HEADER OXIDOREDUCTASE 19-MAY-03 1OGY
TITLE CRYSTAL STRUCTURE OF THE HETERODIMERIC NITRATE REDUCTASE FROM
TITLE 2 RHODOBACTER SPHAEROIDES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PERIPLASMIC NITRATE REDUCTASE;
COMPND 3 CHAIN: A, C, E, G, I, K, M, O;
COMPND 4 FRAGMENT: CATALYTIC SUBUNIT, RESIDUES 30-831;
COMPND 5 SYNONYM: NITRATE REDUCTASE;
COMPND 6 EC: 1.7.99.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DIHEME CYTOCHROME C NAPB MOLECULE: NITRATE REDUCTASE;
COMPND 10 CHAIN: B, D, F, H, J, L, N, P;
COMPND 11 FRAGMENT: CYTOCHROME SUBUNIT, RESIDUES 25-154;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 3 ORGANISM_TAXID: 1063;
SOURCE 4 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 1063;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: RHODOBACTER SPHAEROIDES;
SOURCE 8 ORGANISM_TAXID: 1063;
SOURCE 9 EXPRESSION_SYSTEM: RHODOBACTER SPHAEROIDES;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 1063
KEYWDS NITRATE REDUCTASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.ARNOUX,M.SABATY,J.ALRIC,B.FRANGIONI,B.GUIGLIARELLI,J.-M.ADRIANO,
AUTHOR 2 D.PIGNOL
REVDAT 5 13-DEC-23 1OGY 1 LINK
REVDAT 4 16-OCT-19 1OGY 1 REMARK LINK
REVDAT 3 24-FEB-09 1OGY 1 VERSN
REVDAT 2 05-NOV-03 1OGY 1 JRNL
REVDAT 1 09-OCT-03 1OGY 0
JRNL AUTH P.ARNOUX,M.SABATY,J.ALRIC,B.FRANGIONI,B.GUIGLIARELLI,
JRNL AUTH 2 J.-M.ADRIANO,D.PIGNOL
JRNL TITL STRUCTURAL AND REDOX PLASTICITY IN THE HETERODIMERIC
JRNL TITL 2 PERIPLASMIC NITRATE REDUCTASE
JRNL REF NAT.STRUCT.BIOL. V. 10 928 2003
JRNL REFN ISSN 1072-8368
JRNL PMID 14528294
JRNL DOI 10.1038/NSB994
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.BRIGE,D.LEYS,T.E.MEYER,M.A.CUSANOVICH,J.J.VAN BEEUMEN
REMARK 1 TITL THE 1.25 A RESOLUTION STRUCTURE OF THE DIHEME NAPB SUBUNIT
REMARK 1 TITL 2 OF SOLUBLE NITRATE REDUCTASE REVEALS A NOVEL CYTOCHROME C
REMARK 1 TITL 3 FOLD WITH A STACKED HEME ARRANGEMENT
REMARK 1 REF BIOCHEMISTRY V. 41 4827 2002
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 11939777
REMARK 1 DOI 10.1021/BI012144B
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.M.DIAS,M.THAN,A.HUMM,R.HUBER,G.BOURENKOV,H.BARTUNIK,
REMARK 1 AUTH 2 S.BURSAKOV,J.CALVETE,J.CALDEIRA,C.CARNEIRO,J.MOURA,I.MOURA,
REMARK 1 AUTH 3 M.J.ROMAO
REMARK 1 TITL CRYSTAL STRUCTURE OF THE FIRST DISSIMILATORY NITRATE
REMARK 1 TITL 2 REDUCTASE (NAP) AT 1.9 A SOLVED BY MAD METHODS
REMARK 1 REF STRUCTURE V. 7 65 1999
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 10368307
REMARK 1 DOI 10.1016/S0969-2126(99)80010-0
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 134043
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 SET) : 0.250
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1347
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 26
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.24
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5006
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE : 0.3690
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 47
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 57824
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1512
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.19300
REMARK 3 B22 (A**2) : 3.83100
REMARK 3 B33 (A**2) : 4.36200
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.59800
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.860
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : RESTRAINTS
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THERE ARE 8 HETERODIMERS IN THE ASU BUT
REMARK 3 THE PHYSIOLOGICAL UNIT IS ONE HETERODIMER. RESTRAINTS HAD BEEN
REMARK 3 RELEASED IN THE LAST REFINEMENT STEP. HETERODIMER WITH CHAIN ID
REMARK 3 A AND B IS THE COMPLEX HAVING THE LOWEST TEMPERATURE FACTOR.
REMARK 4
REMARK 4 1OGY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1290012743.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 134043
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.70
REMARK 200 R MERGE FOR SHELL (I) : 0.41100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRIES 2NAP, 1JNI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOUR-DIFFUSION. MIXING EQUAL AMOUNTS
REMARK 280 OF PROTEIN 25MG/ML., PH 8.20, VAPOR DIFFUSION
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 112.60000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: O, P
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 GLN A 1
REMARK 465 PRO A 2
REMARK 465 VAL A 3
REMARK 465 THR A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 ALA A 9
REMARK 465 LEU A 10
REMARK 465 ARG A 11
REMARK 465 VAL A 802
REMARK 465 GLN B 1
REMARK 465 ALA B 129
REMARK 465 GLU B 130
REMARK 465 GLN C 1
REMARK 465 PRO C 2
REMARK 465 VAL C 3
REMARK 465 THR C 4
REMARK 465 GLY C 5
REMARK 465 GLY C 6
REMARK 465 ALA C 7
REMARK 465 GLU C 8
REMARK 465 ALA C 9
REMARK 465 LEU C 10
REMARK 465 ARG C 11
REMARK 465 VAL C 802
REMARK 465 GLN D 1
REMARK 465 ALA D 129
REMARK 465 GLU D 130
REMARK 465 GLN E 1
REMARK 465 PRO E 2
REMARK 465 VAL E 3
REMARK 465 THR E 4
REMARK 465 GLY E 5
REMARK 465 GLY E 6
REMARK 465 ALA E 7
REMARK 465 GLU E 8
REMARK 465 ALA E 9
REMARK 465 LEU E 10
REMARK 465 ARG E 11
REMARK 465 VAL E 802
REMARK 465 GLN F 1
REMARK 465 ALA F 129
REMARK 465 GLU F 130
REMARK 465 GLN G 1
REMARK 465 PRO G 2
REMARK 465 VAL G 3
REMARK 465 THR G 4
REMARK 465 GLY G 5
REMARK 465 GLY G 6
REMARK 465 ALA G 7
REMARK 465 GLU G 8
REMARK 465 ALA G 9
REMARK 465 LEU G 10
REMARK 465 ARG G 11
REMARK 465 VAL G 802
REMARK 465 GLN H 1
REMARK 465 ALA H 129
REMARK 465 GLU H 130
REMARK 465 GLN I 1
REMARK 465 PRO I 2
REMARK 465 VAL I 3
REMARK 465 THR I 4
REMARK 465 GLY I 5
REMARK 465 GLY I 6
REMARK 465 ALA I 7
REMARK 465 GLU I 8
REMARK 465 ALA I 9
REMARK 465 LEU I 10
REMARK 465 ARG I 11
REMARK 465 VAL I 802
REMARK 465 GLN J 1
REMARK 465 ALA J 129
REMARK 465 GLU J 130
REMARK 465 GLN K 1
REMARK 465 PRO K 2
REMARK 465 VAL K 3
REMARK 465 THR K 4
REMARK 465 GLY K 5
REMARK 465 GLY K 6
REMARK 465 ALA K 7
REMARK 465 GLU K 8
REMARK 465 ALA K 9
REMARK 465 LEU K 10
REMARK 465 ARG K 11
REMARK 465 VAL K 802
REMARK 465 GLN L 1
REMARK 465 ALA L 129
REMARK 465 GLU L 130
REMARK 465 GLN M 1
REMARK 465 PRO M 2
REMARK 465 VAL M 3
REMARK 465 THR M 4
REMARK 465 GLY M 5
REMARK 465 GLY M 6
REMARK 465 ALA M 7
REMARK 465 GLU M 8
REMARK 465 ALA M 9
REMARK 465 LEU M 10
REMARK 465 ARG M 11
REMARK 465 VAL M 802
REMARK 465 GLN N 1
REMARK 465 ALA N 129
REMARK 465 GLU N 130
REMARK 465 GLN O 1
REMARK 465 PRO O 2
REMARK 465 VAL O 3
REMARK 465 THR O 4
REMARK 465 GLY O 5
REMARK 465 GLY O 6
REMARK 465 ALA O 7
REMARK 465 GLU O 8
REMARK 465 ALA O 9
REMARK 465 LEU O 10
REMARK 465 ARG O 11
REMARK 465 VAL O 802
REMARK 465 GLN P 1
REMARK 465 ALA P 129
REMARK 465 GLU P 130
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 PHE A 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP A 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 708 CZ3 CH2
REMARK 470 ALA A 801 CA C O CB
REMARK 470 ARG B 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 65 CG CD OE1 NE2
REMARK 470 GLU B 128 CA C O CB CG CD OE1
REMARK 470 GLU B 128 OE2
REMARK 470 PHE C 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP C 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP C 708 CZ3 CH2
REMARK 470 ALA C 801 CA C O CB
REMARK 470 ARG D 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 65 CG CD OE1 NE2
REMARK 470 GLU D 128 CA C O CB CG CD OE1
REMARK 470 GLU D 128 OE2
REMARK 470 PHE E 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP E 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP E 708 CZ3 CH2
REMARK 470 ALA E 801 CA C O CB
REMARK 470 ARG F 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN F 65 CG CD OE1 NE2
REMARK 470 GLU F 128 CA C O CB CG CD OE1
REMARK 470 GLU F 128 OE2
REMARK 470 PHE G 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP G 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP G 708 CZ3 CH2
REMARK 470 ALA G 801 CA C O CB
REMARK 470 ARG H 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN H 65 CG CD OE1 NE2
REMARK 470 GLU H 128 CA C O CB CG CD OE1
REMARK 470 GLU H 128 OE2
REMARK 470 PHE I 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP I 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP I 708 CZ3 CH2
REMARK 470 ALA I 801 CA C O CB
REMARK 470 ARG J 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN J 65 CG CD OE1 NE2
REMARK 470 GLU J 128 CA C O CB CG CD OE1
REMARK 470 GLU J 128 OE2
REMARK 470 PHE K 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP K 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP K 708 CZ3 CH2
REMARK 470 ALA K 801 CA C O CB
REMARK 470 ARG L 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN L 65 CG CD OE1 NE2
REMARK 470 GLU L 128 CA C O CB CG CD OE1
REMARK 470 GLU L 128 OE2
REMARK 470 PHE M 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP M 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP M 708 CZ3 CH2
REMARK 470 ALA M 801 CA C O CB
REMARK 470 ARG N 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN N 65 CG CD OE1 NE2
REMARK 470 GLU N 128 CA C O CB CG CD OE1
REMARK 470 GLU N 128 OE2
REMARK 470 PHE O 386 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TRP O 708 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP O 708 CZ3 CH2
REMARK 470 ALA O 801 CA C O CB
REMARK 470 ARG P 11 CG CD NE CZ NH1 NH2
REMARK 470 GLN P 65 CG CD OE1 NE2
REMARK 470 GLU P 128 CA C O CB CG CD OE1
REMARK 470 GLU P 128 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 C TRP G 632 CD PRO G 633 1.54
REMARK 500 C TRP K 632 CD PRO K 633 1.64
REMARK 500 C TRP O 632 CD PRO O 633 1.72
REMARK 500 C TRP I 632 CD PRO I 633 1.73
REMARK 500 O THR P 121 N MET P 123 2.07
REMARK 500 O THR N 121 N MET N 123 2.11
REMARK 500 O THR H 121 N MET H 123 2.12
REMARK 500 CB CYS A 22 FE1 SF4 A 1801 2.13
REMARK 500 O THR D 121 N MET D 123 2.13
REMARK 500 O THR J 121 N MET J 123 2.13
REMARK 500 O THR B 121 N MET B 123 2.16
REMARK 500 O THR F 121 N MET F 123 2.16
REMARK 500 SG CYS H 58 CAB HEC H 1128 2.17
REMARK 500 O LEU G 267 O MET G 295 2.18
REMARK 500 O THR L 121 N MET L 123 2.19
REMARK 500 O LEU O 267 O MET O 295 2.19
REMARK 500 CB CYS K 22 FE1 SF4 K 1801 2.19
REMARK 500 O SER J 92 O ARG J 94 2.19
REMARK 500 O LEU I 267 O MET I 295 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CG LYS A 109 O GLY C 655 2556 1.82
REMARK 500 CB ARG C 577 NZ LYS K 287 2545 1.90
REMARK 500 CG ARG C 577 NZ LYS K 287 2545 1.97
REMARK 500 OE2 GLU E 411 CG PRO M 410 1556 2.06
REMARK 500 CB PRO A 410 OE2 GLU K 411 1556 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS C 22 CB CYS C 22 SG -0.100
REMARK 500 CYS E 22 CB CYS E 22 SG -0.147
REMARK 500 CYS E 26 CB CYS E 26 SG -0.109
REMARK 500 CYS G 54 CB CYS G 54 SG -0.123
REMARK 500 CYS I 19 CB CYS I 19 SG 0.122
REMARK 500 CYS K 22 CB CYS K 22 SG -0.116
REMARK 500 CYS L 58 CB CYS L 58 SG -0.106
REMARK 500 CYS O 152 CB CYS O 152 SG 0.117
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 80 N - CA - C ANGL. DEV. = -17.8 DEGREES
REMARK 500 LEU A 200 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 GLY A 613 N - CA - C ANGL. DEV. = -17.9 DEGREES
REMARK 500 PRO A 633 C - N - CA ANGL. DEV. = 41.5 DEGREES
REMARK 500 PRO A 633 C - N - CD ANGL. DEV. = -38.6 DEGREES
REMARK 500 ARG B 94 N - CA - C ANGL. DEV. = -20.6 DEGREES
REMARK 500 CYS C 22 CA - CB - SG ANGL. DEV. = 7.0 DEGREES
REMARK 500 GLY C 80 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 LEU C 200 CA - CB - CG ANGL. DEV. = 16.2 DEGREES
REMARK 500 LEU C 594 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 GLY C 613 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 PRO C 633 C - N - CA ANGL. DEV. = 40.6 DEGREES
REMARK 500 PRO C 633 C - N - CD ANGL. DEV. = -38.1 DEGREES
REMARK 500 ARG D 94 N - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 GLY E 80 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU E 200 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU E 594 N - CA - C ANGL. DEV. = -16.5 DEGREES
REMARK 500 GLY E 613 N - CA - C ANGL. DEV. = -19.0 DEGREES
REMARK 500 PRO E 633 C - N - CA ANGL. DEV. = 40.7 DEGREES
REMARK 500 PRO E 633 C - N - CD ANGL. DEV. = -39.5 DEGREES
REMARK 500 THR E 749 N - CA - C ANGL. DEV. = -16.3 DEGREES
REMARK 500 ARG F 94 N - CA - C ANGL. DEV. = -20.8 DEGREES
REMARK 500 CYS G 22 CA - CB - SG ANGL. DEV. = 8.4 DEGREES
REMARK 500 GLY G 80 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500 LEU G 200 CA - CB - CG ANGL. DEV. = 17.1 DEGREES
REMARK 500 LEU G 594 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLY G 613 N - CA - C ANGL. DEV. = -19.1 DEGREES
REMARK 500 PRO G 633 C - N - CA ANGL. DEV. = 49.0 DEGREES
REMARK 500 PRO G 633 C - N - CD ANGL. DEV. = -61.5 DEGREES
REMARK 500 ARG H 94 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 GLY I 80 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 LEU I 200 CA - CB - CG ANGL. DEV. = 16.5 DEGREES
REMARK 500 LEU I 594 N - CA - C ANGL. DEV. = -18.0 DEGREES
REMARK 500 GLY I 613 N - CA - C ANGL. DEV. = -18.1 DEGREES
REMARK 500 PRO I 633 C - N - CA ANGL. DEV. = 51.7 DEGREES
REMARK 500 PRO I 633 C - N - CD ANGL. DEV. = -54.2 DEGREES
REMARK 500 PRO I 633 CA - N - CD ANGL. DEV. = -9.7 DEGREES
REMARK 500 ARG J 94 N - CA - C ANGL. DEV. = -21.7 DEGREES
REMARK 500 GLY K 80 N - CA - C ANGL. DEV. = -17.6 DEGREES
REMARK 500 LEU K 200 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 LEU K 594 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 GLY K 613 N - CA - C ANGL. DEV. = -19.2 DEGREES
REMARK 500 PRO K 633 C - N - CA ANGL. DEV. = 56.1 DEGREES
REMARK 500 PRO K 633 C - N - CD ANGL. DEV. = -56.6 DEGREES
REMARK 500 ARG L 94 N - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 CYS M 22 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 GLY M 80 N - CA - C ANGL. DEV. = -17.0 DEGREES
REMARK 500 LEU M 200 CA - CB - CG ANGL. DEV. = 16.0 DEGREES
REMARK 500 LEU M 594 N - CA - C ANGL. DEV. = -16.4 DEGREES
REMARK 500 GLY M 613 N - CA - C ANGL. DEV. = -18.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA A 17 142.78 -173.98
REMARK 500 PHE A 21 -121.37 -112.77
REMARK 500 CYS A 22 147.74 -10.88
REMARK 500 VAL A 48 -73.34 -56.56
REMARK 500 ARG A 50 66.04 64.01
REMARK 500 ARG A 69 112.40 -16.80
REMARK 500 MET A 77 109.68 103.50
REMARK 500 VAL A 81 -90.93 106.35
REMARK 500 TYR A 82 124.34 168.90
REMARK 500 GLU A 85 19.79 122.90
REMARK 500 GLU A 87 -168.40 -118.86
REMARK 500 LEU A 108 21.14 -74.38
REMARK 500 LYS A 109 -17.84 -147.52
REMARK 500 ALA A 112 -169.38 70.07
REMARK 500 GLU A 114 13.63 -65.40
REMARK 500 ARG A 137 -60.44 -94.94
REMARK 500 PHE A 140 0.26 -66.18
REMARK 500 ASN A 144 39.22 -86.57
REMARK 500 CYS A 152 -66.10 -104.74
REMARK 500 GLU A 168 155.25 66.69
REMARK 500 ALA A 181 139.11 178.54
REMARK 500 ASN A 188 55.46 -141.26
REMARK 500 HIS A 193 57.95 -144.94
REMARK 500 SER A 223 22.13 -75.61
REMARK 500 ILE A 272 160.63 -47.72
REMARK 500 TYR A 274 69.03 2.39
REMARK 500 LEU A 276 -159.91 -111.89
REMARK 500 GLU A 279 -41.61 131.07
REMARK 500 ASP A 291 -91.22 -100.12
REMARK 500 ALA A 292 113.40 66.88
REMARK 500 MET A 295 -76.71 -96.82
REMARK 500 THR A 296 102.87 64.43
REMARK 500 PRO A 297 170.61 -53.60
REMARK 500 THR A 298 -133.13 -151.86
REMARK 500 LEU A 329 -70.03 -60.77
REMARK 500 TYR A 333 -4.18 -59.03
REMARK 500 PRO A 336 34.60 -59.59
REMARK 500 THR A 345 -133.73 -123.60
REMARK 500 VAL A 352 -7.38 -59.91
REMARK 500 THR A 390 -80.60 -111.01
REMARK 500 ALA A 398 -36.35 -36.60
REMARK 500 PRO A 402 160.89 -48.67
REMARK 500 PRO A 486 -88.03 -29.81
REMARK 500 THR A 487 139.99 78.25
REMARK 500 TRP A 502 -104.16 22.77
REMARK 500 LYS A 541 0.00 -46.84
REMARK 500 ASP A 546 -114.83 -70.71
REMARK 500 GLU A 547 -61.25 19.74
REMARK 500 ALA A 559 87.31 -65.18
REMARK 500 TYR A 560 45.24 151.06
REMARK 500
REMARK 500 THIS ENTRY HAS 798 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 19 SG
REMARK 620 2 SF4 A1801 S1 112.0
REMARK 620 3 SF4 A1801 S2 106.9 104.8
REMARK 620 4 SF4 A1801 S3 119.0 105.2 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 22 SG
REMARK 620 2 SF4 A1801 S2 118.8
REMARK 620 3 SF4 A1801 S3 122.1 100.7
REMARK 620 4 SF4 A1801 S4 104.2 105.0 104.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 SF4 A1801 S1 113.7
REMARK 620 3 SF4 A1801 S2 111.9 97.9
REMARK 620 4 SF4 A1801 S4 121.9 106.5 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 A1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 54 SG
REMARK 620 2 SF4 A1801 S1 114.4
REMARK 620 3 SF4 A1801 S3 101.9 98.4
REMARK 620 4 SF4 A1801 S4 128.8 106.3 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO A1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 152 SG
REMARK 620 2 MGD A1803 S13 95.5
REMARK 620 3 MGD A1803 S12 120.4 73.4
REMARK 620 4 MGD A1804 S12 90.9 79.4 139.8
REMARK 620 5 MGD A1804 S13 144.3 116.3 85.8 80.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 44 NE2
REMARK 620 2 HEC B1128 NA 92.7
REMARK 620 3 HEC B1128 NB 94.3 89.5
REMARK 620 4 HEC B1128 NC 88.9 178.1 89.3
REMARK 620 5 HEC B1128 ND 86.5 89.5 178.7 91.6
REMARK 620 6 HIS B 62 NE2 169.2 94.6 93.6 83.9 85.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC B1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 79 NE2
REMARK 620 2 HEC B1129 NA 95.4
REMARK 620 3 HEC B1129 NB 83.2 89.8
REMARK 620 4 HEC B1129 NC 85.2 178.6 88.9
REMARK 620 5 HEC B1129 ND 95.7 90.5 178.9 90.7
REMARK 620 6 HIS B 102 NE2 162.7 85.4 79.5 93.6 101.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 19 SG
REMARK 620 2 SF4 C1801 S1 123.1
REMARK 620 3 SF4 C1801 S2 102.0 104.1
REMARK 620 4 SF4 C1801 S3 112.5 105.5 108.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 22 SG
REMARK 620 2 SF4 C1801 S2 131.8
REMARK 620 3 SF4 C1801 S3 107.3 100.4
REMARK 620 4 SF4 C1801 S4 105.0 105.4 104.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 26 SG
REMARK 620 2 SF4 C1801 S1 118.3
REMARK 620 3 SF4 C1801 S2 108.5 98.5
REMARK 620 4 SF4 C1801 S4 120.7 106.2 101.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 C1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 54 SG
REMARK 620 2 SF4 C1801 S1 119.5
REMARK 620 3 SF4 C1801 S3 106.7 99.0
REMARK 620 4 SF4 C1801 S4 120.8 105.7 101.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO C1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 152 SG
REMARK 620 2 MGD C1803 S12 120.3
REMARK 620 3 MGD C1803 S13 93.3 78.4
REMARK 620 4 MGD C1804 S12 87.3 143.4 76.1
REMARK 620 5 MGD C1804 S13 139.8 92.4 117.5 76.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 44 NE2
REMARK 620 2 HEC D1128 NA 99.0
REMARK 620 3 HEC D1128 NB 93.5 90.7
REMARK 620 4 HEC D1128 NC 79.6 178.5 88.9
REMARK 620 5 HEC D1128 ND 84.8 89.2 178.2 91.1
REMARK 620 6 HIS D 62 NE2 169.0 91.4 89.8 90.0 91.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC D1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 79 NE2
REMARK 620 2 HEC D1129 NA 99.3
REMARK 620 3 HEC D1129 NB 86.8 90.6
REMARK 620 4 HEC D1129 NC 80.9 179.5 88.9
REMARK 620 5 HEC D1129 ND 90.1 90.2 176.9 90.3
REMARK 620 6 HIS D 102 NE2 168.2 87.4 83.3 92.3 99.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 19 SG
REMARK 620 2 SF4 E1801 S1 112.9
REMARK 620 3 SF4 E1801 S2 107.7 104.4
REMARK 620 4 SF4 E1801 S3 117.9 104.7 108.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 26 SG
REMARK 620 2 SF4 E1801 S1 116.2
REMARK 620 3 SF4 E1801 S2 103.7 97.7
REMARK 620 4 SF4 E1801 S4 126.0 106.4 101.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 E1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 54 SG
REMARK 620 2 SF4 E1801 S1 119.9
REMARK 620 3 SF4 E1801 S3 101.5 98.2
REMARK 620 4 SF4 E1801 S4 123.0 106.9 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO E1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 152 SG
REMARK 620 2 MGD E1803 S12 121.1
REMARK 620 3 MGD E1803 S13 100.8 75.7
REMARK 620 4 MGD E1804 S13 137.4 86.6 118.2
REMARK 620 5 MGD E1804 S12 91.8 142.7 81.6 78.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC F1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 44 NE2
REMARK 620 2 HEC F1128 NA 100.5
REMARK 620 3 HEC F1128 NB 90.8 89.5
REMARK 620 4 HEC F1128 NC 81.0 178.3 89.5
REMARK 620 5 HEC F1128 ND 89.0 89.4 178.8 91.6
REMARK 620 6 HIS F 62 NE2 165.9 92.4 94.9 86.2 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC F1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS F 79 NE2
REMARK 620 2 HEC F1129 NA 99.9
REMARK 620 3 HEC F1129 NB 84.4 89.1
REMARK 620 4 HEC F1129 NC 80.4 179.5 90.6
REMARK 620 5 HEC F1129 ND 94.3 88.5 177.1 91.8
REMARK 620 6 HIS F 102 NE2 168.3 80.9 83.9 98.7 97.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 G1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 19 SG
REMARK 620 2 SF4 G1801 S1 114.9
REMARK 620 3 SF4 G1801 S2 105.2 103.4
REMARK 620 4 SF4 G1801 S3 117.7 105.7 108.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 G1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 22 SG
REMARK 620 2 SF4 G1801 S2 123.4
REMARK 620 3 SF4 G1801 S3 118.7 100.7
REMARK 620 4 SF4 G1801 S4 103.1 104.0 104.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 G1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 26 SG
REMARK 620 2 SF4 G1801 S1 116.3
REMARK 620 3 SF4 G1801 S2 105.7 98.6
REMARK 620 4 SF4 G1801 S4 123.8 106.7 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 G1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 54 SG
REMARK 620 2 SF4 G1801 S1 116.3
REMARK 620 3 SF4 G1801 S3 108.1 99.5
REMARK 620 4 SF4 G1801 S4 123.2 104.7 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO G1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 152 SG
REMARK 620 2 MGD G1803 S12 122.5
REMARK 620 3 MGD G1803 S13 101.1 77.1
REMARK 620 4 MGD G1804 S12 89.2 144.6 81.9
REMARK 620 5 MGD G1804 S13 138.0 84.8 116.9 79.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC H1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 44 NE2
REMARK 620 2 HEC H1128 NA 97.0
REMARK 620 3 HEC H1128 NB 94.2 89.8
REMARK 620 4 HEC H1128 NC 83.0 178.1 88.4
REMARK 620 5 HEC H1128 ND 84.5 89.5 178.4 92.3
REMARK 620 6 HIS H 62 NE2 166.7 89.2 97.6 91.1 83.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC H1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS H 79 NE2
REMARK 620 2 HEC H1129 NA 93.4
REMARK 620 3 HEC H1129 NB 86.5 89.5
REMARK 620 4 HEC H1129 NC 86.5 179.8 90.6
REMARK 620 5 HEC H1129 ND 91.8 87.9 176.8 92.0
REMARK 620 6 HIS H 102 NE2 170.1 86.3 83.6 93.9 98.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 I1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 19 SG
REMARK 620 2 SF4 I1801 S1 125.7
REMARK 620 3 SF4 I1801 S2 107.6 102.6
REMARK 620 4 SF4 I1801 S3 103.4 106.9 110.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 I1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 26 SG
REMARK 620 2 SF4 I1801 S1 116.4
REMARK 620 3 SF4 I1801 S2 109.2 97.2
REMARK 620 4 SF4 I1801 S4 121.9 106.0 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 I1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 54 SG
REMARK 620 2 SF4 I1801 S1 113.3
REMARK 620 3 SF4 I1801 S3 99.1 98.0
REMARK 620 4 SF4 I1801 S4 132.3 105.0 102.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO I1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I 152 SG
REMARK 620 2 MGD I1803 S13 95.5
REMARK 620 3 MGD I1803 S12 133.2 74.0
REMARK 620 4 MGD I1804 S13 138.5 109.0 86.6
REMARK 620 5 MGD I1804 S12 82.6 73.0 133.1 73.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC J1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 44 NE2
REMARK 620 2 HEC J1128 NA 97.4
REMARK 620 3 HEC J1128 NB 93.5 89.3
REMARK 620 4 HEC J1128 NC 81.7 178.4 89.5
REMARK 620 5 HEC J1128 ND 85.5 89.2 178.1 92.0
REMARK 620 6 HIS J 62 NE2 160.5 97.2 99.6 84.0 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC J1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS J 79 NE2
REMARK 620 2 HEC J1129 NA 97.1
REMARK 620 3 HEC J1129 NB 82.7 88.9
REMARK 620 4 HEC J1129 NC 83.3 179.3 90.6
REMARK 620 5 HEC J1129 ND 94.8 89.3 176.7 91.2
REMARK 620 6 HIS J 102 NE2 166.7 90.0 86.2 89.5 96.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 K1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 19 SG
REMARK 620 2 SF4 K1801 S1 120.3
REMARK 620 3 SF4 K1801 S2 105.8 105.2
REMARK 620 4 SF4 K1801 S3 110.9 105.4 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 K1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 22 SG
REMARK 620 2 SF4 K1801 S2 120.3
REMARK 620 3 SF4 K1801 S3 120.6 100.2
REMARK 620 4 SF4 K1801 S4 104.1 105.4 104.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 K1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 26 SG
REMARK 620 2 SF4 K1801 S1 121.1
REMARK 620 3 SF4 K1801 S2 107.1 97.9
REMARK 620 4 SF4 K1801 S4 119.1 105.8 102.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 K1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 54 SG
REMARK 620 2 SF4 K1801 S1 112.3
REMARK 620 3 SF4 K1801 S3 100.3 98.2
REMARK 620 4 SF4 K1801 S4 131.0 107.0 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO K1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS K 152 SG
REMARK 620 2 MGD K1803 S13 99.1
REMARK 620 3 MGD K1803 S12 125.9 76.7
REMARK 620 4 MGD K1804 S12 86.4 79.9 142.4
REMARK 620 5 MGD K1804 S13 136.7 116.9 87.2 77.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC L1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 44 NE2
REMARK 620 2 HEC L1128 NA 96.1
REMARK 620 3 HEC L1128 NB 85.3 89.4
REMARK 620 4 HEC L1128 NC 83.1 178.0 88.8
REMARK 620 5 HEC L1128 ND 92.8 89.8 177.9 92.0
REMARK 620 6 HIS L 62 NE2 170.2 93.7 95.4 87.1 86.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC L1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS L 79 NE2
REMARK 620 2 HEC L1129 NA 98.8
REMARK 620 3 HEC L1129 NB 91.4 90.8
REMARK 620 4 HEC L1129 NC 80.1 178.6 90.1
REMARK 620 5 HEC L1129 ND 86.0 87.7 176.7 91.3
REMARK 620 6 HIS L 102 NE2 169.9 83.9 78.8 97.3 103.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 19 SG
REMARK 620 2 SF4 M1801 S1 118.4
REMARK 620 3 SF4 M1801 S2 104.3 103.5
REMARK 620 4 SF4 M1801 S3 114.0 106.1 109.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 22 SG
REMARK 620 2 SF4 M1801 S2 125.7
REMARK 620 3 SF4 M1801 S3 116.0 99.7
REMARK 620 4 SF4 M1801 S4 103.3 104.7 105.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 26 SG
REMARK 620 2 SF4 M1801 S1 121.5
REMARK 620 3 SF4 M1801 S2 103.7 97.6
REMARK 620 4 SF4 M1801 S4 120.7 106.8 101.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 M1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 54 SG
REMARK 620 2 SF4 M1801 S1 116.4
REMARK 620 3 SF4 M1801 S3 98.1 98.7
REMARK 620 4 SF4 M1801 S4 129.6 105.3 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO M1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS M 152 SG
REMARK 620 2 MGD M1803 S12 119.8
REMARK 620 3 MGD M1803 S13 96.3 74.5
REMARK 620 4 MGD M1804 S13 138.0 90.6 120.8
REMARK 620 5 MGD M1804 S12 87.9 144.5 81.1 80.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC N1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 44 NE2
REMARK 620 2 HEC N1128 NA 93.0
REMARK 620 3 HEC N1128 NB 95.7 89.7
REMARK 620 4 HEC N1128 NC 86.7 179.7 90.2
REMARK 620 5 HEC N1128 ND 84.3 88.2 177.9 91.9
REMARK 620 6 HIS N 62 NE2 170.5 89.3 93.4 91.0 86.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC N1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 79 NE2
REMARK 620 2 HEC N1129 NA 97.7
REMARK 620 3 HEC N1129 NB 87.2 89.6
REMARK 620 4 HEC N1129 NC 83.3 178.8 91.1
REMARK 620 5 HEC N1129 ND 91.8 88.4 177.6 90.9
REMARK 620 6 HIS N 102 NE2 171.6 88.4 87.1 90.7 94.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 O1801 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 19 SG
REMARK 620 2 SF4 O1801 S1 127.5
REMARK 620 3 SF4 O1801 S2 102.3 102.7
REMARK 620 4 SF4 O1801 S3 107.2 106.4 110.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 O1801 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 22 SG
REMARK 620 2 SF4 O1801 S2 122.7
REMARK 620 3 SF4 O1801 S3 119.7 100.9
REMARK 620 4 SF4 O1801 S4 101.7 104.1 105.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 O1801 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 26 SG
REMARK 620 2 SF4 O1801 S1 119.2
REMARK 620 3 SF4 O1801 S2 106.2 97.7
REMARK 620 4 SF4 O1801 S4 121.6 106.4 101.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 O1801 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 54 SG
REMARK 620 2 SF4 O1801 S1 109.2
REMARK 620 3 SF4 O1801 S3 98.9 100.1
REMARK 620 4 SF4 O1801 S4 136.0 104.4 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MO O1802 MO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS O 152 SG
REMARK 620 2 MGD O1803 S13 96.3
REMARK 620 3 MGD O1803 S12 124.2 71.7
REMARK 620 4 MGD O1804 S13 138.4 118.9 89.6
REMARK 620 5 MGD O1804 S12 81.8 80.1 142.8 83.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC P1128 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 44 NE2
REMARK 620 2 HEC P1128 NA 89.4
REMARK 620 3 HEC P1128 NB 95.7 89.9
REMARK 620 4 HEC P1128 NC 89.2 177.2 87.8
REMARK 620 5 HEC P1128 ND 82.5 89.7 178.3 92.4
REMARK 620 6 HIS P 62 NE2 171.5 86.9 91.9 94.8 89.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEC P1129 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 79 NE2
REMARK 620 2 HEC P1129 NA 99.5
REMARK 620 3 HEC P1129 NB 81.5 91.2
REMARK 620 4 HEC P1129 NC 80.1 179.0 89.7
REMARK 620 5 HEC P1129 ND 96.1 89.4 177.7 89.7
REMARK 620 6 HIS P 102 NE2 164.9 81.5 83.3 99.1 99.0
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "EF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "GG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "IG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "KF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "MF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "OG" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO A1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD A1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD A1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC B1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO C1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD C1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD C1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC D1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 E1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO E1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD E1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD E1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC F1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC F1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 G1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO G1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD G1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD G1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC H1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC H1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 I1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO I1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD I1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD I1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC J1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC J1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 K1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO K1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD K1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD K1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC L1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC L1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 M1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO M1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD M1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD M1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC N1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC N1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 O1801
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MO O1802
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD O1803
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MGD O1804
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC P1128
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC P1129
DBREF 1OGY A 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY C 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY E 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY G 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY I 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY K 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY M 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY O 1 802 UNP Q53176 NAPA_RHOSH 30 831
DBREF 1OGY B 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY D 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY F 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY H 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY J 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY L 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY N 1 130 UNP Q53177 NAPB_RHOSH 25 154
DBREF 1OGY P 1 130 UNP Q53177 NAPB_RHOSH 25 154
SEQRES 1 A 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 A 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 A 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 A 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 A 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 A 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 A 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 A 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 A 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 A 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 A 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 A 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 A 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 A 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 A 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 A 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 A 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 A 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 A 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 A 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 A 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 A 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 A 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 A 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 A 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 A 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 A 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 A 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 A 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 A 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 A 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 A 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 A 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 A 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 A 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 A 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 A 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 A 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 A 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 A 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 A 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 A 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 A 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 A 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 A 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 A 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 A 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 A 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 A 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 A 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 A 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 A 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 A 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 A 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 A 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 A 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 A 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 A 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 A 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 A 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 A 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 A 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 B 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 B 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 B 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 B 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 B 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 B 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 B 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 B 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 B 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 B 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 C 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 C 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 C 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 C 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 C 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 C 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 C 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 C 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 C 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 C 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 C 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 C 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 C 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 C 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 C 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 C 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 C 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 C 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 C 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 C 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 C 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 C 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 C 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 C 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 C 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 C 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 C 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 C 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 C 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 C 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 C 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 C 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 C 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 C 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 C 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 C 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 C 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 C 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 C 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 C 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 C 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 C 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 C 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 C 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 C 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 C 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 C 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 C 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 C 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 C 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 C 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 C 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 C 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 C 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 C 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 C 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 C 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 C 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 C 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 C 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 C 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 C 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 D 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 D 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 D 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 D 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 D 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 D 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 D 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 D 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 D 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 D 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 E 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 E 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 E 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 E 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 E 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 E 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 E 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 E 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 E 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 E 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 E 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 E 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 E 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 E 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 E 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 E 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 E 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 E 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 E 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 E 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 E 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 E 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 E 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 E 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 E 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 E 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 E 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 E 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 E 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 E 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 E 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 E 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 E 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 E 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 E 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 E 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 E 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 E 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 E 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 E 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 E 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 E 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 E 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 E 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 E 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 E 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 E 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 E 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 E 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 E 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 E 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 E 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 E 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 E 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 E 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 E 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 E 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 E 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 E 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 E 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 E 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 E 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 F 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 F 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 F 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 F 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 F 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 F 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 F 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 F 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 F 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 F 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 G 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 G 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 G 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 G 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 G 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 G 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 G 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 G 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 G 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 G 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 G 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 G 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 G 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 G 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 G 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 G 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 G 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 G 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 G 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 G 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 G 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 G 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 G 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 G 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 G 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 G 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 G 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 G 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 G 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 G 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 G 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 G 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 G 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 G 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 G 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 G 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 G 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 G 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 G 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 G 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 G 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 G 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 G 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 G 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 G 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 G 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 G 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 G 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 G 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 G 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 G 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 G 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 G 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 G 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 G 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 G 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 G 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 G 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 G 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 G 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 G 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 G 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 H 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 H 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 H 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 H 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 H 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 H 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 H 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 H 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 H 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 H 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 I 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 I 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 I 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 I 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 I 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 I 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 I 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 I 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 I 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 I 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 I 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 I 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 I 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 I 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 I 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 I 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 I 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 I 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 I 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 I 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 I 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 I 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 I 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 I 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 I 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 I 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 I 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 I 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 I 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 I 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 I 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 I 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 I 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 I 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 I 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 I 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 I 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 I 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 I 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 I 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 I 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 I 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 I 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 I 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 I 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 I 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 I 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 I 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 I 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 I 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 I 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 I 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 I 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 I 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 I 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 I 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 I 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 I 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 I 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 I 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 I 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 I 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 J 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 J 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 J 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 J 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 J 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 J 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 J 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 J 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 J 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 J 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 K 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 K 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 K 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 K 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 K 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 K 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 K 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 K 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 K 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 K 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 K 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 K 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 K 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 K 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 K 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 K 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 K 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 K 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 K 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 K 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 K 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 K 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 K 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 K 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 K 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 K 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 K 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 K 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 K 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 K 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 K 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 K 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 K 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 K 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 K 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 K 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 K 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 K 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 K 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 K 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 K 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 K 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 K 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 K 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 K 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 K 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 K 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 K 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 K 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 K 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 K 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 K 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 K 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 K 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 K 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 K 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 K 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 K 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 K 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 K 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 K 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 K 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 L 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 L 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 L 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 L 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 L 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 L 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 L 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 L 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 L 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 L 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 M 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 M 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 M 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 M 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 M 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 M 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 M 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 M 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 M 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 M 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 M 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 M 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 M 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 M 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 M 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 M 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 M 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 M 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 M 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 M 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 M 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 M 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 M 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 M 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 M 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 M 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 M 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 M 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 M 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 M 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 M 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 M 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 M 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 M 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 M 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 M 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 M 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 M 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 M 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 M 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 M 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 M 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 M 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 M 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 M 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 M 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 M 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 M 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 M 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 M 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 M 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 M 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 M 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 M 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 M 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 M 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 M 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 M 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 M 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 M 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 M 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 M 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 N 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 N 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 N 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 N 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 N 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 N 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 N 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 N 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 N 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 N 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
SEQRES 1 O 802 GLN PRO VAL THR GLY GLY ALA GLU ALA LEU ARG ILE ARG
SEQRES 2 O 802 TRP SER LYS ALA PRO CYS ARG PHE CYS GLY THR GLY CYS
SEQRES 3 O 802 GLY VAL MET VAL GLY THR ARG ASP GLY GLN VAL VAL ALA
SEQRES 4 O 802 THR HIS GLY ASP THR GLN ALA GLU VAL ASN ARG GLY LEU
SEQRES 5 O 802 ASN CYS VAL LYS GLY TYR PHE LEU SER LYS ILE MET TYR
SEQRES 6 O 802 GLY GLU ASP ARG LEU THR THR PRO LEU LEU ARG MET LYS
SEQRES 7 O 802 ASP GLY VAL TYR HIS LYS GLU GLY GLU PHE ALA PRO VAL
SEQRES 8 O 802 SER TRP ASP GLU ALA PHE ASP VAL MET ALA ALA GLN ALA
SEQRES 9 O 802 LYS LEU VAL LEU LYS GLU LYS ALA PRO GLU ALA VAL GLY
SEQRES 10 O 802 MET PHE GLY SER GLY GLN TRP THR ILE TRP GLU GLY TYR
SEQRES 11 O 802 ALA ALA SER LYS LEU MET ARG ALA GLY PHE ARG SER ASN
SEQRES 12 O 802 ASN LEU ASP PRO ASN ALA ARG HIS CYS MET ALA SER ALA
SEQRES 13 O 802 ALA THR ALA PHE MET ARG THR PHE GLY MET ASP GLU PRO
SEQRES 14 O 802 MET GLY CYS TYR ASP ASP PHE GLU ALA ALA ASP ALA PHE
SEQRES 15 O 802 VAL LEU TRP GLY SER ASN MET ALA GLU MET HIS PRO ILE
SEQRES 16 O 802 LEU TRP SER ARG LEU THR ASP ARG ARG LEU SER HIS GLU
SEQRES 17 O 802 HIS VAL ARG VAL ALA VAL LEU SER THR PHE THR HIS ARG
SEQRES 18 O 802 SER SER ASP LEU SER ASP THR PRO ILE ILE PHE ARG PRO
SEQRES 19 O 802 GLY THR ASP ARG ALA ILE LEU ASN TYR ILE ALA HIS HIS
SEQRES 20 O 802 ILE ILE SER THR GLY ARG VAL ASN ARG ASP PHE VAL ASP
SEQRES 21 O 802 ARG HIS THR ASN PHE ALA LEU GLY ALA THR ASP ILE GLY
SEQRES 22 O 802 TYR GLY LEU ARG PRO GLU HIS GLN LEU GLN LEU ALA ALA
SEQRES 23 O 802 LYS GLY ALA ALA ASP ALA GLY ALA MET THR PRO THR ASP
SEQRES 24 O 802 PHE GLU THR PHE ALA ALA LEU VAL SER GLU TYR THR LEU
SEQRES 25 O 802 GLU LYS ALA ALA GLU ILE SER GLY VAL GLU PRO ALA LEU
SEQRES 26 O 802 LEU GLU GLU LEU ALA GLU LEU TYR ALA ASP PRO ASP ARG
SEQRES 27 O 802 LYS TRP MET SER LEU TRP THR MET GLY PHE ASN GLN HIS
SEQRES 28 O 802 VAL ARG GLY VAL TRP ALA ASN HIS MET VAL TYR ASN LEU
SEQRES 29 O 802 HIS LEU LEU THR GLY LYS ILE SER GLU PRO GLY ASN SER
SEQRES 30 O 802 PRO PHE SER LEU THR GLY GLN PRO PHE ALA CYS GLY THR
SEQRES 31 O 802 ALA ARG GLU VAL GLY THR PHE ALA HIS ARG LEU PRO ALA
SEQRES 32 O 802 ASP MET VAL VAL THR ASN PRO GLU HIS ARG ALA HIS ALA
SEQRES 33 O 802 GLU GLU ILE TRP LYS LEU PRO ALA GLY LEU LEU PRO ASP
SEQRES 34 O 802 TRP VAL GLY ALA HIS ALA VAL GLU GLN ASP ARG LYS LEU
SEQRES 35 O 802 HIS ASP GLY GLU ILE ASN PHE TYR TRP VAL GLN VAL ASN
SEQRES 36 O 802 ASN ASN MET GLN ALA ALA PRO ASN ILE ASP GLN GLU THR
SEQRES 37 O 802 TYR PRO GLY TYR ARG ASN PRO GLU ASN PHE ILE VAL VAL
SEQRES 38 O 802 SER ASP ALA TYR PRO THR VAL THR GLY ARG ALA ALA ASP
SEQRES 39 O 802 LEU VAL LEU PRO ALA ALA MET TRP VAL GLU LYS GLU GLY
SEQRES 40 O 802 ALA TYR GLY ASN ALA GLU ARG ARG THR HIS PHE TRP HIS
SEQRES 41 O 802 GLN LEU VAL GLU ALA PRO GLY GLU ALA ARG SER ASP LEU
SEQRES 42 O 802 TRP GLN LEU MET GLU PHE SER LYS ARG PHE THR THR ASP
SEQRES 43 O 802 GLU VAL TRP PRO GLU GLU ILE LEU SER ALA ALA PRO ALA
SEQRES 44 O 802 TYR ARG GLY LYS THR LEU PHE GLU VAL LEU PHE ALA ASN
SEQRES 45 O 802 GLY SER VAL ASP ARG PHE PRO ALA SER ASP VAL ASN PRO
SEQRES 46 O 802 ASP HIS ALA ASN HIS GLU ALA ALA LEU PHE GLY PHE TYR
SEQRES 47 O 802 PRO GLN LYS GLY LEU PHE GLU GLU TYR ALA ALA PHE GLY
SEQRES 48 O 802 ARG GLY HIS GLY HIS ASP LEU ALA PRO PHE ASP THR TYR
SEQRES 49 O 802 HIS GLU VAL ARG GLY LEU HIS TRP PRO VAL VAL GLU GLY
SEQRES 50 O 802 GLU GLU THR ARG TRP ARG TYR ARG GLU GLY PHE ASP PRO
SEQRES 51 O 802 TYR VAL LYS PRO GLY GLU GLY LEU ARG PHE TYR GLY LYS
SEQRES 52 O 802 PRO ASP GLY ARG ALA VAL ILE LEU GLY VAL PRO TYR GLU
SEQRES 53 O 802 PRO PRO ALA GLU SER PRO ASP GLU GLU PHE GLY PHE TRP
SEQRES 54 O 802 LEU VAL THR GLY ARG VAL LEU GLU HIS TRP HIS SER GLY
SEQRES 55 O 802 SER MET THR LEU ARG TRP PRO GLU LEU TYR LYS ALA PHE
SEQRES 56 O 802 PRO GLY ALA VAL CYS PHE MET HIS PRO GLU ASP ALA ARG
SEQRES 57 O 802 SER ARG GLY LEU ASN ARG GLY SER GLU VAL ARG VAL ILE
SEQRES 58 O 802 SER ARG ARG GLY GLU ILE ARG THR ARG LEU GLU THR ARG
SEQRES 59 O 802 GLY ARG ASN ARG MET PRO ARG GLY VAL VAL PHE VAL PRO
SEQRES 60 O 802 TRP PHE ASP ALA SER GLN LEU ILE ASN LYS VAL THR LEU
SEQRES 61 O 802 ASP ALA ASN ASP PRO ILE SER ARG GLN THR ASP PHE LYS
SEQRES 62 O 802 LYS CYS ALA VAL LYS ILE GLU ALA VAL
SEQRES 1 P 130 GLN ASP ALA PRO ARG LEU THR GLY ALA ASP ARG PRO MET
SEQRES 2 P 130 SER GLU VAL ALA ALA PRO PRO LEU PRO GLU THR ILE THR
SEQRES 3 P 130 ASP ASP ARG ARG VAL GLY ARG ASN TYR PRO GLU GLN PRO
SEQRES 4 P 130 PRO VAL ILE PRO HIS SER ILE GLU GLY TYR GLN LEU SER
SEQRES 5 P 130 VAL ASN ALA ASN ARG CYS LEU GLU CYS HIS ARG ARG GLN
SEQRES 6 P 130 TYR SER GLY LEU VAL ALA ALA PRO MET ILE SER ILE THR
SEQRES 7 P 130 HIS PHE GLN ASP ARG GLU GLY GLN MET LEU ALA ASP VAL
SEQRES 8 P 130 SER PRO ARG ARG TYR PHE CYS THR ALA CYS HIS VAL PRO
SEQRES 9 P 130 GLN THR ASN ALA GLN PRO LEU VAL THR ASN GLU PHE ARG
SEQRES 10 P 130 ASP MET LEU THR LEU MET PRO ALA SER ASN GLU ALA GLU
HET SF4 A1801 8
HET MO A1802 1
HET MGD A1803 47
HET MGD A1804 47
HET HEC B1128 43
HET HEC B1129 43
HET SF4 C1801 8
HET MO C1802 1
HET MGD C1803 47
HET MGD C1804 47
HET HEC D1128 43
HET HEC D1129 43
HET SF4 E1801 8
HET MO E1802 1
HET MGD E1803 47
HET MGD E1804 47
HET HEC F1128 43
HET HEC F1129 43
HET SF4 G1801 8
HET MO G1802 1
HET MGD G1803 47
HET MGD G1804 47
HET HEC H1128 43
HET HEC H1129 43
HET SF4 I1801 8
HET MO I1802 1
HET MGD I1803 47
HET MGD I1804 47
HET HEC J1128 43
HET HEC J1129 43
HET SF4 K1801 8
HET MO K1802 1
HET MGD K1803 47
HET MGD K1804 47
HET HEC L1128 43
HET HEC L1129 43
HET SF4 M1801 8
HET MO M1802 1
HET MGD M1803 47
HET MGD M1804 47
HET HEC N1128 43
HET HEC N1129 43
HET SF4 O1801 8
HET MO O1802 1
HET MGD O1803 47
HET MGD O1804 47
HET HEC P1128 43
HET HEC P1129 43
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM MO MOLYBDENUM ATOM
HETNAM MGD 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-
HETNAM 2 MGD OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE
HETNAM 3 MGD DINUCLEOTIDE
HETNAM HEC HEME C
HETSYN MGD MOLYBDOPTERIN GUANOSINE DINUCLEOTIDE
FORMUL 17 SF4 8(FE4 S4)
FORMUL 18 MO 8(MO)
FORMUL 19 MGD 16(C20 H26 N10 O13 P2 S2)
FORMUL 21 HEC 16(C34 H34 FE N4 O4)
HELIX 1 1 CYS A 54 PHE A 59 1 6
HELIX 2 2 LEU A 60 ILE A 63 5 4
HELIX 3 3 SER A 92 LYS A 111 1 20
HELIX 4 4 ALA A 112 GLU A 114 5 3
HELIX 5 5 THR A 125 ALA A 138 1 14
HELIX 6 6 ASN A 148 MET A 153 1 6
HELIX 7 7 MET A 153 GLY A 165 1 13
HELIX 8 8 ASP A 174 ALA A 179 1 6
HELIX 9 9 ASN A 188 HIS A 193 1 6
HELIX 10 10 HIS A 193 HIS A 207 1 15
HELIX 11 11 HIS A 220 LEU A 225 5 6
HELIX 12 12 THR A 236 THR A 251 1 16
HELIX 13 13 ASN A 255 HIS A 262 1 8
HELIX 14 14 HIS A 280 ALA A 285 1 6
HELIX 15 15 ASP A 299 GLU A 309 1 11
HELIX 16 16 THR A 311 GLY A 320 1 10
HELIX 17 17 GLU A 322 TYR A 333 1 12
HELIX 18 18 THR A 345 GLN A 350 1 6
HELIX 19 19 ARG A 353 GLY A 369 1 17
HELIX 20 20 THR A 390 GLY A 395 1 6
HELIX 21 21 ASN A 409 TRP A 420 1 12
HELIX 22 22 HIS A 434 ASP A 444 1 11
HELIX 23 23 ASN A 456 ALA A 461 1 6
HELIX 24 24 THR A 468 ASN A 474 1 7
HELIX 25 25 THR A 487 ALA A 492 1 6
HELIX 26 26 MET A 501 LYS A 505 5 5
HELIX 27 27 SER A 531 LYS A 541 1 11
HELIX 28 28 THR A 544 TRP A 549 1 6
HELIX 29 29 PRO A 550 ALA A 557 1 8
HELIX 30 30 ASN A 589 LEU A 594 1 6
HELIX 31 31 TYR A 598 ALA A 609 1 12
HELIX 32 32 ASP A 622 VAL A 627 1 6
HELIX 33 33 MET A 704 ARG A 707 5 4
HELIX 34 34 TRP A 708 PHE A 715 1 8
HELIX 35 35 HIS A 723 ARG A 730 1 8
HELIX 36 36 LEU A 774 VAL A 778 5 5
HELIX 37 37 ARG B 57 CYS B 61 5 5
HELIX 38 38 SER B 76 PHE B 80 5 5
HELIX 39 39 PHE B 97 CYS B 101 5 5
HELIX 40 40 CYS C 54 PHE C 59 1 6
HELIX 41 41 LEU C 60 ILE C 63 5 4
HELIX 42 42 SER C 92 LYS C 111 1 20
HELIX 43 43 ALA C 112 GLU C 114 5 3
HELIX 44 44 THR C 125 ALA C 138 1 14
HELIX 45 45 ASN C 148 MET C 153 1 6
HELIX 46 46 MET C 153 GLY C 165 1 13
HELIX 47 47 ASP C 174 ALA C 179 1 6
HELIX 48 48 ASN C 188 HIS C 193 1 6
HELIX 49 49 HIS C 193 HIS C 207 1 15
HELIX 50 50 HIS C 220 LEU C 225 5 6
HELIX 51 51 THR C 236 THR C 251 1 16
HELIX 52 52 ASN C 255 HIS C 262 1 8
HELIX 53 53 HIS C 280 ALA C 286 1 7
HELIX 54 54 ASP C 299 GLU C 309 1 11
HELIX 55 55 THR C 311 GLY C 320 1 10
HELIX 56 56 GLU C 322 TYR C 333 1 12
HELIX 57 57 THR C 345 GLN C 350 1 6
HELIX 58 58 ARG C 353 GLY C 369 1 17
HELIX 59 59 THR C 390 GLY C 395 1 6
HELIX 60 60 ASN C 409 TRP C 420 1 12
HELIX 61 61 HIS C 434 ASP C 444 1 11
HELIX 62 62 ASN C 456 ALA C 461 1 6
HELIX 63 63 THR C 468 ASN C 474 1 7
HELIX 64 64 THR C 487 ALA C 492 1 6
HELIX 65 65 MET C 501 LYS C 505 5 5
HELIX 66 66 SER C 531 LYS C 541 1 11
HELIX 67 67 THR C 544 TRP C 549 1 6
HELIX 68 68 PRO C 550 ALA C 557 1 8
HELIX 69 69 ASN C 589 LEU C 594 1 6
HELIX 70 70 TYR C 598 ALA C 609 1 12
HELIX 71 71 PRO C 620 VAL C 627 1 8
HELIX 72 72 MET C 704 ARG C 707 5 4
HELIX 73 73 TRP C 708 PHE C 715 1 8
HELIX 74 74 HIS C 723 GLY C 731 1 9
HELIX 75 75 LEU C 774 VAL C 778 5 5
HELIX 76 76 ARG D 57 CYS D 61 5 5
HELIX 77 77 SER D 76 PHE D 80 5 5
HELIX 78 78 PHE D 97 CYS D 101 5 5
HELIX 79 79 CYS E 54 PHE E 59 1 6
HELIX 80 80 LEU E 60 TYR E 65 5 6
HELIX 81 81 SER E 92 LYS E 111 1 20
HELIX 82 82 ALA E 112 GLU E 114 5 3
HELIX 83 83 THR E 125 ALA E 138 1 14
HELIX 84 84 ASN E 148 MET E 153 1 6
HELIX 85 85 MET E 153 GLY E 165 1 13
HELIX 86 86 ASP E 174 ALA E 179 1 6
HELIX 87 87 ASN E 188 HIS E 193 1 6
HELIX 88 88 HIS E 193 HIS E 207 1 15
HELIX 89 89 HIS E 220 LEU E 225 5 6
HELIX 90 90 THR E 236 THR E 251 1 16
HELIX 91 91 ASN E 255 HIS E 262 1 8
HELIX 92 92 HIS E 280 ALA E 285 1 6
HELIX 93 93 ASP E 299 SER E 308 1 10
HELIX 94 94 THR E 311 GLY E 320 1 10
HELIX 95 95 GLU E 322 TYR E 333 1 12
HELIX 96 96 THR E 345 GLN E 350 1 6
HELIX 97 97 ARG E 353 GLY E 369 1 17
HELIX 98 98 THR E 390 GLY E 395 1 6
HELIX 99 99 ASN E 409 TRP E 420 1 12
HELIX 100 100 HIS E 434 GLY E 445 1 12
HELIX 101 101 ASN E 456 ALA E 461 1 6
HELIX 102 102 THR E 468 ASN E 474 1 7
HELIX 103 103 THR E 487 ALA E 492 1 6
HELIX 104 104 MET E 501 LYS E 505 5 5
HELIX 105 105 SER E 531 LYS E 541 1 11
HELIX 106 106 THR E 544 TRP E 549 1 6
HELIX 107 107 PRO E 550 ALA E 557 1 8
HELIX 108 108 ASN E 589 LEU E 594 1 6
HELIX 109 109 TYR E 598 ALA E 609 1 12
HELIX 110 110 ASP E 622 VAL E 627 1 6
HELIX 111 111 MET E 704 ARG E 707 5 4
HELIX 112 112 TRP E 708 PHE E 715 1 8
HELIX 113 113 HIS E 723 GLY E 731 1 9
HELIX 114 114 LEU E 774 VAL E 778 5 5
HELIX 115 115 ARG F 57 CYS F 61 5 5
HELIX 116 116 SER F 76 PHE F 80 5 5
HELIX 117 117 PHE F 97 CYS F 101 5 5
HELIX 118 118 CYS G 54 PHE G 59 1 6
HELIX 119 119 LEU G 60 ILE G 63 5 4
HELIX 120 120 SER G 92 LYS G 111 1 20
HELIX 121 121 ALA G 112 GLU G 114 5 3
HELIX 122 122 THR G 125 ALA G 138 1 14
HELIX 123 123 ASN G 148 MET G 153 1 6
HELIX 124 124 MET G 153 GLY G 165 1 13
HELIX 125 125 ASP G 174 ALA G 179 1 6
HELIX 126 126 ASN G 188 HIS G 193 1 6
HELIX 127 127 HIS G 193 HIS G 207 1 15
HELIX 128 128 HIS G 220 LEU G 225 5 6
HELIX 129 129 THR G 236 THR G 251 1 16
HELIX 130 130 ASN G 255 HIS G 262 1 8
HELIX 131 131 HIS G 280 ALA G 285 1 6
HELIX 132 132 ASP G 299 GLU G 309 1 11
HELIX 133 133 THR G 311 GLY G 320 1 10
HELIX 134 134 GLU G 322 TYR G 333 1 12
HELIX 135 135 THR G 345 GLN G 350 1 6
HELIX 136 136 ARG G 353 GLY G 369 1 17
HELIX 137 137 THR G 390 GLY G 395 1 6
HELIX 138 138 ASN G 409 TRP G 420 1 12
HELIX 139 139 HIS G 434 GLY G 445 1 12
HELIX 140 140 ASN G 456 ALA G 461 1 6
HELIX 141 141 THR G 468 ASN G 474 1 7
HELIX 142 142 THR G 487 ALA G 492 1 6
HELIX 143 143 MET G 501 LYS G 505 5 5
HELIX 144 144 SER G 531 LYS G 541 1 11
HELIX 145 145 THR G 544 TRP G 549 1 6
HELIX 146 146 PRO G 550 ALA G 557 1 8
HELIX 147 147 ASN G 589 LEU G 594 1 6
HELIX 148 148 TYR G 598 ALA G 609 1 12
HELIX 149 149 ASP G 622 VAL G 627 1 6
HELIX 150 150 MET G 704 ARG G 707 5 4
HELIX 151 151 TRP G 708 PHE G 715 1 8
HELIX 152 152 HIS G 723 GLY G 731 1 9
HELIX 153 153 LEU G 774 VAL G 778 5 5
HELIX 154 154 ARG H 57 CYS H 61 5 5
HELIX 155 155 SER H 76 PHE H 80 5 5
HELIX 156 156 PHE H 97 CYS H 101 5 5
HELIX 157 157 CYS I 54 PHE I 59 1 6
HELIX 158 158 LEU I 60 ILE I 63 5 4
HELIX 159 159 SER I 92 LYS I 111 1 20
HELIX 160 160 ALA I 112 GLU I 114 5 3
HELIX 161 161 THR I 125 ALA I 138 1 14
HELIX 162 162 ASN I 148 MET I 153 1 6
HELIX 163 163 MET I 153 GLY I 165 1 13
HELIX 164 164 TYR I 173 ALA I 179 1 7
HELIX 165 165 ASN I 188 HIS I 193 1 6
HELIX 166 166 HIS I 193 HIS I 207 1 15
HELIX 167 167 HIS I 220 LEU I 225 5 6
HELIX 168 168 THR I 236 THR I 251 1 16
HELIX 169 169 ASN I 255 HIS I 262 1 8
HELIX 170 170 HIS I 280 ALA I 285 1 6
HELIX 171 171 ASP I 299 SER I 308 1 10
HELIX 172 172 THR I 311 GLY I 320 1 10
HELIX 173 173 GLU I 322 TYR I 333 1 12
HELIX 174 174 THR I 345 GLN I 350 1 6
HELIX 175 175 ARG I 353 GLY I 369 1 17
HELIX 176 176 THR I 390 GLY I 395 1 6
HELIX 177 177 ASN I 409 TRP I 420 1 12
HELIX 178 178 HIS I 434 GLY I 445 1 12
HELIX 179 179 ASN I 456 ALA I 461 1 6
HELIX 180 180 ASN I 463 THR I 468 1 6
HELIX 181 181 THR I 468 ASN I 474 1 7
HELIX 182 182 THR I 487 ALA I 492 1 6
HELIX 183 183 MET I 501 LYS I 505 5 5
HELIX 184 184 SER I 531 LYS I 541 1 11
HELIX 185 185 THR I 544 TRP I 549 1 6
HELIX 186 186 PRO I 550 ALA I 557 1 8
HELIX 187 187 ASN I 589 LEU I 594 1 6
HELIX 188 188 TYR I 598 ALA I 609 1 12
HELIX 189 189 PRO I 620 VAL I 627 1 8
HELIX 190 190 MET I 704 ARG I 707 5 4
HELIX 191 191 TRP I 708 PHE I 715 1 8
HELIX 192 192 HIS I 723 GLY I 731 1 9
HELIX 193 193 LEU I 774 VAL I 778 5 5
HELIX 194 194 ARG J 57 CYS J 61 5 5
HELIX 195 195 SER J 76 PHE J 80 5 5
HELIX 196 196 PHE J 97 CYS J 101 5 5
HELIX 197 197 CYS K 54 PHE K 59 1 6
HELIX 198 198 LEU K 60 ILE K 63 5 4
HELIX 199 199 SER K 92 LYS K 111 1 20
HELIX 200 200 ALA K 112 GLU K 114 5 3
HELIX 201 201 THR K 125 ALA K 138 1 14
HELIX 202 202 ASN K 148 MET K 153 1 6
HELIX 203 203 MET K 153 GLY K 165 1 13
HELIX 204 204 ASP K 174 ALA K 179 1 6
HELIX 205 205 ASN K 188 HIS K 193 1 6
HELIX 206 206 HIS K 193 HIS K 207 1 15
HELIX 207 207 HIS K 220 LEU K 225 5 6
HELIX 208 208 THR K 236 THR K 251 1 16
HELIX 209 209 ASN K 255 HIS K 262 1 8
HELIX 210 210 HIS K 280 ALA K 285 1 6
HELIX 211 211 ASP K 299 GLU K 309 1 11
HELIX 212 212 THR K 311 GLY K 320 1 10
HELIX 213 213 GLU K 322 TYR K 333 1 12
HELIX 214 214 THR K 345 GLN K 350 1 6
HELIX 215 215 ARG K 353 GLY K 369 1 17
HELIX 216 216 THR K 390 GLY K 395 1 6
HELIX 217 217 ASN K 409 TRP K 420 1 12
HELIX 218 218 HIS K 434 ASP K 444 1 11
HELIX 219 219 ASN K 456 ALA K 461 1 6
HELIX 220 220 ASN K 463 THR K 468 1 6
HELIX 221 221 THR K 468 ASN K 474 1 7
HELIX 222 222 THR K 487 ALA K 492 1 6
HELIX 223 223 MET K 501 LYS K 505 5 5
HELIX 224 224 SER K 531 LYS K 541 1 11
HELIX 225 225 THR K 544 TRP K 549 1 6
HELIX 226 226 PRO K 550 ALA K 557 1 8
HELIX 227 227 ASN K 589 LEU K 594 1 6
HELIX 228 228 TYR K 598 ALA K 609 1 12
HELIX 229 229 PRO K 620 VAL K 627 1 8
HELIX 230 230 MET K 704 ARG K 707 5 4
HELIX 231 231 TRP K 708 PHE K 715 1 8
HELIX 232 232 HIS K 723 GLY K 731 1 9
HELIX 233 233 LEU K 774 VAL K 778 5 5
HELIX 234 234 ARG L 57 CYS L 61 5 5
HELIX 235 235 SER L 76 PHE L 80 5 5
HELIX 236 236 PHE L 97 CYS L 101 5 5
HELIX 237 237 CYS M 54 PHE M 59 1 6
HELIX 238 238 LEU M 60 ILE M 63 5 4
HELIX 239 239 SER M 92 LYS M 111 1 20
HELIX 240 240 ALA M 112 GLU M 114 5 3
HELIX 241 241 THR M 125 ALA M 138 1 14
HELIX 242 242 ASN M 148 MET M 153 1 6
HELIX 243 243 MET M 153 GLY M 165 1 13
HELIX 244 244 ASP M 174 ALA M 179 1 6
HELIX 245 245 ASN M 188 HIS M 193 1 6
HELIX 246 246 HIS M 193 HIS M 207 1 15
HELIX 247 247 HIS M 220 LEU M 225 5 6
HELIX 248 248 THR M 236 THR M 251 1 16
HELIX 249 249 ASN M 255 HIS M 262 1 8
HELIX 250 250 HIS M 280 ALA M 286 1 7
HELIX 251 251 ASP M 299 GLU M 309 1 11
HELIX 252 252 THR M 311 GLY M 320 1 10
HELIX 253 253 GLU M 322 TYR M 333 1 12
HELIX 254 254 THR M 345 GLN M 350 1 6
HELIX 255 255 ARG M 353 GLY M 369 1 17
HELIX 256 256 THR M 390 GLY M 395 1 6
HELIX 257 257 ASN M 409 TRP M 420 1 12
HELIX 258 258 HIS M 434 ASP M 444 1 11
HELIX 259 259 ASN M 456 ALA M 461 1 6
HELIX 260 260 THR M 468 ASN M 474 1 7
HELIX 261 261 THR M 487 ALA M 492 1 6
HELIX 262 262 MET M 501 LYS M 505 5 5
HELIX 263 263 SER M 531 LYS M 541 1 11
HELIX 264 264 THR M 544 TRP M 549 1 6
HELIX 265 265 PRO M 550 ALA M 557 1 8
HELIX 266 266 ASN M 589 LEU M 594 1 6
HELIX 267 267 TYR M 598 ALA M 609 1 12
HELIX 268 268 PRO M 620 VAL M 627 1 8
HELIX 269 269 MET M 704 ARG M 707 5 4
HELIX 270 270 TRP M 708 PHE M 715 1 8
HELIX 271 271 HIS M 723 GLY M 731 1 9
HELIX 272 272 LEU M 774 VAL M 778 5 5
HELIX 273 273 ARG N 57 CYS N 61 5 5
HELIX 274 274 SER N 76 PHE N 80 5 5
HELIX 275 275 PHE N 97 CYS N 101 5 5
HELIX 276 276 CYS O 54 PHE O 59 1 6
HELIX 277 277 LEU O 60 ILE O 63 5 4
HELIX 278 278 SER O 92 LYS O 111 1 20
HELIX 279 279 ALA O 112 GLU O 114 5 3
HELIX 280 280 THR O 125 ALA O 138 1 14
HELIX 281 281 ASN O 148 MET O 153 1 6
HELIX 282 282 MET O 153 GLY O 165 1 13
HELIX 283 283 ASP O 174 ALA O 179 1 6
HELIX 284 284 ASN O 188 HIS O 193 1 6
HELIX 285 285 HIS O 193 HIS O 207 1 15
HELIX 286 286 HIS O 220 LEU O 225 5 6
HELIX 287 287 THR O 236 THR O 251 1 16
HELIX 288 288 ASN O 255 HIS O 262 1 8
HELIX 289 289 HIS O 280 ALA O 285 1 6
HELIX 290 290 ASP O 299 SER O 308 1 10
HELIX 291 291 THR O 311 GLY O 320 1 10
HELIX 292 292 GLU O 322 TYR O 333 1 12
HELIX 293 293 THR O 345 GLN O 350 1 6
HELIX 294 294 ARG O 353 GLY O 369 1 17
HELIX 295 295 ILE A 12 THR O 396 1 385
HELIX 296 296 ASN O 409 TRP O 420 1 12
HELIX 297 297 HIS O 434 ASP O 444 1 11
HELIX 298 298 ASN O 456 ALA O 461 1 6
HELIX 299 299 ASN O 463 THR O 468 1 6
HELIX 300 300 THR O 468 ASN O 474 1 7
HELIX 301 301 THR O 487 ALA O 492 1 6
HELIX 302 302 MET O 501 LYS O 505 5 5
HELIX 303 303 SER O 531 LYS O 541 1 11
HELIX 304 304 THR O 544 TRP O 549 1 6
HELIX 305 305 PRO O 550 ALA O 557 1 8
HELIX 306 306 ASN O 589 LEU O 594 1 6
HELIX 307 307 TYR O 598 ALA O 609 1 12
HELIX 308 308 PRO O 620 VAL O 627 1 8
HELIX 309 309 MET O 704 ARG O 707 5 4
HELIX 310 310 TRP O 708 PHE O 715 1 8
HELIX 311 311 HIS O 723 GLY O 731 1 9
HELIX 312 312 LEU O 774 VAL O 778 5 5
HELIX 313 313 ARG P 57 CYS P 61 5 5
HELIX 314 314 SER P 76 PHE P 80 5 5
HELIX 315 315 PHE P 97 CYS P 101 5 5
SHEET 1 AA 3 ARG A 13 PRO A 18 0
SHEET 2 AA 3 GLY A 27 ARG A 33 -1 O VAL A 28 N ALA A 17
SHEET 3 AA 3 GLN A 36 GLY A 42 -1 O GLN A 36 N ARG A 33
SHEET 1 AB 7 ALA A 89 PRO A 90 0
SHEET 2 AB 7 LEU A 74 LEU A 75 -1 O LEU A 75 N ALA A 89
SHEET 3 AB 7 LEU A 495 PRO A 498 -1 O VAL A 496 N LEU A 74
SHEET 4 AB 7 PHE A 478 ASP A 483 1 O VAL A 481 N LEU A 497
SHEET 5 AB 7 PHE A 449 GLN A 453 1 O TYR A 450 N VAL A 480
SHEET 6 AB 7 VAL A 116 GLY A 120 1 O GLY A 117 N TRP A 451
SHEET 7 AB 7 LEU A 145 PRO A 147 1 O ASP A 146 N GLY A 120
SHEET 1 AC 5 THR A 228 ILE A 231 0
SHEET 2 AC 5 ARG A 211 SER A 216 1 O VAL A 214 N ILE A 230
SHEET 3 AC 5 ALA A 181 TRP A 185 1 O PHE A 182 N ALA A 213
SHEET 4 AC 5 TRP A 340 TRP A 344 1 O MET A 341 N VAL A 183
SHEET 5 AC 5 SER A 377 SER A 380 1 N SER A 377 O TRP A 340
SHEET 1 AD 2 THR A 263 LEU A 267 0
SHEET 2 AD 2 ALA A 668 GLY A 672 1 O ALA A 668 N ASN A 264
SHEET 1 AE 2 ARG A 400 LEU A 401 0
SHEET 2 AE 2 MET A 405 VAL A 406 -1 O MET A 405 N LEU A 401
SHEET 1 AF 3 GLY A 507 GLY A 510 0
SHEET 2 AF 3 ARG A 515 TRP A 519 -1 O HIS A 517 N TYR A 509
SHEET 3 AF 3 LEU A 630 HIS A 631 -1 O LEU A 630 N THR A 516
SHEET 1 AG 7 PHE A 688 GLY A 693 0
SHEET 2 AG 7 ALA A 796 GLU A 800 -1 O VAL A 797 N PHE A 688
SHEET 3 AG 7 GLU A 737 ILE A 741 -1 O ARG A 739 N GLU A 800
SHEET 4 AG 7 GLU A 746 GLU A 752 -1 O ILE A 747 N VAL A 740
SHEET 5 AG 7 VAL A 719 PHE A 721 1 O CYS A 720 N GLU A 752
SHEET 6 AG 7 VAL A 763 PRO A 767 -1 O PHE A 765 N PHE A 721
SHEET 7 AG 7 PHE A 688 GLY A 693 1 O TRP A 689 N VAL A 764
SHEET 1 CA 3 ARG C 13 PRO C 18 0
SHEET 2 CA 3 GLY C 27 ARG C 33 -1 O VAL C 28 N ALA C 17
SHEET 3 CA 3 GLN C 36 GLY C 42 -1 O GLN C 36 N ARG C 33
SHEET 1 CB 7 ALA C 89 PRO C 90 0
SHEET 2 CB 7 LEU C 74 LEU C 75 -1 O LEU C 75 N ALA C 89
SHEET 3 CB 7 LEU C 495 PRO C 498 -1 O VAL C 496 N LEU C 74
SHEET 4 CB 7 PHE C 478 ASP C 483 1 O VAL C 481 N LEU C 497
SHEET 5 CB 7 PHE C 449 GLN C 453 1 O TYR C 450 N VAL C 480
SHEET 6 CB 7 VAL C 116 GLY C 120 1 O GLY C 117 N TRP C 451
SHEET 7 CB 7 LEU C 145 PRO C 147 1 O ASP C 146 N GLY C 120
SHEET 1 CC 5 THR C 228 ILE C 231 0
SHEET 2 CC 5 ARG C 211 SER C 216 1 O VAL C 214 N ILE C 230
SHEET 3 CC 5 ALA C 181 TRP C 185 1 O PHE C 182 N ALA C 213
SHEET 4 CC 5 TRP C 340 TRP C 344 1 O MET C 341 N VAL C 183
SHEET 5 CC 5 SER C 377 SER C 380 1 N SER C 377 O TRP C 340
SHEET 1 CD 2 THR C 263 LEU C 267 0
SHEET 2 CD 2 ALA C 668 GLY C 672 1 O ALA C 668 N ASN C 264
SHEET 1 CE 2 ARG C 400 LEU C 401 0
SHEET 2 CE 2 MET C 405 VAL C 406 -1 O MET C 405 N LEU C 401
SHEET 1 CF 3 GLY C 507 ASN C 511 0
SHEET 2 CF 3 ARG C 515 TRP C 519 -1 O ARG C 515 N ASN C 511
SHEET 3 CF 3 LEU C 630 HIS C 631 -1 O LEU C 630 N THR C 516
SHEET 1 CG 7 PHE C 688 GLY C 693 0
SHEET 2 CG 7 ALA C 796 GLU C 800 -1 O VAL C 797 N PHE C 688
SHEET 3 CG 7 GLU C 737 ILE C 741 -1 O ARG C 739 N GLU C 800
SHEET 4 CG 7 GLU C 746 GLU C 752 -1 O ILE C 747 N VAL C 740
SHEET 5 CG 7 VAL C 719 PHE C 721 1 O CYS C 720 N GLU C 752
SHEET 6 CG 7 VAL C 763 PRO C 767 -1 O PHE C 765 N PHE C 721
SHEET 7 CG 7 PHE C 688 GLY C 693 1 O TRP C 689 N VAL C 764
SHEET 1 EA 3 ARG E 13 PRO E 18 0
SHEET 2 EA 3 GLY E 27 ARG E 33 -1 O VAL E 28 N ALA E 17
SHEET 3 EA 3 GLN E 36 GLY E 42 -1 O GLN E 36 N ARG E 33
SHEET 1 EB 7 ALA E 89 PRO E 90 0
SHEET 2 EB 7 LEU E 74 LEU E 75 -1 O LEU E 75 N ALA E 89
SHEET 3 EB 7 LEU E 495 PRO E 498 -1 O VAL E 496 N LEU E 74
SHEET 4 EB 7 PHE E 478 ASP E 483 1 O VAL E 481 N LEU E 497
SHEET 5 EB 7 PHE E 449 GLN E 453 1 O TYR E 450 N VAL E 480
SHEET 6 EB 7 VAL E 116 GLY E 120 1 O GLY E 117 N TRP E 451
SHEET 7 EB 7 LEU E 145 PRO E 147 1 O ASP E 146 N GLY E 120
SHEET 1 EC 5 THR E 228 ILE E 231 0
SHEET 2 EC 5 ARG E 211 SER E 216 1 O VAL E 214 N ILE E 230
SHEET 3 EC 5 ALA E 181 TRP E 185 1 O PHE E 182 N ALA E 213
SHEET 4 EC 5 TRP E 340 TRP E 344 1 O MET E 341 N VAL E 183
SHEET 5 EC 5 SER E 377 SER E 380 1 N SER E 377 O TRP E 340
SHEET 1 ED 2 THR E 263 LEU E 267 0
SHEET 2 ED 2 ALA E 668 GLY E 672 1 O ALA E 668 N ASN E 264
SHEET 1 EE 3 GLY E 507 GLY E 510 0
SHEET 2 EE 3 ARG E 515 TRP E 519 -1 O HIS E 517 N TYR E 509
SHEET 3 EE 3 LEU E 630 HIS E 631 -1 O LEU E 630 N THR E 516
SHEET 1 EF 7 PHE E 688 GLY E 693 0
SHEET 2 EF 7 ALA E 796 GLU E 800 -1 O VAL E 797 N PHE E 688
SHEET 3 EF 7 GLU E 737 ILE E 741 -1 O ARG E 739 N GLU E 800
SHEET 4 EF 7 GLU E 746 GLU E 752 -1 O ILE E 747 N VAL E 740
SHEET 5 EF 7 VAL E 719 PHE E 721 1 O CYS E 720 N GLU E 752
SHEET 6 EF 7 VAL E 763 PRO E 767 -1 O PHE E 765 N PHE E 721
SHEET 7 EF 7 PHE E 688 GLY E 693 1 O TRP E 689 N VAL E 764
SHEET 1 GA 3 ARG G 13 PRO G 18 0
SHEET 2 GA 3 GLY G 27 ARG G 33 -1 O VAL G 28 N ALA G 17
SHEET 3 GA 3 GLN G 36 GLY G 42 -1 O GLN G 36 N ARG G 33
SHEET 1 GB 7 ALA G 89 PRO G 90 0
SHEET 2 GB 7 LEU G 74 LEU G 75 -1 O LEU G 75 N ALA G 89
SHEET 3 GB 7 LEU G 495 PRO G 498 -1 O VAL G 496 N LEU G 74
SHEET 4 GB 7 PHE G 478 ASP G 483 1 O VAL G 481 N LEU G 497
SHEET 5 GB 7 PHE G 449 GLN G 453 1 O TYR G 450 N VAL G 480
SHEET 6 GB 7 VAL G 116 GLY G 120 1 O GLY G 117 N TRP G 451
SHEET 7 GB 7 LEU G 145 PRO G 147 1 O ASP G 146 N GLY G 120
SHEET 1 GC 5 THR G 228 ILE G 231 0
SHEET 2 GC 5 ARG G 211 SER G 216 1 O VAL G 214 N ILE G 230
SHEET 3 GC 5 ALA G 181 TRP G 185 1 O PHE G 182 N ALA G 213
SHEET 4 GC 5 TRP G 340 TRP G 344 1 O MET G 341 N VAL G 183
SHEET 5 GC 5 SER G 377 SER G 380 1 N SER G 377 O TRP G 340
SHEET 1 GD 2 THR G 263 LEU G 267 0
SHEET 2 GD 2 ALA G 668 GLY G 672 1 O ALA G 668 N ASN G 264
SHEET 1 GE 2 ARG G 400 LEU G 401 0
SHEET 2 GE 2 MET G 405 VAL G 406 -1 O MET G 405 N LEU G 401
SHEET 1 GF 3 GLY G 507 GLY G 510 0
SHEET 2 GF 3 ARG G 515 TRP G 519 -1 O HIS G 517 N TYR G 509
SHEET 3 GF 3 LEU G 630 HIS G 631 -1 O LEU G 630 N THR G 516
SHEET 1 GG 7 PHE G 688 GLY G 693 0
SHEET 2 GG 7 ALA G 796 GLU G 800 -1 O VAL G 797 N PHE G 688
SHEET 3 GG 7 GLU G 737 ILE G 741 -1 O ARG G 739 N GLU G 800
SHEET 4 GG 7 GLU G 746 GLU G 752 -1 O ILE G 747 N VAL G 740
SHEET 5 GG 7 VAL G 719 PHE G 721 1 O CYS G 720 N GLU G 752
SHEET 6 GG 7 VAL G 763 PRO G 767 -1 O PHE G 765 N PHE G 721
SHEET 7 GG 7 PHE G 688 GLY G 693 1 O TRP G 689 N VAL G 764
SHEET 1 GH 2 ASN G 783 ASP G 784 0
SHEET 2 GH 2 GLN G 789 THR G 790 -1 O GLN G 789 N ASP G 784
SHEET 1 IA 3 ARG I 13 PRO I 18 0
SHEET 2 IA 3 GLY I 27 ARG I 33 -1 O VAL I 28 N ALA I 17
SHEET 3 IA 3 GLN I 36 GLY I 42 -1 O GLN I 36 N ARG I 33
SHEET 1 IB 7 ALA I 89 PRO I 90 0
SHEET 2 IB 7 LEU I 74 LEU I 75 -1 O LEU I 75 N ALA I 89
SHEET 3 IB 7 LEU I 495 PRO I 498 -1 O VAL I 496 N LEU I 74
SHEET 4 IB 7 PHE I 478 ASP I 483 1 O VAL I 481 N LEU I 497
SHEET 5 IB 7 PHE I 449 GLN I 453 1 O TYR I 450 N VAL I 480
SHEET 6 IB 7 VAL I 116 GLY I 120 1 O GLY I 117 N TRP I 451
SHEET 7 IB 7 LEU I 145 PRO I 147 1 O ASP I 146 N GLY I 120
SHEET 1 IC 5 THR I 228 ILE I 231 0
SHEET 2 IC 5 ARG I 211 SER I 216 1 O VAL I 214 N ILE I 230
SHEET 3 IC 5 ALA I 181 TRP I 185 1 O PHE I 182 N ALA I 213
SHEET 4 IC 5 TRP I 340 TRP I 344 1 O MET I 341 N VAL I 183
SHEET 5 IC 5 SER I 377 SER I 380 1 N SER I 377 O TRP I 340
SHEET 1 ID 2 THR I 263 LEU I 267 0
SHEET 2 ID 2 ALA I 668 GLY I 672 1 O ALA I 668 N ASN I 264
SHEET 1 IE 2 ARG I 400 LEU I 401 0
SHEET 2 IE 2 MET I 405 VAL I 406 -1 O MET I 405 N LEU I 401
SHEET 1 IF 3 GLY I 507 ASN I 511 0
SHEET 2 IF 3 ARG I 515 TRP I 519 -1 O ARG I 515 N ASN I 511
SHEET 3 IF 3 LEU I 630 HIS I 631 -1 O LEU I 630 N THR I 516
SHEET 1 IG 7 PHE I 688 GLY I 693 0
SHEET 2 IG 7 ALA I 796 GLU I 800 -1 O VAL I 797 N PHE I 688
SHEET 3 IG 7 GLU I 737 ILE I 741 -1 O ARG I 739 N GLU I 800
SHEET 4 IG 7 GLU I 746 GLU I 752 -1 O ILE I 747 N VAL I 740
SHEET 5 IG 7 VAL I 719 PHE I 721 1 O CYS I 720 N GLU I 752
SHEET 6 IG 7 VAL I 763 PRO I 767 -1 O PHE I 765 N PHE I 721
SHEET 7 IG 7 PHE I 688 GLY I 693 1 O TRP I 689 N VAL I 764
SHEET 1 KA 3 ARG K 13 PRO K 18 0
SHEET 2 KA 3 GLY K 27 ARG K 33 -1 O VAL K 28 N ALA K 17
SHEET 3 KA 3 GLN K 36 GLY K 42 -1 O GLN K 36 N ARG K 33
SHEET 1 KB 7 ALA K 89 PRO K 90 0
SHEET 2 KB 7 LEU K 74 LEU K 75 -1 O LEU K 75 N ALA K 89
SHEET 3 KB 7 LEU K 495 PRO K 498 -1 O VAL K 496 N LEU K 74
SHEET 4 KB 7 PHE K 478 ASP K 483 1 O VAL K 481 N LEU K 497
SHEET 5 KB 7 PHE K 449 GLN K 453 1 O TYR K 450 N VAL K 480
SHEET 6 KB 7 VAL K 116 GLY K 120 1 O GLY K 117 N TRP K 451
SHEET 7 KB 7 LEU K 145 PRO K 147 1 O ASP K 146 N GLY K 120
SHEET 1 KC 5 THR K 228 ILE K 231 0
SHEET 2 KC 5 ARG K 211 SER K 216 1 O VAL K 214 N ILE K 230
SHEET 3 KC 5 ALA K 181 TRP K 185 1 O PHE K 182 N ALA K 213
SHEET 4 KC 5 TRP K 340 TRP K 344 1 O MET K 341 N VAL K 183
SHEET 5 KC 5 SER K 377 SER K 380 1 N SER K 377 O TRP K 340
SHEET 1 KD 2 THR K 263 LEU K 267 0
SHEET 2 KD 2 ALA K 668 GLY K 672 1 O ALA K 668 N ASN K 264
SHEET 1 KE 3 GLY K 507 ASN K 511 0
SHEET 2 KE 3 ARG K 515 TRP K 519 -1 O ARG K 515 N ASN K 511
SHEET 3 KE 3 LEU K 630 HIS K 631 -1 O LEU K 630 N THR K 516
SHEET 1 KF12 PHE K 688 GLY K 693 0
SHEET 2 KF12 ALA K 796 GLU K 800 -1 O VAL K 797 N PHE K 688
SHEET 3 KF12 VAL K 719 PHE K 721 0
SHEET 4 KF12 GLU K 746 GLU K 752 1 O ARG K 750 N CYS K 720
SHEET 5 KF12 GLU K 737 ILE K 741 -1 O VAL K 738 N THR K 749
SHEET 6 KF12 GLU K 746 GLU K 752 -1 O ILE K 747 N VAL K 740
SHEET 7 KF12 GLU K 746 GLU K 752 0
SHEET 8 KF12 VAL K 719 PHE K 721 1 O CYS K 720 N GLU K 752
SHEET 9 KF12 VAL K 763 PRO K 767 -1 O PHE K 765 N PHE K 721
SHEET 10 KF12 PHE K 688 GLY K 693 1 O TRP K 689 N VAL K 764
SHEET 11 KF12 ALA K 796 GLU K 800 -1 O VAL K 797 N PHE K 688
SHEET 12 KF12 PHE K 688 GLY K 693 -1 O PHE K 688 N VAL K 797
SHEET 1 KG 2 ASN K 783 ASP K 784 0
SHEET 2 KG 2 GLN K 789 THR K 790 -1 O GLN K 789 N ASP K 784
SHEET 1 MA 3 ARG M 13 PRO M 18 0
SHEET 2 MA 3 GLY M 27 ARG M 33 -1 O VAL M 28 N ALA M 17
SHEET 3 MA 3 GLN M 36 GLY M 42 -1 O GLN M 36 N ARG M 33
SHEET 1 MB 7 ALA M 89 PRO M 90 0
SHEET 2 MB 7 LEU M 74 LEU M 75 -1 O LEU M 75 N ALA M 89
SHEET 3 MB 7 LEU M 495 PRO M 498 -1 O VAL M 496 N LEU M 74
SHEET 4 MB 7 PHE M 478 ASP M 483 1 O VAL M 481 N LEU M 497
SHEET 5 MB 7 PHE M 449 GLN M 453 1 O TYR M 450 N VAL M 480
SHEET 6 MB 7 VAL M 116 GLY M 120 1 O GLY M 117 N TRP M 451
SHEET 7 MB 7 LEU M 145 PRO M 147 1 O ASP M 146 N GLY M 120
SHEET 1 MC 5 THR M 228 ILE M 231 0
SHEET 2 MC 5 ARG M 211 SER M 216 1 O VAL M 214 N ILE M 230
SHEET 3 MC 5 ALA M 181 TRP M 185 1 O PHE M 182 N ALA M 213
SHEET 4 MC 5 TRP M 340 TRP M 344 1 O MET M 341 N VAL M 183
SHEET 5 MC 5 SER M 377 SER M 380 1 N SER M 377 O TRP M 340
SHEET 1 MD 2 THR M 263 LEU M 267 0
SHEET 2 MD 2 ALA M 668 GLY M 672 1 O ALA M 668 N ASN M 264
SHEET 1 ME 3 GLY M 507 GLY M 510 0
SHEET 2 ME 3 ARG M 515 TRP M 519 -1 O HIS M 517 N TYR M 509
SHEET 3 ME 3 LEU M 630 HIS M 631 -1 O LEU M 630 N THR M 516
SHEET 1 MF12 PHE M 688 GLY M 693 0
SHEET 2 MF12 ALA M 796 GLU M 800 -1 O VAL M 797 N PHE M 688
SHEET 3 MF12 VAL M 719 PHE M 721 0
SHEET 4 MF12 GLU M 746 GLU M 752 1 O ARG M 750 N CYS M 720
SHEET 5 MF12 GLU M 737 ILE M 741 -1 O VAL M 738 N THR M 749
SHEET 6 MF12 GLU M 746 GLU M 752 -1 O ILE M 747 N VAL M 740
SHEET 7 MF12 GLU M 746 GLU M 752 0
SHEET 8 MF12 VAL M 719 PHE M 721 1 O CYS M 720 N GLU M 752
SHEET 9 MF12 VAL M 763 PRO M 767 -1 O PHE M 765 N PHE M 721
SHEET 10 MF12 PHE M 688 GLY M 693 1 O TRP M 689 N VAL M 764
SHEET 11 MF12 ALA M 796 GLU M 800 -1 O VAL M 797 N PHE M 688
SHEET 12 MF12 PHE M 688 GLY M 693 -1 O PHE M 688 N VAL M 797
SHEET 1 MG 2 ASN M 783 ASP M 784 0
SHEET 2 MG 2 GLN M 789 THR M 790 -1 O GLN M 789 N ASP M 784
SHEET 1 OA 3 ARG O 13 PRO O 18 0
SHEET 2 OA 3 GLY O 27 ARG O 33 -1 O VAL O 28 N ALA O 17
SHEET 3 OA 3 GLN O 36 GLY O 42 -1 O GLN O 36 N ARG O 33
SHEET 1 OB 7 ALA O 89 PRO O 90 0
SHEET 2 OB 7 LEU O 74 LEU O 75 -1 O LEU O 75 N ALA O 89
SHEET 3 OB 7 LEU O 495 PRO O 498 -1 O VAL O 496 N LEU O 74
SHEET 4 OB 7 PHE O 478 ASP O 483 1 O VAL O 481 N LEU O 497
SHEET 5 OB 7 PHE O 449 GLN O 453 1 O TYR O 450 N VAL O 480
SHEET 6 OB 7 VAL O 116 GLY O 120 1 O GLY O 117 N TRP O 451
SHEET 7 OB 7 LEU O 145 PRO O 147 1 O ASP O 146 N GLY O 120
SHEET 1 OC 5 THR O 228 ILE O 231 0
SHEET 2 OC 5 ARG O 211 SER O 216 1 O VAL O 214 N ILE O 230
SHEET 3 OC 5 ALA O 181 TRP O 185 1 O PHE O 182 N ALA O 213
SHEET 4 OC 5 TRP O 340 TRP O 344 1 O MET O 341 N VAL O 183
SHEET 5 OC 5 SER O 377 SER O 380 1 N SER O 377 O TRP O 340
SHEET 1 OD 2 THR O 263 LEU O 267 0
SHEET 2 OD 2 ALA O 668 GLY O 672 1 O ALA O 668 N ASN O 264
SHEET 1 OE 2 ARG O 400 LEU O 401 0
SHEET 2 OE 2 MET O 405 VAL O 406 -1 O MET O 405 N LEU O 401
SHEET 1 OF 3 GLY O 507 ASN O 511 0
SHEET 2 OF 3 ARG O 515 TRP O 519 -1 O ARG O 515 N ASN O 511
SHEET 3 OF 3 LEU O 630 HIS O 631 -1 O LEU O 630 N THR O 516
SHEET 1 OG12 PHE O 688 GLY O 693 0
SHEET 2 OG12 ALA O 796 GLU O 800 -1 O VAL O 797 N PHE O 688
SHEET 3 OG12 VAL O 719 PHE O 721 0
SHEET 4 OG12 GLU O 746 GLU O 752 1 O ARG O 750 N CYS O 720
SHEET 5 OG12 GLU O 737 ILE O 741 -1 O VAL O 738 N THR O 749
SHEET 6 OG12 GLU O 746 GLU O 752 -1 O ILE O 747 N VAL O 740
SHEET 7 OG12 GLU O 746 GLU O 752 0
SHEET 8 OG12 VAL O 719 PHE O 721 1 O CYS O 720 N GLU O 752
SHEET 9 OG12 VAL O 763 PRO O 767 -1 O PHE O 765 N PHE O 721
SHEET 10 OG12 PHE O 688 GLY O 693 1 O TRP O 689 N VAL O 764
SHEET 11 OG12 ALA O 796 GLU O 800 -1 O VAL O 797 N PHE O 688
SHEET 12 OG12 PHE O 688 GLY O 693 -1 O PHE O 688 N VAL O 797
LINK SG CYS B 58 CAB HEC B1128 1555 1555 1.84
LINK SG CYS B 61 CAC HEC B1128 1555 1555 2.02
LINK SG CYS B 98 CAB HEC B1129 1555 1555 1.84
LINK SG CYS B 101 CAC HEC B1129 1555 1555 1.98
LINK SG CYS A 19 FE4 SF4 A1801 1555 1555 2.21
LINK SG CYS A 22 FE1 SF4 A1801 1555 1555 2.28
LINK SG CYS A 26 FE3 SF4 A1801 1555 1555 2.17
LINK SG CYS A 54 FE2 SF4 A1801 1555 1555 2.27
LINK SG CYS A 152 MO MO A1802 1555 1555 2.13
LINK MO MO A1802 S13 MGD A1803 1555 1555 2.70
LINK MO MO A1802 S12 MGD A1803 1555 1555 2.50
LINK MO MO A1802 S12 MGD A1804 1555 1555 2.38
LINK MO MO A1802 S13 MGD A1804 1555 1555 2.42
LINK NE2 HIS B 44 FE HEC B1128 1555 1555 1.93
LINK NE2 HIS B 62 FE HEC B1128 1555 1555 1.98
LINK NE2 HIS B 79 FE HEC B1129 1555 1555 1.96
LINK NE2 HIS B 102 FE HEC B1129 1555 1555 1.96
LINK SG CYS C 19 FE4 SF4 C1801 1555 1555 2.33
LINK SG CYS C 22 FE1 SF4 C1801 1555 1555 2.49
LINK SG CYS C 26 FE3 SF4 C1801 1555 1555 2.20
LINK SG CYS C 54 FE2 SF4 C1801 1555 1555 2.27
LINK SG CYS C 152 MO MO C1802 1555 1555 2.26
LINK MO MO C1802 S12 MGD C1803 1555 1555 2.40
LINK MO MO C1802 S13 MGD C1803 1555 1555 2.72
LINK MO MO C1802 S12 MGD C1804 1555 1555 2.55
LINK MO MO C1802 S13 MGD C1804 1555 1555 2.47
LINK NE2 HIS D 44 FE HEC D1128 1555 1555 2.08
LINK NE2 HIS D 62 FE HEC D1128 1555 1555 1.97
LINK NE2 HIS D 79 FE HEC D1129 1555 1555 2.11
LINK NE2 HIS D 102 FE HEC D1129 1555 1555 1.94
LINK SG CYS E 19 FE4 SF4 E1801 1555 1555 2.20
LINK SG CYS E 26 FE3 SF4 E1801 1555 1555 2.29
LINK SG CYS E 54 FE2 SF4 E1801 1555 1555 2.29
LINK SG CYS E 152 MO MO E1802 1555 1555 2.13
LINK MO MO E1802 S12 MGD E1803 1555 1555 2.41
LINK MO MO E1802 S13 MGD E1803 1555 1555 2.46
LINK MO MO E1802 S13 MGD E1804 1555 1555 2.63
LINK MO MO E1802 S12 MGD E1804 1555 1555 2.35
LINK NE2 HIS F 44 FE HEC F1128 1555 1555 1.96
LINK NE2 HIS F 62 FE HEC F1128 1555 1555 2.22
LINK NE2 HIS F 79 FE HEC F1129 1555 1555 2.12
LINK NE2 HIS F 102 FE HEC F1129 1555 1555 2.03
LINK SG CYS G 19 FE4 SF4 G1801 1555 1555 2.33
LINK SG CYS G 22 FE1 SF4 G1801 1555 1555 2.54
LINK SG CYS G 26 FE3 SF4 G1801 1555 1555 2.05
LINK SG CYS G 54 FE2 SF4 G1801 1555 1555 2.29
LINK SG CYS G 152 MO MO G1802 1555 1555 2.17
LINK MO MO G1802 S12 MGD G1803 1555 1555 2.51
LINK MO MO G1802 S13 MGD G1803 1555 1555 2.47
LINK MO MO G1802 S12 MGD G1804 1555 1555 2.29
LINK MO MO G1802 S13 MGD G1804 1555 1555 2.63
LINK NE2 HIS H 44 FE HEC H1128 1555 1555 2.04
LINK NE2 HIS H 62 FE HEC H1128 1555 1555 2.15
LINK NE2 HIS H 79 FE HEC H1129 1555 1555 2.08
LINK NE2 HIS H 102 FE HEC H1129 1555 1555 2.10
LINK SG CYS I 19 FE4 SF4 I1801 1555 1555 2.61
LINK SG CYS I 26 FE3 SF4 I1801 1555 1555 2.24
LINK SG CYS I 54 FE2 SF4 I1801 1555 1555 2.61
LINK SG CYS I 152 MO MO I1802 1555 1555 2.28
LINK MO MO I1802 S13 MGD I1803 1555 1555 2.76
LINK MO MO I1802 S12 MGD I1803 1555 1555 2.41
LINK MO MO I1802 S13 MGD I1804 1555 1555 2.73
LINK MO MO I1802 S12 MGD I1804 1555 1555 2.64
LINK NE2 HIS J 44 FE HEC J1128 1555 1555 1.97
LINK NE2 HIS J 62 FE HEC J1128 1555 1555 2.18
LINK NE2 HIS J 79 FE HEC J1129 1555 1555 1.97
LINK NE2 HIS J 102 FE HEC J1129 1555 1555 1.98
LINK SG CYS K 19 FE4 SF4 K1801 1555 1555 2.41
LINK SG CYS K 22 FE1 SF4 K1801 1555 1555 2.47
LINK SG CYS K 26 FE3 SF4 K1801 1555 1555 2.21
LINK SG CYS K 54 FE2 SF4 K1801 1555 1555 2.46
LINK SG CYS K 152 MO MO K1802 1555 1555 2.28
LINK MO MO K1802 S13 MGD K1803 1555 1555 2.47
LINK MO MO K1802 S12 MGD K1803 1555 1555 2.44
LINK MO MO K1802 S12 MGD K1804 1555 1555 2.47
LINK MO MO K1802 S13 MGD K1804 1555 1555 2.53
LINK NE2 HIS L 44 FE HEC L1128 1555 1555 2.05
LINK NE2 HIS L 62 FE HEC L1128 1555 1555 2.12
LINK NE2 HIS L 79 FE HEC L1129 1555 1555 2.09
LINK NE2 HIS L 102 FE HEC L1129 1555 1555 2.07
LINK SG CYS M 19 FE4 SF4 M1801 1555 1555 2.18
LINK SG CYS M 22 FE1 SF4 M1801 1555 1555 2.64
LINK SG CYS M 26 FE3 SF4 M1801 1555 1555 2.02
LINK SG CYS M 54 FE2 SF4 M1801 1555 1555 2.46
LINK SG CYS M 152 MO MO M1802 1555 1555 2.26
LINK MO MO M1802 S12 MGD M1803 1555 1555 2.45
LINK MO MO M1802 S13 MGD M1803 1555 1555 2.57
LINK MO MO M1802 S13 MGD M1804 1555 1555 2.47
LINK MO MO M1802 S12 MGD M1804 1555 1555 2.47
LINK NE2 HIS N 44 FE HEC N1128 1555 1555 2.02
LINK NE2 HIS N 62 FE HEC N1128 1555 1555 2.14
LINK NE2 HIS N 79 FE HEC N1129 1555 1555 2.04
LINK NE2 HIS N 102 FE HEC N1129 1555 1555 2.04
LINK SG CYS O 19 FE4 SF4 O1801 1555 1555 2.47
LINK SG CYS O 22 FE1 SF4 O1801 1555 1555 2.89
LINK SG CYS O 26 FE3 SF4 O1801 1555 1555 2.06
LINK SG CYS O 54 FE2 SF4 O1801 1555 1555 2.54
LINK SG CYS O 152 MO MO O1802 1555 1555 2.44
LINK MO MO O1802 S13 MGD O1803 1555 1555 2.58
LINK MO MO O1802 S12 MGD O1803 1555 1555 2.51
LINK MO MO O1802 S13 MGD O1804 1555 1555 2.57
LINK MO MO O1802 S12 MGD O1804 1555 1555 2.44
LINK NE2 HIS P 44 FE HEC P1128 1555 1555 1.98
LINK NE2 HIS P 62 FE HEC P1128 1555 1555 1.98
LINK NE2 HIS P 79 FE HEC P1129 1555 1555 2.08
LINK NE2 HIS P 102 FE HEC P1129 1555 1555 2.03
CISPEP 1 TRP A 632 PRO A 633 0 7.54
CISPEP 2 TRP C 632 PRO C 633 0 8.10
CISPEP 3 TRP E 632 PRO E 633 0 -7.96
CISPEP 4 TRP M 632 PRO M 633 0 -2.47
SITE 1 AC1 6 CYS A 19 CYS A 22 CYS A 26 CYS A 54
SITE 2 AC1 6 GLY A 57 PRO A 194
SITE 1 AC2 3 CYS A 152 MGD A1803 MGD A1804
SITE 1 AC3 31 ARG A 20 GLN A 123 ASN A 148 CYS A 152
SITE 2 AC3 31 GLN A 350 GLN A 384 VAL A 454 ASN A 455
SITE 3 AC3 31 ASN A 456 ASN A 457 ALA A 460 SER A 482
SITE 4 AC3 31 ASP A 483 THR A 487 ALA A 499 ALA A 500
SITE 5 AC3 31 MET A 501 LYS A 505 ASP A 532 THR A 692
SITE 6 AC3 31 ARG A 694 TRP A 699 HIS A 700 SER A 701
SITE 7 AC3 31 SER A 703 TRP A 768 ASN A 776 PHE A 792
SITE 8 AC3 31 LYS A 793 MO A1802 MGD A1804
SITE 1 AC4 31 LYS A 56 CYS A 152 TRP A 185 GLY A 186
SITE 2 AC4 31 SER A 187 ASN A 188 GLU A 191 MET A 192
SITE 3 AC4 31 SER A 216 THR A 217 HIS A 220 PHE A 232
SITE 4 AC4 31 GLY A 235 ASP A 237 THR A 345 MET A 346
SITE 5 AC4 31 GLY A 347 PHE A 348 GLY A 383 GLN A 384
SITE 6 AC4 31 GLY A 693 ARG A 694 VAL A 695 LEU A 696
SITE 7 AC4 31 HIS A 698 TRP A 699 HIS A 700 LYS A 793
SITE 8 AC4 31 LYS A 794 MO A1802 MGD A1803
SITE 1 AC5 13 ARG B 30 PRO B 40 VAL B 41 ILE B 42
SITE 2 AC5 13 PRO B 43 HIS B 44 TYR B 49 ARG B 57
SITE 3 AC5 13 CYS B 58 CYS B 61 HIS B 62 CYS B 98
SITE 4 AC5 13 HIS B 102
SITE 1 AC6 21 LEU A 52 ASN A 53 TYR A 58 ARG B 33
SITE 2 AC6 21 TYR B 35 PRO B 36 GLU B 37 GLN B 38
SITE 3 AC6 21 PRO B 40 HIS B 62 MET B 74 ILE B 75
SITE 4 AC6 21 HIS B 79 ARG B 95 TYR B 96 PHE B 97
SITE 5 AC6 21 CYS B 98 CYS B 101 HIS B 102 ARG F 64
SITE 6 AC6 21 ILE F 77
SITE 1 AC7 7 CYS C 19 CYS C 22 CYS C 26 ASN C 53
SITE 2 AC7 7 CYS C 54 GLY C 57 PRO C 194
SITE 1 AC8 3 CYS C 152 MGD C1803 MGD C1804
SITE 1 AC9 32 ARG C 20 GLN C 123 ASN C 148 CYS C 152
SITE 2 AC9 32 MET C 346 GLN C 350 GLN C 384 VAL C 454
SITE 3 AC9 32 ASN C 455 ASN C 456 ASN C 457 ALA C 460
SITE 4 AC9 32 SER C 482 ASP C 483 THR C 487 ALA C 499
SITE 5 AC9 32 ALA C 500 MET C 501 LYS C 505 ASP C 532
SITE 6 AC9 32 THR C 692 ARG C 694 TRP C 699 HIS C 700
SITE 7 AC9 32 SER C 701 SER C 703 TRP C 768 ASN C 776
SITE 8 AC9 32 PHE C 792 LYS C 793 MO C1802 MGD C1804
SITE 1 BC1 30 LYS C 56 CYS C 152 TRP C 185 GLY C 186
SITE 2 BC1 30 ASN C 188 GLU C 191 MET C 192 SER C 216
SITE 3 BC1 30 THR C 217 HIS C 220 PHE C 232 GLY C 235
SITE 4 BC1 30 ASP C 237 THR C 345 MET C 346 GLY C 347
SITE 5 BC1 30 PHE C 348 GLY C 383 GLN C 384 GLY C 693
SITE 6 BC1 30 ARG C 694 VAL C 695 LEU C 696 HIS C 698
SITE 7 BC1 30 TRP C 699 HIS C 700 LYS C 793 LYS C 794
SITE 8 BC1 30 MO C1802 MGD C1803
SITE 1 BC2 12 ARG D 30 PRO D 40 VAL D 41 ILE D 42
SITE 2 BC2 12 PRO D 43 HIS D 44 TYR D 49 CYS D 58
SITE 3 BC2 12 CYS D 61 HIS D 62 CYS D 98 HEC D1129
SITE 1 BC3 21 LEU C 52 ASN C 53 TYR C 58 ARG D 33
SITE 2 BC3 21 TYR D 35 PRO D 36 GLU D 37 GLN D 38
SITE 3 BC3 21 PRO D 40 HIS D 62 MET D 74 ILE D 75
SITE 4 BC3 21 HIS D 79 ARG D 95 PHE D 97 CYS D 98
SITE 5 BC3 21 CYS D 101 HIS D 102 HEC D1128 ARG H 64
SITE 6 BC3 21 ILE H 77
SITE 1 BC4 6 CYS E 19 CYS E 22 CYS E 26 CYS E 54
SITE 2 BC4 6 GLY E 57 PRO E 194
SITE 1 BC5 3 CYS E 152 MGD E1803 MGD E1804
SITE 1 BC6 31 ARG E 20 GLN E 123 ASN E 148 CYS E 152
SITE 2 BC6 31 MET E 346 GLN E 350 GLN E 384 VAL E 454
SITE 3 BC6 31 ASN E 455 ASN E 456 ALA E 460 SER E 482
SITE 4 BC6 31 ASP E 483 THR E 487 ALA E 499 ALA E 500
SITE 5 BC6 31 MET E 501 LYS E 505 ASP E 532 THR E 692
SITE 6 BC6 31 ARG E 694 TRP E 699 HIS E 700 SER E 701
SITE 7 BC6 31 SER E 703 TRP E 768 ASN E 776 PHE E 792
SITE 8 BC6 31 LYS E 793 MO E1802 MGD E1804
SITE 1 BC7 30 LYS E 56 CYS E 152 TRP E 185 GLY E 186
SITE 2 BC7 30 ASN E 188 GLU E 191 MET E 192 SER E 216
SITE 3 BC7 30 THR E 217 HIS E 220 PHE E 232 GLY E 235
SITE 4 BC7 30 ASP E 237 THR E 345 MET E 346 GLY E 347
SITE 5 BC7 30 PHE E 348 GLY E 383 GLN E 384 GLY E 693
SITE 6 BC7 30 ARG E 694 VAL E 695 LEU E 696 HIS E 698
SITE 7 BC7 30 TRP E 699 HIS E 700 LYS E 793 LYS E 794
SITE 8 BC7 30 MO E1802 MGD E1803
SITE 1 BC8 11 ARG F 30 VAL F 41 ILE F 42 PRO F 43
SITE 2 BC8 11 HIS F 44 TYR F 49 ARG F 57 CYS F 58
SITE 3 BC8 11 CYS F 61 HIS F 62 HEC F1129
SITE 1 BC9 22 ARG B 64 TYR B 66 ILE B 77 LEU E 52
SITE 2 BC9 22 ASN E 53 TYR E 58 ARG F 33 TYR F 35
SITE 3 BC9 22 PRO F 36 GLU F 37 GLN F 38 PRO F 40
SITE 4 BC9 22 HIS F 62 MET F 74 ILE F 75 HIS F 79
SITE 5 BC9 22 ARG F 95 PHE F 97 CYS F 98 CYS F 101
SITE 6 BC9 22 HIS F 102 HEC F1128
SITE 1 CC1 5 CYS G 19 CYS G 22 CYS G 26 CYS G 54
SITE 2 CC1 5 PRO G 194
SITE 1 CC2 3 CYS G 152 MGD G1803 MGD G1804
SITE 1 CC3 32 ARG G 20 GLN G 123 ASN G 148 CYS G 152
SITE 2 CC3 32 MET G 346 GLN G 350 GLN G 384 VAL G 454
SITE 3 CC3 32 ASN G 455 ASN G 456 ASN G 457 ALA G 460
SITE 4 CC3 32 SER G 482 ASP G 483 THR G 487 ALA G 499
SITE 5 CC3 32 ALA G 500 MET G 501 LYS G 505 ASP G 532
SITE 6 CC3 32 THR G 692 ARG G 694 TRP G 699 HIS G 700
SITE 7 CC3 32 SER G 701 SER G 703 TRP G 768 ASN G 776
SITE 8 CC3 32 PHE G 792 LYS G 793 MO G1802 MGD G1804
SITE 1 CC4 30 LYS G 56 CYS G 152 TRP G 185 GLY G 186
SITE 2 CC4 30 SER G 187 ASN G 188 GLU G 191 MET G 192
SITE 3 CC4 30 SER G 216 THR G 217 HIS G 220 GLY G 235
SITE 4 CC4 30 ASP G 237 THR G 345 MET G 346 GLY G 347
SITE 5 CC4 30 PHE G 348 GLY G 383 GLN G 384 GLY G 693
SITE 6 CC4 30 ARG G 694 VAL G 695 LEU G 696 HIS G 698
SITE 7 CC4 30 TRP G 699 HIS G 700 LYS G 793 LYS G 794
SITE 8 CC4 30 MO G1802 MGD G1803
SITE 1 CC5 14 ARG H 30 ARG H 33 PRO H 40 VAL H 41
SITE 2 CC5 14 ILE H 42 PRO H 43 HIS H 44 TYR H 49
SITE 3 CC5 14 ARG H 57 CYS H 58 CYS H 61 HIS H 62
SITE 4 CC5 14 HIS H 102 HEC H1129
SITE 1 CC6 21 ARG D 64 TYR D 66 ILE D 77 LEU G 52
SITE 2 CC6 21 ASN G 53 TYR G 58 ARG H 33 TYR H 35
SITE 3 CC6 21 PRO H 36 GLU H 37 GLN H 38 PRO H 40
SITE 4 CC6 21 HIS H 62 MET H 74 ILE H 75 HIS H 79
SITE 5 CC6 21 ARG H 95 CYS H 98 CYS H 101 HIS H 102
SITE 6 CC6 21 HEC H1128
SITE 1 CC7 7 CYS I 19 PHE I 21 CYS I 22 GLY I 25
SITE 2 CC7 7 CYS I 26 CYS I 54 PRO I 194
SITE 1 CC8 3 CYS I 152 MGD I1803 MGD I1804
SITE 1 CC9 32 ARG I 20 GLN I 123 ASN I 148 CYS I 152
SITE 2 CC9 32 MET I 346 GLN I 350 GLN I 384 VAL I 454
SITE 3 CC9 32 ASN I 455 ASN I 456 ASN I 457 ALA I 460
SITE 4 CC9 32 SER I 482 ASP I 483 THR I 487 ALA I 499
SITE 5 CC9 32 ALA I 500 MET I 501 LYS I 505 ASP I 532
SITE 6 CC9 32 THR I 692 ARG I 694 TRP I 699 HIS I 700
SITE 7 CC9 32 SER I 701 SER I 703 TRP I 768 ASN I 776
SITE 8 CC9 32 PHE I 792 LYS I 793 MO I1802 MGD I1804
SITE 1 DC1 31 LYS I 56 CYS I 152 TRP I 185 GLY I 186
SITE 2 DC1 31 SER I 187 ASN I 188 GLU I 191 MET I 192
SITE 3 DC1 31 SER I 216 THR I 217 HIS I 220 PHE I 232
SITE 4 DC1 31 GLY I 235 ASP I 237 THR I 345 MET I 346
SITE 5 DC1 31 GLY I 347 PHE I 348 GLY I 383 GLN I 384
SITE 6 DC1 31 GLY I 693 ARG I 694 VAL I 695 LEU I 696
SITE 7 DC1 31 HIS I 698 TRP I 699 HIS I 700 LYS I 793
SITE 8 DC1 31 LYS I 794 MO I1802 MGD I1803
SITE 1 DC2 13 ARG J 30 ARG J 33 PRO J 40 VAL J 41
SITE 2 DC2 13 ILE J 42 PRO J 43 HIS J 44 TYR J 49
SITE 3 DC2 13 ARG J 57 CYS J 58 CYS J 61 HIS J 62
SITE 4 DC2 13 HEC J1129
SITE 1 DC3 23 LEU I 52 TYR I 58 ARG J 33 TYR J 35
SITE 2 DC3 23 PRO J 36 GLU J 37 GLN J 38 PRO J 40
SITE 3 DC3 23 LEU J 59 HIS J 62 MET J 74 ILE J 75
SITE 4 DC3 23 SER J 76 HIS J 79 ARG J 95 PHE J 97
SITE 5 DC3 23 CYS J 98 CYS J 101 HIS J 102 HEC J1128
SITE 6 DC3 23 ARG P 64 TYR P 66 ILE P 77
SITE 1 DC4 6 CYS K 19 CYS K 22 CYS K 26 CYS K 54
SITE 2 DC4 6 GLY K 57 PRO K 194
SITE 1 DC5 3 CYS K 152 MGD K1803 MGD K1804
SITE 1 DC6 31 ARG K 20 GLN K 123 ASN K 148 CYS K 152
SITE 2 DC6 31 GLN K 350 GLN K 384 VAL K 454 ASN K 455
SITE 3 DC6 31 ASN K 456 ASN K 457 ALA K 460 SER K 482
SITE 4 DC6 31 ASP K 483 THR K 487 ALA K 499 ALA K 500
SITE 5 DC6 31 MET K 501 LYS K 505 ASP K 532 THR K 692
SITE 6 DC6 31 ARG K 694 TRP K 699 HIS K 700 SER K 701
SITE 7 DC6 31 SER K 703 TRP K 768 ASN K 776 PHE K 792
SITE 8 DC6 31 LYS K 793 MO K1802 MGD K1804
SITE 1 DC7 31 LYS K 56 CYS K 152 TRP K 185 GLY K 186
SITE 2 DC7 31 SER K 187 ASN K 188 GLU K 191 MET K 192
SITE 3 DC7 31 SER K 216 THR K 217 HIS K 220 PHE K 232
SITE 4 DC7 31 GLY K 235 ASP K 237 THR K 345 MET K 346
SITE 5 DC7 31 GLY K 347 PHE K 348 GLY K 383 GLN K 384
SITE 6 DC7 31 GLY K 693 ARG K 694 VAL K 695 LEU K 696
SITE 7 DC7 31 HIS K 698 TRP K 699 HIS K 700 LYS K 793
SITE 8 DC7 31 LYS K 794 MO K1802 MGD K1803
SITE 1 DC8 14 ARG L 30 ARG L 33 PRO L 40 VAL L 41
SITE 2 DC8 14 ILE L 42 PRO L 43 HIS L 44 TYR L 49
SITE 3 DC8 14 ARG L 57 CYS L 58 CYS L 61 HIS L 62
SITE 4 DC8 14 HIS L 102 HEC L1129
SITE 1 DC9 22 LEU K 52 ASN K 53 TYR K 58 ARG L 33
SITE 2 DC9 22 TYR L 35 PRO L 36 GLU L 37 GLN L 38
SITE 3 DC9 22 PRO L 40 HIS L 62 MET L 74 ILE L 75
SITE 4 DC9 22 HIS L 79 ARG L 95 PHE L 97 CYS L 98
SITE 5 DC9 22 CYS L 101 HIS L 102 HEC L1128 ARG N 64
SITE 6 DC9 22 TYR N 66 ILE N 77
SITE 1 EC1 6 CYS M 19 CYS M 22 CYS M 26 CYS M 54
SITE 2 EC1 6 GLY M 57 PRO M 194
SITE 1 EC2 3 CYS M 152 MGD M1803 MGD M1804
SITE 1 EC3 32 ARG M 20 GLN M 123 ASN M 148 CYS M 152
SITE 2 EC3 32 MET M 346 GLN M 350 GLN M 384 VAL M 454
SITE 3 EC3 32 ASN M 455 ASN M 456 ASN M 457 ALA M 460
SITE 4 EC3 32 SER M 482 ASP M 483 THR M 487 ALA M 499
SITE 5 EC3 32 ALA M 500 MET M 501 LYS M 505 ASP M 532
SITE 6 EC3 32 THR M 692 ARG M 694 TRP M 699 HIS M 700
SITE 7 EC3 32 SER M 701 SER M 703 TRP M 768 ASN M 776
SITE 8 EC3 32 PHE M 792 LYS M 793 MO M1802 MGD M1804
SITE 1 EC4 31 LYS M 56 CYS M 152 TRP M 185 GLY M 186
SITE 2 EC4 31 SER M 187 ASN M 188 GLU M 191 MET M 192
SITE 3 EC4 31 SER M 216 THR M 217 HIS M 220 PHE M 232
SITE 4 EC4 31 GLY M 235 ASP M 237 THR M 345 MET M 346
SITE 5 EC4 31 GLY M 347 PHE M 348 GLY M 383 GLN M 384
SITE 6 EC4 31 GLY M 693 ARG M 694 VAL M 695 LEU M 696
SITE 7 EC4 31 HIS M 698 TRP M 699 HIS M 700 LYS M 793
SITE 8 EC4 31 LYS M 794 MO M1802 MGD M1803
SITE 1 EC5 14 ARG N 30 ARG N 33 PRO N 40 VAL N 41
SITE 2 EC5 14 ILE N 42 PRO N 43 HIS N 44 TYR N 49
SITE 3 EC5 14 ARG N 57 CYS N 58 CYS N 61 HIS N 62
SITE 4 EC5 14 HIS N 102 HEC N1129
SITE 1 EC6 20 ARG L 64 ILE L 77 LEU M 52 ASN M 53
SITE 2 EC6 20 TYR M 58 ARG N 33 PRO N 36 GLU N 37
SITE 3 EC6 20 GLN N 38 PRO N 40 HIS N 62 MET N 74
SITE 4 EC6 20 ILE N 75 HIS N 79 ARG N 95 PHE N 97
SITE 5 EC6 20 CYS N 98 CYS N 101 HIS N 102 HEC N1128
SITE 1 EC7 7 CYS O 19 CYS O 22 CYS O 26 ASN O 53
SITE 2 EC7 7 CYS O 54 GLY O 57 PRO O 194
SITE 1 EC8 3 CYS O 152 MGD O1803 MGD O1804
SITE 1 EC9 32 ARG O 20 GLN O 123 ASN O 148 CYS O 152
SITE 2 EC9 32 MET O 346 GLN O 350 GLN O 384 VAL O 454
SITE 3 EC9 32 ASN O 455 ASN O 456 ASN O 457 ALA O 460
SITE 4 EC9 32 SER O 482 ASP O 483 THR O 487 ALA O 499
SITE 5 EC9 32 ALA O 500 MET O 501 LYS O 505 ASP O 532
SITE 6 EC9 32 THR O 692 ARG O 694 TRP O 699 HIS O 700
SITE 7 EC9 32 SER O 701 SER O 703 TRP O 768 ASN O 776
SITE 8 EC9 32 PHE O 792 LYS O 793 MO O1802 MGD O1804
SITE 1 FC1 31 LYS O 56 CYS O 152 TRP O 185 GLY O 186
SITE 2 FC1 31 SER O 187 ASN O 188 GLU O 191 MET O 192
SITE 3 FC1 31 SER O 216 THR O 217 HIS O 220 PHE O 232
SITE 4 FC1 31 GLY O 235 ASP O 237 THR O 345 MET O 346
SITE 5 FC1 31 GLY O 347 PHE O 348 GLY O 383 GLN O 384
SITE 6 FC1 31 GLY O 693 ARG O 694 VAL O 695 LEU O 696
SITE 7 FC1 31 HIS O 698 TRP O 699 HIS O 700 LYS O 793
SITE 8 FC1 31 LYS O 794 MO O1802 MGD O1803
SITE 1 FC2 14 ARG P 30 ARG P 33 VAL P 41 ILE P 42
SITE 2 FC2 14 PRO P 43 HIS P 44 TYR P 49 ARG P 57
SITE 3 FC2 14 CYS P 58 CYS P 61 HIS P 62 CYS P 98
SITE 4 FC2 14 HIS P 102 HEC P1129
SITE 1 FC3 22 ARG J 64 TYR J 66 ILE J 77 LEU O 52
SITE 2 FC3 22 ASN O 53 TYR O 58 ARG P 33 TYR P 35
SITE 3 FC3 22 PRO P 36 GLU P 37 GLN P 38 PRO P 40
SITE 4 FC3 22 HIS P 62 MET P 74 ILE P 75 HIS P 79
SITE 5 FC3 22 ARG P 95 PHE P 97 CYS P 98 CYS P 101
SITE 6 FC3 22 HIS P 102 HEC P1128
CRYST1 123.000 225.200 154.600 90.00 92.10 90.00 P 1 21 1 16
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 0.008130 0.000000 0.000298 0.00000
SCALE2 0.000000 0.004440 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006473 0.00000
MTRIX1 1 -0.900680 0.303780 -0.310630 26.35580 1
MTRIX2 1 0.314900 -0.036180 -0.948440 141.15700 1
MTRIX3 1 -0.299350 -0.952060 -0.063070 152.48648 1
MTRIX1 2 -0.999950 -0.009180 -0.003850 50.95316 1
MTRIX2 2 0.009390 -0.998350 -0.056700 218.29327 1
MTRIX3 2 -0.003320 -0.056730 0.998380 6.28691 1
MTRIX1 3 0.904530 -0.271560 -0.328770 44.40434 1
MTRIX2 3 -0.311480 0.105790 -0.944350 141.14537 1
MTRIX3 3 0.291230 0.956590 0.011100 -72.44903 1
MTRIX1 4 -0.906980 0.274880 0.319110 4.94960 1
MTRIX2 4 0.292250 -0.134870 0.946790 78.56278 1
MTRIX3 4 0.303290 0.951970 0.041990 -73.14667 1
MTRIX1 5 0.813870 -0.580610 -0.022610 68.41241 1
MTRIX2 5 -0.580650 -0.814140 0.005410 210.24144 1
MTRIX3 5 -0.021550 0.008720 -0.999730 77.56707 1
MTRIX1 6 -0.810280 0.585640 0.021530 -19.67288 1
MTRIX2 6 0.586010 0.809340 0.039370 4.42967 1
MTRIX3 6 0.005630 0.044510 -0.998990 73.00153 1
MTRIX1 7 0.913530 -0.290440 0.284790 22.70364 1
MTRIX2 7 -0.276230 0.070970 0.958470 70.02680 1
MTRIX3 7 -0.298590 -0.954260 -0.015390 150.88237 1
(ATOM LINES ARE NOT SHOWN.)
END
