HEADER OXIDOREDUCTASE/PROTEIN BINDING 28-NOV-05 2F5Z
TITLE CRYSTAL STRUCTURE OF HUMAN DIHYDROLIPOAMIDE DEHYDROGENASE (E3)
TITLE 2 COMPLEXED TO THE E3-BINDING DOMAIN OF HUMAN E3-BINDING PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROLIPOYL DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J;
COMPND 4 FRAGMENT: DIHYDROLIPOYL DEHYDROGENASE, RESIDUES 36-509;
COMPND 5 SYNONYM: DIHYDROLIPOAMIDE DEHYDROGENASE, GLYCINE CLEAVAGE SYSTEM L
COMPND 6 PROTEIN;
COMPND 7 EC: 1.8.1.4;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PYRUVATE DEHYDROGENASE PROTEIN X COMPONENT;
COMPND 11 CHAIN: K, L, M, N, O;
COMPND 12 FRAGMENT: E3-BINDING DOMAIN, RESIDUES 173-230;
COMPND 13 SYNONYM: DIHYDROLIPOAMIDE DEHYDROGENASE-BINDING PROTEIN OF PYRUVATE
COMPND 14 DEHYDROGENASE COMPLEX, LIPOYL-CONTAINING PYRUVATE DEHYDROGENASE
COMPND 15 COMPLEX COMPONENT X, E3-BINDING PROTEIN, E3BP, PROX;
COMPND 16 ENGINEERED: YES;
COMPND 17 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DLD, GCSL, LAD, PHE3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: XL-1 BLUE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTRCHISTHE3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: PDHX, PDX1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-LTE3BD
KEYWDS PROTEIN-PROTEIN COMPLEX, OXIDOREDUCTASE-PROTEIN BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.A.BRAUTIGAM,J.L.CHUANG,R.M.WYNN,D.R.TOMCHICK,M.MACHIUS,D.T.CHUANG
REVDAT 5 23-AUG-23 2F5Z 1 REMARK
REVDAT 4 20-OCT-21 2F5Z 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2F5Z 1 VERSN
REVDAT 2 28-MAR-06 2F5Z 1 JRNL
REVDAT 1 17-JAN-06 2F5Z 0
JRNL AUTH C.A.BRAUTIGAM,R.M.WYNN,J.L.CHUANG,M.MACHIUS,D.R.TOMCHICK,
JRNL AUTH 2 D.T.CHUANG
JRNL TITL STRUCTURAL INSIGHT INTO INTERACTIONS BETWEEN
JRNL TITL 2 DIHYDROLIPOAMIDE DEHYDROGENASE (E3) AND E3 BINDING PROTEIN
JRNL TITL 3 OF HUMAN PYRUVATE DEHYDROGENASE COMPLEX.
JRNL REF STRUCTURE V. 14 611 2006
JRNL REFN ISSN 0969-2126
JRNL PMID 16442803
JRNL DOI 10.1016/J.STR.2006.01.001
REMARK 2
REMARK 2 RESOLUTION. 2.18 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.40
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) (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 367068
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) : 0.205
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 4518
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.18
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.32
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 749
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 36495
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 725
REMARK 3 SOLVENT ATOMS : 1776
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.68000
REMARK 3 B22 (A**2) : -0.94000
REMARK 3 B33 (A**2) : 6.62000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.26
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: RESIDUES OF E3BD WITH MISSING ATOMS
REMARK 3 WERE MODELED AS ALANINE DUE TO MISSING DENSITY FOR THE SIDE CHAIN
REMARK 4
REMARK 4 2F5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035492.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979426
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 367237
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 37.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1ZMD WITHOUT NADH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% (W/V) PEG4000, 0.2 M AMMONIUM
REMARK 280 SULFATE, 0.1 M SODIUM ACETATE, 0.03 M SPERMIDINE, 8% (V/V)
REMARK 280 GLYCEROL, PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 85.57650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 112.19600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 93.86400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.19600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 85.57650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 93.86400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 15CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300 AUTHORS INDICATE THAT BIOMOLECULE 1 BEST REPRESENTS THE
REMARK 300 PHYSIOLOGICAL COMPLEX
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, K
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, M
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, O
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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 GLN D 3
REMARK 465 ALA E 1
REMARK 465 ASP E 2
REMARK 465 ALA F 1
REMARK 465 ASP F 2
REMARK 465 GLN F 3
REMARK 465 ALA G 1
REMARK 465 ASP G 2
REMARK 465 ALA H 1
REMARK 465 ASP H 2
REMARK 465 ALA I 1
REMARK 465 ASP I 2
REMARK 465 GLY I 263
REMARK 465 GLY I 264
REMARK 465 ALA J 1
REMARK 465 ASP J 2
REMARK 465 GLY K 120
REMARK 465 GLU K 121
REMARK 465 HIS K 122
REMARK 465 ILE K 123
REMARK 465 PRO K 124
REMARK 465 GLY K 125
REMARK 465 THR K 126
REMARK 465 LEU K 127
REMARK 465 ARG K 128
REMARK 465 PHE K 129
REMARK 465 GLY K 173
REMARK 465 LYS K 174
REMARK 465 ILE K 175
REMARK 465 LEU K 176
REMARK 465 GLU K 177
REMARK 465 HIS K 178
REMARK 465 HIS K 179
REMARK 465 HIS K 180
REMARK 465 HIS K 181
REMARK 465 HIS K 182
REMARK 465 HIS K 183
REMARK 465 GLY L 120
REMARK 465 GLU L 121
REMARK 465 HIS L 122
REMARK 465 ILE L 123
REMARK 465 PRO L 124
REMARK 465 GLY L 125
REMARK 465 THR L 126
REMARK 465 LEU L 127
REMARK 465 ARG L 128
REMARK 465 PHE L 129
REMARK 465 GLY L 173
REMARK 465 LYS L 174
REMARK 465 ILE L 175
REMARK 465 LEU L 176
REMARK 465 GLU L 177
REMARK 465 HIS L 178
REMARK 465 HIS L 179
REMARK 465 HIS L 180
REMARK 465 HIS L 181
REMARK 465 HIS L 182
REMARK 465 HIS L 183
REMARK 465 GLY M 120
REMARK 465 GLU M 121
REMARK 465 HIS M 122
REMARK 465 ILE M 123
REMARK 465 PRO M 124
REMARK 465 GLY M 125
REMARK 465 THR M 126
REMARK 465 LEU M 127
REMARK 465 ARG M 128
REMARK 465 PHE M 129
REMARK 465 GLY M 173
REMARK 465 LYS M 174
REMARK 465 ILE M 175
REMARK 465 LEU M 176
REMARK 465 GLU M 177
REMARK 465 HIS M 178
REMARK 465 HIS M 179
REMARK 465 HIS M 180
REMARK 465 HIS M 181
REMARK 465 HIS M 182
REMARK 465 HIS M 183
REMARK 465 GLY N 120
REMARK 465 GLU N 121
REMARK 465 HIS N 122
REMARK 465 ILE N 123
REMARK 465 PRO N 124
REMARK 465 GLY N 125
REMARK 465 THR N 126
REMARK 465 LEU N 127
REMARK 465 ARG N 128
REMARK 465 PHE N 129
REMARK 465 GLY N 173
REMARK 465 LYS N 174
REMARK 465 ILE N 175
REMARK 465 LEU N 176
REMARK 465 GLU N 177
REMARK 465 HIS N 178
REMARK 465 HIS N 179
REMARK 465 HIS N 180
REMARK 465 HIS N 181
REMARK 465 HIS N 182
REMARK 465 HIS N 183
REMARK 465 GLY O 120
REMARK 465 GLU O 121
REMARK 465 HIS O 122
REMARK 465 ILE O 123
REMARK 465 PRO O 124
REMARK 465 GLY O 125
REMARK 465 THR O 126
REMARK 465 LEU O 127
REMARK 465 ARG O 128
REMARK 465 PHE O 129
REMARK 465 GLY O 173
REMARK 465 LYS O 174
REMARK 465 ILE O 175
REMARK 465 LEU O 176
REMARK 465 GLU O 177
REMARK 465 HIS O 178
REMARK 465 HIS O 179
REMARK 465 HIS O 180
REMARK 465 HIS O 181
REMARK 465 HIS O 182
REMARK 465 HIS O 183
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS K 141 CG CD CE NZ
REMARK 470 GLN K 148 CG CD OE1 NE2
REMARK 470 GLN K 168 CG CD OE1 NE2
REMARK 470 LEU K 169 CB CG CD1 CD2
REMARK 470 LYS K 170 CG CD CE NZ
REMARK 470 GLN K 171 CG CD OE1 NE2
REMARK 470 THR K 172 OG1 CG2
REMARK 470 LYS L 141 CG CD CE NZ
REMARK 470 GLN L 148 CG CD OE1 NE2
REMARK 470 THR L 150 OG1 CG2
REMARK 470 LYS L 165 CG CD CE NZ
REMARK 470 GLN L 168 CG CD OE1 NE2
REMARK 470 LEU L 169 CB CG CD1 CD2
REMARK 470 LYS L 170 CG CD CE NZ
REMARK 470 GLN L 171 CG CD OE1 NE2
REMARK 470 THR L 172 OG1 CG2
REMARK 470 LYS M 141 CG CD CE NZ
REMARK 470 GLN M 148 CG CD OE1 NE2
REMARK 470 THR M 150 OG1 CG2
REMARK 470 LYS M 165 CG CD CE NZ
REMARK 470 GLN M 168 CG CD OE1 NE2
REMARK 470 LEU M 169 CB CG CD1 CD2
REMARK 470 LYS M 170 CG CD CE NZ
REMARK 470 GLN M 171 CG CD OE1 NE2
REMARK 470 THR M 172 OG1 CG2
REMARK 470 LYS N 141 CG CD CE NZ
REMARK 470 GLN N 148 CG CD OE1 NE2
REMARK 470 THR N 150 OG1 CG2
REMARK 470 LYS N 165 CG CD CE NZ
REMARK 470 GLN N 168 CG CD OE1 NE2
REMARK 470 LEU N 169 CB CG CD1 CD2
REMARK 470 LYS N 170 CG CD CE NZ
REMARK 470 GLN N 171 CG CD OE1 NE2
REMARK 470 THR N 172 OG1 CG2
REMARK 470 LYS O 141 CG CD CE NZ
REMARK 470 GLN O 148 CG CD OE1 NE2
REMARK 470 THR O 150 OG1 CG2
REMARK 470 LYS O 165 CG CD CE NZ
REMARK 470 GLN O 168 CG CD OE1 NE2
REMARK 470 LEU O 169 CB CG CD1 CD2
REMARK 470 LYS O 170 CG CD CE NZ
REMARK 470 GLN O 171 CG CD OE1 NE2
REMARK 470 THR O 172 OG1 CG2
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 OE2 GLU N 140 O HOH N 1791 2.08
REMARK 500 NH1 ARG H 307 O HOH H 2731 2.08
REMARK 500 OD2 ASP I 444 O PRO O 133 2.16
REMARK 500 NH1 ARG F 307 O HOH F 2714 2.16
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 CYS A 50 CA - CB - SG ANGL. DEV. = 10.4 DEGREES
REMARK 500 CYS B 50 CA - CB - SG ANGL. DEV. = 8.1 DEGREES
REMARK 500 CYS C 50 CA - CB - SG ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO C 313 C - N - CA ANGL. DEV. = 11.2 DEGREES
REMARK 500 CYS D 50 CA - CB - SG ANGL. DEV. = 10.1 DEGREES
REMARK 500 CYS E 50 CA - CB - SG ANGL. DEV. = 10.5 DEGREES
REMARK 500 PRO E 313 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 CYS F 50 CA - CB - SG ANGL. DEV. = 11.1 DEGREES
REMARK 500 PRO F 313 C - N - CA ANGL. DEV. = 9.8 DEGREES
REMARK 500 CYS G 50 CA - CB - SG ANGL. DEV. = 10.7 DEGREES
REMARK 500 PRO G 313 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 CYS H 50 CA - CB - SG ANGL. DEV. = 12.8 DEGREES
REMARK 500 CYS I 50 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 PRO I 313 C - N - CA ANGL. DEV. = 12.6 DEGREES
REMARK 500 CYS J 50 CA - CB - SG ANGL. DEV. = 10.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 4 173.44 -53.49
REMARK 500 VAL A 48 23.03 -148.22
REMARK 500 SER A 79 -78.91 -56.72
REMARK 500 ALA A 147 42.76 -148.12
REMARK 500 ASP A 163 -83.23 -114.99
REMARK 500 ALA A 186 45.13 -108.04
REMARK 500 THR A 284 17.34 -142.07
REMARK 500 GLU A 291 7.86 -59.63
REMARK 500 PRO A 313 -16.76 -45.61
REMARK 500 ALA A 323 174.46 -56.12
REMARK 500 TYR A 359 30.99 -86.58
REMARK 500 ASP A 413 26.83 49.48
REMARK 500 VAL B 48 21.83 -144.00
REMARK 500 ILE B 121 97.80 -67.63
REMARK 500 ASP B 163 -86.86 -127.20
REMARK 500 ALA B 186 43.01 -100.54
REMARK 500 ALA B 260 151.59 -47.63
REMARK 500 ARG B 299 9.39 -68.03
REMARK 500 THR B 310 -141.55 -101.90
REMARK 500 PRO B 313 -13.18 -49.96
REMARK 500 ALA B 323 171.41 -57.01
REMARK 500 ILE B 349 91.84 175.69
REMARK 500 TYR B 351 2.60 -55.14
REMARK 500 ASP B 413 14.39 57.67
REMARK 500 VAL C 48 20.49 -145.28
REMARK 500 ALA C 132 -43.77 64.10
REMARK 500 ALA C 147 51.20 -146.44
REMARK 500 ASP C 163 -71.56 -117.19
REMARK 500 LYS C 265 99.41 0.76
REMARK 500 CYS C 277 76.22 -157.24
REMARK 500 TYR C 359 31.53 -85.99
REMARK 500 VAL D 48 22.21 -140.10
REMARK 500 SER D 79 -86.12 -48.70
REMARK 500 ASP D 163 -76.17 -117.86
REMARK 500 ALA D 186 45.46 -105.37
REMARK 500 THR D 284 23.85 -140.11
REMARK 500 PRO D 313 -35.09 -32.09
REMARK 500 ALA D 398 37.75 70.75
REMARK 500 VAL E 48 19.90 -140.88
REMARK 500 ALA E 147 51.16 -143.67
REMARK 500 ASP E 163 -82.15 -126.52
REMARK 500 GLU E 291 3.76 -63.64
REMARK 500 PRO E 313 -32.35 -37.94
REMARK 500 VAL E 347 -107.90 -114.68
REMARK 500 HIS E 348 138.25 55.26
REMARK 500 ILE E 349 -48.14 -136.05
REMARK 500 ASP E 350 83.50 76.31
REMARK 500 THR E 360 -169.84 -77.72
REMARK 500 GLU E 376 0.89 -65.86
REMARK 500 VAL F 48 28.82 -143.28
REMARK 500
REMARK 500 THIS ENTRY HAS 147 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2483
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2484
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2485
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 2493
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2486
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2494
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2487
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2495
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2488
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2496
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2489
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 2497
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2498
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2499
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2500
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 2501
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2502
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2503
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2504
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 2505
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 2506
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 2507
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 2508
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 2509
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 2510
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 2511
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 2512
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 2513
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 2514
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 2515
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 2516
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 2517
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 2518
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 2519
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 2520
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD F 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD G 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD H 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 480
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD J 480
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZMC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED
REMARK 900 TO NAD+
REMARK 900 RELATED ID: 1ZMD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN DIHYDROLIPOAMIDE DEHYDROGENASE COMPLEXED
REMARK 900 TO NADH
REMARK 900 RELATED ID: 2F60 RELATED DB: PDB
DBREF 2F5Z A 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z B 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z C 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z D 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z E 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z F 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z G 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z H 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z I 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z J 1 474 UNP P09622 DLDH_HUMAN 36 509
DBREF 2F5Z K 120 177 UNP O00330 ODPX_HUMAN 173 230
DBREF 2F5Z L 120 177 UNP O00330 ODPX_HUMAN 173 230
DBREF 2F5Z M 120 177 UNP O00330 ODPX_HUMAN 173 230
DBREF 2F5Z N 120 177 UNP O00330 ODPX_HUMAN 173 230
DBREF 2F5Z O 120 177 UNP O00330 ODPX_HUMAN 173 230
SEQADV 2F5Z GLY K 120 UNP O00330 LYS 173 ENGINEERED MUTATION
SEQADV 2F5Z LEU K 176 UNP O00330 THR 229 ENGINEERED MUTATION
SEQADV 2F5Z HIS K 178 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS K 179 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS K 180 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS K 181 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS K 182 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS K 183 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z GLY L 120 UNP O00330 LYS 173 ENGINEERED MUTATION
SEQADV 2F5Z LEU L 176 UNP O00330 THR 229 ENGINEERED MUTATION
SEQADV 2F5Z HIS L 178 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS L 179 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS L 180 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS L 181 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS L 182 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS L 183 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z GLY M 120 UNP O00330 LYS 173 ENGINEERED MUTATION
SEQADV 2F5Z LEU M 176 UNP O00330 THR 229 ENGINEERED MUTATION
SEQADV 2F5Z HIS M 178 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS M 179 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS M 180 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS M 181 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS M 182 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS M 183 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z GLY N 120 UNP O00330 LYS 173 ENGINEERED MUTATION
SEQADV 2F5Z LEU N 176 UNP O00330 THR 229 ENGINEERED MUTATION
SEQADV 2F5Z HIS N 178 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS N 179 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS N 180 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS N 181 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS N 182 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS N 183 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z GLY O 120 UNP O00330 LYS 173 ENGINEERED MUTATION
SEQADV 2F5Z LEU O 176 UNP O00330 THR 229 ENGINEERED MUTATION
SEQADV 2F5Z HIS O 178 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS O 179 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS O 180 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS O 181 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS O 182 UNP O00330 EXPRESSION TAG
SEQADV 2F5Z HIS O 183 UNP O00330 EXPRESSION TAG
SEQRES 1 A 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 A 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 A 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 A 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 A 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 A 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 A 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 A 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 A 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 A 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 A 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 A 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 A 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 A 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 A 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 A 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 A 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 A 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 A 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 A 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 A 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 A 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 A 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 A 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 A 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 A 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 A 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 A 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 A 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 A 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 A 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 A 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 A 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 A 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 A 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 A 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 A 474 GLY LYS SER ILE ASN PHE
SEQRES 1 B 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 B 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 B 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 B 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 B 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 B 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 B 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 B 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 B 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 B 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 B 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 B 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 B 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 B 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 B 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 B 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 B 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 B 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 B 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 B 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 B 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 B 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 B 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 B 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 B 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 B 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 B 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 B 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 B 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 B 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 B 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 B 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 B 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 B 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 B 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 B 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 B 474 GLY LYS SER ILE ASN PHE
SEQRES 1 C 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 C 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 C 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 C 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 C 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 C 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 C 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 C 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 C 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 C 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 C 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 C 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 C 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 C 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 C 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 C 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 C 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 C 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 C 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 C 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 C 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 C 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 C 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 C 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 C 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 C 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 C 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 C 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 C 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 C 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 C 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 C 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 C 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 C 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 C 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 C 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 C 474 GLY LYS SER ILE ASN PHE
SEQRES 1 D 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 D 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 D 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 D 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 D 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 D 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 D 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 D 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 D 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 D 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 D 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 D 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 D 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 D 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 D 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 D 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 D 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 D 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 D 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 D 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 D 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 D 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 D 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 D 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 D 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 D 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 D 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 D 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 D 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 D 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 D 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 D 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 D 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 D 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 D 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 D 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 D 474 GLY LYS SER ILE ASN PHE
SEQRES 1 E 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 E 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 E 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 E 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 E 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 E 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 E 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 E 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 E 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 E 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 E 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 E 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 E 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 E 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 E 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 E 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 E 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 E 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 E 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 E 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 E 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 E 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 E 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 E 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 E 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 E 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 E 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 E 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 E 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 E 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 E 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 E 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 E 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 E 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 E 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 E 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 E 474 GLY LYS SER ILE ASN PHE
SEQRES 1 F 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 F 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 F 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 F 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 F 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 F 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 F 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 F 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 F 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 F 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 F 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 F 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 F 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 F 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 F 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 F 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 F 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 F 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 F 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 F 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 F 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 F 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 F 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 F 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 F 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 F 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 F 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 F 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 F 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 F 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 F 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 F 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 F 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 F 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 F 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 F 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 F 474 GLY LYS SER ILE ASN PHE
SEQRES 1 G 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 G 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 G 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 G 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 G 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 G 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 G 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 G 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 G 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 G 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 G 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 G 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 G 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 G 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 G 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 G 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 G 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 G 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 G 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 G 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 G 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 G 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 G 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 G 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 G 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 G 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 G 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 G 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 G 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 G 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 G 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 G 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 G 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 G 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 G 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 G 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 G 474 GLY LYS SER ILE ASN PHE
SEQRES 1 H 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 H 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 H 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 H 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 H 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 H 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 H 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 H 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 H 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 H 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 H 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 H 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 H 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 H 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 H 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 H 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 H 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 H 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 H 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 H 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 H 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 H 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 H 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 H 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 H 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 H 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 H 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 H 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 H 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 H 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 H 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 H 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 H 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 H 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 H 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 H 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 H 474 GLY LYS SER ILE ASN PHE
SEQRES 1 I 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 I 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 I 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 I 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 I 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 I 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 I 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 I 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 I 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 I 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 I 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 I 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 I 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 I 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 I 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 I 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 I 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 I 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 I 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 I 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 I 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 I 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 I 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 I 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 I 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 I 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 I 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 I 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 I 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 I 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 I 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 I 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 I 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 I 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 I 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 I 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 I 474 GLY LYS SER ILE ASN PHE
SEQRES 1 J 474 ALA ASP GLN PRO ILE ASP ALA ASP VAL THR VAL ILE GLY
SEQRES 2 J 474 SER GLY PRO GLY GLY TYR VAL ALA ALA ILE LYS ALA ALA
SEQRES 3 J 474 GLN LEU GLY PHE LYS THR VAL CYS ILE GLU LYS ASN GLU
SEQRES 4 J 474 THR LEU GLY GLY THR CYS LEU ASN VAL GLY CYS ILE PRO
SEQRES 5 J 474 SER LYS ALA LEU LEU ASN ASN SER HIS TYR TYR HIS MET
SEQRES 6 J 474 ALA HIS GLY THR ASP PHE ALA SER ARG GLY ILE GLU MET
SEQRES 7 J 474 SER GLU VAL ARG LEU ASN LEU ASP LYS MET MET GLU GLN
SEQRES 8 J 474 LYS SER THR ALA VAL LYS ALA LEU THR GLY GLY ILE ALA
SEQRES 9 J 474 HIS LEU PHE LYS GLN ASN LYS VAL VAL HIS VAL ASN GLY
SEQRES 10 J 474 TYR GLY LYS ILE THR GLY LYS ASN GLN VAL THR ALA THR
SEQRES 11 J 474 LYS ALA ASP GLY GLY THR GLN VAL ILE ASP THR LYS ASN
SEQRES 12 J 474 ILE LEU ILE ALA THR GLY SER GLU VAL THR PRO PHE PRO
SEQRES 13 J 474 GLY ILE THR ILE ASP GLU ASP THR ILE VAL SER SER THR
SEQRES 14 J 474 GLY ALA LEU SER LEU LYS LYS VAL PRO GLU LYS MET VAL
SEQRES 15 J 474 VAL ILE GLY ALA GLY VAL ILE GLY VAL GLU LEU GLY SER
SEQRES 16 J 474 VAL TRP GLN ARG LEU GLY ALA ASP VAL THR ALA VAL GLU
SEQRES 17 J 474 PHE LEU GLY HIS VAL GLY GLY VAL GLY ILE ASP MET GLU
SEQRES 18 J 474 ILE SER LYS ASN PHE GLN ARG ILE LEU GLN LYS GLN GLY
SEQRES 19 J 474 PHE LYS PHE LYS LEU ASN THR LYS VAL THR GLY ALA THR
SEQRES 20 J 474 LYS LYS SER ASP GLY LYS ILE ASP VAL SER ILE GLU ALA
SEQRES 21 J 474 ALA SER GLY GLY LYS ALA GLU VAL ILE THR CYS ASP VAL
SEQRES 22 J 474 LEU LEU VAL CYS ILE GLY ARG ARG PRO PHE THR LYS ASN
SEQRES 23 J 474 LEU GLY LEU GLU GLU LEU GLY ILE GLU LEU ASP PRO ARG
SEQRES 24 J 474 GLY ARG ILE PRO VAL ASN THR ARG PHE GLN THR LYS ILE
SEQRES 25 J 474 PRO ASN ILE TYR ALA ILE GLY ASP VAL VAL ALA GLY PRO
SEQRES 26 J 474 MET LEU ALA HIS LYS ALA GLU ASP GLU GLY ILE ILE CYS
SEQRES 27 J 474 VAL GLU GLY MET ALA GLY GLY ALA VAL HIS ILE ASP TYR
SEQRES 28 J 474 ASN CYS VAL PRO SER VAL ILE TYR THR HIS PRO GLU VAL
SEQRES 29 J 474 ALA TRP VAL GLY LYS SER GLU GLU GLN LEU LYS GLU GLU
SEQRES 30 J 474 GLY ILE GLU TYR LYS VAL GLY LYS PHE PRO PHE ALA ALA
SEQRES 31 J 474 ASN SER ARG ALA LYS THR ASN ALA ASP THR ASP GLY MET
SEQRES 32 J 474 VAL LYS ILE LEU GLY GLN LYS SER THR ASP ARG VAL LEU
SEQRES 33 J 474 GLY ALA HIS ILE LEU GLY PRO GLY ALA GLY GLU MET VAL
SEQRES 34 J 474 ASN GLU ALA ALA LEU ALA LEU GLU TYR GLY ALA SER CYS
SEQRES 35 J 474 GLU ASP ILE ALA ARG VAL CYS HIS ALA HIS PRO THR LEU
SEQRES 36 J 474 SER GLU ALA PHE ARG GLU ALA ASN LEU ALA ALA SER PHE
SEQRES 37 J 474 GLY LYS SER ILE ASN PHE
SEQRES 1 K 64 GLY GLU HIS ILE PRO GLY THR LEU ARG PHE ARG LEU SER
SEQRES 2 K 64 PRO ALA ALA ARG ASN ILE LEU GLU LYS HIS SER LEU ASP
SEQRES 3 K 64 ALA SER GLN GLY THR ALA THR GLY PRO ARG GLY ILE PHE
SEQRES 4 K 64 THR LYS GLU ASP ALA LEU LYS LEU VAL GLN LEU LYS GLN
SEQRES 5 K 64 THR GLY LYS ILE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 L 64 GLY GLU HIS ILE PRO GLY THR LEU ARG PHE ARG LEU SER
SEQRES 2 L 64 PRO ALA ALA ARG ASN ILE LEU GLU LYS HIS SER LEU ASP
SEQRES 3 L 64 ALA SER GLN GLY THR ALA THR GLY PRO ARG GLY ILE PHE
SEQRES 4 L 64 THR LYS GLU ASP ALA LEU LYS LEU VAL GLN LEU LYS GLN
SEQRES 5 L 64 THR GLY LYS ILE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 M 64 GLY GLU HIS ILE PRO GLY THR LEU ARG PHE ARG LEU SER
SEQRES 2 M 64 PRO ALA ALA ARG ASN ILE LEU GLU LYS HIS SER LEU ASP
SEQRES 3 M 64 ALA SER GLN GLY THR ALA THR GLY PRO ARG GLY ILE PHE
SEQRES 4 M 64 THR LYS GLU ASP ALA LEU LYS LEU VAL GLN LEU LYS GLN
SEQRES 5 M 64 THR GLY LYS ILE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 N 64 GLY GLU HIS ILE PRO GLY THR LEU ARG PHE ARG LEU SER
SEQRES 2 N 64 PRO ALA ALA ARG ASN ILE LEU GLU LYS HIS SER LEU ASP
SEQRES 3 N 64 ALA SER GLN GLY THR ALA THR GLY PRO ARG GLY ILE PHE
SEQRES 4 N 64 THR LYS GLU ASP ALA LEU LYS LEU VAL GLN LEU LYS GLN
SEQRES 5 N 64 THR GLY LYS ILE LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 O 64 GLY GLU HIS ILE PRO GLY THR LEU ARG PHE ARG LEU SER
SEQRES 2 O 64 PRO ALA ALA ARG ASN ILE LEU GLU LYS HIS SER LEU ASP
SEQRES 3 O 64 ALA SER GLN GLY THR ALA THR GLY PRO ARG GLY ILE PHE
SEQRES 4 O 64 THR LYS GLU ASP ALA LEU LYS LEU VAL GLN LEU LYS GLN
SEQRES 5 O 64 THR GLY LYS ILE LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A2482 5
HET SO4 A2483 5
HET SO4 A2484 5
HET SO4 A2485 5
HET FAD A 480 53
HET SO4 B2486 5
HET SO4 B2487 5
HET SO4 B2488 5
HET SO4 B2489 5
HET FAD B 480 53
HET SO4 C2490 5
HET SO4 C2491 5
HET SO4 C2492 5
HET SO4 C2493 5
HET FAD C 480 53
HET SO4 D2494 5
HET SO4 D2495 5
HET SO4 D2496 5
HET SO4 D2497 5
HET FAD D 480 53
HET SO4 E2498 5
HET SO4 E2499 5
HET SO4 E2500 5
HET SO4 E2501 5
HET FAD E 480 53
HET SO4 F2502 5
HET SO4 F2503 5
HET SO4 F2504 5
HET SO4 F2505 5
HET FAD F 480 53
HET SO4 G2506 5
HET SO4 G2507 5
HET SO4 G2508 5
HET SO4 G2509 5
HET FAD G 480 53
HET SO4 H2510 5
HET SO4 H2511 5
HET SO4 H2512 5
HET SO4 H2513 5
HET FAD H 480 53
HET SO4 I2514 5
HET SO4 I2515 5
HET SO4 I2516 5
HET FAD I 480 53
HET SO4 J2517 5
HET SO4 J2518 5
HET SO4 J2519 5
HET SO4 J2520 5
HET FAD J 480 53
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 16 SO4 39(O4 S 2-)
FORMUL 20 FAD 10(C27 H33 N9 O15 P2)
FORMUL 65 HOH *1776(H2 O)
HELIX 1 1 GLY A 15 LEU A 28 1 14
HELIX 2 2 GLY A 42 GLY A 49 1 8
HELIX 3 3 GLY A 49 GLY A 68 1 20
HELIX 4 4 THR A 69 ARG A 74 1 6
HELIX 5 5 ASN A 84 ASN A 110 1 27
HELIX 6 6 SER A 167 LEU A 172 1 6
HELIX 7 7 GLY A 187 LEU A 200 1 14
HELIX 8 8 ASP A 219 GLY A 234 1 16
HELIX 9 9 LEU A 289 GLY A 293 5 5
HELIX 10 10 GLY A 319 VAL A 322 5 4
HELIX 11 11 LEU A 327 ALA A 343 1 17
HELIX 12 12 ASP A 350 VAL A 354 5 5
HELIX 13 13 SER A 370 GLU A 377 1 8
HELIX 14 14 ASN A 391 ALA A 398 1 8
HELIX 15 15 GLY A 424 TYR A 438 1 15
HELIX 16 16 SER A 441 VAL A 448 1 8
HELIX 17 17 LEU A 455 PHE A 468 1 14
HELIX 18 18 GLY B 15 GLN B 27 1 13
HELIX 19 19 GLY B 42 VAL B 48 1 7
HELIX 20 20 GLY B 49 GLY B 68 1 20
HELIX 21 21 THR B 69 ARG B 74 1 6
HELIX 22 22 ASN B 84 ASN B 110 1 27
HELIX 23 23 SER B 167 LEU B 172 1 6
HELIX 24 24 GLY B 187 LEU B 200 1 14
HELIX 25 25 ASP B 219 GLY B 234 1 16
HELIX 26 26 GLY B 288 GLY B 293 1 6
HELIX 27 27 GLY B 319 VAL B 322 5 4
HELIX 28 28 LEU B 327 ALA B 343 1 17
HELIX 29 29 SER B 370 GLY B 378 1 9
HELIX 30 30 ASN B 391 ASN B 397 1 7
HELIX 31 31 GLY B 424 GLU B 437 1 14
HELIX 32 32 SER B 441 ARG B 447 1 7
HELIX 33 33 LEU B 455 GLY B 469 1 15
HELIX 34 34 GLY C 15 LEU C 28 1 14
HELIX 35 35 GLY C 42 GLY C 49 1 8
HELIX 36 36 GLY C 49 GLY C 68 1 20
HELIX 37 37 PHE C 71 ARG C 74 5 4
HELIX 38 38 ASN C 84 ASN C 110 1 27
HELIX 39 39 SER C 167 LEU C 172 1 6
HELIX 40 40 GLY C 187 LEU C 200 1 14
HELIX 41 41 ASP C 219 GLY C 234 1 16
HELIX 42 42 GLY C 288 GLY C 293 1 6
HELIX 43 43 GLY C 319 VAL C 322 5 4
HELIX 44 44 LEU C 327 ALA C 343 1 17
HELIX 45 45 ASP C 350 VAL C 354 5 5
HELIX 46 46 SER C 370 GLY C 378 1 9
HELIX 47 47 ASN C 391 ASN C 397 1 7
HELIX 48 48 GLY C 424 TYR C 438 1 15
HELIX 49 49 SER C 441 ARG C 447 1 7
HELIX 50 50 LEU C 455 GLY C 469 1 15
HELIX 51 51 GLY D 15 LEU D 28 1 14
HELIX 52 52 GLY D 42 GLY D 49 1 8
HELIX 53 53 GLY D 49 GLY D 68 1 20
HELIX 54 54 THR D 69 ARG D 74 1 6
HELIX 55 55 ASN D 84 ASN D 110 1 27
HELIX 56 56 SER D 167 LEU D 172 1 6
HELIX 57 57 GLY D 187 LEU D 200 1 14
HELIX 58 58 ASP D 219 GLN D 233 1 15
HELIX 59 59 GLY D 288 GLY D 293 1 6
HELIX 60 60 GLY D 319 VAL D 322 5 4
HELIX 61 61 LEU D 327 ALA D 343 1 17
HELIX 62 62 ASP D 350 VAL D 354 5 5
HELIX 63 63 SER D 370 GLY D 378 1 9
HELIX 64 64 ASN D 391 ALA D 398 1 8
HELIX 65 65 GLY D 424 TYR D 438 1 15
HELIX 66 66 SER D 441 VAL D 448 1 8
HELIX 67 67 LEU D 455 GLY D 469 1 15
HELIX 68 68 GLY E 15 LEU E 28 1 14
HELIX 69 69 GLY E 42 GLY E 49 1 8
HELIX 70 70 GLY E 49 GLY E 68 1 20
HELIX 71 71 THR E 69 ARG E 74 1 6
HELIX 72 72 ASN E 84 ASN E 110 1 27
HELIX 73 73 SER E 167 LEU E 172 1 6
HELIX 74 74 GLY E 187 LEU E 200 1 14
HELIX 75 75 ASP E 219 GLY E 234 1 16
HELIX 76 76 LEU E 289 GLY E 293 5 5
HELIX 77 77 GLY E 319 VAL E 322 5 4
HELIX 78 78 LEU E 327 ALA E 343 1 17
HELIX 79 79 ASP E 350 VAL E 354 5 5
HELIX 80 80 SER E 370 GLU E 376 1 7
HELIX 81 81 ASN E 391 ASN E 397 1 7
HELIX 82 82 GLY E 424 TYR E 438 1 15
HELIX 83 83 SER E 441 ARG E 447 1 7
HELIX 84 84 LEU E 455 GLY E 469 1 15
HELIX 85 85 GLY F 15 LEU F 28 1 14
HELIX 86 86 GLY F 42 GLY F 49 1 8
HELIX 87 87 GLY F 49 GLY F 68 1 20
HELIX 88 88 PHE F 71 ARG F 74 5 4
HELIX 89 89 ASN F 84 ASN F 110 1 27
HELIX 90 90 SER F 167 LEU F 172 1 6
HELIX 91 91 GLY F 187 LEU F 200 1 14
HELIX 92 92 ASP F 219 GLY F 234 1 16
HELIX 93 93 GLY F 288 GLY F 293 1 6
HELIX 94 94 GLY F 319 VAL F 322 5 4
HELIX 95 95 LEU F 327 ALA F 343 1 17
HELIX 96 96 ASP F 350 VAL F 354 5 5
HELIX 97 97 SER F 370 GLY F 378 1 9
HELIX 98 98 ASN F 391 ALA F 398 1 8
HELIX 99 99 GLY F 424 TYR F 438 1 15
HELIX 100 100 SER F 441 ARG F 447 1 7
HELIX 101 101 LEU F 455 GLY F 469 1 15
HELIX 102 102 GLY G 15 LEU G 28 1 14
HELIX 103 103 GLY G 42 GLY G 49 1 8
HELIX 104 104 GLY G 49 GLY G 68 1 20
HELIX 105 105 THR G 69 ARG G 74 1 6
HELIX 106 106 ASN G 84 LYS G 111 1 28
HELIX 107 107 SER G 167 LEU G 172 1 6
HELIX 108 108 GLY G 187 LEU G 200 1 14
HELIX 109 109 ASP G 219 GLY G 234 1 16
HELIX 110 110 GLY G 288 GLY G 293 1 6
HELIX 111 111 GLY G 319 VAL G 322 5 4
HELIX 112 112 LEU G 327 ALA G 343 1 17
HELIX 113 113 ASP G 350 VAL G 354 5 5
HELIX 114 114 SER G 370 GLU G 377 1 8
HELIX 115 115 ASN G 391 ASN G 397 1 7
HELIX 116 116 GLY G 424 TYR G 438 1 15
HELIX 117 117 SER G 441 VAL G 448 1 8
HELIX 118 118 LEU G 455 GLY G 469 1 15
HELIX 119 119 GLY H 15 LEU H 28 1 14
HELIX 120 120 GLY H 42 GLY H 49 1 8
HELIX 121 121 GLY H 49 GLY H 68 1 20
HELIX 122 122 PHE H 71 ARG H 74 5 4
HELIX 123 123 ASN H 84 LYS H 111 1 28
HELIX 124 124 SER H 167 LEU H 172 1 6
HELIX 125 125 GLY H 187 LEU H 200 1 14
HELIX 126 126 ASP H 219 GLY H 234 1 16
HELIX 127 127 GLY H 288 GLY H 293 1 6
HELIX 128 128 GLY H 319 VAL H 322 5 4
HELIX 129 129 LEU H 327 ALA H 343 1 17
HELIX 130 130 ASP H 350 VAL H 354 5 5
HELIX 131 131 SER H 370 GLU H 377 1 8
HELIX 132 132 ASN H 391 ALA H 398 1 8
HELIX 133 133 GLY H 424 TYR H 438 1 15
HELIX 134 134 SER H 441 VAL H 448 1 8
HELIX 135 135 LEU H 455 GLY H 469 1 15
HELIX 136 136 GLY I 15 LEU I 28 1 14
HELIX 137 137 GLY I 42 GLY I 49 1 8
HELIX 138 138 GLY I 49 GLY I 68 1 20
HELIX 139 139 THR I 69 ARG I 74 1 6
HELIX 140 140 ASN I 84 ASN I 110 1 27
HELIX 141 141 SER I 167 LEU I 172 1 6
HELIX 142 142 GLY I 187 GLY I 201 1 15
HELIX 143 143 ASP I 219 GLN I 233 1 15
HELIX 144 144 GLY I 288 GLY I 293 1 6
HELIX 145 145 GLY I 319 VAL I 322 5 4
HELIX 146 146 LEU I 327 ALA I 343 1 17
HELIX 147 147 ASP I 350 VAL I 354 5 5
HELIX 148 148 SER I 370 GLY I 378 1 9
HELIX 149 149 ASN I 391 ASN I 397 1 7
HELIX 150 150 GLY I 424 TYR I 438 1 15
HELIX 151 151 SER I 441 ARG I 447 1 7
HELIX 152 152 LEU I 455 GLY I 469 1 15
HELIX 153 153 GLY J 15 LEU J 28 1 14
HELIX 154 154 GLY J 42 GLY J 49 1 8
HELIX 155 155 GLY J 49 GLY J 68 1 20
HELIX 156 156 GLY J 68 ARG J 74 1 7
HELIX 157 157 ASN J 84 ASN J 110 1 27
HELIX 158 158 SER J 167 LEU J 172 1 6
HELIX 159 159 GLY J 187 GLY J 201 1 15
HELIX 160 160 ASP J 219 GLY J 234 1 16
HELIX 161 161 GLY J 288 GLY J 293 1 6
HELIX 162 162 GLY J 319 VAL J 322 5 4
HELIX 163 163 LEU J 327 ALA J 343 1 17
HELIX 164 164 ASP J 350 VAL J 354 5 5
HELIX 165 165 SER J 370 GLY J 378 1 9
HELIX 166 166 ASN J 391 ALA J 398 1 8
HELIX 167 167 GLY J 424 TYR J 438 1 15
HELIX 168 168 SER J 441 VAL J 448 1 8
HELIX 169 169 LEU J 455 GLY J 469 1 15
HELIX 170 170 ALA K 134 HIS K 142 1 9
HELIX 171 171 ASP K 145 GLY K 149 5 5
HELIX 172 172 GLY K 153 ILE K 157 5 5
HELIX 173 173 THR K 159 THR K 172 1 14
HELIX 174 174 ALA L 134 LYS L 141 1 8
HELIX 175 175 ASP L 145 GLY L 149 5 5
HELIX 176 176 GLU L 161 LYS L 170 1 10
HELIX 177 177 SER M 132 HIS M 142 1 11
HELIX 178 178 GLY M 153 ILE M 157 5 5
HELIX 179 179 PHE M 158 THR M 172 1 15
HELIX 180 180 SER N 132 HIS N 142 1 11
HELIX 181 181 GLY N 153 ILE N 157 5 5
HELIX 182 182 PHE N 158 LEU N 166 1 9
HELIX 183 183 ALA O 134 GLU O 140 1 7
HELIX 184 184 ASP O 145 GLY O 149 5 5
HELIX 185 185 THR O 159 GLN O 168 1 10
SHEET 1 A 6 VAL A 113 ASN A 116 0
SHEET 2 A 6 THR A 32 GLU A 36 1 N CYS A 34 O VAL A 113
SHEET 3 A 6 ILE A 5 ILE A 12 1 N VAL A 11 O ILE A 35
SHEET 4 A 6 THR A 136 ILE A 146 1 O LEU A 145 N THR A 10
SHEET 5 A 6 GLN A 126 THR A 130 -1 N ALA A 129 O GLN A 137
SHEET 6 A 6 ILE A 121 GLY A 123 -1 N GLY A 123 O GLN A 126
SHEET 1 B 5 VAL A 113 ASN A 116 0
SHEET 2 B 5 THR A 32 GLU A 36 1 N CYS A 34 O VAL A 113
SHEET 3 B 5 ILE A 5 ILE A 12 1 N VAL A 11 O ILE A 35
SHEET 4 B 5 THR A 136 ILE A 146 1 O LEU A 145 N THR A 10
SHEET 5 B 5 ILE A 315 ALA A 317 1 O TYR A 316 N ILE A 144
SHEET 1 C 2 ILE A 76 MET A 78 0
SHEET 2 C 2 VAL B 81 LEU B 83 -1 O ARG B 82 N GLU A 77
SHEET 1 D 2 VAL A 81 LEU A 83 0
SHEET 2 D 2 ILE B 76 MET B 78 -1 O GLU B 77 N ARG A 82
SHEET 1 E 2 SER A 150 VAL A 152 0
SHEET 2 E 2 ARG A 280 PRO A 282 -1 O ARG A 281 N GLU A 151
SHEET 1 F 5 ILE A 165 VAL A 166 0
SHEET 2 F 5 VAL A 273 VAL A 276 1 O VAL A 276 N VAL A 166
SHEET 3 F 5 LYS A 180 ILE A 184 1 N ILE A 184 O LEU A 275
SHEET 4 F 5 ASP A 203 GLU A 208 1 O VAL A 207 N VAL A 183
SHEET 5 F 5 LYS A 236 LEU A 239 1 O LYS A 238 N GLU A 208
SHEET 1 G 3 THR A 241 LYS A 248 0
SHEET 2 G 3 ILE A 254 ALA A 260 -1 O SER A 257 N THR A 244
SHEET 3 G 3 GLU A 267 CYS A 271 -1 O CYS A 271 N ILE A 254
SHEET 1 H 5 SER A 356 ILE A 358 0
SHEET 2 H 5 GLU A 363 GLY A 368 -1 O VAL A 364 N ILE A 358
SHEET 3 H 5 VAL A 415 GLY A 422 -1 O ILE A 420 N ALA A 365
SHEET 4 H 5 MET A 403 GLN A 409 -1 N LEU A 407 O LEU A 416
SHEET 5 H 5 TYR A 381 PRO A 387 -1 N GLY A 384 O ILE A 406
SHEET 1 I 6 VAL B 113 ASN B 116 0
SHEET 2 I 6 THR B 32 GLU B 36 1 N CYS B 34 O VAL B 113
SHEET 3 I 6 ILE B 5 ILE B 12 1 N VAL B 11 O VAL B 33
SHEET 4 I 6 THR B 136 ILE B 146 1 O LEU B 145 N THR B 10
SHEET 5 I 6 GLN B 126 THR B 130 -1 N VAL B 127 O ILE B 139
SHEET 6 I 6 TYR B 118 LYS B 120 -1 N LYS B 120 O THR B 128
SHEET 1 J 5 VAL B 113 ASN B 116 0
SHEET 2 J 5 THR B 32 GLU B 36 1 N CYS B 34 O VAL B 113
SHEET 3 J 5 ILE B 5 ILE B 12 1 N VAL B 11 O VAL B 33
SHEET 4 J 5 THR B 136 ILE B 146 1 O LEU B 145 N THR B 10
SHEET 5 J 5 ILE B 315 ALA B 317 1 O TYR B 316 N ILE B 146
SHEET 1 K 2 SER B 150 VAL B 152 0
SHEET 2 K 2 ARG B 280 PRO B 282 -1 O ARG B 281 N GLU B 151
SHEET 1 L 5 ILE B 165 VAL B 166 0
SHEET 2 L 5 VAL B 273 VAL B 276 1 O VAL B 276 N VAL B 166
SHEET 3 L 5 LYS B 180 ILE B 184 1 N ILE B 184 O LEU B 275
SHEET 4 L 5 ASP B 203 GLU B 208 1 O VAL B 207 N VAL B 183
SHEET 5 L 5 LYS B 236 LEU B 239 1 O LYS B 238 N GLU B 208
SHEET 1 M 3 THR B 241 LYS B 248 0
SHEET 2 M 3 ILE B 254 ALA B 260 -1 O SER B 257 N GLY B 245
SHEET 3 M 3 GLU B 267 CYS B 271 -1 O ILE B 269 N VAL B 256
SHEET 1 N 5 SER B 356 ILE B 358 0
SHEET 2 N 5 GLU B 363 GLY B 368 -1 O VAL B 364 N ILE B 358
SHEET 3 N 5 VAL B 415 GLY B 422 -1 O ILE B 420 N ALA B 365
SHEET 4 N 5 MET B 403 GLN B 409 -1 N LEU B 407 O LEU B 416
SHEET 5 N 5 TYR B 381 PRO B 387 -1 N GLY B 384 O ILE B 406
SHEET 1 O 6 VAL C 113 ASN C 116 0
SHEET 2 O 6 THR C 32 GLU C 36 1 N CYS C 34 O VAL C 113
SHEET 3 O 6 ILE C 5 ILE C 12 1 N VAL C 11 O VAL C 33
SHEET 4 O 6 THR C 136 ILE C 146 1 O LEU C 145 N ILE C 12
SHEET 5 O 6 GLN C 126 THR C 130 -1 N ALA C 129 O GLN C 137
SHEET 6 O 6 TYR C 118 GLY C 123 -1 N LYS C 120 O THR C 128
SHEET 1 P 5 VAL C 113 ASN C 116 0
SHEET 2 P 5 THR C 32 GLU C 36 1 N CYS C 34 O VAL C 113
SHEET 3 P 5 ILE C 5 ILE C 12 1 N VAL C 11 O VAL C 33
SHEET 4 P 5 THR C 136 ILE C 146 1 O LEU C 145 N ILE C 12
SHEET 5 P 5 ILE C 315 ALA C 317 1 O TYR C 316 N ILE C 144
SHEET 1 Q 2 ILE C 76 MET C 78 0
SHEET 2 Q 2 VAL D 81 LEU D 83 -1 O ARG D 82 N GLU C 77
SHEET 1 R 2 VAL C 81 LEU C 83 0
SHEET 2 R 2 ILE D 76 MET D 78 -1 O GLU D 77 N ARG C 82
SHEET 1 S 2 SER C 150 VAL C 152 0
SHEET 2 S 2 ARG C 280 PRO C 282 -1 O ARG C 281 N GLU C 151
SHEET 1 T 5 ILE C 165 VAL C 166 0
SHEET 2 T 5 VAL C 273 VAL C 276 1 O VAL C 276 N VAL C 166
SHEET 3 T 5 LYS C 180 ILE C 184 1 N VAL C 182 O LEU C 275
SHEET 4 T 5 ASP C 203 VAL C 207 1 O VAL C 207 N VAL C 183
SHEET 5 T 5 LYS C 236 LYS C 238 1 O LYS C 236 N ALA C 206
SHEET 1 U 3 THR C 241 LYS C 248 0
SHEET 2 U 3 ILE C 254 ALA C 260 -1 O SER C 257 N THR C 244
SHEET 3 U 3 GLU C 267 CYS C 271 -1 O ILE C 269 N VAL C 256
SHEET 1 V 5 SER C 356 ILE C 358 0
SHEET 2 V 5 GLU C 363 GLY C 368 -1 O VAL C 364 N ILE C 358
SHEET 3 V 5 VAL C 415 GLY C 422 -1 O ILE C 420 N ALA C 365
SHEET 4 V 5 MET C 403 GLN C 409 -1 N LEU C 407 O LEU C 416
SHEET 5 V 5 TYR C 381 PRO C 387 -1 N GLY C 384 O ILE C 406
SHEET 1 W 6 VAL D 113 ASN D 116 0
SHEET 2 W 6 THR D 32 GLU D 36 1 N THR D 32 O VAL D 113
SHEET 3 W 6 ILE D 5 ILE D 12 1 N VAL D 11 O VAL D 33
SHEET 4 W 6 THR D 136 ILE D 146 1 O LEU D 145 N THR D 10
SHEET 5 W 6 GLN D 126 THR D 130 -1 N ALA D 129 O GLN D 137
SHEET 6 W 6 TYR D 118 GLY D 123 -1 N LYS D 120 O THR D 128
SHEET 1 X 5 VAL D 113 ASN D 116 0
SHEET 2 X 5 THR D 32 GLU D 36 1 N THR D 32 O VAL D 113
SHEET 3 X 5 ILE D 5 ILE D 12 1 N VAL D 11 O VAL D 33
SHEET 4 X 5 THR D 136 ILE D 146 1 O LEU D 145 N THR D 10
SHEET 5 X 5 ILE D 315 ALA D 317 1 O TYR D 316 N ILE D 146
SHEET 1 Y 2 SER D 150 VAL D 152 0
SHEET 2 Y 2 ARG D 280 PRO D 282 -1 O ARG D 281 N GLU D 151
SHEET 1 Z 5 ILE D 165 VAL D 166 0
SHEET 2 Z 5 VAL D 273 VAL D 276 1 O VAL D 276 N VAL D 166
SHEET 3 Z 5 LYS D 180 ILE D 184 1 N ILE D 184 O LEU D 275
SHEET 4 Z 5 ASP D 203 VAL D 207 1 O VAL D 207 N VAL D 183
SHEET 5 Z 5 LYS D 236 LYS D 238 1 O LYS D 238 N ALA D 206
SHEET 1 AA 3 THR D 241 LYS D 248 0
SHEET 2 AA 3 ILE D 254 ALA D 260 -1 O SER D 257 N THR D 244
SHEET 3 AA 3 GLU D 267 CYS D 271 -1 O ILE D 269 N VAL D 256
SHEET 1 AB 5 SER D 356 ILE D 358 0
SHEET 2 AB 5 GLU D 363 GLY D 368 -1 O VAL D 364 N ILE D 358
SHEET 3 AB 5 VAL D 415 GLY D 422 -1 O ILE D 420 N ALA D 365
SHEET 4 AB 5 MET D 403 GLN D 409 -1 N LEU D 407 O LEU D 416
SHEET 5 AB 5 TYR D 381 PRO D 387 -1 N LYS D 382 O GLY D 408
SHEET 1 AC 6 VAL E 113 ASN E 116 0
SHEET 2 AC 6 THR E 32 GLU E 36 1 N CYS E 34 O VAL E 113
SHEET 3 AC 6 ILE E 5 ILE E 12 1 N VAL E 11 O VAL E 33
SHEET 4 AC 6 THR E 136 ILE E 146 1 O LEU E 145 N THR E 10
SHEET 5 AC 6 GLN E 126 THR E 130 -1 N ALA E 129 O GLN E 137
SHEET 6 AC 6 TYR E 118 GLY E 123 -1 N LYS E 120 O THR E 128
SHEET 1 AD 5 VAL E 113 ASN E 116 0
SHEET 2 AD 5 THR E 32 GLU E 36 1 N CYS E 34 O VAL E 113
SHEET 3 AD 5 ILE E 5 ILE E 12 1 N VAL E 11 O VAL E 33
SHEET 4 AD 5 THR E 136 ILE E 146 1 O LEU E 145 N THR E 10
SHEET 5 AD 5 ILE E 315 ALA E 317 1 O TYR E 316 N ILE E 144
SHEET 1 AE 2 ILE E 76 MET E 78 0
SHEET 2 AE 2 VAL F 81 LEU F 83 -1 O ARG F 82 N GLU E 77
SHEET 1 AF 2 VAL E 81 LEU E 83 0
SHEET 2 AF 2 ILE F 76 MET F 78 -1 O GLU F 77 N ARG E 82
SHEET 1 AG 2 SER E 150 VAL E 152 0
SHEET 2 AG 2 ARG E 280 PRO E 282 -1 O ARG E 281 N GLU E 151
SHEET 1 AH 5 ILE E 165 VAL E 166 0
SHEET 2 AH 5 VAL E 273 VAL E 276 1 O VAL E 276 N VAL E 166
SHEET 3 AH 5 LYS E 180 ILE E 184 1 N ILE E 184 O LEU E 275
SHEET 4 AH 5 ASP E 203 GLU E 208 1 O VAL E 207 N VAL E 183
SHEET 5 AH 5 LYS E 236 LEU E 239 1 O LYS E 238 N ALA E 206
SHEET 1 AI 3 THR E 241 LYS E 248 0
SHEET 2 AI 3 ILE E 254 ALA E 260 -1 O SER E 257 N GLY E 245
SHEET 3 AI 3 GLU E 267 CYS E 271 -1 O GLU E 267 N ILE E 258
SHEET 1 AJ 5 SER E 356 ILE E 358 0
SHEET 2 AJ 5 GLU E 363 GLY E 368 -1 O VAL E 364 N ILE E 358
SHEET 3 AJ 5 VAL E 415 GLY E 422 -1 O ILE E 420 N ALA E 365
SHEET 4 AJ 5 MET E 403 GLN E 409 -1 N LEU E 407 O LEU E 416
SHEET 5 AJ 5 TYR E 381 PRO E 387 -1 N GLY E 384 O ILE E 406
SHEET 1 AK 6 VAL F 113 ASN F 116 0
SHEET 2 AK 6 THR F 32 GLU F 36 1 N THR F 32 O VAL F 113
SHEET 3 AK 6 ILE F 5 ILE F 12 1 N VAL F 11 O VAL F 33
SHEET 4 AK 6 THR F 136 ILE F 146 1 O ASP F 140 N ALA F 7
SHEET 5 AK 6 GLN F 126 THR F 130 -1 N ALA F 129 O GLN F 137
SHEET 6 AK 6 TYR F 118 GLY F 123 -1 N GLY F 123 O GLN F 126
SHEET 1 AL 5 VAL F 113 ASN F 116 0
SHEET 2 AL 5 THR F 32 GLU F 36 1 N THR F 32 O VAL F 113
SHEET 3 AL 5 ILE F 5 ILE F 12 1 N VAL F 11 O VAL F 33
SHEET 4 AL 5 THR F 136 ILE F 146 1 O ASP F 140 N ALA F 7
SHEET 5 AL 5 ILE F 315 ALA F 317 1 O TYR F 316 N ILE F 146
SHEET 1 AM 2 SER F 150 VAL F 152 0
SHEET 2 AM 2 ARG F 280 PRO F 282 -1 O ARG F 281 N GLU F 151
SHEET 1 AN 5 ILE F 165 VAL F 166 0
SHEET 2 AN 5 VAL F 273 VAL F 276 1 O VAL F 276 N VAL F 166
SHEET 3 AN 5 LYS F 180 ILE F 184 1 N ILE F 184 O LEU F 275
SHEET 4 AN 5 ASP F 203 VAL F 207 1 O VAL F 207 N VAL F 183
SHEET 5 AN 5 LYS F 236 LYS F 238 1 O LYS F 238 N ALA F 206
SHEET 1 AO 3 THR F 241 LYS F 248 0
SHEET 2 AO 3 ILE F 254 ALA F 260 -1 O GLU F 259 N LYS F 242
SHEET 3 AO 3 GLU F 267 CYS F 271 -1 O ILE F 269 N VAL F 256
SHEET 1 AP 5 SER F 356 ILE F 358 0
SHEET 2 AP 5 GLU F 363 GLY F 368 -1 O VAL F 364 N ILE F 358
SHEET 3 AP 5 VAL F 415 GLY F 422 -1 O ILE F 420 N ALA F 365
SHEET 4 AP 5 MET F 403 GLN F 409 -1 N LYS F 405 O HIS F 419
SHEET 5 AP 5 TYR F 381 PRO F 387 -1 N LYS F 382 O GLY F 408
SHEET 1 AQ 6 VAL G 113 ASN G 116 0
SHEET 2 AQ 6 THR G 32 GLU G 36 1 N THR G 32 O VAL G 113
SHEET 3 AQ 6 ILE G 5 ILE G 12 1 N VAL G 11 O VAL G 33
SHEET 4 AQ 6 THR G 136 ILE G 146 1 O LEU G 145 N ILE G 12
SHEET 5 AQ 6 GLN G 126 THR G 130 -1 N ALA G 129 O GLN G 137
SHEET 6 AQ 6 TYR G 118 GLY G 123 -1 N LYS G 120 O THR G 128
SHEET 1 AR 5 VAL G 113 ASN G 116 0
SHEET 2 AR 5 THR G 32 GLU G 36 1 N THR G 32 O VAL G 113
SHEET 3 AR 5 ILE G 5 ILE G 12 1 N VAL G 11 O VAL G 33
SHEET 4 AR 5 THR G 136 ILE G 146 1 O LEU G 145 N ILE G 12
SHEET 5 AR 5 ILE G 315 ALA G 317 1 O TYR G 316 N ILE G 144
SHEET 1 AS 2 ILE G 76 MET G 78 0
SHEET 2 AS 2 VAL H 81 LEU H 83 -1 O ARG H 82 N GLU G 77
SHEET 1 AT 2 VAL G 81 LEU G 83 0
SHEET 2 AT 2 ILE H 76 MET H 78 -1 O GLU H 77 N ARG G 82
SHEET 1 AU 2 SER G 150 VAL G 152 0
SHEET 2 AU 2 ARG G 280 PRO G 282 -1 O ARG G 281 N GLU G 151
SHEET 1 AV 5 ILE G 165 VAL G 166 0
SHEET 2 AV 5 VAL G 273 VAL G 276 1 O VAL G 276 N VAL G 166
SHEET 3 AV 5 LYS G 180 ILE G 184 1 N ILE G 184 O LEU G 275
SHEET 4 AV 5 ASP G 203 VAL G 207 1 O VAL G 207 N VAL G 183
SHEET 5 AV 5 LYS G 236 LYS G 238 1 O LYS G 236 N ALA G 206
SHEET 1 AW 3 THR G 241 LYS G 248 0
SHEET 2 AW 3 ILE G 254 ALA G 260 -1 O SER G 257 N THR G 244
SHEET 3 AW 3 GLU G 267 CYS G 271 -1 O GLU G 267 N ILE G 258
SHEET 1 AX 5 SER G 356 ILE G 358 0
SHEET 2 AX 5 GLU G 363 GLY G 368 -1 O VAL G 364 N ILE G 358
SHEET 3 AX 5 VAL G 415 GLY G 422 -1 O ILE G 420 N ALA G 365
SHEET 4 AX 5 MET G 403 GLN G 409 -1 N LEU G 407 O LEU G 416
SHEET 5 AX 5 TYR G 381 PRO G 387 -1 N GLY G 384 O ILE G 406
SHEET 1 AY 6 VAL H 113 ASN H 116 0
SHEET 2 AY 6 THR H 32 GLU H 36 1 N CYS H 34 O VAL H 115
SHEET 3 AY 6 ILE H 5 ILE H 12 1 N VAL H 11 O VAL H 33
SHEET 4 AY 6 THR H 136 ILE H 146 1 O LEU H 145 N ILE H 12
SHEET 5 AY 6 GLN H 126 THR H 130 -1 N ALA H 129 O GLN H 137
SHEET 6 AY 6 TYR H 118 GLY H 123 -1 N LYS H 120 O THR H 128
SHEET 1 AZ 5 VAL H 113 ASN H 116 0
SHEET 2 AZ 5 THR H 32 GLU H 36 1 N CYS H 34 O VAL H 115
SHEET 3 AZ 5 ILE H 5 ILE H 12 1 N VAL H 11 O VAL H 33
SHEET 4 AZ 5 THR H 136 ILE H 146 1 O LEU H 145 N ILE H 12
SHEET 5 AZ 5 ILE H 315 ALA H 317 1 O TYR H 316 N ILE H 144
SHEET 1 BA 2 SER H 150 VAL H 152 0
SHEET 2 BA 2 ARG H 280 PRO H 282 -1 O ARG H 281 N GLU H 151
SHEET 1 BB 5 ILE H 165 VAL H 166 0
SHEET 2 BB 5 VAL H 273 VAL H 276 1 O VAL H 276 N VAL H 166
SHEET 3 BB 5 LYS H 180 ILE H 184 1 N ILE H 184 O LEU H 275
SHEET 4 BB 5 ASP H 203 VAL H 207 1 O VAL H 207 N VAL H 183
SHEET 5 BB 5 LYS H 236 LYS H 238 1 O LYS H 236 N ALA H 206
SHEET 1 BC 3 THR H 241 LYS H 248 0
SHEET 2 BC 3 ILE H 254 ALA H 260 -1 O GLU H 259 N LYS H 242
SHEET 3 BC 3 GLU H 267 CYS H 271 -1 O ILE H 269 N VAL H 256
SHEET 1 BD 5 SER H 356 ILE H 358 0
SHEET 2 BD 5 GLU H 363 GLY H 368 -1 O VAL H 364 N ILE H 358
SHEET 3 BD 5 VAL H 415 GLY H 422 -1 O ILE H 420 N ALA H 365
SHEET 4 BD 5 MET H 403 GLN H 409 -1 N LEU H 407 O LEU H 416
SHEET 5 BD 5 TYR H 381 PRO H 387 -1 N GLY H 384 O ILE H 406
SHEET 1 BE 6 VAL I 113 ASN I 116 0
SHEET 2 BE 6 THR I 32 GLU I 36 1 N CYS I 34 O VAL I 113
SHEET 3 BE 6 ILE I 5 ILE I 12 1 N VAL I 11 O VAL I 33
SHEET 4 BE 6 THR I 136 ILE I 146 1 O LEU I 145 N THR I 10
SHEET 5 BE 6 GLN I 126 THR I 130 -1 N VAL I 127 O ILE I 139
SHEET 6 BE 6 LYS I 120 GLY I 123 -1 N LYS I 120 O THR I 128
SHEET 1 BF 5 VAL I 113 ASN I 116 0
SHEET 2 BF 5 THR I 32 GLU I 36 1 N CYS I 34 O VAL I 113
SHEET 3 BF 5 ILE I 5 ILE I 12 1 N VAL I 11 O VAL I 33
SHEET 4 BF 5 THR I 136 ILE I 146 1 O LEU I 145 N THR I 10
SHEET 5 BF 5 ILE I 315 ALA I 317 1 O TYR I 316 N ILE I 144
SHEET 1 BG 2 ILE I 76 MET I 78 0
SHEET 2 BG 2 VAL J 81 LEU J 83 -1 O ARG J 82 N GLU I 77
SHEET 1 BH 2 VAL I 81 LEU I 83 0
SHEET 2 BH 2 ILE J 76 MET J 78 -1 O GLU J 77 N ARG I 82
SHEET 1 BI 2 SER I 150 VAL I 152 0
SHEET 2 BI 2 ARG I 280 PRO I 282 -1 O ARG I 281 N GLU I 151
SHEET 1 BJ 4 LYS I 236 LYS I 238 0
SHEET 2 BJ 4 ASP I 203 VAL I 207 1 N ALA I 206 O LYS I 238
SHEET 3 BJ 4 LYS I 180 ILE I 184 1 N MET I 181 O ASP I 203
SHEET 4 BJ 4 VAL I 273 VAL I 276 1 O LEU I 275 N ILE I 184
SHEET 1 BK 3 THR I 241 LYS I 248 0
SHEET 2 BK 3 ILE I 254 ALA I 260 -1 O SER I 257 N GLY I 245
SHEET 3 BK 3 GLU I 267 CYS I 271 -1 O CYS I 271 N ILE I 254
SHEET 1 BL 5 SER I 356 ILE I 358 0
SHEET 2 BL 5 GLU I 363 GLY I 368 -1 O VAL I 364 N ILE I 358
SHEET 3 BL 5 VAL I 415 GLY I 422 -1 O ILE I 420 N ALA I 365
SHEET 4 BL 5 MET I 403 GLN I 409 -1 N LEU I 407 O LEU I 416
SHEET 5 BL 5 TYR I 381 PRO I 387 -1 N GLY I 384 O ILE I 406
SHEET 1 BM 6 VAL J 113 ASN J 116 0
SHEET 2 BM 6 THR J 32 GLU J 36 1 N THR J 32 O VAL J 113
SHEET 3 BM 6 ILE J 5 ILE J 12 1 N VAL J 11 O VAL J 33
SHEET 4 BM 6 THR J 136 ILE J 146 1 O ASN J 143 N ASP J 8
SHEET 5 BM 6 GLN J 126 THR J 130 -1 N ALA J 129 O GLN J 137
SHEET 6 BM 6 TYR J 118 GLY J 123 -1 N LYS J 120 O THR J 128
SHEET 1 BN 5 VAL J 113 ASN J 116 0
SHEET 2 BN 5 THR J 32 GLU J 36 1 N THR J 32 O VAL J 113
SHEET 3 BN 5 ILE J 5 ILE J 12 1 N VAL J 11 O VAL J 33
SHEET 4 BN 5 THR J 136 ILE J 146 1 O ASN J 143 N ASP J 8
SHEET 5 BN 5 ILE J 315 ALA J 317 1 O TYR J 316 N ILE J 144
SHEET 1 BO 2 SER J 150 VAL J 152 0
SHEET 2 BO 2 ARG J 280 PRO J 282 -1 O ARG J 281 N GLU J 151
SHEET 1 BP 5 ILE J 165 VAL J 166 0
SHEET 2 BP 5 VAL J 273 VAL J 276 1 O VAL J 276 N VAL J 166
SHEET 3 BP 5 LYS J 180 ILE J 184 1 N VAL J 182 O LEU J 275
SHEET 4 BP 5 ASP J 203 VAL J 207 1 O ASP J 203 N MET J 181
SHEET 5 BP 5 LYS J 236 LYS J 238 1 O LYS J 236 N ALA J 206
SHEET 1 BQ 3 THR J 241 LYS J 248 0
SHEET 2 BQ 3 ILE J 254 ALA J 260 -1 O GLU J 259 N LYS J 242
SHEET 3 BQ 3 GLU J 267 CYS J 271 -1 O ILE J 269 N VAL J 256
SHEET 1 BR 5 SER J 356 ILE J 358 0
SHEET 2 BR 5 GLU J 363 GLY J 368 -1 O VAL J 364 N ILE J 358
SHEET 3 BR 5 VAL J 415 GLY J 422 -1 O ILE J 420 N ALA J 365
SHEET 4 BR 5 MET J 403 GLN J 409 -1 N LEU J 407 O LEU J 416
SHEET 5 BR 5 TYR J 381 PRO J 387 -1 N GLY J 384 O ILE J 406
SSBOND 1 CYS A 45 CYS A 50 1555 1555 2.07
SSBOND 2 CYS B 45 CYS B 50 1555 1555 2.06
SSBOND 3 CYS C 45 CYS C 50 1555 1555 2.09
SSBOND 4 CYS D 45 CYS D 50 1555 1555 2.10
SSBOND 5 CYS E 45 CYS E 50 1555 1555 2.08
SSBOND 6 CYS F 45 CYS F 50 1555 1555 2.09
SSBOND 7 CYS G 45 CYS G 50 1555 1555 2.09
SSBOND 8 CYS H 45 CYS H 50 1555 1555 2.13
SSBOND 9 CYS I 45 CYS I 50 1555 1555 2.07
SSBOND 10 CYS J 45 CYS J 50 1555 1555 2.09
CISPEP 1 HIS A 361 PRO A 362 0 0.55
CISPEP 2 HIS A 452 PRO A 453 0 0.21
CISPEP 3 HIS B 361 PRO B 362 0 1.39
CISPEP 4 HIS B 452 PRO B 453 0 0.19
CISPEP 5 HIS C 361 PRO C 362 0 0.17
CISPEP 6 HIS C 452 PRO C 453 0 -1.55
CISPEP 7 HIS D 361 PRO D 362 0 -0.35
CISPEP 8 HIS D 452 PRO D 453 0 1.50
CISPEP 9 HIS E 361 PRO E 362 0 1.07
CISPEP 10 HIS E 452 PRO E 453 0 -0.29
CISPEP 11 HIS F 361 PRO F 362 0 0.15
CISPEP 12 HIS F 452 PRO F 453 0 -0.12
CISPEP 13 HIS G 361 PRO G 362 0 1.56
CISPEP 14 HIS G 452 PRO G 453 0 1.63
CISPEP 15 HIS H 361 PRO H 362 0 2.05
CISPEP 16 HIS H 452 PRO H 453 0 2.93
CISPEP 17 HIS I 361 PRO I 362 0 0.16
CISPEP 18 HIS I 452 PRO I 453 0 0.52
CISPEP 19 HIS J 361 PRO J 362 0 0.57
CISPEP 20 HIS J 452 PRO J 453 0 0.23
SITE 1 AC1 4 ARG A 299 ARG A 301 ALA A 323 GLY A 324
SITE 1 AC2 6 ARG C 299 ARG C 301 ALA C 323 GLY C 324
SITE 2 AC2 6 HOH C2594 HOH C2601
SITE 1 AC3 4 HIS A 64 GLY A 68 THR A 69 HOH A2498
SITE 1 AC4 5 HIS C 64 GLY C 68 THR C 69 ASP C 70
SITE 2 AC4 5 HOH C2543
SITE 1 AC5 3 LEU A 210 GLY A 211 HIS A 212
SITE 1 AC6 3 LEU C 210 GLY C 211 HIS C 212
SITE 1 AC7 6 ASN A 286 LEU A 287 GLY A 288 LEU A 289
SITE 2 AC7 6 GLU A 290 GLU A 291
SITE 1 AC8 6 ASN C 286 LEU C 287 GLY C 288 LEU C 289
SITE 2 AC8 6 GLU C 290 GLU C 291
SITE 1 AC9 4 ARG B 299 ARG B 301 ALA B 323 GLY B 324
SITE 1 BC1 6 HOH A2597 ARG D 299 ARG D 301 ALA D 323
SITE 2 BC1 6 GLY D 324 HOH D2571
SITE 1 BC2 3 HIS B 64 THR B 69 HOH B2491
SITE 1 BC3 3 HIS D 64 GLY D 68 THR D 69
SITE 1 BC4 2 GLY B 211 HIS B 212
SITE 1 BC5 3 LEU D 210 GLY D 211 HIS D 212
SITE 1 BC6 6 THR B 284 ASN B 286 LEU B 287 GLY B 288
SITE 2 BC6 6 LEU B 289 GLU B 290
SITE 1 BC7 7 THR D 284 ASN D 286 LEU D 287 GLY D 288
SITE 2 BC7 7 LEU D 289 GLU D 290 HOH D2657
SITE 1 BC8 4 ARG E 299 ARG E 301 ALA E 323 GLY E 324
SITE 1 BC9 5 HIS E 64 GLY E 68 THR E 69 ASP E 70
SITE 2 BC9 5 HOH E2564
SITE 1 CC1 3 LEU E 210 GLY E 211 HIS E 212
SITE 1 CC2 7 THR E 284 ASN E 286 LEU E 287 GLY E 288
SITE 2 CC2 7 LEU E 289 GLU E 290 GLU E 291
SITE 1 CC3 7 ARG F 299 ARG F 301 ALA F 323 GLY F 324
SITE 2 CC3 7 HOH F2717 HOH F2718 HOH H2698
SITE 1 CC4 5 HIS F 64 GLY F 68 THR F 69 HOH F2507
SITE 2 CC4 5 HOH F2686
SITE 1 CC5 2 GLY F 211 HIS F 212
SITE 1 CC6 7 THR F 284 ASN F 286 LEU F 287 GLY F 288
SITE 2 CC6 7 LEU F 289 GLU F 290 HOH F2681
SITE 1 CC7 4 ARG G 299 ARG G 301 ALA G 323 GLY G 324
SITE 1 CC8 5 HIS G 64 GLY G 68 THR G 69 HOH G2521
SITE 2 CC8 5 HOH G2682
SITE 1 CC9 3 LEU G 210 GLY G 211 HIS G 212
SITE 1 DC1 7 THR G 284 ASN G 286 LEU G 287 GLY G 288
SITE 2 DC1 7 LEU G 289 GLU G 290 GLU G 291
SITE 1 DC2 4 ARG H 299 ARG H 301 ALA H 323 GLY H 324
SITE 1 DC3 4 HIS H 64 GLY H 68 THR H 69 HOH H2604
SITE 1 DC4 4 LEU H 210 GLY H 211 HIS H 212 HOH H2784
SITE 1 DC5 8 THR H 284 ASN H 286 LEU H 287 GLY H 288
SITE 2 DC5 8 LEU H 289 GLU H 290 HOH H2622 HOH H2736
SITE 1 DC6 5 LYS G 253 ARG I 299 ARG I 301 ALA I 323
SITE 2 DC6 5 GLY I 324
SITE 1 DC7 3 LEU I 210 GLY I 211 HIS I 212
SITE 1 DC8 6 THR I 284 ASN I 286 LEU I 287 GLY I 288
SITE 2 DC8 6 LEU I 289 GLU I 290
SITE 1 DC9 5 HOH B2497 ARG J 299 ARG J 301 ALA J 323
SITE 2 DC9 5 GLY J 324
SITE 1 EC1 2 HIS J 64 THR J 69
SITE 1 EC2 3 LEU J 210 GLY J 211 HIS J 212
SITE 1 EC3 6 THR J 284 ASN J 286 LEU J 287 GLY J 288
SITE 2 EC3 6 LEU J 289 GLU J 290
SITE 1 EC4 38 ILE A 12 GLY A 13 GLY A 15 PRO A 16
SITE 2 EC4 38 GLY A 17 GLU A 36 LYS A 37 ASN A 38
SITE 3 EC4 38 GLY A 43 THR A 44 CYS A 45 VAL A 48
SITE 4 EC4 38 GLY A 49 CYS A 50 LYS A 54 GLY A 117
SITE 5 EC4 38 TYR A 118 GLY A 119 ALA A 147 THR A 148
SITE 6 EC4 38 GLY A 149 SER A 150 SER A 168 ILE A 189
SITE 7 EC4 38 ARG A 280 PHE A 283 GLY A 319 ASP A 320
SITE 8 EC4 38 MET A 326 LEU A 327 ALA A 328 HIS A 329
SITE 9 EC4 38 TYR A 359 HOH A2491 HOH A2502 HOH A2507
SITE 10 EC4 38 HOH A2525 HIS B 452
SITE 1 EC5 38 HIS A 452 ILE B 12 GLY B 13 GLY B 15
SITE 2 EC5 38 PRO B 16 GLY B 17 GLU B 36 LYS B 37
SITE 3 EC5 38 ASN B 38 GLY B 43 THR B 44 CYS B 45
SITE 4 EC5 38 VAL B 48 GLY B 49 CYS B 50 SER B 53
SITE 5 EC5 38 LYS B 54 GLY B 117 TYR B 118 GLY B 119
SITE 6 EC5 38 ALA B 147 THR B 148 GLY B 149 SER B 150
SITE 7 EC5 38 SER B 168 ILE B 189 ARG B 280 GLY B 319
SITE 8 EC5 38 ASP B 320 MET B 326 LEU B 327 ALA B 328
SITE 9 EC5 38 HIS B 329 ALA B 331 TYR B 359 HOH B2496
SITE 10 EC5 38 HOH B2514 HOH B2545
SITE 1 EC6 39 GLY C 13 SER C 14 GLY C 15 PRO C 16
SITE 2 EC6 39 GLY C 17 GLU C 36 LYS C 37 ASN C 38
SITE 3 EC6 39 GLY C 43 THR C 44 CYS C 45 VAL C 48
SITE 4 EC6 39 GLY C 49 CYS C 50 SER C 53 LYS C 54
SITE 5 EC6 39 GLY C 117 TYR C 118 GLY C 119 ALA C 147
SITE 6 EC6 39 THR C 148 GLY C 149 SER C 150 ILE C 189
SITE 7 EC6 39 ARG C 280 PHE C 283 GLY C 319 ASP C 320
SITE 8 EC6 39 MET C 326 LEU C 327 ALA C 328 HIS C 329
SITE 9 EC6 39 TYR C 359 HOH C2496 HOH C2497 HOH C2502
SITE 10 EC6 39 HOH C2524 HOH C2602 HIS D 452
SITE 1 EC7 42 HIS C 452 ILE D 12 GLY D 13 SER D 14
SITE 2 EC7 42 GLY D 15 PRO D 16 GLY D 17 GLU D 36
SITE 3 EC7 42 LYS D 37 ASN D 38 GLY D 43 THR D 44
SITE 4 EC7 42 CYS D 45 VAL D 48 GLY D 49 CYS D 50
SITE 5 EC7 42 SER D 53 LYS D 54 GLY D 117 TYR D 118
SITE 6 EC7 42 GLY D 119 ALA D 147 THR D 148 GLY D 149
SITE 7 EC7 42 SER D 150 SER D 168 ILE D 189 ARG D 280
SITE 8 EC7 42 PHE D 283 GLY D 319 ASP D 320 MET D 326
SITE 9 EC7 42 LEU D 327 ALA D 328 HIS D 329 ALA D 331
SITE 10 EC7 42 TYR D 359 HOH D2500 HOH D2503 HOH D2557
SITE 11 EC7 42 HOH D2574 HOH D2654
SITE 1 EC8 41 ILE E 12 GLY E 13 SER E 14 GLY E 15
SITE 2 EC8 41 PRO E 16 GLY E 17 GLU E 36 LYS E 37
SITE 3 EC8 41 ASN E 38 GLY E 43 THR E 44 CYS E 45
SITE 4 EC8 41 GLY E 49 CYS E 50 SER E 53 LYS E 54
SITE 5 EC8 41 GLY E 117 TYR E 118 GLY E 119 ALA E 147
SITE 6 EC8 41 THR E 148 GLY E 149 SER E 150 SER E 168
SITE 7 EC8 41 ILE E 189 ARG E 280 GLY E 319 ASP E 320
SITE 8 EC8 41 MET E 326 LEU E 327 ALA E 328 HIS E 329
SITE 9 EC8 41 ALA E 331 TYR E 359 HOH E2502 HOH E2505
SITE 10 EC8 41 HOH E2515 HOH E2522 HOH E2536 HOH E2600
SITE 11 EC8 41 HIS F 452
SITE 1 EC9 39 HIS E 452 GLY F 13 SER F 14 GLY F 15
SITE 2 EC9 39 PRO F 16 GLY F 17 ILE F 35 GLU F 36
SITE 3 EC9 39 LYS F 37 ASN F 38 GLY F 43 THR F 44
SITE 4 EC9 39 CYS F 45 VAL F 48 GLY F 49 CYS F 50
SITE 5 EC9 39 LYS F 54 GLY F 117 TYR F 118 GLY F 119
SITE 6 EC9 39 ALA F 147 THR F 148 GLY F 149 SER F 150
SITE 7 EC9 39 ILE F 189 ARG F 280 PHE F 283 GLY F 319
SITE 8 EC9 39 ASP F 320 MET F 326 LEU F 327 ALA F 328
SITE 9 EC9 39 HIS F 329 TYR F 359 HOH F2512 HOH F2517
SITE 10 EC9 39 HOH F2532 HOH F2535 HOH F2650
SITE 1 FC1 38 ILE G 12 GLY G 13 GLY G 15 PRO G 16
SITE 2 FC1 38 GLY G 17 GLU G 36 LYS G 37 ASN G 38
SITE 3 FC1 38 GLY G 43 THR G 44 CYS G 45 VAL G 48
SITE 4 FC1 38 GLY G 49 CYS G 50 LYS G 54 GLY G 117
SITE 5 FC1 38 TYR G 118 GLY G 119 ALA G 147 THR G 148
SITE 6 FC1 38 GLY G 149 SER G 150 SER G 168 ARG G 280
SITE 7 FC1 38 PHE G 283 GLY G 319 ASP G 320 MET G 326
SITE 8 FC1 38 LEU G 327 ALA G 328 HIS G 329 TYR G 359
SITE 9 FC1 38 HOH G2522 HOH G2524 HOH G2533 HOH G2544
SITE 10 FC1 38 HOH G2631 HIS H 452
SITE 1 FC2 37 HIS G 452 ILE H 12 GLY H 13 SER H 14
SITE 2 FC2 37 GLY H 15 PRO H 16 GLY H 17 GLU H 36
SITE 3 FC2 37 LYS H 37 ASN H 38 GLY H 43 THR H 44
SITE 4 FC2 37 CYS H 45 GLY H 49 CYS H 50 LYS H 54
SITE 5 FC2 37 GLY H 117 TYR H 118 GLY H 119 ALA H 147
SITE 6 FC2 37 THR H 148 GLY H 149 SER H 150 ARG H 280
SITE 7 FC2 37 PHE H 283 GLY H 319 ASP H 320 MET H 326
SITE 8 FC2 37 LEU H 327 ALA H 328 HIS H 329 TYR H 359
SITE 9 FC2 37 HOH H2515 HOH H2516 HOH H2517 HOH H2528
SITE 10 FC2 37 HOH H2545
SITE 1 FC3 38 ILE I 12 GLY I 13 SER I 14 GLY I 15
SITE 2 FC3 38 PRO I 16 GLY I 17 ILE I 35 GLU I 36
SITE 3 FC3 38 LYS I 37 ASN I 38 GLY I 43 THR I 44
SITE 4 FC3 38 CYS I 45 GLY I 49 CYS I 50 SER I 53
SITE 5 FC3 38 LYS I 54 GLY I 117 TYR I 118 GLY I 119
SITE 6 FC3 38 ALA I 147 THR I 148 GLY I 149 SER I 150
SITE 7 FC3 38 ILE I 189 ARG I 280 PHE I 283 GLY I 319
SITE 8 FC3 38 ASP I 320 MET I 326 LEU I 327 ALA I 328
SITE 9 FC3 38 HIS I 329 TYR I 359 HOH I2532 HOH I2533
SITE 10 FC3 38 HOH I2562 HIS J 452
SITE 1 FC4 41 HIS I 452 ILE J 12 GLY J 13 SER J 14
SITE 2 FC4 41 GLY J 15 PRO J 16 GLY J 17 GLU J 36
SITE 3 FC4 41 LYS J 37 ASN J 38 GLY J 43 THR J 44
SITE 4 FC4 41 CYS J 45 GLY J 49 CYS J 50 SER J 53
SITE 5 FC4 41 LYS J 54 GLY J 117 TYR J 118 GLY J 119
SITE 6 FC4 41 ALA J 147 THR J 148 GLY J 149 SER J 150
SITE 7 FC4 41 ILE J 189 ARG J 280 PHE J 283 LEU J 287
SITE 8 FC4 41 GLY J 319 ASP J 320 MET J 326 LEU J 327
SITE 9 FC4 41 ALA J 328 HIS J 329 ALA J 331 TYR J 359
SITE 10 FC4 41 HOH J2521 HOH J2523 HOH J2533 HOH J2562
SITE 11 FC4 41 HOH J2608
CRYST1 171.153 187.728 224.392 90.00 90.00 90.00 P 21 21 21 40
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 0.005843 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005327 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004456 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
