HEADER ISOMERASE 09-NOV-11 3UKL
TITLE CRYSTAL STRUCTURE OF UDP-GALACTOPYRANOSE MUTASE FROM ASPERGILLUS
TITLE 2 FUMIGATUS IN COMPLEX WITH UDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GALACTOPYRANOSE MUTASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 EC: 5.4.99.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS FUMIGATUS;
SOURCE 3 ORGANISM_TAXID: 746128;
SOURCE 4 STRAIN: CBS 144-89;
SOURCE 5 GENE: GLF, GLFA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS FLAVOENZYME, FAD, UDP, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.VAN STRAATEN,D.A.R.SANDERS
REVDAT 5 28-FEB-24 3UKL 1 REMARK SEQADV
REVDAT 4 08-NOV-17 3UKL 1 REMARK
REVDAT 3 18-JUL-12 3UKL 1 JRNL
REVDAT 2 07-MAR-12 3UKL 1 JRNL
REVDAT 1 22-FEB-12 3UKL 0
JRNL AUTH K.E.VAN STRAATEN,F.H.ROUTIER,D.A.SANDERS
JRNL TITL STRUCTURAL INSIGHT INTO THE UNIQUE SUBSTRATE BINDING
JRNL TITL 2 MECHANISM AND FLAVIN REDOX STATE OF UDP-GALACTOPYRANOSE
JRNL TITL 3 MUTASE FROM ASPERGILLUS FUMIGATUS.
JRNL REF J.BIOL.CHEM. V. 287 10780 2012
JRNL REFN ISSN 0021-9258
JRNL PMID 22334662
JRNL DOI 10.1074/JBC.M111.322974
REMARK 2
REMARK 2 RESOLUTION. 2.63 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.63
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 3 NUMBER OF REFLECTIONS : 165250
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8263
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.0409 - 5.6634 0.98 16907 890 0.1576 0.1826
REMARK 3 2 5.6634 - 4.4962 0.98 16758 882 0.1289 0.1688
REMARK 3 3 4.4962 - 3.9282 0.97 16678 878 0.1365 0.1847
REMARK 3 4 3.9282 - 3.5692 0.96 16425 865 0.1748 0.2240
REMARK 3 5 3.5692 - 3.3134 0.94 16202 852 0.2043 0.2563
REMARK 3 6 3.3134 - 3.1181 0.92 15768 830 0.2190 0.2819
REMARK 3 7 3.1181 - 2.9620 0.89 15332 806 0.2403 0.3082
REMARK 3 8 2.9620 - 2.8330 0.86 14773 778 0.2589 0.3146
REMARK 3 9 2.8330 - 2.7240 0.84 14371 756 0.2868 0.3427
REMARK 3 10 2.7240 - 2.6300 0.80 13773 726 0.3015 0.3602
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 23.43
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.790
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.380
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.49890
REMARK 3 B22 (A**2) : -2.80770
REMARK 3 B33 (A**2) : -1.27510
REMARK 3 B12 (A**2) : -7.82230
REMARK 3 B13 (A**2) : 1.40180
REMARK 3 B23 (A**2) : -2.25550
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 33546
REMARK 3 ANGLE : 0.776 45712
REMARK 3 CHIRALITY : 0.051 4940
REMARK 3 PLANARITY : 0.003 5844
REMARK 3 DIHEDRAL : 17.527 12846
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 3993
REMARK 3 RMSD : 0.199
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN C AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 3993
REMARK 3 RMSD : 0.181
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN D AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 4004
REMARK 3 RMSD : 0.187
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN E AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 3993
REMARK 3 RMSD : 0.197
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN F AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 4004
REMARK 3 RMSD : 0.188
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN G AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 4004
REMARK 3 RMSD : 0.183
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 SELECTION : CHAIN H AND (RESSEQ 2:511 ) AND (NOT
REMARK 3 ELEMENT H) AND (NOT ELEMENT D)
REMARK 3 ATOM PAIRS NUMBER : 3993
REMARK 3 RMSD : 0.170
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3UKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08B1-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : COLLIMATING MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 165288
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.630
REMARK 200 RESOLUTION RANGE LOW (A) : 48.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.3
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.63
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.53500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.550
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: REDUCED AFUGM:UDPGALP COMPLEX STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS-PROPANE PH 7.5-8.5, 0.1
REMARK 280 -0.2M SODIUM CITRATE, 15-20% PEG 3350, MICROBATCH, TEMPERATURE
REMARK 280 295K, PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 76360 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 76550 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -135.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, E
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 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 17.44508
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 128.01683
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 GLN A 98 71.67 44.75
REMARK 500 PHE A 158 -63.59 -127.26
REMARK 500 ALA A 201 80.69 -155.97
REMARK 500 ALA A 208 -70.56 -30.96
REMARK 500 CYS A 314 -71.00 -94.03
REMARK 500 PHE B 158 -62.27 -127.50
REMARK 500 ALA B 201 81.08 -161.41
REMARK 500 ALA B 208 -70.39 -34.01
REMARK 500 CYS B 314 -71.39 -94.11
REMARK 500 LYS B 380 79.66 -154.24
REMARK 500 THR B 431 0.52 -69.26
REMARK 500 VAL B 455 40.37 -141.86
REMARK 500 PHE C 158 -59.06 -129.48
REMARK 500 ALA C 201 78.05 -156.84
REMARK 500 CYS C 314 -70.73 -97.03
REMARK 500 LYS C 380 83.23 -154.88
REMARK 500 GLU C 454 -18.93 -49.73
REMARK 500 VAL C 455 37.59 -140.32
REMARK 500 TYR C 483 59.74 -140.58
REMARK 500 GLN D 98 72.28 43.88
REMARK 500 PHE D 158 -61.64 -128.46
REMARK 500 ALA D 201 79.54 -158.80
REMARK 500 CYS D 314 -73.44 -96.61
REMARK 500 PHE E 158 -63.53 -128.56
REMARK 500 ALA E 201 79.70 -157.08
REMARK 500 ALA E 208 -71.95 -32.71
REMARK 500 CYS E 314 -67.56 -99.47
REMARK 500 LYS E 380 77.37 -154.36
REMARK 500 ASP F 59 174.23 -54.21
REMARK 500 PHE F 158 -64.22 -131.49
REMARK 500 ALA F 201 81.81 -162.04
REMARK 500 ALA F 208 -75.54 -32.96
REMARK 500 CYS F 314 -64.52 -99.46
REMARK 500 PHE G 158 -67.83 -129.57
REMARK 500 ALA G 201 80.31 -159.70
REMARK 500 CYS G 314 -69.78 -95.64
REMARK 500 LYS G 380 82.45 -151.52
REMARK 500 GLU G 454 -17.64 -49.52
REMARK 500 VAL G 455 40.37 -143.33
REMARK 500 PHE H 158 -59.75 -126.31
REMARK 500 ALA H 201 81.67 -159.58
REMARK 500 ALA H 208 -72.70 -29.08
REMARK 500 ARG H 235 80.86 -153.71
REMARK 500 ASP H 312 31.41 -94.52
REMARK 500 CYS H 314 -70.51 -96.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG E 303 0.13 SIDE CHAIN
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 UDP A 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP B 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP C 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP D 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP E 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP F 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD F 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP G 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD G 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP H 800
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD H 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3UKA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF UNLIGANDED AFUGM
REMARK 900 RELATED ID: 3UKF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AFUGM:UDPGALP COMPLEX (REDUCED)
REMARK 900 RELATED ID: 3UKH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AFUGM:UDPGALP COMPLEX (NON-REDUCED)
REMARK 900 RELATED ID: 3UKK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF R182K-AFUGM IN COMPLEX WITH UDPGALP
REMARK 900 RELATED ID: 3UKP RELATED DB: PDB
REMARK 900 RELATED ID: 3UKQ RELATED DB: PDB
DBREF 3UKL A 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL B 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL C 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL D 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL E 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL F 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL G 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
DBREF 3UKL H 2 510 UNP Q4W1X2 Q4W1X2_ASPFM 2 510
SEQADV 3UKL LEU A 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU B 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU C 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU D 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU E 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU F 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU G 511 UNP Q4W1X2 EXPRESSION TAG
SEQADV 3UKL LEU H 511 UNP Q4W1X2 EXPRESSION TAG
SEQRES 1 A 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 A 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 A 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 A 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 A 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 A 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 A 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 A 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 A 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 A 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 A 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 A 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 A 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 A 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 A 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 A 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 A 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 A 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 A 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 A 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 A 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 A 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 A 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 A 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 A 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 A 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 A 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 A 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 A 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 A 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 A 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 A 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 A 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 A 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 A 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 A 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 A 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 A 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 A 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 A 510 ALA GLN LEU
SEQRES 1 B 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 B 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 B 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 B 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 B 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 B 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 B 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 B 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 B 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 B 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 B 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 B 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 B 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 B 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 B 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 B 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 B 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 B 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 B 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 B 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 B 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 B 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 B 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 B 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 B 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 B 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 B 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 B 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 B 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 B 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 B 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 B 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 B 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 B 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 B 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 B 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 B 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 B 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 B 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 B 510 ALA GLN LEU
SEQRES 1 C 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 C 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 C 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 C 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 C 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 C 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 C 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 C 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 C 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 C 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 C 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 C 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 C 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 C 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 C 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 C 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 C 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 C 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 C 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 C 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 C 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 C 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 C 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 C 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 C 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 C 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 C 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 C 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 C 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 C 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 C 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 C 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 C 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 C 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 C 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 C 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 C 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 C 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 C 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 C 510 ALA GLN LEU
SEQRES 1 D 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 D 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 D 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 D 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 D 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 D 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 D 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 D 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 D 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 D 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 D 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 D 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 D 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 D 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 D 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 D 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 D 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 D 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 D 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 D 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 D 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 D 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 D 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 D 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 D 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 D 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 D 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 D 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 D 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 D 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 D 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 D 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 D 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 D 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 D 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 D 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 D 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 D 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 D 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 D 510 ALA GLN LEU
SEQRES 1 E 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 E 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 E 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 E 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 E 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 E 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 E 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 E 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 E 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 E 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 E 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 E 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 E 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 E 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 E 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 E 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 E 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 E 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 E 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 E 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 E 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 E 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 E 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 E 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 E 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 E 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 E 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 E 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 E 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 E 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 E 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 E 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 E 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 E 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 E 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 E 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 E 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 E 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 E 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 E 510 ALA GLN LEU
SEQRES 1 F 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 F 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 F 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 F 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 F 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 F 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 F 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 F 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 F 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 F 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 F 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 F 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 F 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 F 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 F 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 F 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 F 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 F 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 F 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 F 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 F 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 F 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 F 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 F 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 F 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 F 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 F 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 F 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 F 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 F 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 F 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 F 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 F 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 F 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 F 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 F 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 F 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 F 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 F 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 F 510 ALA GLN LEU
SEQRES 1 G 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 G 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 G 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 G 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 G 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 G 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 G 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 G 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 G 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 G 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 G 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 G 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 G 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 G 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 G 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 G 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 G 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 G 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 G 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 G 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 G 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 G 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 G 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 G 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 G 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 G 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 G 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 G 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 G 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 G 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 G 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 G 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 G 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 G 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 G 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 G 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 G 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 G 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 G 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 G 510 ALA GLN LEU
SEQRES 1 H 510 THR HIS PRO ASP ILE SER VAL ASP VAL LEU VAL ILE GLY
SEQRES 2 H 510 ALA GLY PRO THR GLY LEU GLY ALA ALA LYS ARG LEU ASN
SEQRES 3 H 510 GLN ILE ASP GLY PRO SER TRP MET ILE VAL ASP SER ASN
SEQRES 4 H 510 GLU THR PRO GLY GLY LEU ALA SER THR ASP VAL THR PRO
SEQRES 5 H 510 GLU GLY PHE LEU TYR ASP VAL GLY GLY HIS VAL ILE PHE
SEQRES 6 H 510 SER HIS TYR LYS TYR PHE ASP ASP CYS LEU ASP GLU ALA
SEQRES 7 H 510 LEU PRO LYS GLU ASP ASP TRP TYR THR HIS GLN ARG ILE
SEQRES 8 H 510 SER TYR VAL ARG CYS GLN GLY GLN TRP VAL PRO TYR PRO
SEQRES 9 H 510 PHE GLN ASN ASN ILE SER MET LEU PRO LYS GLU GLU GLN
SEQRES 10 H 510 VAL LYS CYS ILE ASP GLY MET ILE ASP ALA ALA LEU GLU
SEQRES 11 H 510 ALA ARG VAL ALA ASN THR LYS PRO LYS THR PHE ASP GLU
SEQRES 12 H 510 TRP ILE VAL ARG MET MET GLY THR GLY ILE ALA ASP LEU
SEQRES 13 H 510 PHE MET ARG PRO TYR ASN PHE LYS VAL TRP ALA VAL PRO
SEQRES 14 H 510 THR THR LYS MET GLN CYS ALA TRP LEU GLY GLU ARG VAL
SEQRES 15 H 510 ALA ALA PRO ASN LEU LYS ALA VAL THR THR ASN VAL ILE
SEQRES 16 H 510 LEU GLY LYS THR ALA GLY ASN TRP GLY PRO ASN ALA THR
SEQRES 17 H 510 PHE ARG PHE PRO ALA ARG GLY GLY THR GLY GLY ILE TRP
SEQRES 18 H 510 ILE ALA VAL ALA ASN THR LEU PRO LYS GLU LYS THR ARG
SEQRES 19 H 510 PHE GLY GLU LYS GLY LYS VAL THR LYS VAL ASN ALA ASN
SEQRES 20 H 510 ASN LYS THR VAL THR LEU GLN ASP GLY THR THR ILE GLY
SEQRES 21 H 510 TYR LYS LYS LEU VAL SER THR MET ALA VAL ASP PHE LEU
SEQRES 22 H 510 ALA GLU ALA MET ASN ASP GLN GLU LEU VAL GLY LEU THR
SEQRES 23 H 510 LYS GLN LEU PHE TYR SER SER THR HIS VAL ILE GLY VAL
SEQRES 24 H 510 GLY VAL ARG GLY SER ARG PRO GLU ARG ILE GLY ASP LYS
SEQRES 25 H 510 CYS TRP LEU TYR PHE PRO GLU ASP ASN CYS PRO PHE TYR
SEQRES 26 H 510 ARG ALA THR ILE PHE SER ASN TYR SER PRO TYR ASN GLN
SEQRES 27 H 510 PRO GLU ALA SER LYS LYS LEU PRO THR MET GLN LEU ALA
SEQRES 28 H 510 ASP GLY SER ARG PRO GLN SER THR GLU ALA LYS GLU GLY
SEQRES 29 H 510 PRO TYR TRP SER ILE MET LEU GLU VAL SER GLU SER SER
SEQRES 30 H 510 MET LYS PRO VAL ASN GLN GLU THR ILE LEU ALA ASP CYS
SEQRES 31 H 510 ILE GLN GLY LEU VAL ASN THR GLU MET LEU LYS PRO THR
SEQRES 32 H 510 ASP GLU ILE VAL SER THR TYR HIS ARG ARG PHE ASP HIS
SEQRES 33 H 510 GLY TYR PRO THR PRO THR LEU GLU ARG GLU GLY ALA LEU
SEQRES 34 H 510 THR GLN ILE LEU PRO LYS LEU GLN ASP LYS ASP ILE TRP
SEQRES 35 H 510 SER ARG GLY ARG PHE GLY SER TRP ARG TYR GLU VAL GLY
SEQRES 36 H 510 ASN GLN ASP HIS SER PHE MET LEU GLY VAL GLU ALA VAL
SEQRES 37 H 510 ASP ASN ILE VAL ASN GLY ALA VAL GLU LEU THR LEU ASN
SEQRES 38 H 510 TYR PRO ASP PHE VAL ASN GLY ARG GLN ASN THR GLU ARG
SEQRES 39 H 510 ARG LEU VAL ASP GLY ALA GLN VAL PHE ALA LYS SER LYS
SEQRES 40 H 510 ALA GLN LEU
HET UDP A 800 25
HET FAD A 602 53
HET CL A 1 1
HET CL A 512 1
HET UDP B 800 25
HET FAD B 604 53
HET CL B 1 1
HET UDP C 800 25
HET FAD C 600 53
HET CL C 1 1
HET UDP D 800 25
HET FAD D 601 53
HET UDP E 800 25
HET FAD E 606 53
HET CL E 1 1
HET UDP F 800 25
HET FAD F 603 53
HET CL F 1 1
HET CL F 512 1
HET UDP G 800 25
HET FAD G 607 53
HET UDP H 800 25
HET FAD H 605 53
HET CL H 1 1
HETNAM UDP URIDINE-5'-DIPHOSPHATE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM CL CHLORIDE ION
FORMUL 9 UDP 8(C9 H14 N2 O12 P2)
FORMUL 10 FAD 8(C27 H33 N9 O15 P2)
FORMUL 11 CL 8(CL 1-)
FORMUL 33 HOH *1039(H2 O)
HELIX 1 1 GLY A 16 ASP A 30 1 15
HELIX 2 2 GLY A 44 ALA A 47 5 4
HELIX 3 3 TYR A 69 LEU A 80 1 12
HELIX 4 4 LYS A 82 ASP A 84 5 3
HELIX 5 5 PRO A 105 LEU A 113 5 9
HELIX 6 6 PRO A 114 ARG A 133 1 20
HELIX 7 7 THR A 141 PHE A 158 1 18
HELIX 8 8 PHE A 158 ALA A 168 1 11
HELIX 9 9 PRO A 170 MET A 174 5 5
HELIX 10 10 ASN A 187 GLY A 198 1 12
HELIX 11 11 GLY A 216 THR A 228 1 13
HELIX 12 12 LEU A 229 GLU A 232 5 4
HELIX 13 13 GLU A 238 GLY A 240 5 3
HELIX 14 14 ALA A 270 ASN A 279 1 10
HELIX 15 15 ASP A 280 LYS A 288 1 9
HELIX 16 16 PHE A 331 TYR A 334 5 4
HELIX 17 17 SER A 335 GLN A 339 5 5
HELIX 18 18 ASN A 383 THR A 398 1 16
HELIX 19 19 GLU A 425 ASP A 439 1 15
HELIX 20 20 ARG A 452 GLY A 456 5 5
HELIX 21 21 ASN A 457 GLY A 475 1 19
HELIX 22 22 GLU A 478 TYR A 483 1 6
HELIX 23 23 TYR A 483 GLY A 489 1 7
HELIX 24 24 ASP A 499 LEU A 511 1 13
HELIX 25 25 GLY B 16 ASP B 30 1 15
HELIX 26 26 GLY B 44 SER B 48 5 5
HELIX 27 27 TYR B 69 LEU B 80 1 12
HELIX 28 28 LYS B 82 ASP B 84 5 3
HELIX 29 29 PRO B 105 LEU B 113 5 9
HELIX 30 30 PRO B 114 ARG B 133 1 20
HELIX 31 31 THR B 141 PHE B 158 1 18
HELIX 32 32 PHE B 158 ALA B 168 1 11
HELIX 33 33 PRO B 170 MET B 174 5 5
HELIX 34 34 ASN B 187 GLY B 198 1 12
HELIX 35 35 THR B 218 THR B 228 1 11
HELIX 36 36 LEU B 229 GLU B 232 5 4
HELIX 37 37 GLU B 238 GLY B 240 5 3
HELIX 38 38 ALA B 270 ASN B 279 1 10
HELIX 39 39 ASP B 280 LYS B 288 1 9
HELIX 40 40 PHE B 331 TYR B 334 5 4
HELIX 41 41 SER B 335 GLN B 339 5 5
HELIX 42 42 ASN B 383 THR B 398 1 16
HELIX 43 43 GLU B 425 ASP B 439 1 15
HELIX 44 44 ARG B 452 GLY B 456 5 5
HELIX 45 45 ASN B 457 GLY B 475 1 19
HELIX 46 46 GLU B 478 TYR B 483 1 6
HELIX 47 47 TYR B 483 GLY B 489 1 7
HELIX 48 48 ASP B 499 LEU B 511 1 13
HELIX 49 49 GLY C 16 ASP C 30 1 15
HELIX 50 50 GLY C 44 ALA C 47 5 4
HELIX 51 51 TYR C 69 LEU C 80 1 12
HELIX 52 52 LYS C 82 ASP C 84 5 3
HELIX 53 53 PRO C 105 LEU C 113 5 9
HELIX 54 54 PRO C 114 ARG C 133 1 20
HELIX 55 55 THR C 141 PHE C 158 1 18
HELIX 56 56 PHE C 158 ALA C 168 1 11
HELIX 57 57 PRO C 170 MET C 174 5 5
HELIX 58 58 ASN C 187 GLY C 198 1 12
HELIX 59 59 GLY C 216 THR C 228 1 13
HELIX 60 60 LEU C 229 GLU C 232 5 4
HELIX 61 61 GLU C 238 GLY C 240 5 3
HELIX 62 62 ALA C 270 ASN C 279 1 10
HELIX 63 63 ASP C 280 LYS C 288 1 9
HELIX 64 64 PHE C 331 TYR C 334 5 4
HELIX 65 65 SER C 335 GLN C 339 5 5
HELIX 66 66 ASN C 383 THR C 398 1 16
HELIX 67 67 GLU C 425 ASP C 439 1 15
HELIX 68 68 ARG C 452 GLY C 456 5 5
HELIX 69 69 ASN C 457 GLY C 475 1 19
HELIX 70 70 GLU C 478 TYR C 483 1 6
HELIX 71 71 TYR C 483 GLY C 489 1 7
HELIX 72 72 ASP C 499 LEU C 511 1 13
HELIX 73 73 GLY D 16 ASP D 30 1 15
HELIX 74 74 GLY D 44 ALA D 47 5 4
HELIX 75 75 TYR D 69 LEU D 80 1 12
HELIX 76 76 LYS D 82 ASP D 84 5 3
HELIX 77 77 PRO D 105 LEU D 113 5 9
HELIX 78 78 PRO D 114 ARG D 133 1 20
HELIX 79 79 THR D 141 PHE D 158 1 18
HELIX 80 80 PHE D 158 ALA D 168 1 11
HELIX 81 81 PRO D 170 MET D 174 5 5
HELIX 82 82 CYS D 176 GLY D 180 5 5
HELIX 83 83 ASN D 187 GLY D 198 1 12
HELIX 84 84 GLY D 217 THR D 228 1 12
HELIX 85 85 LEU D 229 GLU D 232 5 4
HELIX 86 86 GLU D 238 GLY D 240 5 3
HELIX 87 87 ALA D 247 ASN D 249 5 3
HELIX 88 88 ALA D 270 ASN D 279 1 10
HELIX 89 89 ASP D 280 LYS D 288 1 9
HELIX 90 90 PHE D 331 TYR D 334 5 4
HELIX 91 91 ASN D 383 THR D 398 1 16
HELIX 92 92 GLU D 425 ASP D 439 1 15
HELIX 93 93 ARG D 452 GLY D 456 5 5
HELIX 94 94 ASN D 457 GLY D 475 1 19
HELIX 95 95 GLU D 478 TYR D 483 1 6
HELIX 96 96 TYR D 483 GLY D 489 1 7
HELIX 97 97 ASP D 499 LEU D 511 1 13
HELIX 98 98 GLY E 16 ASP E 30 1 15
HELIX 99 99 GLY E 44 SER E 48 5 5
HELIX 100 100 TYR E 69 LEU E 80 1 12
HELIX 101 101 LYS E 82 ASP E 84 5 3
HELIX 102 102 PRO E 105 LEU E 113 5 9
HELIX 103 103 PRO E 114 ARG E 133 1 20
HELIX 104 104 THR E 141 PHE E 158 1 18
HELIX 105 105 PHE E 158 ALA E 168 1 11
HELIX 106 106 PRO E 170 MET E 174 5 5
HELIX 107 107 ASN E 187 GLY E 198 1 12
HELIX 108 108 THR E 218 THR E 228 1 11
HELIX 109 109 LEU E 229 GLU E 232 5 4
HELIX 110 110 GLU E 238 GLY E 240 5 3
HELIX 111 111 ALA E 270 ASN E 279 1 10
HELIX 112 112 ASP E 280 LYS E 288 1 9
HELIX 113 113 PHE E 331 TYR E 334 5 4
HELIX 114 114 SER E 335 GLN E 339 5 5
HELIX 115 115 ASN E 383 THR E 398 1 16
HELIX 116 116 GLU E 425 ASP E 439 1 15
HELIX 117 117 ARG E 452 GLY E 456 5 5
HELIX 118 118 ASN E 457 GLY E 475 1 19
HELIX 119 119 GLU E 478 TYR E 483 1 6
HELIX 120 120 TYR E 483 GLY E 489 1 7
HELIX 121 121 ASP E 499 LEU E 511 1 13
HELIX 122 122 GLY F 16 ASP F 30 1 15
HELIX 123 123 GLY F 44 SER F 48 5 5
HELIX 124 124 TYR F 69 LEU F 80 1 12
HELIX 125 125 LYS F 82 ASP F 84 5 3
HELIX 126 126 PRO F 105 LEU F 113 5 9
HELIX 127 127 PRO F 114 ARG F 133 1 20
HELIX 128 128 THR F 141 PHE F 158 1 18
HELIX 129 129 PHE F 158 ALA F 168 1 11
HELIX 130 130 PRO F 170 MET F 174 5 5
HELIX 131 131 CYS F 176 GLY F 180 5 5
HELIX 132 132 ASN F 187 GLY F 198 1 12
HELIX 133 133 THR F 218 THR F 228 1 11
HELIX 134 134 LEU F 229 GLU F 232 5 4
HELIX 135 135 GLU F 238 GLY F 240 5 3
HELIX 136 136 ALA F 270 ASN F 279 1 10
HELIX 137 137 ASP F 280 LYS F 288 1 9
HELIX 138 138 PHE F 331 TYR F 334 5 4
HELIX 139 139 SER F 335 GLN F 339 5 5
HELIX 140 140 ASN F 383 THR F 398 1 16
HELIX 141 141 GLU F 425 ASP F 439 1 15
HELIX 142 142 ARG F 452 GLY F 456 5 5
HELIX 143 143 ASN F 457 GLY F 475 1 19
HELIX 144 144 GLU F 478 TYR F 483 1 6
HELIX 145 145 TYR F 483 GLY F 489 1 7
HELIX 146 146 ASP F 499 LEU F 511 1 13
HELIX 147 147 GLY G 16 ASP G 30 1 15
HELIX 148 148 GLY G 44 ALA G 47 5 4
HELIX 149 149 TYR G 69 LEU G 80 1 12
HELIX 150 150 LYS G 82 ASP G 84 5 3
HELIX 151 151 PRO G 105 LEU G 113 5 9
HELIX 152 152 PRO G 114 ARG G 133 1 20
HELIX 153 153 THR G 141 PHE G 158 1 18
HELIX 154 154 PHE G 158 ALA G 168 1 11
HELIX 155 155 PRO G 170 MET G 174 5 5
HELIX 156 156 CYS G 176 GLY G 180 5 5
HELIX 157 157 ASN G 187 GLY G 198 1 12
HELIX 158 158 THR G 218 THR G 228 1 11
HELIX 159 159 LEU G 229 GLU G 232 5 4
HELIX 160 160 GLU G 238 GLY G 240 5 3
HELIX 161 161 ALA G 270 ASN G 279 1 10
HELIX 162 162 ASP G 280 LYS G 288 1 9
HELIX 163 163 PHE G 331 TYR G 334 5 4
HELIX 164 164 SER G 335 GLN G 339 5 5
HELIX 165 165 ASN G 383 THR G 398 1 16
HELIX 166 166 GLU G 425 ASP G 439 1 15
HELIX 167 167 ARG G 452 GLY G 456 5 5
HELIX 168 168 ASN G 457 GLY G 475 1 19
HELIX 169 169 GLU G 478 TYR G 483 1 6
HELIX 170 170 TYR G 483 GLY G 489 1 7
HELIX 171 171 ASP G 499 ALA G 509 1 11
HELIX 172 172 GLY H 16 ASP H 30 1 15
HELIX 173 173 GLY H 44 SER H 48 5 5
HELIX 174 174 TYR H 69 LEU H 80 1 12
HELIX 175 175 LYS H 82 ASP H 84 5 3
HELIX 176 176 PRO H 105 LEU H 113 5 9
HELIX 177 177 PRO H 114 ARG H 133 1 20
HELIX 178 178 THR H 141 PHE H 158 1 18
HELIX 179 179 PHE H 158 ALA H 168 1 11
HELIX 180 180 PRO H 170 MET H 174 5 5
HELIX 181 181 ASN H 187 GLY H 198 1 12
HELIX 182 182 THR H 218 ASN H 227 1 10
HELIX 183 183 THR H 228 LEU H 229 5 2
HELIX 184 184 PRO H 230 GLU H 232 5 3
HELIX 185 185 GLU H 238 GLY H 240 5 3
HELIX 186 186 ALA H 270 ASN H 279 1 10
HELIX 187 187 ASP H 280 LYS H 288 1 9
HELIX 188 188 PHE H 331 TYR H 334 5 4
HELIX 189 189 ASN H 383 THR H 398 1 16
HELIX 190 190 GLU H 425 ASP H 439 1 15
HELIX 191 191 ARG H 452 GLY H 456 5 5
HELIX 192 192 ASN H 457 GLY H 475 1 19
HELIX 193 193 GLU H 478 TYR H 483 1 6
HELIX 194 194 TYR H 483 GLY H 489 1 7
HELIX 195 195 ASP H 499 LEU H 511 1 13
SHEET 1 A 6 THR A 234 PHE A 236 0
SHEET 2 A 6 TRP A 34 ASP A 38 1 N ASP A 38 O ARG A 235
SHEET 3 A 6 ILE A 6 ILE A 13 1 N VAL A 12 O MET A 35
SHEET 4 A 6 THR A 259 SER A 267 1 O GLY A 261 N ILE A 6
SHEET 5 A 6 THR A 251 LEU A 254 -1 N VAL A 252 O ILE A 260
SHEET 6 A 6 VAL A 242 ASN A 246 -1 N THR A 243 O THR A 253
SHEET 1 B 5 THR A 234 PHE A 236 0
SHEET 2 B 5 TRP A 34 ASP A 38 1 N ASP A 38 O ARG A 235
SHEET 3 B 5 ILE A 6 ILE A 13 1 N VAL A 12 O MET A 35
SHEET 4 B 5 THR A 259 SER A 267 1 O GLY A 261 N ILE A 6
SHEET 5 B 5 ILE A 442 SER A 444 1 O TRP A 443 N LEU A 265
SHEET 1 C 2 THR A 49 VAL A 51 0
SHEET 2 C 2 LEU A 57 ASP A 59 -1 O TYR A 58 N ASP A 50
SHEET 1 D 2 TRP A 86 GLN A 90 0
SHEET 2 D 2 THR A 209 PRO A 213 -1 O PHE A 210 N HIS A 89
SHEET 1 E 8 GLN A 100 PRO A 103 0
SHEET 2 E 8 SER A 93 CYS A 97 -1 N VAL A 95 O VAL A 102
SHEET 3 E 8 TRP A 315 TYR A 317 1 O TYR A 317 N ARG A 96
SHEET 4 E 8 ARG A 327 THR A 329 -1 O ALA A 328 N LEU A 316
SHEET 5 E 8 TYR A 367 GLU A 376 -1 O MET A 371 N THR A 329
SHEET 6 E 8 TYR A 292 ARG A 303 -1 N ILE A 298 O LEU A 372
SHEET 7 E 8 GLU A 406 PRO A 420 -1 O PHE A 415 N THR A 295
SHEET 8 E 8 GLN A 350 LEU A 351 -1 N GLN A 350 O ILE A 407
SHEET 1 F 6 THR B 234 PHE B 236 0
SHEET 2 F 6 TRP B 34 ASP B 38 1 N ILE B 36 O ARG B 235
SHEET 3 F 6 ILE B 6 ILE B 13 1 N VAL B 12 O MET B 35
SHEET 4 F 6 THR B 259 SER B 267 1 O GLY B 261 N ILE B 6
SHEET 5 F 6 THR B 251 LEU B 254 -1 N VAL B 252 O ILE B 260
SHEET 6 F 6 VAL B 242 ASN B 246 -1 N LYS B 244 O THR B 253
SHEET 1 G 5 THR B 234 PHE B 236 0
SHEET 2 G 5 TRP B 34 ASP B 38 1 N ILE B 36 O ARG B 235
SHEET 3 G 5 ILE B 6 ILE B 13 1 N VAL B 12 O MET B 35
SHEET 4 G 5 THR B 259 SER B 267 1 O GLY B 261 N ILE B 6
SHEET 5 G 5 ILE B 442 SER B 444 1 O TRP B 443 N LEU B 265
SHEET 1 H 2 ASP B 50 VAL B 51 0
SHEET 2 H 2 LEU B 57 TYR B 58 -1 O TYR B 58 N ASP B 50
SHEET 1 I 2 TRP B 86 GLN B 90 0
SHEET 2 I 2 THR B 209 PRO B 213 -1 O PHE B 210 N HIS B 89
SHEET 1 J 8 GLN B 100 PRO B 103 0
SHEET 2 J 8 SER B 93 CYS B 97 -1 N VAL B 95 O VAL B 102
SHEET 3 J 8 TRP B 315 TYR B 317 1 O TYR B 317 N ARG B 96
SHEET 4 J 8 ARG B 327 THR B 329 -1 O ALA B 328 N LEU B 316
SHEET 5 J 8 TYR B 367 GLU B 376 -1 O MET B 371 N THR B 329
SHEET 6 J 8 TYR B 292 ARG B 303 -1 N ILE B 298 O LEU B 372
SHEET 7 J 8 GLU B 406 PRO B 420 -1 O VAL B 408 N GLY B 301
SHEET 8 J 8 GLN B 350 LEU B 351 -1 N GLN B 350 O ILE B 407
SHEET 1 K 2 LEU B 346 PRO B 347 0
SHEET 2 K 2 ALA B 362 LYS B 363 -1 O LYS B 363 N LEU B 346
SHEET 1 L 4 ILE C 6 SER C 7 0
SHEET 2 L 4 THR C 259 GLY C 261 1 O GLY C 261 N ILE C 6
SHEET 3 L 4 THR C 251 LEU C 254 -1 N VAL C 252 O ILE C 260
SHEET 4 L 4 VAL C 242 ASN C 246 -1 N THR C 243 O THR C 253
SHEET 1 M 5 THR C 234 PHE C 236 0
SHEET 2 M 5 TRP C 34 ASP C 38 1 N ASP C 38 O ARG C 235
SHEET 3 M 5 VAL C 10 ILE C 13 1 N VAL C 12 O MET C 35
SHEET 4 M 5 LYS C 264 SER C 267 1 O VAL C 266 N LEU C 11
SHEET 5 M 5 ILE C 442 SER C 444 1 O TRP C 443 N LEU C 265
SHEET 1 N 2 THR C 49 VAL C 51 0
SHEET 2 N 2 LEU C 57 ASP C 59 -1 O TYR C 58 N ASP C 50
SHEET 1 O 2 TRP C 86 GLN C 90 0
SHEET 2 O 2 THR C 209 PRO C 213 -1 O PHE C 210 N HIS C 89
SHEET 1 P 8 GLN C 100 PRO C 103 0
SHEET 2 P 8 SER C 93 CYS C 97 -1 N VAL C 95 O VAL C 102
SHEET 3 P 8 TRP C 315 TYR C 317 1 O TYR C 317 N ARG C 96
SHEET 4 P 8 ARG C 327 THR C 329 -1 O ALA C 328 N LEU C 316
SHEET 5 P 8 TYR C 367 GLU C 376 -1 O MET C 371 N THR C 329
SHEET 6 P 8 TYR C 292 ARG C 303 -1 N ILE C 298 O LEU C 372
SHEET 7 P 8 GLU C 406 PRO C 420 -1 O TYR C 411 N GLY C 299
SHEET 8 P 8 GLN C 350 LEU C 351 -1 N GLN C 350 O ILE C 407
SHEET 1 Q 6 THR D 234 PHE D 236 0
SHEET 2 Q 6 TRP D 34 ASP D 38 1 N ASP D 38 O ARG D 235
SHEET 3 Q 6 ILE D 6 ILE D 13 1 N VAL D 12 O MET D 35
SHEET 4 Q 6 THR D 259 SER D 267 1 O GLY D 261 N ILE D 6
SHEET 5 Q 6 THR D 251 LEU D 254 -1 N VAL D 252 O ILE D 260
SHEET 6 Q 6 VAL D 242 ASN D 246 -1 N LYS D 244 O THR D 253
SHEET 1 R 5 THR D 234 PHE D 236 0
SHEET 2 R 5 TRP D 34 ASP D 38 1 N ASP D 38 O ARG D 235
SHEET 3 R 5 ILE D 6 ILE D 13 1 N VAL D 12 O MET D 35
SHEET 4 R 5 THR D 259 SER D 267 1 O GLY D 261 N ILE D 6
SHEET 5 R 5 ILE D 442 SER D 444 1 O TRP D 443 N LEU D 265
SHEET 1 S 2 THR D 49 VAL D 51 0
SHEET 2 S 2 LEU D 57 ASP D 59 -1 O TYR D 58 N ASP D 50
SHEET 1 T 2 TRP D 86 GLN D 90 0
SHEET 2 T 2 THR D 209 PRO D 213 -1 O PHE D 210 N HIS D 89
SHEET 1 U 8 GLN D 100 PRO D 103 0
SHEET 2 U 8 SER D 93 CYS D 97 -1 N VAL D 95 O VAL D 102
SHEET 3 U 8 TRP D 315 TYR D 317 1 O TYR D 317 N ARG D 96
SHEET 4 U 8 ARG D 327 THR D 329 -1 O ALA D 328 N LEU D 316
SHEET 5 U 8 TYR D 367 GLU D 376 -1 O MET D 371 N THR D 329
SHEET 6 U 8 TYR D 292 ARG D 303 -1 N ILE D 298 O LEU D 372
SHEET 7 U 8 GLU D 406 PRO D 420 -1 O TYR D 411 N GLY D 299
SHEET 8 U 8 GLN D 350 LEU D 351 -1 N GLN D 350 O ILE D 407
SHEET 1 V 6 THR E 234 PHE E 236 0
SHEET 2 V 6 TRP E 34 ASP E 38 1 N ASP E 38 O ARG E 235
SHEET 3 V 6 ILE E 6 ILE E 13 1 N VAL E 12 O MET E 35
SHEET 4 V 6 THR E 259 SER E 267 1 O GLY E 261 N ILE E 6
SHEET 5 V 6 THR E 251 LEU E 254 -1 N VAL E 252 O ILE E 260
SHEET 6 V 6 VAL E 242 ASN E 246 -1 N THR E 243 O THR E 253
SHEET 1 W 5 THR E 234 PHE E 236 0
SHEET 2 W 5 TRP E 34 ASP E 38 1 N ASP E 38 O ARG E 235
SHEET 3 W 5 ILE E 6 ILE E 13 1 N VAL E 12 O MET E 35
SHEET 4 W 5 THR E 259 SER E 267 1 O GLY E 261 N ILE E 6
SHEET 5 W 5 ILE E 442 SER E 444 1 O TRP E 443 N LEU E 265
SHEET 1 X 2 ASP E 50 VAL E 51 0
SHEET 2 X 2 LEU E 57 TYR E 58 -1 O TYR E 58 N ASP E 50
SHEET 1 Y 2 TRP E 86 GLN E 90 0
SHEET 2 Y 2 THR E 209 PRO E 213 -1 O PHE E 210 N HIS E 89
SHEET 1 Z 8 GLN E 100 PRO E 103 0
SHEET 2 Z 8 SER E 93 CYS E 97 -1 N VAL E 95 O VAL E 102
SHEET 3 Z 8 TRP E 315 TYR E 317 1 O TYR E 317 N ARG E 96
SHEET 4 Z 8 ARG E 327 THR E 329 -1 O ALA E 328 N LEU E 316
SHEET 5 Z 8 TYR E 367 GLU E 376 -1 O MET E 371 N THR E 329
SHEET 6 Z 8 TYR E 292 ARG E 303 -1 N ILE E 298 O LEU E 372
SHEET 7 Z 8 GLU E 406 PRO E 420 -1 O TYR E 411 N GLY E 299
SHEET 8 Z 8 GLN E 350 LEU E 351 -1 N GLN E 350 O ILE E 407
SHEET 1 AA 4 ILE F 6 SER F 7 0
SHEET 2 AA 4 THR F 259 GLY F 261 1 O GLY F 261 N ILE F 6
SHEET 3 AA 4 THR F 251 LEU F 254 -1 N VAL F 252 O ILE F 260
SHEET 4 AA 4 VAL F 242 ASN F 246 -1 N THR F 243 O THR F 253
SHEET 1 AB 5 THR F 234 PHE F 236 0
SHEET 2 AB 5 TRP F 34 ASP F 38 1 N ILE F 36 O ARG F 235
SHEET 3 AB 5 VAL F 10 ILE F 13 1 N VAL F 12 O MET F 35
SHEET 4 AB 5 LYS F 264 SER F 267 1 O VAL F 266 N LEU F 11
SHEET 5 AB 5 ILE F 442 SER F 444 1 O TRP F 443 N LEU F 265
SHEET 1 AC 2 ASP F 50 VAL F 51 0
SHEET 2 AC 2 LEU F 57 TYR F 58 -1 O TYR F 58 N ASP F 50
SHEET 1 AD 2 TRP F 86 GLN F 90 0
SHEET 2 AD 2 THR F 209 PRO F 213 -1 O PHE F 210 N HIS F 89
SHEET 1 AE 8 GLN F 100 PRO F 103 0
SHEET 2 AE 8 SER F 93 CYS F 97 -1 N VAL F 95 O VAL F 102
SHEET 3 AE 8 TRP F 315 TYR F 317 1 O TYR F 317 N ARG F 96
SHEET 4 AE 8 ARG F 327 THR F 329 -1 O ALA F 328 N LEU F 316
SHEET 5 AE 8 TYR F 367 GLU F 376 -1 O MET F 371 N THR F 329
SHEET 6 AE 8 TYR F 292 ARG F 303 -1 N ILE F 298 O LEU F 372
SHEET 7 AE 8 GLU F 406 PRO F 420 -1 O TYR F 411 N GLY F 299
SHEET 8 AE 8 GLN F 350 LEU F 351 -1 N GLN F 350 O ILE F 407
SHEET 1 AF 2 LEU F 346 PRO F 347 0
SHEET 2 AF 2 ALA F 362 LYS F 363 -1 O LYS F 363 N LEU F 346
SHEET 1 AG 6 THR G 234 PHE G 236 0
SHEET 2 AG 6 TRP G 34 ASP G 38 1 N ASP G 38 O ARG G 235
SHEET 3 AG 6 ILE G 6 ILE G 13 1 N VAL G 12 O MET G 35
SHEET 4 AG 6 THR G 259 SER G 267 1 O GLY G 261 N ILE G 6
SHEET 5 AG 6 THR G 251 LEU G 254 -1 N VAL G 252 O ILE G 260
SHEET 6 AG 6 VAL G 242 ASN G 246 -1 N THR G 243 O THR G 253
SHEET 1 AH 5 THR G 234 PHE G 236 0
SHEET 2 AH 5 TRP G 34 ASP G 38 1 N ASP G 38 O ARG G 235
SHEET 3 AH 5 ILE G 6 ILE G 13 1 N VAL G 12 O MET G 35
SHEET 4 AH 5 THR G 259 SER G 267 1 O GLY G 261 N ILE G 6
SHEET 5 AH 5 ILE G 442 SER G 444 1 O TRP G 443 N LEU G 265
SHEET 1 AI 2 THR G 49 VAL G 51 0
SHEET 2 AI 2 LEU G 57 ASP G 59 -1 O TYR G 58 N ASP G 50
SHEET 1 AJ 2 TRP G 86 GLN G 90 0
SHEET 2 AJ 2 THR G 209 PRO G 213 -1 O PHE G 210 N HIS G 89
SHEET 1 AK 8 GLN G 100 PRO G 103 0
SHEET 2 AK 8 SER G 93 CYS G 97 -1 N VAL G 95 O VAL G 102
SHEET 3 AK 8 TRP G 315 TYR G 317 1 O TYR G 317 N ARG G 96
SHEET 4 AK 8 ARG G 327 THR G 329 -1 O ALA G 328 N LEU G 316
SHEET 5 AK 8 TYR G 367 GLU G 376 -1 O MET G 371 N THR G 329
SHEET 6 AK 8 TYR G 292 ARG G 303 -1 N HIS G 296 O VAL G 374
SHEET 7 AK 8 GLU G 406 PRO G 420 -1 O VAL G 408 N GLY G 301
SHEET 8 AK 8 GLN G 350 LEU G 351 -1 N GLN G 350 O ILE G 407
SHEET 1 AL 6 THR H 234 PHE H 236 0
SHEET 2 AL 6 TRP H 34 ASP H 38 1 N ASP H 38 O ARG H 235
SHEET 3 AL 6 ILE H 6 ILE H 13 1 N VAL H 12 O MET H 35
SHEET 4 AL 6 THR H 259 SER H 267 1 O GLY H 261 N ILE H 6
SHEET 5 AL 6 THR H 251 LEU H 254 -1 N VAL H 252 O ILE H 260
SHEET 6 AL 6 VAL H 242 ASN H 246 -1 N LYS H 244 O THR H 253
SHEET 1 AM 5 THR H 234 PHE H 236 0
SHEET 2 AM 5 TRP H 34 ASP H 38 1 N ASP H 38 O ARG H 235
SHEET 3 AM 5 ILE H 6 ILE H 13 1 N VAL H 12 O MET H 35
SHEET 4 AM 5 THR H 259 SER H 267 1 O GLY H 261 N ILE H 6
SHEET 5 AM 5 ILE H 442 SER H 444 1 O TRP H 443 N LEU H 265
SHEET 1 AN 2 ASP H 50 VAL H 51 0
SHEET 2 AN 2 LEU H 57 TYR H 58 -1 O TYR H 58 N ASP H 50
SHEET 1 AO 2 TRP H 86 GLN H 90 0
SHEET 2 AO 2 THR H 209 PRO H 213 -1 O PHE H 210 N HIS H 89
SHEET 1 AP 8 GLN H 100 PRO H 103 0
SHEET 2 AP 8 SER H 93 CYS H 97 -1 N VAL H 95 O VAL H 102
SHEET 3 AP 8 TRP H 315 TYR H 317 1 O TYR H 317 N ARG H 96
SHEET 4 AP 8 ARG H 327 THR H 329 -1 O ALA H 328 N LEU H 316
SHEET 5 AP 8 TYR H 367 GLU H 376 -1 O MET H 371 N THR H 329
SHEET 6 AP 8 TYR H 292 ARG H 303 -1 N ILE H 298 O LEU H 372
SHEET 7 AP 8 GLU H 406 PRO H 420 -1 O TYR H 411 N GLY H 299
SHEET 8 AP 8 GLN H 350 LEU H 351 -1 N GLN H 350 O ILE H 407
SHEET 1 AQ 2 LEU H 346 PRO H 347 0
SHEET 2 AQ 2 ALA H 362 LYS H 363 -1 O LYS H 363 N LEU H 346
CISPEP 1 TYR A 104 PRO A 105 0 -0.43
CISPEP 2 GLY A 365 PRO A 366 0 1.45
CISPEP 3 TYR B 104 PRO B 105 0 -0.91
CISPEP 4 GLY B 365 PRO B 366 0 0.40
CISPEP 5 TYR C 104 PRO C 105 0 0.11
CISPEP 6 GLY C 365 PRO C 366 0 -1.19
CISPEP 7 TYR D 104 PRO D 105 0 -2.14
CISPEP 8 GLY D 365 PRO D 366 0 -1.88
CISPEP 9 TYR E 104 PRO E 105 0 -2.90
CISPEP 10 GLY E 365 PRO E 366 0 1.84
CISPEP 11 TYR F 104 PRO F 105 0 -3.53
CISPEP 12 GLY F 365 PRO F 366 0 -0.83
CISPEP 13 TYR G 104 PRO G 105 0 -3.72
CISPEP 14 GLY G 365 PRO G 366 0 0.50
CISPEP 15 TYR H 104 PRO H 105 0 -0.44
CISPEP 16 GLY H 365 PRO H 366 0 -0.06
SITE 1 AC1 16 TYR A 104 PHE A 106 GLN A 107 PHE A 142
SITE 2 AC1 16 PHE A 158 MET A 159 ASN A 163 TRP A 167
SITE 3 AC1 16 ARG A 182 VAL A 183 TYR A 317 ARG A 327
SITE 4 AC1 16 TYR A 419 TYR A 453 HOH A 554 HOH A1052
SITE 1 AC2 30 GLY A 14 GLY A 16 PRO A 17 THR A 18
SITE 2 AC2 30 ASP A 38 SER A 39 GLY A 45 LEU A 46
SITE 3 AC2 30 VAL A 60 GLY A 62 HIS A 63 VAL A 64
SITE 4 AC2 30 GLY A 240 LYS A 241 VAL A 242 MET A 269
SITE 5 AC2 30 THR A 295 GLU A 373 GLY A 418 TYR A 419
SITE 6 AC2 30 GLY A 446 ARG A 447 GLY A 456 ASN A 457
SITE 7 AC2 30 GLN A 458 SER A 461 HOH A 653 HOH A 798
SITE 8 AC2 30 HOH A 807 HOH A 833
SITE 1 AC3 1 GLN A 358
SITE 1 AC4 1 ALA A 270
SITE 1 AC5 17 VAL B 95 TYR B 104 PHE B 106 GLN B 107
SITE 2 AC5 17 PHE B 158 MET B 159 ASN B 163 TRP B 167
SITE 3 AC5 17 ARG B 182 VAL B 183 TYR B 317 ARG B 327
SITE 4 AC5 17 TYR B 419 TYR B 453 HOH B 566 HOH B 936
SITE 5 AC5 17 HOH B1053
SITE 1 AC6 29 GLY B 14 GLY B 16 PRO B 17 THR B 18
SITE 2 AC6 29 ASP B 38 SER B 39 GLY B 45 LEU B 46
SITE 3 AC6 29 VAL B 60 GLY B 62 HIS B 63 VAL B 64
SITE 4 AC6 29 GLY B 240 VAL B 242 THR B 295 GLU B 373
SITE 5 AC6 29 GLY B 418 TYR B 419 GLY B 446 ARG B 447
SITE 6 AC6 29 GLY B 456 ASN B 457 GLN B 458 SER B 461
SITE 7 AC6 29 HOH B 558 HOH B 588 HOH B 605 HOH B 606
SITE 8 AC6 29 HOH B 808
SITE 1 AC7 17 VAL C 95 TYR C 104 PHE C 106 GLN C 107
SITE 2 AC7 17 PHE C 158 MET C 159 ASN C 163 TRP C 167
SITE 3 AC7 17 ARG C 182 VAL C 183 TYR C 317 ARG C 327
SITE 4 AC7 17 TYR C 419 TYR C 453 HOH C 589 HOH C 969
SITE 5 AC7 17 HOH C1054
SITE 1 AC8 25 GLY C 14 GLY C 16 PRO C 17 THR C 18
SITE 2 AC8 25 ASP C 38 SER C 39 GLY C 45 LEU C 46
SITE 3 AC8 25 VAL C 60 HIS C 63 VAL C 64 GLY C 240
SITE 4 AC8 25 VAL C 242 MET C 269 GLU C 373 GLY C 418
SITE 5 AC8 25 GLY C 446 ARG C 447 GLY C 456 ASN C 457
SITE 6 AC8 25 GLN C 458 SER C 461 HOH C 514 HOH C 519
SITE 7 AC8 25 HOH C 619
SITE 1 AC9 2 GLN C 358 HOH C 618
SITE 1 BC1 16 VAL D 95 TYR D 104 PHE D 106 GLN D 107
SITE 2 BC1 16 PHE D 142 PHE D 158 MET D 159 ASN D 163
SITE 3 BC1 16 TRP D 167 ARG D 182 VAL D 183 TYR D 317
SITE 4 BC1 16 ARG D 327 TYR D 419 TYR D 453 HOH D 546
SITE 1 BC2 31 GLY D 14 GLY D 16 PRO D 17 THR D 18
SITE 2 BC2 31 ASP D 38 SER D 39 GLY D 45 LEU D 46
SITE 3 BC2 31 ALA D 47 VAL D 60 GLY D 62 HIS D 63
SITE 4 BC2 31 VAL D 64 GLY D 240 LYS D 241 VAL D 242
SITE 5 BC2 31 MET D 269 THR D 295 GLU D 373 GLY D 418
SITE 6 BC2 31 TYR D 419 GLY D 446 ARG D 447 GLY D 456
SITE 7 BC2 31 ASN D 457 GLN D 458 SER D 461 HOH D 517
SITE 8 BC2 31 HOH D 558 HOH D 585 HOH D 799
SITE 1 BC3 15 TYR E 104 PHE E 106 GLN E 107 PHE E 158
SITE 2 BC3 15 MET E 159 ASN E 163 TRP E 167 ARG E 182
SITE 3 BC3 15 VAL E 183 TYR E 317 ARG E 327 TYR E 419
SITE 4 BC3 15 TYR E 453 HOH E 547 HOH E 576
SITE 1 BC4 29 GLY E 14 GLY E 16 PRO E 17 THR E 18
SITE 2 BC4 29 ASP E 38 SER E 39 GLY E 45 LEU E 46
SITE 3 BC4 29 VAL E 60 GLY E 62 HIS E 63 VAL E 64
SITE 4 BC4 29 GLY E 240 VAL E 242 MET E 269 THR E 295
SITE 5 BC4 29 GLU E 373 GLY E 418 TYR E 419 GLY E 446
SITE 6 BC4 29 ARG E 447 GLY E 456 ASN E 457 GLN E 458
SITE 7 BC4 29 SER E 461 HOH E 517 HOH E 558 HOH E 586
SITE 8 BC4 29 HOH E 809
SITE 1 BC5 16 VAL F 95 TYR F 104 PHE F 106 GLN F 107
SITE 2 BC5 16 PHE F 158 MET F 159 ASN F 163 TRP F 167
SITE 3 BC5 16 ARG F 182 VAL F 183 TYR F 317 ARG F 327
SITE 4 BC5 16 TYR F 419 TYR F 453 HOH F 555 HOH F 564
SITE 1 BC6 28 GLY F 14 GLY F 16 PRO F 17 THR F 18
SITE 2 BC6 28 ASP F 38 SER F 39 GLY F 45 LEU F 46
SITE 3 BC6 28 ALA F 47 VAL F 60 GLY F 62 HIS F 63
SITE 4 BC6 28 VAL F 64 GLY F 240 VAL F 242 MET F 269
SITE 5 BC6 28 THR F 295 GLU F 373 GLY F 418 TYR F 419
SITE 6 BC6 28 GLY F 446 ARG F 447 GLY F 456 ASN F 457
SITE 7 BC6 28 GLN F 458 SER F 461 HOH F 513 HOH F 515
SITE 1 BC7 1 GLN F 358
SITE 1 BC8 1 ALA F 270
SITE 1 BC9 14 TYR G 104 PHE G 106 GLN G 107 PHE G 158
SITE 2 BC9 14 MET G 159 ASN G 163 TRP G 167 ARG G 182
SITE 3 BC9 14 VAL G 183 TYR G 317 ARG G 327 TYR G 419
SITE 4 BC9 14 TYR G 453 HOH G1049
SITE 1 CC1 29 GLY G 14 GLY G 16 PRO G 17 THR G 18
SITE 2 CC1 29 ASP G 38 SER G 39 GLY G 45 LEU G 46
SITE 3 CC1 29 ALA G 47 VAL G 60 HIS G 63 VAL G 64
SITE 4 CC1 29 GLY G 240 LYS G 241 VAL G 242 MET G 269
SITE 5 CC1 29 THR G 295 GLU G 373 GLY G 418 TYR G 419
SITE 6 CC1 29 GLY G 446 ARG G 447 GLY G 456 ASN G 457
SITE 7 CC1 29 GLN G 458 SER G 461 HOH G 512 HOH G 554
SITE 8 CC1 29 HOH G 556
SITE 1 CC2 15 VAL H 95 TYR H 104 PHE H 106 GLN H 107
SITE 2 CC2 15 PHE H 158 MET H 159 ASN H 163 TRP H 167
SITE 3 CC2 15 ARG H 182 VAL H 183 TYR H 317 ARG H 327
SITE 4 CC2 15 TYR H 419 TYR H 453 HOH H 875
SITE 1 CC3 27 GLY H 14 GLY H 16 PRO H 17 THR H 18
SITE 2 CC3 27 ASP H 38 SER H 39 GLY H 45 LEU H 46
SITE 3 CC3 27 VAL H 60 GLY H 62 HIS H 63 VAL H 64
SITE 4 CC3 27 GLY H 240 VAL H 242 MET H 269 THR H 295
SITE 5 CC3 27 GLU H 373 GLY H 418 TYR H 419 GLY H 446
SITE 6 CC3 27 ARG H 447 GLY H 456 ASN H 457 GLN H 458
SITE 7 CC3 27 SER H 461 HOH H 806 HOH H 810
SITE 1 CC4 1 GLN H 358
CRYST1 71.440 129.200 172.820 90.07 84.22 82.24 P 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013998 -0.001907 -0.001446 0.00000
SCALE2 0.000000 0.007811 0.000117 0.00000
SCALE3 0.000000 0.000000 0.005817 0.00000
MTRIX1 1 -0.979090 0.001222 0.203423 36.90060 1
MTRIX2 1 -0.081816 -0.917906 -0.388271 61.17880 1
MTRIX3 1 0.186248 -0.396795 0.898813 9.11182 1
MTRIX1 2 -0.964122 0.264699 -0.020057 -15.26790 1
MTRIX2 2 0.264773 0.964310 -0.001090 -63.38590 1
MTRIX3 2 0.019052 -0.006361 -0.999798 -35.45130 1
MTRIX1 3 0.941516 -0.254810 -0.220497 12.87460 1
MTRIX2 3 -0.254864 -0.966551 0.028701 56.56320 1
MTRIX3 3 -0.220435 0.029174 -0.974965 49.72250 1
MTRIX1 4 0.999941 0.001828 0.010696 31.63910 1
MTRIX2 4 0.002285 0.928161 -0.372172 -84.80250 1
MTRIX3 4 -0.010608 0.372174 0.928102 42.95640 1
MTRIX1 5 -0.965160 0.260191 0.027679 33.72860 1
MTRIX2 5 0.251940 0.895533 0.366806 -11.12920 1
MTRIX3 5 0.070653 0.360999 -0.929886 34.10220 1
MTRIX1 6 0.947826 -0.263300 -0.179721 27.81470 1
MTRIX2 6 -0.178165 -0.905015 0.386270 15.12450 1
MTRIX3 6 -0.264355 -0.334096 -0.904708 -48.50650 1
MTRIX1 7 -0.978944 0.003155 0.204106 6.53731 1
MTRIX2 7 -0.009579 -0.999489 -0.030490 -8.02302 1
MTRIX3 7 0.203905 -0.031803 0.978474 86.22690 1
(ATOM LINES ARE NOT SHOWN.)
END