A 309 1 11
HELIX 13 13 GLY A 310 GLY A 313 5 4
HELIX 14 14 PRO A 315 ARG A 317 5 3
HELIX 15 15 PRO A 363 SER A 379 1 17
HELIX 16 16 PHE A 384 LEU A 399 1 16
HELIX 17 17 TYR A 402 SER A 406 5 5
HELIX 18 18 GLU A 435 GLU A 451 1 17
HELIX 19 19 SER A 453 LYS A 458 1 6
HELIX 20 20 GLY B 20 HIS B 40 1 21
HELIX 21 21 ALA B 42 ALA B 48 1 7
HELIX 22 22 MET B 65 GLU B 72 5 8
HELIX 23 23 THR B 85 THR B 97 1 13
HELIX 24 24 GLY B 101 ASN B 105 5 5
HELIX 25 25 THR C 20 LEU C 27 1 8
HELIX 26 26 PRO C 37 ALA C 41 5 5
HELIX 27 27 ASP C 42 VAL C 53 1 12
HELIX 28 28 SER C 65 VAL C 67 5 3
HELIX 29 29 ASP C 154 TRP C 158 5 5
HELIX 30 30 ASP C 182 GLY C 188 1 7
HELIX 31 31 ALA C 190 ASP C 199 1 10
HELIX 32 32 ASN C 219 ASP C 230 1 12
HELIX 33 33 MET C 231 THR C 236 1 6
HELIX 34 34 HIS C 239 ILE C 247 1 9
HELIX 35 35 PRO C 281 GLY C 289 1 9
HELIX 36 36 GLY C 289 GLU C 298 1 10
HELIX 37 37 GLY C 299 LEU C 309 1 11
HELIX 38 38 GLY C 310 GLY C 313 5 4
HELIX 39 39 PRO C 315 ARG C 317 5 3
HELIX 40 40 PRO C 363 SER C 379 1 17
HELIX 41 41 PHE C 384 LEU C 399 1 16
HELIX 42 42 TYR C 402 SER C 406 5 5
HELIX 43 43 GLU C 435 GLU C 451 1 17
HELIX 44 44 SER C 453 LYS C 458 1 6
HELIX 45 45 GLY D 20 HIS D 40 1 21
HELIX 46 46 ALA D 42 ALA D 48 1 7
HELIX 47 47 MET D 65 GLU D 72 5 8
HELIX 48 48 THR D 85 THR D 97 1 13
HELIX 49 49 GLY D 101 ASN D 105 5 5
HELIX 50 50 THR E 20 GLY E 26 1 7
HELIX 51 51 PRO E 37 ALA E 41 5 5
HELIX 52 52 ASP E 42 VAL E 53 1 12
HELIX 53 53 SER E 65 VAL E 67 5 3
HELIX 54 54 ASP E 154 TRP E 158 5 5
HELIX 55 55 ASP E 182 GLY E 188 1 7
HELIX 56 56 ALA E 190 ASP E 199 1 10
HELIX 57 57 ASN E 219 ASP E 230 1 12
HELIX 58 58 HIS E 239 ILE E 247 1 9
HELIX 59 59 ASP E 252 ALA E 256 5 5
HELIX 60 60 GLU E 280 GLY E 289 1 10
HELIX 61 61 GLY E 289 GLU E 298 1 10
HELIX 62 62 GLY E 299 LEU E 309 1 11
HELIX 63 63 PRO E 363 SER E 379 1 17
HELIX 64 64 PHE E 384 LEU E 399 1 16
HELIX 65 65 TYR E 402 SER E 406 5 5
HELIX 66 66 GLU E 435 GLU E 451 1 17
HELIX 67 67 SER E 453 LYS E 458 1 6
HELIX 68 68 GLY F 20 HIS F 40 1 21
HELIX 69 69 ALA F 42 ALA F 48 1 7
HELIX 70 70 MET F 65 GLU F 72 5 8
HELIX 71 71 THR F 85 THR F 97 1 13
HELIX 72 72 GLY F 101 ASN F 105 5 5
HELIX 73 73 THR G 20 GLY G 26 1 7
HELIX 74 74 PRO G 37 ALA G 41 5 5
HELIX 75 75 ASP G 42 VAL G 53 1 12
HELIX 76 76 SER G 65 VAL G 67 5 3
HELIX 77 77 ASP G 154 TRP G 158 5 5
HELIX 78 78 ASP G 182 GLY G 188 1 7
HELIX 79 79 ALA G 190 ASP G 199 1 10
HELIX 80 80 ASN G 219 ASP G 230 1 12
HELIX 81 81 MET G 231 THR G 236 1 6
HELIX 82 82 HIS G 239 ILE G 247 1 9
HELIX 83 83 GLU G 280 GLY G 289 1 10
HELIX 84 84 GLY G 289 GLU G 298 1 10
HELIX 85 85 GLY G 299 LEU G 309 1 11
HELIX 86 86 PRO G 363 SER G 379 1 17
HELIX 87 87 PHE G 384 LEU G 399 1 16
HELIX 88 88 TYR G 402 SER G 406 5 5
HELIX 89 89 GLU G 435 GLU G 451 1 17
HELIX 90 90 SER G 453 LYS G 458 1 6
HELIX 91 91 GLY H 20 HIS H 40 1 21
HELIX 92 92 ALA H 42 ALA H 48 1 7
HELIX 93 93 MET H 65 GLU H 72 5 8
HELIX 94 94 THR H 85 THR H 97 1 13
HELIX 95 95 GLY H 101 ASN H 105 5 5
HELIX 96 96 THR I 20 GLY I 26 1 7
HELIX 97 97 PRO I 37 ALA I 41 5 5
HELIX 98 98 ASP I 42 VAL I 53 1 12
HELIX 99 99 SER I 65 VAL I 67 5 3
HELIX 100 100 ASP I 182 GLY I 188 1 7
HELIX 101 101 ALA I 190 ASP I 199 1 10
HELIX 102 102 ASN I 219 ASP I 230 1 12
HELIX 103 103 MET I 231 THR I 236 1 6
HELIX 104 104 HIS I 239 ILE I 247 1 9
HELIX 105 105 GLU I 280 GLY I 289 1 10
HELIX 106 106 GLY I 289 GLU I 298 1 10
HELIX 107 107 GLU I 298 LEU I 309 1 12
HELIX 108 108 GLY I 310 GLY I 313 5 4
HELIX 109 109 PRO I 315 ARG I 317 5 3
HELIX 110 110 PRO I 363 SER I 379 1 17
HELIX 111 111 PHE I 384 LEU I 399 1 16
HELIX 112 112 GLU I 435 GLU I 451 1 17
HELIX 113 113 SER I 453 LYS I 458 1 6
HELIX 114 114 GLY J 20 HIS J 40 1 21
HELIX 115 115 ALA J 42 ALA J 48 1 7
HELIX 116 116 MET J 65 GLU J 72 5 8
HELIX 117 117 THR J 85 THR J 97 1 13
HELIX 118 118 GLY J 101 ASN J 105 5 5
HELIX 119 119 THR K 20 ARG K 25 1 6
HELIX 120 120 PRO K 37 ASP K 42 1 6
HELIX 121 121 ASP K 42 VAL K 53 1 12
HELIX 122 122 PHE K 54 SER K 57 5 4
HELIX 123 123 SER K 65 VAL K 67 5 3
HELIX 124 124 ASP K 182 GLY K 188 1 7
HELIX 125 125 ALA K 190 ASP K 199 1 10
HELIX 126 126 ASN K 219 ASP K 230 1 12
HELIX 127 127 HIS K 239 ILE K 247 1 9
HELIX 128 128 ASP K 252 ALA K 256 5 5
HELIX 129 129 GLU K 280 GLY K 289 1 10
HELIX 130 130 GLY K 289 GLU K 298 1 10
HELIX 131 131 GLY K 299 LEU K 309 1 11
HELIX 132 132 GLY K 310 GLY K 313 5 4
HELIX 133 133 PRO K 363 SER K 379 1 17
HELIX 134 134 PHE K 384 LEU K 399 1 16
HELIX 135 135 GLY K 401 SER K 406 1 6
HELIX 136 136 GLU K 435 GLU K 451 1 17
HELIX 137 137 SER K 453 LYS K 458 1 6
HELIX 138 138 GLY L 20 ASP L 39 1 20
HELIX 139 139 ALA L 42 ALA L 48 1 7
HELIX 140 140 MET L 65 GLU L 72 5 8
HELIX 141 141 THR L 85 THR L 97 1 13
HELIX 142 142 GLY L 101 ASN L 105 5 5
HELIX 143 143 THR M 20 GLY M 26 1 7
HELIX 144 144 PRO M 37 ALA M 41 5 5
HELIX 145 145 ASP M 42 VAL M 53 1 12
HELIX 146 146 SER M 65 VAL M 67 5 3
HELIX 147 147 ASP M 154 TRP M 158 5 5
HELIX 148 148 ASP M 182 GLY M 188 1 7
HELIX 149 149 ALA M 190 ASP M 199 1 10
HELIX 150 150 ASN M 219 ASP M 230 1 12
HELIX 151 151 HIS M 239 GLY M 246 1 8
HELIX 152 152 GLU M 280 GLU M 298 1 19
HELIX 153 153 GLY M 299 LEU M 309 1 11
HELIX 154 154 GLY M 310 GLY M 313 5 4
HELIX 155 155 PRO M 363 SER M 379 1 17
HELIX 156 156 PHE M 384 LEU M 399 1 16
HELIX 157 157 TYR M 402 SER M 406 5 5
HELIX 158 158 GLU M 435 GLU M 451 1 17
HELIX 159 159 SER M 453 LYS M 458 1 6
HELIX 160 160 PHE N 8 PHE N 12 5 5
HELIX 161 161 GLY N 20 HIS N 40 1 21
HELIX 162 162 ALA N 42 ALA N 48 1 7
HELIX 163 163 MET N 65 GLU N 72 5 8
HELIX 164 164 THR N 85 THR N 97 1 13
HELIX 165 165 GLY N 101 ASN N 105 5 5
HELIX 166 166 THR O 20 GLY O 26 1 7
HELIX 167 167 PRO O 37 ALA O 41 5 5
HELIX 168 168 ASP O 42 VAL O 53 1 12
HELIX 169 169 PHE O 54 SER O 57 5 4
HELIX 170 170 SER O 65 VAL O 67 5 3
HELIX 171 171 ASP O 154 TRP O 158 5 5
HELIX 172 172 ASP O 182 GLY O 188 1 7
HELIX 173 173 ALA O 190 ASP O 199 1 10
HELIX 174 174 ASN O 219 ASP O 230 1 12
HELIX 175 175 HIS O 239 ILE O 247 1 9
HELIX 176 176 GLU O 280 GLU O 298 1 19
HELIX 177 177 GLY O 299 LEU O 309 1 11
HELIX 178 178 GLY O 310 THR O 312 5 3
HELIX 179 179 PRO O 315 ARG O 317 5 3
HELIX 180 180 PRO O 334 PHE O 336 5 3
HELIX 181 181 PRO O 363 SER O 379 1 17
HELIX 182 182 PHE O 384 LEU O 399 1 16
HELIX 183 183 TYR O 402 SER O 406 5 5
HELIX 184 184 GLU O 435 GLU O 451 1 17
HELIX 185 185 SER O 453 LYS O 458 1 6
HELIX 186 186 GLY P 20 HIS P 40 1 21
HELIX 187 187 ALA P 42 ALA P 48 1 7
HELIX 188 188 MET P 65 GLU P 72 5 8
HELIX 189 189 THR P 85 THR P 97 1 13
HELIX 190 190 GLY P 101 ASN P 105 5 5
HELIX 191 191 THR Q 20 GLY Q 26 1 7
HELIX 192 192 PRO Q 37 ALA Q 41 5 5
HELIX 193 193 ASP Q 42 VAL Q 53 1 12
HELIX 194 194 PHE Q 54 SER Q 57 5 4
HELIX 195 195 SER Q 65 VAL Q 67 5 3
HELIX 196 196 ASP Q 154 TRP Q 158 5 5
HELIX 197 197 ASP Q 182 GLY Q 188 1 7
HELIX 198 198 ALA Q 190 ASP Q 199 1 10
HELIX 199 199 ASN Q 219 ASP Q 230 1 12
HELIX 200 200 HIS Q 239 GLY Q 246 1 8
HELIX 201 201 GLU Q 280 GLY Q 289 1 10
HELIX 202 202 GLY Q 289 GLU Q 298 1 10
HELIX 203 203 GLY Q 299 LEU Q 309 1 11
HELIX 204 204 GLY Q 310 GLY Q 313 5 4
HELIX 205 205 PRO Q 315 ARG Q 317 5 3
HELIX 206 206 PRO Q 363 SER Q 379 1 17
HELIX 207 207 PHE Q 384 LEU Q 399 1 16
HELIX 208 208 TYR Q 402 SER Q 406 5 5
HELIX 209 209 GLU Q 435 GLU Q 451 1 17
HELIX 210 210 SER Q 453 LYS Q 458 1 6
HELIX 211 211 GLY R 20 HIS R 40 1 21
HELIX 212 212 ALA R 42 ALA R 48 1 7
HELIX 213 213 MET R 65 GLU R 72 5 8
HELIX 214 214 THR R 85 THR R 97 1 13
HELIX 215 215 GLY R 101 ASN R 105 5 5
HELIX 216 216 THR S 20 GLY S 26 1 7
HELIX 217 217 PRO S 37 ALA S 41 5 5
HELIX 218 218 ASP S 42 VAL S 53 1 12
HELIX 219 219 SER S 65 VAL S 67 5 3
HELIX 220 220 ASP S 154 TRP S 158 5 5
HELIX 221 221 ASP S 182 GLY S 188 1 7
HELIX 222 222 ALA S 190 ASP S 199 1 10
HELIX 223 223 ASN S 219 ASP S 230 1 12
HELIX 224 224 HIS S 239 ILE S 247 1 9
HELIX 225 225 ASP S 252 ALA S 256 5 5
HELIX 226 226 GLU S 280 GLU S 298 1 19
HELIX 227 227 GLY S 299 LEU S 309 1 11
HELIX 228 228 GLY S 310 GLY S 313 5 4
HELIX 229 229 PRO S 315 ARG S 317 5 3
HELIX 230 230 PRO S 363 PHE S 378 1 16
HELIX 231 231 PHE S 384 LEU S 399 1 16
HELIX 232 232 TYR S 402 SER S 406 5 5
HELIX 233 233 GLU S 435 GLU S 451 1 17
HELIX 234 234 SER S 453 LYS S 458 1 6
HELIX 235 235 GLY T 20 HIS T 40 1 21
HELIX 236 236 ALA T 42 ALA T 48 1 7
HELIX 237 237 MET T 65 GLY T 69 5 5
HELIX 238 238 THR T 85 THR T 97 1 13
HELIX 239 239 GLY T 101 ASN T 105 5 5
HELIX 240 240 THR U 20 GLY U 26 1 7
HELIX 241 241 PRO U 37 TYR U 40 5 4
HELIX 242 242 ASP U 42 VAL U 53 1 12
HELIX 243 243 SER U 65 VAL U 67 5 3
HELIX 244 244 ASP U 154 TRP U 158 5 5
HELIX 245 245 ASP U 182 GLY U 188 1 7
HELIX 246 246 ALA U 190 ASP U 199 1 10
HELIX 247 247 ASN U 219 ASP U 230 1 12
HELIX 248 248 HIS U 239 ALA U 245 1 7
HELIX 249 249 GLU U 280 MET U 288 1 9
HELIX 250 250 GLY U 289 GLU U 298 1 10
HELIX 251 251 GLY U 299 LEU U 309 1 11
HELIX 252 252 PRO U 363 SER U 379 1 17
HELIX 253 253 PHE U 384 LEU U 399 1 16
HELIX 254 254 GLU U 435 GLU U 451 1 17
HELIX 255 255 SER U 453 LYS U 458 1 6
HELIX 256 256 GLY V 20 HIS V 40 1 21
HELIX 257 257 ALA V 42 ALA V 48 1 7
HELIX 258 258 MET V 65 GLU V 72 5 8
HELIX 259 259 THR V 85 THR V 97 1 13
HELIX 260 260 GLY V 101 ASN V 105 5 5
HELIX 261 261 THR W 20 LEU W 27 1 8
HELIX 262 262 PRO W 37 TYR W 40 5 4
HELIX 263 263 ASP W 42 VAL W 53 1 12
HELIX 264 264 SER W 65 VAL W 67 5 3
HELIX 265 265 ASP W 182 GLY W 188 1 7
HELIX 266 266 ALA W 190 ASP W 199 1 10
HELIX 267 267 ASN W 219 ASP W 230 1 12
HELIX 268 268 ASP W 230 GLY W 235 1 6
HELIX 269 269 HIS W 239 ALA W 245 1 7
HELIX 270 270 ASP W 252 ALA W 256 5 5
HELIX 271 271 GLU W 280 GLY W 289 1 10
HELIX 272 272 GLY W 289 GLU W 298 1 10
HELIX 273 273 GLU W 298 LEU W 309 1 12
HELIX 274 274 GLY W 310 GLY W 313 5 4
HELIX 275 275 PRO W 363 SER W 379 1 17
HELIX 276 276 PHE W 384 LEU W 399 1 16
HELIX 277 277 TYR W 402 SER W 406 5 5
HELIX 278 278 GLU W 435 GLU W 451 1 17
HELIX 279 279 SER W 453 LYS W 458 1 6
HELIX 280 280 GLY X 20 HIS X 40 1 21
HELIX 281 281 ALA X 42 ALA X 48 1 7
HELIX 282 282 MET X 65 GLU X 72 5 8
HELIX 283 283 THR X 85 THR X 97 1 13
HELIX 284 284 GLY X 101 ASN X 105 5 5
SHEET 1 AA 3 VAL A 28 ASP A 29 0
SHEET 2 AA 3 LEU A 34 LEU A 35 -1 O LEU A 34 N ASP A 29
SHEET 3 AA 3 LEU A 409 ASN A 410 -1 O LEU A 409 N LEU A 35
SHEET 1 AB 7 LEU A 59 HIS A 63 0
SHEET 2 AB 7 LEU A 171 ASN A 175 -1 O VAL A 172 N LEU A 61
SHEET 3 AB 7 GLN A 162 TYR A 168 -1 O ARG A 164 N ASN A 175
SHEET 4 AB 7 ILE A 93 LEU A 97 -1 O VAL A 95 N ALA A 163
SHEET 5 AB 7 ASP A 81 ARG A 87 -1 O VAL A 84 N PHE A 96
SHEET 6 AB 7 ASP A 72 MET A 78 -1 O ASP A 72 N ARG A 87
SHEET 7 AB 7 ALA A 112 ASN A 114 -1 O GLY A 113 N PHE A 73
SHEET 1 AC 3 PHE A 118 THR A 119 0
SHEET 2 AC 3 ALA A 126 TYR A 127 -1 O TYR A 127 N PHE A 118
SHEET 3 AC 3 LEU A 133 ASN A 135 -1 N VAL A 134 O ALA A 126
SHEET 1 AD 2 THR A 205 ALA A 207 0
SHEET 2 AD 2 ILE A 350 ASP A 359 -1 O VAL A 358 N VAL A 206
SHEET 1 AE 2 GLN A 212 ILE A 216 0
SHEET 2 AE 2 ILE A 350 ASP A 359 -1 O ILE A 350 N ILE A 216
SHEET 1 AF 8 ASN A 428 TYR A 431 0
SHEET 2 AF 8 GLY A 262 ARG A 266 -1 O GLN A 264 N GLY A 430
SHEET 3 AF 8 GLY A 273 VAL A 278 -1 O SER A 274 N PHE A 265
SHEET 4 AF 8 MET A 319 ILE A 326 -1 O VAL A 320 N TYR A 277
SHEET 5 AF 8 CYS A 330 LEU A 333 -1 O CYS A 330 N ILE A 326
SHEET 6 AF 8 ASN A 338 PRO A 344 -1 O ASN A 338 N LEU A 333
SHEET 7 AF 8 ILE A 350 ASP A 359 -1 O GLU A 351 N HIS A 343
SHEET 8 AF 8 GLN A 212 ILE A 216 -1 O GLN A 212 N ALA A 354
SHEET 1 AG 8 ASN A 428 TYR A 431 0
SHEET 2 AG 8 GLY A 262 ARG A 266 -1 O GLN A 264 N GLY A 430
SHEET 3 AG 8 GLY A 273 VAL A 278 -1 O SER A 274 N PHE A 265
SHEET 4 AG 8 MET A 319 ILE A 326 -1 O VAL A 320 N TYR A 277
SHEET 5 AG 8 CYS A 330 LEU A 333 -1 O CYS A 330 N ILE A 326
SHEET 6 AG 8 ASN A 338 PRO A 344 -1 O ASN A 338 N LEU A 333
SHEET 7 AG 8 ILE A 350 ASP A 359 -1 O GLU A 351 N HIS A 343
SHEET 8 AG 8 THR A 205 ALA A 207 -1 O VAL A 206 N VAL A 358
SHEET 1 BA 6 ALA B 80 GLU B 84 0
SHEET 2 BA 6 TYR B 56 PRO B 59 -1 O TYR B 56 N GLU B 84
SHEET 3 BA 6 PHE B 165 LEU B 174 1 O ARG B 170 N PHE B 57
SHEET 4 BA 6 GLN B 144 ARG B 158 -1 O GLU B 151 N LEU B 173
SHEET 5 BA 6 THR B 127 ARG B 140 -1 O PHE B 128 N LEU B 156
SHEET 6 BA 6 ARG B 109 GLU B 121 -1 O ARG B 109 N ASN B 139
SHEET 1 CA 3 VAL C 28 ASP C 29 0
SHEET 2 CA 3 LEU C 34 LEU C 35 -1 O LEU C 34 N ASP C 29
SHEET 3 CA 3 LEU C 409 ASN C 410 -1 O LEU C 409 N LEU C 35
SHEET 1 CB 7 LEU C 59 HIS C 63 0
SHEET 2 CB 7 LEU C 171 ASN C 175 -1 O VAL C 172 N LEU C 61
SHEET 3 CB 7 GLN C 162 TYR C 168 -1 O ARG C 164 N ASN C 175
SHEET 4 CB 7 ILE C 93 LEU C 97 -1 O VAL C 95 N ALA C 163
SHEET 5 CB 7 ASP C 81 ARG C 87 -1 O VAL C 84 N PHE C 96
SHEET 6 CB 7 ASP C 72 MET C 78 -1 O ASP C 72 N ARG C 87
SHEET 7 CB 7 ALA C 112 ASN C 114 -1 O GLY C 113 N PHE C 73
SHEET 1 CC 3 PHE C 118 THR C 119 0
SHEET 2 CC 3 ALA C 126 TYR C 127 -1 O TYR C 127 N PHE C 118
SHEET 3 CC 3 LEU C 133 ASN C 135 -1 N VAL C 134 O ALA C 126
SHEET 1 CD 2 THR C 205 ALA C 207 0
SHEET 2 CD 2 ILE C 350 ASP C 359 -1 O VAL C 358 N VAL C 206
SHEET 1 CE 2 GLN C 212 ILE C 216 0
SHEET 2 CE 2 ILE C 350 ASP C 359 -1 O ILE C 350 N ILE C 216
SHEET 1 CF 8 ASN C 428 TYR C 431 0
SHEET 2 CF 8 GLY C 262 ARG C 266 -1 O GLN C 264 N GLY C 430
SHEET 3 CF 8 GLY C 273 VAL C 278 -1 O SER C 274 N PHE C 265
SHEET 4 CF 8 MET C 319 ILE C 326 -1 O VAL C 320 N TYR C 277
SHEET 5 CF 8 CYS C 330 LEU C 333 -1 O CYS C 330 N ILE C 326
SHEET 6 CF 8 ASN C 338 PRO C 344 -1 O ASN C 338 N LEU C 333
SHEET 7 CF 8 ILE C 350 ASP C 359 -1 O GLU C 351 N HIS C 343
SHEET 8 CF 8 GLN C 212 ILE C 216 -1 O GLN C 212 N ALA C 354
SHEET 1 CG 8 ASN C 428 TYR C 431 0
SHEET 2 CG 8 GLY C 262 ARG C 266 -1 O GLN C 264 N GLY C 430
SHEET 3 CG 8 GLY C 273 VAL C 278 -1 O SER C 274 N PHE C 265
SHEET 4 CG 8 MET C 319 ILE C 326 -1 O VAL C 320 N TYR C 277
SHEET 5 CG 8 CYS C 330 LEU C 333 -1 O CYS C 330 N ILE C 326
SHEET 6 CG 8 ASN C 338 PRO C 344 -1 O ASN C 338 N LEU C 333
SHEET 7 CG 8 ILE C 350 ASP C 359 -1 O GLU C 351 N HIS C 343
SHEET 8 CG 8 THR C 205 ALA C 207 -1 O VAL C 206 N VAL C 358
SHEET 1 DA 6 ALA D 80 GLU D 84 0
SHEET 2 DA 6 LEU D 50 PRO D 59 -1 O TYR D 56 N GLU D 84
SHEET 3 DA 6 PHE D 165 LEU D 174 1 O ILE D 167 N ASP D 51
SHEET 4 DA 6 GLN D 144 ARG D 158 -1 O GLU D 151 N LEU D 173
SHEET 5 DA 6 THR D 127 ARG D 140 -1 O PHE D 128 N LEU D 156
SHEET 6 DA 6 ARG D 109 GLU D 121 -1 O ARG D 109 N ASN D 139
SHEET 1 EA 3 VAL E 28 ASP E 29 0
SHEET 2 EA 3 LEU E 34 LEU E 35 -1 O LEU E 34 N ASP E 29
SHEET 3 EA 3 LEU E 409 ASN E 410 -1 O LEU E 409 N LEU E 35
SHEET 1 EB 3 LEU E 59 HIS E 63 0
SHEET 2 EB 3 LEU E 171 ASN E 175 -1 O VAL E 172 N LEU E 61
SHEET 3 EB 3 ARG E 164 TYR E 168 -1 O ARG E 164 N ASN E 175
SHEET 1 EC 4 ILE E 93 LEU E 97 0
SHEET 2 EC 4 ASP E 81 ARG E 87 -1 O VAL E 84 N PHE E 96
SHEET 3 EC 4 ASP E 72 MET E 78 -1 O ASP E 72 N ARG E 87
SHEET 4 EC 4 ALA E 112 ASN E 114 -1 O GLY E 113 N PHE E 73
SHEET 1 ED 3 PHE E 118 THR E 119 0
SHEET 2 ED 3 ALA E 126 TYR E 127 -1 O TYR E 127 N PHE E 118
SHEET 3 ED 3 LEU E 133 ASN E 135 -1 N VAL E 134 O ALA E 126
SHEET 1 EE 8 THR E 205 ILE E 216 0
SHEET 2 EE 8 ILE E 350 ASP E 359 -1 O ILE E 350 N ILE E 216
SHEET 3 EE 8 ASN E 338 PRO E 344 -1 O ILE E 339 N PHE E 355
SHEET 4 EE 8 CYS E 330 PHE E 332 -1 O SER E 331 N ARG E 340
SHEET 5 EE 8 MET E 319 ILE E 326 -1 O MET E 324 N PHE E 332
SHEET 6 EE 8 GLY E 273 VAL E 278 -1 O GLY E 273 N THR E 325
SHEET 7 EE 8 GLY E 262 ARG E 266 -1 O ASN E 263 N TRP E 276
SHEET 8 EE 8 ASN E 428 TYR E 431 -1 O ASN E 428 N ARG E 266
SHEET 1 FA 6 ALA F 80 GLU F 84 0
SHEET 2 FA 6 LEU F 50 PRO F 59 -1 O TYR F 56 N GLU F 84
SHEET 3 FA 6 PHE F 165 LEU F 174 1 O ILE F 167 N ASP F 51
SHEET 4 FA 6 GLN F 144 ARG F 158 -1 O GLU F 151 N LEU F 173
SHEET 5 FA 6 THR F 127 ARG F 140 -1 O PHE F 128 N LEU F 156
SHEET 6 FA 6 ARG F 109 GLU F 121 -1 O ARG F 109 N ASN F 139
SHEET 1 GA 3 VAL G 28 ASP G 29 0
SHEET 2 GA 3 LEU G 34 LEU G 35 -1 O LEU G 34 N ASP G 29
SHEET 3 GA 3 LEU G 409 ASN G 410 -1 O LEU G 409 N LEU G 35
SHEET 1 GB 7 LEU G 59 HIS G 63 0
SHEET 2 GB 7 LEU G 171 ASN G 175 -1 O VAL G 172 N LEU G 61
SHEET 3 GB 7 GLN G 162 TYR G 168 -1 O ARG G 164 N ASN G 175
SHEET 4 GB 7 ILE G 93 LEU G 97 -1 O VAL G 95 N ALA G 163
SHEET 5 GB 7 ASP G 81 ARG G 87 -1 O VAL G 84 N PHE G 96
SHEET 6 GB 7 ASP G 72 MET G 78 -1 O ASP G 72 N ARG G 87
SHEET 7 GB 7 ALA G 112 ASN G 114 -1 O GLY G 113 N PHE G 73
SHEET 1 GC 3 PHE G 118 THR G 119 0
SHEET 2 GC 3 ALA G 126 TYR G 127 -1 O TYR G 127 N PHE G 118
SHEET 3 GC 3 LEU G 133 ASN G 135 -1 N VAL G 134 O ALA G 126
SHEET 1 GD 2 THR G 205 ALA G 207 0
SHEET 2 GD 2 ILE G 350 ASP G 359 -1 O VAL G 358 N VAL G 206
SHEET 1 GE 2 GLN G 212 ILE G 216 0
SHEET 2 GE 2 ILE G 350 ASP G 359 -1 O ILE G 350 N ILE G 216
SHEET 1 GF 8 ASN G 428 TYR G 431 0
SHEET 2 GF 8 GLY G 262 ARG G 266 -1 O GLN G 264 N GLY G 430
SHEET 3 GF 8 GLY G 273 VAL G 278 -1 O SER G 274 N PHE G 265
SHEET 4 GF 8 MET G 319 ILE G 326 -1 O VAL G 320 N TYR G 277
SHEET 5 GF 8 CYS G 330 LEU G 333 -1 O CYS G 330 N ILE G 326
SHEET 6 GF 8 ASN G 338 PRO G 344 -1 O ASN G 338 N LEU G 333
SHEET 7 GF 8 ILE G 350 ASP G 359 -1 O GLU G 351 N HIS G 343
SHEET 8 GF 8 GLN G 212 ILE G 216 -1 O GLN G 212 N ALA G 354
SHEET 1 GG 8 ASN G 428 TYR G 431 0
SHEET 2 GG 8 GLY G 262 ARG G 266 -1 O GLN G 264 N GLY G 430
SHEET 3 GG 8 GLY G 273 VAL G 278 -1 O SER G 274 N PHE G 265
SHEET 4 GG 8 MET G 319 ILE G 326 -1 O VAL G 320 N TYR G 277
SHEET 5 GG 8 CYS G 330 LEU G 333 -1 O CYS G 330 N ILE G 326
SHEET 6 GG 8 ASN G 338 PRO G 344 -1 O ASN G 338 N LEU G 333
SHEET 7 GG 8 ILE G 350 ASP G 359 -1 O GLU G 351 N HIS G 343
SHEET 8 GG 8 THR G 205 ALA G 207 -1 O VAL G 206 N VAL G 358
SHEET 1 HA 6 ALA H 80 GLU H 84 0
SHEET 2 HA 6 LEU H 50 PRO H 59 -1 O TYR H 56 N GLU H 84
SHEET 3 HA 6 PHE H 165 LEU H 174 1 O ILE H 167 N ASP H 51
SHEET 4 HA 6 GLN H 144 ARG H 158 -1 O GLU H 151 N LEU H 173
SHEET 5 HA 6 THR H 127 ARG H 140 -1 O PHE H 128 N LEU H 156
SHEET 6 HA 6 ARG H 109 GLU H 121 -1 O ARG H 109 N ASN H 139
SHEET 1 IA 3 VAL I 28 ASP I 29 0
SHEET 2 IA 3 LEU I 34 LEU I 35 -1 O LEU I 34 N ASP I 29
SHEET 3 IA 3 LEU I 409 ASN I 410 -1 O LEU I 409 N LEU I 35
SHEET 1 IB 7 LEU I 59 HIS I 63 0
SHEET 2 IB 7 LEU I 171 ASN I 175 -1 O VAL I 172 N LEU I 61
SHEET 3 IB 7 GLN I 162 TYR I 168 -1 O ARG I 164 N ASN I 175
SHEET 4 IB 7 ILE I 93 LEU I 97 -1 O VAL I 95 N ALA I 163
SHEET 5 IB 7 ASP I 81 ARG I 87 -1 O VAL I 84 N PHE I 96
SHEET 6 IB 7 ASP I 72 MET I 78 -1 O ASP I 72 N ARG I 87
SHEET 7 IB 7 ALA I 112 ASN I 114 -1 O GLY I 113 N PHE I 73
SHEET 1 IC 3 PHE I 118 THR I 119 0
SHEET 2 IC 3 ALA I 126 TYR I 127 -1 O TYR I 127 N PHE I 118
SHEET 3 IC 3 LEU I 133 ASN I 135 -1 N VAL I 134 O ALA I 126
SHEET 1 ID 2 THR I 205 ALA I 207 0
SHEET 2 ID 2 ILE I 350 ASP I 359 -1 O VAL I 358 N VAL I 206
SHEET 1 IE 2 GLN I 212 ILE I 216 0
SHEET 2 IE 2 ILE I 350 ASP I 359 -1 O ILE I 350 N ILE I 216
SHEET 1 IF 8 ASN I 428 TYR I 431 0
SHEET 2 IF 8 GLY I 262 ARG I 266 -1 O GLN I 264 N GLY I 430
SHEET 3 IF 8 GLY I 273 VAL I 278 -1 O SER I 274 N PHE I 265
SHEET 4 IF 8 MET I 319 ILE I 326 -1 O VAL I 320 N TYR I 277
SHEET 5 IF 8 CYS I 330 LEU I 333 -1 O CYS I 330 N ILE I 326
SHEET 6 IF 8 ASN I 338 PRO I 344 -1 O ASN I 338 N LEU I 333
SHEET 7 IF 8 ILE I 350 ASP I 359 -1 O GLU I 351 N HIS I 343
SHEET 8 IF 8 GLN I 212 ILE I 216 -1 O GLN I 212 N ALA I 354
SHEET 1 IG 8 ASN I 428 TYR I 431 0
SHEET 2 IG 8 GLY I 262 ARG I 266 -1 O GLN I 264 N GLY I 430
SHEET 3 IG 8 GLY I 273 VAL I 278 -1 O SER I 274 N PHE I 265
SHEET 4 IG 8 MET I 319 ILE I 326 -1 O VAL I 320 N TYR I 277
SHEET 5 IG 8 CYS I 330 LEU I 333 -1 O CYS I 330 N ILE I 326
SHEET 6 IG 8 ASN I 338 PRO I 344 -1 O ASN I 338 N LEU I 333
SHEET 7 IG 8 ILE I 350 ASP I 359 -1 O GLU I 351 N HIS I 343
SHEET 8 IG 8 THR I 205 ALA I 207 -1 O VAL I 206 N VAL I 358
SHEET 1 JA 6 ALA J 80 GLU J 84 0
SHEET 2 JA 6 LEU J 50 PRO J 59 -1 O TYR J 56 N GLU J 84
SHEET 3 JA 6 PHE J 165 LEU J 174 1 O ILE J 167 N ASP J 51
SHEET 4 JA 6 GLN J 144 ARG J 158 -1 O GLU J 151 N LEU J 173
SHEET 5 JA 6 THR J 127 ARG J 140 -1 O PHE J 128 N LEU J 156
SHEET 6 JA 6 ARG J 109 GLU J 121 -1 O ARG J 109 N ASN J 139
SHEET 1 KA 3 VAL K 28 ASP K 29 0
SHEET 2 KA 3 LEU K 34 LEU K 35 -1 O LEU K 34 N ASP K 29
SHEET 3 KA 3 LEU K 409 ASN K 410 -1 O LEU K 409 N LEU K 35
SHEET 1 KB 7 LEU K 59 HIS K 63 0
SHEET 2 KB 7 LEU K 171 ASN K 175 -1 O VAL K 172 N LEU K 61
SHEET 3 KB 7 GLN K 162 TYR K 168 -1 O ARG K 164 N ASN K 175
SHEET 4 KB 7 ILE K 93 LEU K 97 -1 O VAL K 95 N ALA K 163
SHEET 5 KB 7 ASP K 81 ARG K 87 -1 O VAL K 84 N PHE K 96
SHEET 6 KB 7 ASP K 72 MET K 78 -1 O ASP K 72 N ARG K 87
SHEET 7 KB 7 ALA K 112 ASN K 114 -1 O GLY K 113 N PHE K 73
SHEET 1 KC 3 PHE K 118 THR K 119 0
SHEET 2 KC 3 ALA K 126 TYR K 127 -1 O TYR K 127 N PHE K 118
SHEET 3 KC 3 LEU K 133 ASN K 135 -1 N VAL K 134 O ALA K 126
SHEET 1 KD 2 THR K 205 ALA K 207 0
SHEET 2 KD 2 ILE K 350 ASP K 359 -1 O VAL K 358 N VAL K 206
SHEET 1 KE 2 GLN K 212 ILE K 216 0
SHEET 2 KE 2 ILE K 350 ASP K 359 -1 O ILE K 350 N ILE K 216
SHEET 1 KF 8 ASN K 428 TYR K 431 0
SHEET 2 KF 8 GLY K 262 ARG K 266 -1 O GLN K 264 N GLY K 430
SHEET 3 KF 8 GLY K 273 VAL K 278 -1 O SER K 274 N PHE K 265
SHEET 4 KF 8 MET K 319 ILE K 326 -1 O VAL K 320 N TYR K 277
SHEET 5 KF 8 CYS K 330 LEU K 333 -1 O CYS K 330 N ILE K 326
SHEET 6 KF 8 ASN K 338 PRO K 344 -1 O ASN K 338 N LEU K 333
SHEET 7 KF 8 ILE K 350 ASP K 359 -1 O GLU K 351 N HIS K 343
SHEET 8 KF 8 GLN K 212 ILE K 216 -1 O GLN K 212 N ALA K 354
SHEET 1 KG 8 ASN K 428 TYR K 431 0
SHEET 2 KG 8 GLY K 262 ARG K 266 -1 O GLN K 264 N GLY K 430
SHEET 3 KG 8 GLY K 273 VAL K 278 -1 O SER K 274 N PHE K 265
SHEET 4 KG 8 MET K 319 ILE K 326 -1 O VAL K 320 N TYR K 277
SHEET 5 KG 8 CYS K 330 LEU K 333 -1 O CYS K 330 N ILE K 326
SHEET 6 KG 8 ASN K 338 PRO K 344 -1 O ASN K 338 N LEU K 333
SHEET 7 KG 8 ILE K 350 ASP K 359 -1 O GLU K 351 N HIS K 343
SHEET 8 KG 8 THR K 205 ALA K 207 -1 O VAL K 206 N VAL K 358
SHEET 1 LA 6 ALA L 80 GLU L 84 0
SHEET 2 LA 6 LEU L 50 PRO L 59 -1 O TYR L 56 N GLU L 84
SHEET 3 LA 6 PHE L 165 LEU L 174 1 O ILE L 167 N ASP L 51
SHEET 4 LA 6 GLN L 144 ARG L 158 -1 O GLU L 151 N LEU L 173
SHEET 5 LA 6 THR L 127 ARG L 140 -1 O PHE L 128 N LEU L 156
SHEET 6 LA 6 ARG L 109 GLU L 121 -1 O ARG L 109 N ASN L 139
SHEET 1 MA 3 VAL M 28 ASP M 29 0
SHEET 2 MA 3 LEU M 34 LEU M 35 -1 O LEU M 34 N ASP M 29
SHEET 3 MA 3 LEU M 409 ASN M 410 -1 O LEU M 409 N LEU M 35
SHEET 1 MB 7 LEU M 59 HIS M 63 0
SHEET 2 MB 7 LEU M 171 ASN M 175 -1 O VAL M 172 N LEU M 61
SHEET 3 MB 7 GLN M 162 TYR M 168 -1 O ARG M 164 N ASN M 175
SHEET 4 MB 7 ILE M 93 LEU M 97 -1 O VAL M 95 N ALA M 163
SHEET 5 MB 7 ASP M 81 ARG M 87 -1 O VAL M 84 N PHE M 96
SHEET 6 MB 7 ASP M 72 MET M 78 -1 O ASP M 72 N ARG M 87
SHEET 7 MB 7 ALA M 112 ASN M 114 -1 O GLY M 113 N PHE M 73
SHEET 1 MC 3 ALA M 117 THR M 119 0
SHEET 2 MC 3 ALA M 126 ASP M 128 -1 O TYR M 127 N PHE M 118
SHEET 3 MC 3 LEU M 133 ASN M 135 -1 N VAL M 134 O ALA M 126
SHEET 1 MD 2 THR M 205 ALA M 207 0
SHEET 2 MD 2 ILE M 350 ASP M 359 -1 O VAL M 358 N VAL M 206
SHEET 1 ME 2 GLN M 212 ILE M 216 0
SHEET 2 ME 2 ILE M 350 ASP M 359 -1 O ILE M 350 N ILE M 216
SHEET 1 MF 8 ASN M 428 TYR M 431 0
SHEET 2 MF 8 GLY M 262 ARG M 266 -1 O GLN M 264 N GLY M 430
SHEET 3 MF 8 GLY M 273 VAL M 278 -1 O SER M 274 N PHE M 265
SHEET 4 MF 8 MET M 319 ILE M 326 -1 O VAL M 320 N TYR M 277
SHEET 5 MF 8 CYS M 330 LEU M 333 -1 O CYS M 330 N ILE M 326
SHEET 6 MF 8 ASN M 338 PRO M 344 -1 O ASN M 338 N LEU M 333
SHEET 7 MF 8 ILE M 350 ASP M 359 -1 O GLU M 351 N HIS M 343
SHEET 8 MF 8 GLN M 212 ILE M 216 -1 O GLN M 212 N ALA M 354
SHEET 1 MG 8 ASN M 428 TYR M 431 0
SHEET 2 MG 8 GLY M 262 ARG M 266 -1 O GLN M 264 N GLY M 430
SHEET 3 MG 8 GLY M 273 VAL M 278 -1 O SER M 274 N PHE M 265
SHEET 4 MG 8 MET M 319 ILE M 326 -1 O VAL M 320 N TYR M 277
SHEET 5 MG 8 CYS M 330 LEU M 333 -1 O CYS M 330 N ILE M 326
SHEET 6 MG 8 ASN M 338 PRO M 344 -1 O ASN M 338 N LEU M 333
SHEET 7 MG 8 ILE M 350 ASP M 359 -1 O GLU M 351 N HIS M 343
SHEET 8 MG 8 THR M 205 ALA M 207 -1 O VAL M 206 N VAL M 358
SHEET 1 NA 6 ALA N 80 GLU N 84 0
SHEET 2 NA 6 LEU N 50 PRO N 59 -1 O TYR N 56 N GLU N 84
SHEET 3 NA 6 PHE N 165 LEU N 174 1 O ILE N 167 N ASP N 51
SHEET 4 NA 6 GLN N 144 ARG N 158 -1 O GLU N 151 N LEU N 173
SHEET 5 NA 6 THR N 127 ARG N 140 -1 O PHE N 128 N LEU N 156
SHEET 6 NA 6 ARG N 109 GLU N 121 -1 O ARG N 109 N ASN N 139
SHEET 1 OA 3 VAL O 28 ASP O 29 0
SHEET 2 OA 3 LEU O 34 LEU O 35 -1 O LEU O 34 N ASP O 29
SHEET 3 OA 3 LEU O 409 ASN O 410 -1 O LEU O 409 N LEU O 35
SHEET 1 OB 7 LEU O 59 HIS O 63 0
SHEET 2 OB 7 LEU O 171 ASN O 175 -1 O VAL O 172 N LEU O 61
SHEET 3 OB 7 GLN O 162 TYR O 168 -1 O ARG O 164 N ASN O 175
SHEET 4 OB 7 ILE O 93 LEU O 97 -1 O VAL O 95 N ALA O 163
SHEET 5 OB 7 ASP O 81 ARG O 87 -1 O VAL O 84 N PHE O 96
SHEET 6 OB 7 ASP O 72 MET O 78 -1 O ASP O 72 N ARG O 87
SHEET 7 OB 7 ALA O 112 ASN O 114 -1 O GLY O 113 N PHE O 73
SHEET 1 OC 3 PHE O 118 THR O 119 0
SHEET 2 OC 3 ALA O 126 TYR O 127 -1 O TYR O 127 N PHE O 118
SHEET 3 OC 3 LEU O 133 ASN O 135 -1 N VAL O 134 O ALA O 126
SHEET 1 OD 2 THR O 205 ALA O 207 0
SHEET 2 OD 2 ILE O 350 ASP O 359 -1 O VAL O 358 N VAL O 206
SHEET 1 OE 2 GLN O 212 ILE O 216 0
SHEET 2 OE 2 ILE O 350 ASP O 359 -1 O ILE O 350 N ILE O 216
SHEET 1 OF 8 ASN O 428 TYR O 431 0
SHEET 2 OF 8 GLY O 262 ARG O 266 -1 O GLN O 264 N GLY O 430
SHEET 3 OF 8 GLY O 273 VAL O 278 -1 O SER O 274 N PHE O 265
SHEET 4 OF 8 MET O 319 ILE O 326 -1 O VAL O 320 N TYR O 277
SHEET 5 OF 8 CYS O 330 LEU O 333 -1 O CYS O 330 N ILE O 326
SHEET 6 OF 8 ASN O 338 PRO O 344 -1 O ASN O 338 N LEU O 333
SHEET 7 OF 8 ILE O 350 ASP O 359 -1 O GLU O 351 N HIS O 343
SHEET 8 OF 8 GLN O 212 ILE O 216 -1 O GLN O 212 N ALA O 354
SHEET 1 OG 8 ASN O 428 TYR O 431 0
SHEET 2 OG 8 GLY O 262 ARG O 266 -1 O GLN O 264 N GLY O 430
SHEET 3 OG 8 GLY O 273 VAL O 278 -1 O SER O 274 N PHE O 265
SHEET 4 OG 8 MET O 319 ILE O 326 -1 O VAL O 320 N TYR O 277
SHEET 5 OG 8 CYS O 330 LEU O 333 -1 O CYS O 330 N ILE O 326
SHEET 6 OG 8 ASN O 338 PRO O 344 -1 O ASN O 338 N LEU O 333
SHEET 7 OG 8 ILE O 350 ASP O 359 -1 O GLU O 351 N HIS O 343
SHEET 8 OG 8 THR O 205 ALA O 207 -1 O VAL O 206 N VAL O 358
SHEET 1 PA 6 ALA P 80 GLU P 84 0
SHEET 2 PA 6 LEU P 50 PRO P 59 -1 O TYR P 56 N GLU P 84
SHEET 3 PA 6 PHE P 165 LEU P 174 1 O ILE P 167 N ASP P 51
SHEET 4 PA 6 GLN P 144 ARG P 158 -1 O GLU P 151 N LEU P 173
SHEET 5 PA 6 THR P 127 ARG P 140 -1 O PHE P 128 N LEU P 156
SHEET 6 PA 6 ARG P 109 GLU P 121 -1 O ARG P 109 N ASN P 139
SHEET 1 QA 3 VAL Q 28 ASP Q 29 0
SHEET 2 QA 3 LEU Q 34 LEU Q 35 -1 O LEU Q 34 N ASP Q 29
SHEET 3 QA 3 LEU Q 409 ASN Q 410 -1 O LEU Q 409 N LEU Q 35
SHEET 1 QB 7 LEU Q 59 HIS Q 63 0
SHEET 2 QB 7 LEU Q 171 ASN Q 175 -1 O VAL Q 172 N LEU Q 61
SHEET 3 QB 7 GLN Q 162 TYR Q 168 -1 O ARG Q 164 N ASN Q 175
SHEET 4 QB 7 ILE Q 93 LEU Q 97 -1 O VAL Q 95 N ALA Q 163
SHEET 5 QB 7 ASP Q 81 ARG Q 87 -1 O VAL Q 84 N PHE Q 96
SHEET 6 QB 7 ASP Q 72 MET Q 78 -1 O ASP Q 72 N ARG Q 87
SHEET 7 QB 7 ALA Q 112 ASN Q 114 -1 O GLY Q 113 N PHE Q 73
SHEET 1 QC 3 PHE Q 118 THR Q 119 0
SHEET 2 QC 3 ALA Q 126 TYR Q 127 -1 O TYR Q 127 N PHE Q 118
SHEET 3 QC 3 LEU Q 133 ASN Q 135 -1 N VAL Q 134 O ALA Q 126
SHEET 1 QD 2 THR Q 205 ALA Q 207 0
SHEET 2 QD 2 ILE Q 350 ASP Q 359 -1 O VAL Q 358 N VAL Q 206
SHEET 1 QE 2 GLN Q 212 ILE Q 216 0
SHEET 2 QE 2 ILE Q 350 ASP Q 359 -1 O ILE Q 350 N ILE Q 216
SHEET 1 QF 8 ASN Q 428 TYR Q 431 0
SHEET 2 QF 8 GLY Q 262 ARG Q 266 -1 O GLN Q 264 N GLY Q 430
SHEET 3 QF 8 GLY Q 273 VAL Q 278 -1 O SER Q 274 N PHE Q 265
SHEET 4 QF 8 MET Q 319 ILE Q 326 -1 O VAL Q 320 N TYR Q 277
SHEET 5 QF 8 CYS Q 330 LEU Q 333 -1 O CYS Q 330 N ILE Q 326
SHEET 6 QF 8 ASN Q 338 PRO Q 344 -1 O ASN Q 338 N LEU Q 333
SHEET 7 QF 8 ILE Q 350 ASP Q 359 -1 O GLU Q 351 N HIS Q 343
SHEET 8 QF 8 GLN Q 212 ILE Q 216 -1 O GLN Q 212 N ALA Q 354
SHEET 1 QG 8 ASN Q 428 TYR Q 431 0
SHEET 2 QG 8 GLY Q 262 ARG Q 266 -1 O GLN Q 264 N GLY Q 430
SHEET 3 QG 8 GLY Q 273 VAL Q 278 -1 O SER Q 274 N PHE Q 265
SHEET 4 QG 8 MET Q 319 ILE Q 326 -1 O VAL Q 320 N TYR Q 277
SHEET 5 QG 8 CYS Q 330 LEU Q 333 -1 O CYS Q 330 N ILE Q 326
SHEET 6 QG 8 ASN Q 338 PRO Q 344 -1 O ASN Q 338 N LEU Q 333
SHEET 7 QG 8 ILE Q 350 ASP Q 359 -1 O GLU Q 351 N HIS Q 343
SHEET 8 QG 8 THR Q 205 ALA Q 207 -1 O VAL Q 206 N VAL Q 358
SHEET 1 RA 6 ALA R 80 GLU R 84 0
SHEET 2 RA 6 TYR R 56 PRO R 59 -1 O TYR R 56 N GLU R 84
SHEET 3 RA 6 PHE R 165 LEU R 174 1 O ARG R 170 N PHE R 57
SHEET 4 RA 6 GLN R 144 ARG R 158 -1 O GLU R 151 N LEU R 173
SHEET 5 RA 6 THR R 127 ARG R 140 -1 O PHE R 128 N LEU R 156
SHEET 6 RA 6 ARG R 109 GLU R 121 -1 O ARG R 109 N ASN R 139
SHEET 1 SA 3 VAL S 28 ASP S 29 0
SHEET 2 SA 3 LEU S 34 LEU S 35 -1 O LEU S 34 N ASP S 29
SHEET 3 SA 3 LEU S 409 ASN S 410 -1 O LEU S 409 N LEU S 35
SHEET 1 SB 7 LEU S 59 HIS S 63 0
SHEET 2 SB 7 LEU S 171 ASN S 175 -1 O VAL S 172 N LEU S 61
SHEET 3 SB 7 GLN S 162 TYR S 168 -1 O ARG S 164 N ASN S 175
SHEET 4 SB 7 ILE S 93 LEU S 97 -1 O VAL S 95 N ALA S 163
SHEET 5 SB 7 ASP S 81 ARG S 87 -1 O VAL S 84 N PHE S 96
SHEET 6 SB 7 ASP S 72 MET S 78 -1 O ASP S 72 N ARG S 87
SHEET 7 SB 7 ALA S 112 ASN S 114 -1 O GLY S 113 N PHE S 73
SHEET 1 SC 3 PHE S 118 THR S 119 0
SHEET 2 SC 3 ALA S 126 TYR S 127 -1 O TYR S 127 N PHE S 118
SHEET 3 SC 3 LEU S 133 ASN S 135 -1 N VAL S 134 O ALA S 126
SHEET 1 SD 2 THR S 205 ALA S 207 0
SHEET 2 SD 2 ILE S 350 ASP S 359 -1 O VAL S 358 N VAL S 206
SHEET 1 SE 2 GLN S 212 ILE S 216 0
SHEET 2 SE 2 ILE S 350 ASP S 359 -1 O ILE S 350 N ILE S 216
SHEET 1 SF 8 ASN S 428 TYR S 431 0
SHEET 2 SF 8 GLY S 262 ARG S 266 -1 O GLN S 264 N GLY S 430
SHEET 3 SF 8 GLY S 273 VAL S 278 -1 O SER S 274 N PHE S 265
SHEET 4 SF 8 MET S 319 ILE S 326 -1 O VAL S 320 N TYR S 277
SHEET 5 SF 8 CYS S 330 LEU S 333 -1 O CYS S 330 N ILE S 326
SHEET 6 SF 8 ASN S 338 PRO S 344 -1 O ASN S 338 N LEU S 333
SHEET 7 SF 8 ILE S 350 ASP S 359 -1 O GLU S 351 N HIS S 343
SHEET 8 SF 8 GLN S 212 ILE S 216 -1 O GLN S 212 N ALA S 354
SHEET 1 SG 8 ASN S 428 TYR S 431 0
SHEET 2 SG 8 GLY S 262 ARG S 266 -1 O GLN S 264 N GLY S 430
SHEET 3 SG 8 GLY S 273 VAL S 278 -1 O SER S 274 N PHE S 265
SHEET 4 SG 8 MET S 319 ILE S 326 -1 O VAL S 320 N TYR S 277
SHEET 5 SG 8 CYS S 330 LEU S 333 -1 O CYS S 330 N ILE S 326
SHEET 6 SG 8 ASN S 338 PRO S 344 -1 O ASN S 338 N LEU S 333
SHEET 7 SG 8 ILE S 350 ASP S 359 -1 O GLU S 351 N HIS S 343
SHEET 8 SG 8 THR S 205 ALA S 207 -1 O VAL S 206 N VAL S 358
SHEET 1 TA 6 ALA T 80 GLU T 84 0
SHEET 2 TA 6 LEU T 50 PRO T 59 -1 O TYR T 56 N GLU T 84
SHEET 3 TA 6 PHE T 165 LEU T 174 1 O ILE T 167 N ASP T 51
SHEET 4 TA 6 GLN T 144 ARG T 158 -1 O GLU T 151 N LEU T 173
SHEET 5 TA 6 THR T 127 ARG T 140 -1 O PHE T 128 N LEU T 156
SHEET 6 TA 6 ARG T 109 GLU T 121 -1 O ARG T 109 N ASN T 139
SHEET 1 UA 3 VAL U 28 ASP U 29 0
SHEET 2 UA 3 LEU U 34 LEU U 35 -1 O LEU U 34 N ASP U 29
SHEET 3 UA 3 LEU U 409 ASN U 410 -1 O LEU U 409 N LEU U 35
SHEET 1 UB 7 LEU U 59 HIS U 63 0
SHEET 2 UB 7 LEU U 171 ASN U 175 -1 O VAL U 172 N LEU U 61
SHEET 3 UB 7 GLN U 162 TYR U 168 -1 O ARG U 164 N ASN U 175
SHEET 4 UB 7 ILE U 93 LEU U 97 -1 O VAL U 95 N ALA U 163
SHEET 5 UB 7 ASP U 81 ARG U 87 -1 O VAL U 84 N PHE U 96
SHEET 6 UB 7 ASP U 72 MET U 78 -1 O ASP U 72 N ARG U 87
SHEET 7 UB 7 ALA U 112 ASN U 114 -1 O GLY U 113 N PHE U 73
SHEET 1 UC 3 PHE U 118 THR U 119 0
SHEET 2 UC 3 ALA U 126 TYR U 127 -1 O TYR U 127 N PHE U 118
SHEET 3 UC 3 LEU U 133 ASN U 135 -1 N VAL U 134 O ALA U 126
SHEET 1 UD 2 THR U 205 ALA U 207 0
SHEET 2 UD 2 ILE U 350 ASP U 359 -1 O VAL U 358 N VAL U 206
SHEET 1 UE 2 GLN U 212 ILE U 216 0
SHEET 2 UE 2 ILE U 350 ASP U 359 -1 O ILE U 350 N ILE U 216
SHEET 1 UF 8 ASN U 428 TYR U 431 0
SHEET 2 UF 8 GLY U 262 ARG U 266 -1 O GLN U 264 N GLY U 430
SHEET 3 UF 8 GLY U 273 VAL U 278 -1 O SER U 274 N PHE U 265
SHEET 4 UF 8 MET U 319 ILE U 326 -1 O VAL U 320 N TYR U 277
SHEET 5 UF 8 CYS U 330 LEU U 333 -1 O CYS U 330 N ILE U 326
SHEET 6 UF 8 ASN U 338 PRO U 344 -1 O ASN U 338 N LEU U 333
SHEET 7 UF 8 ILE U 350 ASP U 359 -1 O GLU U 351 N HIS U 343
SHEET 8 UF 8 GLN U 212 ILE U 216 -1 O GLN U 212 N ALA U 354
SHEET 1 UG 8 ASN U 428 TYR U 431 0
SHEET 2 UG 8 GLY U 262 ARG U 266 -1 O GLN U 264 N GLY U 430
SHEET 3 UG 8 GLY U 273 VAL U 278 -1 O SER U 274 N PHE U 265
SHEET 4 UG 8 MET U 319 ILE U 326 -1 O VAL U 320 N TYR U 277
SHEET 5 UG 8 CYS U 330 LEU U 333 -1 O CYS U 330 N ILE U 326
SHEET 6 UG 8 ASN U 338 PRO U 344 -1 O ASN U 338 N LEU U 333
SHEET 7 UG 8 ILE U 350 ASP U 359 -1 O GLU U 351 N HIS U 343
SHEET 8 UG 8 THR U 205 ALA U 207 -1 O VAL U 206 N VAL U 358
SHEET 1 VA 6 ALA V 80 GLU V 84 0
SHEET 2 VA 6 LEU V 50 PRO V 59 -1 O TYR V 56 N GLU V 84
SHEET 3 VA 6 PHE V 165 LEU V 174 1 O ILE V 167 N ASP V 51
SHEET 4 VA 6 GLN V 144 ARG V 158 -1 O GLU V 151 N LEU V 173
SHEET 5 VA 6 THR V 127 ARG V 140 -1 O PHE V 128 N LEU V 156
SHEET 6 VA 6 ARG V 109 GLU V 121 -1 O ARG V 109 N ASN V 139
SHEET 1 WA 3 VAL W 28 ASP W 29 0
SHEET 2 WA 3 LEU W 34 LEU W 35 -1 O LEU W 34 N ASP W 29
SHEET 3 WA 3 LEU W 409 ASN W 410 -1 O LEU W 409 N LEU W 35
SHEET 1 WB 3 LEU W 59 HIS W 63 0
SHEET 2 WB 3 LEU W 171 ASN W 175 -1 O VAL W 172 N LEU W 61
SHEET 3 WB 3 ARG W 164 TYR W 168 -1 O ARG W 164 N ASN W 175
SHEET 1 WC 4 ILE W 93 LEU W 97 0
SHEET 2 WC 4 ASP W 81 ARG W 87 -1 O VAL W 84 N PHE W 96
SHEET 3 WC 4 ASP W 72 MET W 78 -1 O ASP W 72 N ARG W 87
SHEET 4 WC 4 ALA W 112 ASN W 114 -1 O GLY W 113 N PHE W 73
SHEET 1 WD 3 PHE W 118 THR W 119 0
SHEET 2 WD 3 ALA W 126 TYR W 127 -1 O TYR W 127 N PHE W 118
SHEET 3 WD 3 LEU W 133 ASN W 135 -1 N VAL W 134 O ALA W 126
SHEET 1 WE 2 THR W 205 ALA W 207 0
SHEET 2 WE 2 ILE W 350 ASP W 359 -1 O VAL W 358 N VAL W 206
SHEET 1 WF 2 GLN W 212 ILE W 216 0
SHEET 2 WF 2 ILE W 350 ASP W 359 -1 O ILE W 350 N ILE W 216
SHEET 1 WG 8 ASN W 428 TYR W 431 0
SHEET 2 WG 8 GLY W 262 ARG W 266 -1 O GLN W 264 N GLY W 430
SHEET 3 WG 8 GLY W 273 VAL W 278 -1 O SER W 274 N PHE W 265
SHEET 4 WG 8 MET W 319 ILE W 326 -1 O VAL W 320 N TYR W 277
SHEET 5 WG 8 CYS W 330 PHE W 332 -1 O CYS W 330 N ILE W 326
SHEET 6 WG 8 ASN W 338 PRO W 344 -1 O ARG W 340 N SER W 331
SHEET 7 WG 8 ILE W 350 ASP W 359 -1 O GLU W 351 N HIS W 343
SHEET 8 WG 8 GLN W 212 ILE W 216 -1 O GLN W 212 N ALA W 354
SHEET 1 WH 8 ASN W 428 TYR W 431 0
SHEET 2 WH 8 GLY W 262 ARG W 266 -1 O GLN W 264 N GLY W 430
SHEET 3 WH 8 GLY W 273 VAL W 278 -1 O SER W 274 N PHE W 265
SHEET 4 WH 8 MET W 319 ILE W 326 -1 O VAL W 320 N TYR W 277
SHEET 5 WH 8 CYS W 330 PHE W 332 -1 O CYS W 330 N ILE W 326
SHEET 6 WH 8 ASN W 338 PRO W 344 -1 O ARG W 340 N SER W 331
SHEET 7 WH 8 ILE W 350 ASP W 359 -1 O GLU W 351 N HIS W 343
SHEET 8 WH 8 THR W 205 ALA W 207 -1 O VAL W 206 N VAL W 358
SHEET 1 XA 6 ALA X 80 GLU X 84 0
SHEET 2 XA 6 LEU X 50 PRO X 59 -1 O TYR X 56 N GLU X 84
SHEET 3 XA 6 PHE X 165 LEU X 174 1 O ILE X 167 N ASP X 51
SHEET 4 XA 6 GLN X 144 ARG X 158 -1 O GLU X 151 N LEU X 173
SHEET 5 XA 6 THR X 127 ARG X 140 -1 O PHE X 128 N LEU X 156
SHEET 6 XA 6 ARG X 109 GLU X 121 -1 O ARG X 109 N ASN X 139
LINK SG CYS A 100 FE2 FES A1460 1555 1555 2.14
LINK ND1 HIS A 102 FE1 FES A1460 1555 1555 2.20
LINK SG CYS A 120 FE2 FES A1460 1555 1555 2.36
LINK ND1 HIS A 123 FE1 FES A1460 1555 1555 2.03
LINK NE2 HIS A 233 FE FE2 A1461 1555 1555 2.34
LINK NE2 HIS A 239 FE FE2 A1461 1555 1555 2.30
LINK OD2 ASP A 388 FE FE2 A1461 1555 1555 2.49
LINK OD1 ASP A 388 FE FE2 A1461 1555 1555 2.32
LINK SG CYS C 100 FE2 FES C1460 1555 1555 2.14
LINK ND1 HIS C 102 FE1 FES C1460 1555 1555 2.15
LINK SG CYS C 120 FE2 FES C1460 1555 1555 2.48
LINK ND1 HIS C 123 FE1 FES C1460 1555 1555 2.04
LINK NE2 HIS C 233 FE FE2 C1461 1555 1555 2.10
LINK NE2 HIS C 239 FE FE2 C1461 1555 1555 2.09
LINK OD1 ASP C 388 FE FE2 C1461 1555 1555 2.09
LINK OD2 ASP C 388 FE FE2 C1461 1555 1555 2.72
LINK FE FE2 C1461 O HOH C2027 1555 1555 2.64
LINK SG CYS E 100 FE2 FES E1460 1555 1555 2.34
LINK ND1 HIS E 102 FE1 FES E1460 1555 1555 2.10
LINK SG CYS E 120 FE2 FES E1460 1555 1555 2.30
LINK ND1 HIS E 123 FE1 FES E1460 1555 1555 2.11
LINK NE2 HIS E 233 FE FE2 E1461 1555 1555 2.19
LINK NE2 HIS E 239 FE FE2 E1461 1555 1555 2.09
LINK OD1 ASP E 388 FE FE2 E1461 1555 1555 2.14
LINK OD2 ASP E 388 FE FE2 E1461 1555 1555 2.60
LINK SG CYS G 100 FE2 FES G1460 1555 1555 2.40
LINK ND1 HIS G 102 FE1 FES G1460 1555 1555 2.21
LINK SG CYS G 120 FE2 FES G1460 1555 1555 2.33
LINK ND1 HIS G 123 FE1 FES G1460 1555 1555 2.07
LINK NE2 HIS G 233 FE FE2 G1461 1555 1555 2.14
LINK NE2 HIS G 239 FE FE2 G1461 1555 1555 2.17
LINK OD1 ASP G 388 FE FE2 G1461 1555 1555 1.86
LINK OD2 ASP G 388 FE FE2 G1461 1555 1555 2.75
LINK FE FE2 G1461 O HOH G2013 1555 1555 1.93
LINK SG CYS I 100 FE2 FES I1460 1555 1555 2.21
LINK ND1 HIS I 102 FE1 FES I1460 1555 1555 2.07
LINK SG CYS I 120 FE2 FES I1460 1555 1555 2.32
LINK ND1 HIS I 123 FE1 FES I1460 1555 1555 2.03
LINK NE2 HIS I 233 FE FE2 I1461 1555 1555 2.08
LINK NE2 HIS I 239 FE FE2 I1461 1555 1555 2.12
LINK OD1 ASP I 388 FE FE2 I1461 1555 1555 2.22
LINK OD2 ASP I 388 FE FE2 I1461 1555 1555 2.66
LINK SG CYS K 100 FE2 FES K1460 1555 1555 2.17
LINK ND1 HIS K 102 FE1 FES K1460 1555 1555 2.27
LINK SG CYS K 120 FE2 FES K1460 1555 1555 2.47
LINK ND1 HIS K 123 FE1 FES K1460 1555 1555 2.09
LINK NE2 HIS K 233 FE FE2 K1461 1555 1555 2.28
LINK NE2 HIS K 239 FE FE2 K1461 1555 1555 2.30
LINK OD2 ASP K 388 FE FE2 K1461 1555 1555 2.66
LINK OD1 ASP K 388 FE FE2 K1461 1555 1555 2.30
LINK SG CYS M 100 FE2 FES M1460 1555 1555 2.29
LINK ND1 HIS M 102 FE1 FES M1460 1555 1555 2.06
LINK SG CYS M 120 FE2 FES M1460 1555 1555 2.23
LINK ND1 HIS M 123 FE1 FES M1460 1555 1555 2.04
LINK NE2 HIS M 233 FE FE2 M1461 1555 1555 2.14
LINK NE2 HIS M 239 FE FE2 M1461 1555 1555 2.14
LINK OD1 ASP M 388 FE FE2 M1461 1555 1555 2.13
LINK OD2 ASP M 388 FE FE2 M1461 1555 1555 2.53
LINK FE FE2 M1461 O HOH M2034 1555 1555 2.04
LINK SG CYS O 100 FE2 FES O1460 1555 1555 2.47
LINK ND1 HIS O 102 FE1 FES O1460 1555 1555 2.03
LINK SG CYS O 120 FE2 FES O1460 1555 1555 2.06
LINK ND1 HIS O 123 FE1 FES O1460 1555 1555 2.19
LINK NE2 HIS O 233 FE FE2 O1461 1555 1555 2.09
LINK NE2 HIS O 239 FE FE2 O1461 1555 1555 2.00
LINK OD1 ASP O 388 FE FE2 O1461 1555 1555 2.10
LINK OD2 ASP O 388 FE FE2 O1461 1555 1555 2.51
LINK FE FE2 O1461 O HOH O2053 1555 1555 1.89
LINK SG CYS Q 100 FE2 FES Q1460 1555 1555 2.27
LINK ND1 HIS Q 102 FE1 FES Q1460 1555 1555 2.16
LINK SG CYS Q 120 FE2 FES Q1460 1555 1555 2.34
LINK ND1 HIS Q 123 FE1 FES Q1460 1555 1555 2.00
LINK NE2 HIS Q 233 FE FE2 Q1461 1555 1555 2.44
LINK NE2 HIS Q 239 FE FE2 Q1461 1555 1555 2.27
LINK OD1 ASP Q 388 FE FE2 Q1461 1555 1555 1.93
LINK OD2 ASP Q 388 FE FE2 Q1461 1555 1555 2.40
LINK FE FE2 Q1461 O HOH Q2048 1555 1555 1.77
LINK SG CYS S 100 FE2 FES S1460 1555 1555 2.17
LINK ND1 HIS S 102 FE1 FES S1460 1555 1555 2.49
LINK SG CYS S 120 FE2 FES S1460 1555 1555 2.39
LINK ND1 HIS S 123 FE1 FES S1460 1555 1555 2.06
LINK NE2 HIS S 233 FE FE2 S1461 1555 1555 2.27
LINK NE2 HIS S 239 FE FE2 S1461 1555 1555 2.18
LINK OD1 ASP S 388 FE FE2 S1461 1555 1555 2.16
LINK SG CYS U 100 FE2 FES U1460 1555 1555 2.63
LINK ND1 HIS U 102 FE1 FES U1460 1555 1555 2.02
LINK SG CYS U 120 FE2 FES U1460 1555 1555 1.98
LINK ND1 HIS U 123 FE1 FES U1460 1555 1555 2.42
LINK NE2 HIS U 233 FE FE2 U1461 1555 1555 2.15
LINK NE2 HIS U 239 FE FE2 U1461 1555 1555 2.19
LINK OD1 ASP U 388 FE FE2 U1461 1555 1555 2.10
LINK SG CYS W 100 FE2 FES W1460 1555 1555 2.16
LINK ND1 HIS W 102 FE1 FES W1460 1555 1555 2.24
LINK SG CYS W 120 FE2 FES W1460 1555 1555 2.24
LINK ND1 HIS W 123 FE1 FES W1460 1555 1555 2.02
LINK NE2 HIS W 233 FE FE2 W1461 1555 1555 2.22
LINK NE2 HIS W 239 FE FE2 W1461 1555 1555 2.10
LINK OD2 ASP W 388 FE FE2 W1461 1555 1555 2.59
LINK OD1 ASP W 388 FE FE2 W1461 1555 1555 2.00
CISPEP 1 PHE A 327 PRO A 328 0 -2.11
CISPEP 2 ASN B 105 PRO B 106 0 1.66
CISPEP 3 PHE C 327 PRO C 328 0 2.97
CISPEP 4 ASN D 105 PRO D 106 0 0.36
CISPEP 5 PHE E 327 PRO E 328 0 -2.30
CISPEP 6 ASN F 105 PRO F 106 0 0.69
CISPEP 7 PHE G 327 PRO G 328 0 1.67
CISPEP 8 PHE H 8 PHE H 9 0 -19.82
CISPEP 9 ASN H 105 PRO H 106 0 2.04
CISPEP 10 PHE I 327 PRO I 328 0 3.06
CISPEP 11 ASN J 105 PRO J 106 0 0.58
CISPEP 12 PHE K 327 PRO K 328 0 -0.03
CISPEP 13 ASN L 105 PRO L 106 0 0.40
CISPEP 14 PHE M 327 PRO M 328 0 -0.06
CISPEP 15 ASN N 105 PRO N 106 0 0.85
CISPEP 16 PHE O 327 PRO O 328 0 -2.03
CISPEP 17 ASN P 105 PRO P 106 0 1.95
CISPEP 18 PHE Q 327 PRO Q 328 0 -0.44
CISPEP 19 PHE R 8 PHE R 9 0 10.66
CISPEP 20 ASN R 105 PRO R 106 0 1.42
CISPEP 21 PHE S 327 PRO S 328 0 1.77
CISPEP 22 ASN T 105 PRO T 106 0 -0.99
CISPEP 23 PHE U 327 PRO U 328 0 3.64
CISPEP 24 ASN V 105 PRO V 106 0 5.13
CISPEP 25 PHE W 327 PRO W 328 0 5.02
CISPEP 26 ASN X 105 PRO X 106 0 -0.11
SITE 1 AC1 6 CYS A 100 HIS A 102 ARG A 103 CYS A 120
SITE 2 AC1 6 HIS A 123 TRP A 125
SITE 1 AC2 4 GLN A 226 HIS A 233 HIS A 239 ASP A 388
SITE 1 AC3 9 GLN A 226 PHE A 227 ASP A 230 HIS A 233
SITE 2 AC3 9 GLY A 321 HIS A 323 LEU A 333 PHE A 336
SITE 3 AC3 9 PHE A 384
SITE 1 AC4 6 CYS C 100 HIS C 102 ARG C 103 CYS C 120
SITE 2 AC4 6 HIS C 123 TRP C 125
SITE 1 AC5 5 GLN C 226 HIS C 233 HIS C 239 ASP C 388
SITE 2 AC5 5 HOH C2027
SITE 1 AC6 9 GLN C 226 PHE C 227 ASP C 230 MET C 231
SITE 2 AC6 9 HIS C 233 GLY C 321 HIS C 323 LEU C 333
SITE 3 AC6 9 PHE C 384
SITE 1 AC7 6 CYS E 100 HIS E 102 ARG E 103 CYS E 120
SITE 2 AC7 6 HIS E 123 TRP E 125
SITE 1 AC8 4 GLN E 226 HIS E 233 HIS E 239 ASP E 388
SITE 1 AC9 7 GLN E 226 PHE E 227 ASP E 230 HIS E 233
SITE 2 AC9 7 HIS E 323 PHE E 336 PHE E 384
SITE 1 BC1 6 CYS G 100 HIS G 102 ARG G 103 CYS G 120
SITE 2 BC1 6 HIS G 123 TRP G 125
SITE 1 BC2 5 GLN G 226 HIS G 233 HIS G 239 ASP G 388
SITE 2 BC2 5 HOH G2013
SITE 1 BC3 9 GLN G 226 PHE G 227 ASP G 230 MET G 231
SITE 2 BC3 9 HIS G 233 GLY G 321 HIS G 323 LEU G 333
SITE 3 BC3 9 HOH G2013
SITE 1 BC4 6 CYS I 100 HIS I 102 ARG I 103 CYS I 120
SITE 2 BC4 6 HIS I 123 TRP I 125
SITE 1 BC5 4 GLN I 226 HIS I 233 HIS I 239 ASP I 388
SITE 1 BC6 9 GLN I 226 PHE I 227 ASP I 230 HIS I 233
SITE 2 BC6 9 ALA I 234 GLY I 321 HIS I 323 LEU I 333
SITE 3 BC6 9 PHE I 336
SITE 1 BC7 6 CYS K 100 HIS K 102 ARG K 103 CYS K 120
SITE 2 BC7 6 HIS K 123 TRP K 125
SITE 1 BC8 5 GLN K 226 HIS K 233 HIS K 239 ASP K 388
SITE 2 BC8 5 BNL K1462
SITE 1 BC9 6 GLN K 226 ASP K 230 HIS K 233 HIS K 323
SITE 2 BC9 6 PHE K 384 FE2 K1461
SITE 1 CC1 7 CYS M 100 HIS M 102 ARG M 103 CYS M 120
SITE 2 CC1 7 TYR M 122 HIS M 123 TRP M 125
SITE 1 CC2 5 GLN M 226 HIS M 233 HIS M 239 ASP M 388
SITE 2 CC2 5 HOH M2034
SITE 1 CC3 9 GLN M 226 ASP M 230 MET M 231 HIS M 233
SITE 2 CC3 9 GLY M 321 HIS M 323 LEU M 333 PHE M 336
SITE 3 CC3 9 PHE M 384
SITE 1 CC4 6 CYS O 100 HIS O 102 ARG O 103 CYS O 120
SITE 2 CC4 6 HIS O 123 TRP O 125
SITE 1 CC5 5 GLN O 226 HIS O 233 HIS O 239 ASP O 388
SITE 2 CC5 5 HOH O2053
SITE 1 CC6 7 GLN O 226 ASP O 230 HIS O 233 GLY O 321
SITE 2 CC6 7 HIS O 323 LEU O 333 PHE O 336
SITE 1 CC7 6 CYS Q 100 HIS Q 102 ARG Q 103 CYS Q 120
SITE 2 CC7 6 HIS Q 123 TRP Q 125
SITE 1 CC8 5 GLN Q 226 HIS Q 233 HIS Q 239 ASP Q 388
SITE 2 CC8 5 HOH Q2048
SITE 1 CC9 6 GLN Q 226 ASP Q 230 HIS Q 233 HIS Q 323
SITE 2 CC9 6 LEU Q 333 HOH Q2048
SITE 1 DC1 7 CYS S 100 HIS S 102 ARG S 103 MET S 105
SITE 2 DC1 7 CYS S 120 HIS S 123 TRP S 125
SITE 1 DC2 5 GLN S 226 HIS S 233 HIS S 239 ASP S 388
SITE 2 DC2 5 BNL S1462
SITE 1 DC3 8 GLN S 226 PHE S 227 ASP S 230 HIS S 233
SITE 2 DC3 8 GLY S 321 HIS S 323 PHE S 336 FE2 S1461
SITE 1 DC4 6 CYS U 100 HIS U 102 ARG U 103 CYS U 120
SITE 2 DC4 6 HIS U 123 TRP U 125
SITE 1 DC5 4 GLN U 226 HIS U 233 HIS U 239 ASP U 388
SITE 1 DC6 8 GLN U 226 PHE U 227 ASP U 230 HIS U 233
SITE 2 DC6 8 HIS U 323 LEU U 333 PHE U 336 PHE U 384
SITE 1 DC7 6 CYS W 100 HIS W 102 ARG W 103 CYS W 120
SITE 2 DC7 6 HIS W 123 TRP W 125
SITE 1 DC8 4 GLN W 226 HIS W 233 HIS W 239 ASP W 388
SITE 1 DC9 9 GLN W 226 PHE W 227 ASP W 230 HIS W 233
SITE 2 DC9 9 ALA W 234 GLY W 321 HIS W 323 LEU W 333
SITE 3 DC9 9 PHE W 336
CRYST1 132.824 132.646 130.423 102.65 101.11 105.31 P 1 12
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 0.007529 0.002061 0.002156 0.00000
SCALE2 0.000000 0.007816 0.002325 0.00000
SCALE3 0.000000 0.000000 0.008152 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
