HEADER TRANSCRIPTION 06-SEP-05 2AXU
TITLE STRUCTURE OF PRGX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRGX;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROCOCCUS FAECALIS;
SOURCE 3 ORGANISM_TAXID: 1351;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS REPRESSOR, PHEROMONE, DNA BINDING, DOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR K.SHI,C.K.BROWN,Z.Y.GU,B.K.KOZLOWICZ,G.M.DUNNY,
AUTHOR 2 D.H.OHLENDORF,C.A.EARHART
REVDAT 2 24-FEB-09 2AXU 1 VERSN
REVDAT 1 06-DEC-05 2AXU 0
JRNL AUTH K.SHI,C.K.BROWN,Z.Y.GU,B.K.KOZLOWICZ,G.M.DUNNY,
JRNL AUTH 2 D.H.OHLENDORF,C.A.EARHART
JRNL TITL STRUCTURE OF PEPTIDE SEX PHEROMONE RECEPTOR PRGX
JRNL TITL 2 AND PRGX/PHEROMONE COMPLEXES AND REGULATION OF
JRNL TITL 3 CONJUGATION IN ENTEROCOCCUS FAECALIS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 102 18596 2005
JRNL REFN ISSN 0027-8424
JRNL PMID 16339309
JRNL DOI 10.1073/PNAS.0506163102
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 104010
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5265
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 29763
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 384
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : 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: NULL
REMARK 4
REMARK 4 2AXU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-05.
REMARK 100 THE RCSB ID CODE IS RCSB034442.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-MAR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
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) : 0.97940
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104010
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISO TO Y153C
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, CITRATE-PHOPHATE , PH
REMARK 280 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 67.35900
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 13050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR A 69
REMARK 465 LYS A 70
REMARK 465 GLU A 306
REMARK 465 ASN A 307
REMARK 465 ASN A 308
REMARK 465 PRO A 309
REMARK 465 ILE A 310
REMARK 465 PRO A 311
REMARK 465 GLU A 312
REMARK 465 ILE A 313
REMARK 465 LYS A 314
REMARK 465 GLU A 315
REMARK 465 GLN A 316
REMARK 465 SER A 317
REMARK 465 MSE B 1
REMARK 465 THR B 69
REMARK 465 LYS B 70
REMARK 465 ALA B 304
REMARK 465 ILE B 305
REMARK 465 GLU B 306
REMARK 465 ASN B 307
REMARK 465 ASN B 308
REMARK 465 PRO B 309
REMARK 465 ILE B 310
REMARK 465 PRO B 311
REMARK 465 GLU B 312
REMARK 465 ILE B 313
REMARK 465 LYS B 314
REMARK 465 GLU B 315
REMARK 465 GLN B 316
REMARK 465 SER B 317
REMARK 465 MSE C 1
REMARK 465 PHE C 2
REMARK 465 THR C 69
REMARK 465 LYS C 70
REMARK 465 ALA C 304
REMARK 465 ILE C 305
REMARK 465 GLU C 306
REMARK 465 ASN C 307
REMARK 465 ASN C 308
REMARK 465 PRO C 309
REMARK 465 ILE C 310
REMARK 465 PRO C 311
REMARK 465 GLU C 312
REMARK 465 ILE C 313
REMARK 465 LYS C 314
REMARK 465 GLU C 315
REMARK 465 GLN C 316
REMARK 465 SER C 317
REMARK 465 MSE D 1
REMARK 465 PHE D 2
REMARK 465 THR D 69
REMARK 465 LYS D 70
REMARK 465 VAL D 303
REMARK 465 ALA D 304
REMARK 465 ILE D 305
REMARK 465 GLU D 306
REMARK 465 ASN D 307
REMARK 465 ASN D 308
REMARK 465 PRO D 309
REMARK 465 ILE D 310
REMARK 465 PRO D 311
REMARK 465 GLU D 312
REMARK 465 ILE D 313
REMARK 465 LYS D 314
REMARK 465 GLU D 315
REMARK 465 GLN D 316
REMARK 465 SER D 317
REMARK 465 MSE E 1
REMARK 465 PHE E 2
REMARK 465 THR E 69
REMARK 465 LYS E 70
REMARK 465 ILE E 305
REMARK 465 GLU E 306
REMARK 465 ASN E 307
REMARK 465 ASN E 308
REMARK 465 PRO E 309
REMARK 465 ILE E 310
REMARK 465 PRO E 311
REMARK 465 GLU E 312
REMARK 465 ILE E 313
REMARK 465 LYS E 314
REMARK 465 GLU E 315
REMARK 465 GLN E 316
REMARK 465 SER E 317
REMARK 465 MSE F 1
REMARK 465 PHE F 2
REMARK 465 THR F 69
REMARK 465 LYS F 70
REMARK 465 GLU F 306
REMARK 465 ASN F 307
REMARK 465 ASN F 308
REMARK 465 PRO F 309
REMARK 465 ILE F 310
REMARK 465 PRO F 311
REMARK 465 GLU F 312
REMARK 465 ILE F 313
REMARK 465 LYS F 314
REMARK 465 GLU F 315
REMARK 465 GLN F 316
REMARK 465 SER F 317
REMARK 465 MSE G 1
REMARK 465 THR G 69
REMARK 465 LYS G 70
REMARK 465 ASN G 307
REMARK 465 ASN G 308
REMARK 465 PRO G 309
REMARK 465 ILE G 310
REMARK 465 PRO G 311
REMARK 465 GLU G 312
REMARK 465 ILE G 313
REMARK 465 LYS G 314
REMARK 465 GLU G 315
REMARK 465 GLN G 316
REMARK 465 SER G 317
REMARK 465 MSE H 1
REMARK 465 PHE H 2
REMARK 465 THR H 69
REMARK 465 LYS H 70
REMARK 465 VAL H 303
REMARK 465 ALA H 304
REMARK 465 ILE H 305
REMARK 465 GLU H 306
REMARK 465 ASN H 307
REMARK 465 ASN H 308
REMARK 465 PRO H 309
REMARK 465 ILE H 310
REMARK 465 PRO H 311
REMARK 465 GLU H 312
REMARK 465 ILE H 313
REMARK 465 LYS H 314
REMARK 465 GLU H 315
REMARK 465 GLN H 316
REMARK 465 SER H 317
REMARK 465 MSE I 1
REMARK 465 THR I 69
REMARK 465 LYS I 70
REMARK 465 ALA I 304
REMARK 465 ILE I 305
REMARK 465 GLU I 306
REMARK 465 ASN I 307
REMARK 465 ASN I 308
REMARK 465 PRO I 309
REMARK 465 ILE I 310
REMARK 465 PRO I 311
REMARK 465 GLU I 312
REMARK 465 ILE I 313
REMARK 465 LYS I 314
REMARK 465 GLU I 315
REMARK 465 GLN I 316
REMARK 465 SER I 317
REMARK 465 MSE J 1
REMARK 465 PHE J 2
REMARK 465 LYS J 3
REMARK 465 THR J 69
REMARK 465 LYS J 70
REMARK 465 TYR J 302
REMARK 465 VAL J 303
REMARK 465 ALA J 304
REMARK 465 ILE J 305
REMARK 465 GLU J 306
REMARK 465 ASN J 307
REMARK 465 ASN J 308
REMARK 465 PRO J 309
REMARK 465 ILE J 310
REMARK 465 PRO J 311
REMARK 465 GLU J 312
REMARK 465 ILE J 313
REMARK 465 LYS J 314
REMARK 465 GLU J 315
REMARK 465 GLN J 316
REMARK 465 SER J 317
REMARK 465 MSE K 1
REMARK 465 PHE K 2
REMARK 465 LYS K 3
REMARK 465 THR K 69
REMARK 465 LYS K 70
REMARK 465 ILE K 305
REMARK 465 GLU K 306
REMARK 465 ASN K 307
REMARK 465 ASN K 308
REMARK 465 PRO K 309
REMARK 465 ILE K 310
REMARK 465 PRO K 311
REMARK 465 GLU K 312
REMARK 465 ILE K 313
REMARK 465 LYS K 314
REMARK 465 GLU K 315
REMARK 465 GLN K 316
REMARK 465 SER K 317
REMARK 465 MSE L 1
REMARK 465 THR L 69
REMARK 465 LYS L 70
REMARK 465 VAL L 303
REMARK 465 ALA L 304
REMARK 465 ILE L 305
REMARK 465 GLU L 306
REMARK 465 ASN L 307
REMARK 465 ASN L 308
REMARK 465 PRO L 309
REMARK 465 ILE L 310
REMARK 465 PRO L 311
REMARK 465 GLU L 312
REMARK 465 ILE L 313
REMARK 465 LYS L 314
REMARK 465 GLU L 315
REMARK 465 GLN L 316
REMARK 465 SER L 317
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 LYS A 3 56.91 -98.37
REMARK 500 ASP A 93 -76.61 -45.71
REMARK 500 ARG A 103 -9.60 -54.38
REMARK 500 HIS A 122 -70.64 -57.34
REMARK 500 TYR A 123 45.97 -75.56
REMARK 500 ASN A 124 28.70 33.04
REMARK 500 THR A 146 -36.95 -133.73
REMARK 500 LYS A 173 -60.73 -23.83
REMARK 500 ASP A 248 32.45 -157.19
REMARK 500 LYS A 249 77.50 31.44
REMARK 500 LYS B 3 50.68 -103.49
REMARK 500 SER B 24 93.43 -57.74
REMARK 500 ASP B 38 30.90 70.36
REMARK 500 ARG B 40 120.52 -170.06
REMARK 500 ASN B 88 59.36 -155.90
REMARK 500 PRO B 89 -34.45 -38.78
REMARK 500 ASN B 225 -1.51 76.70
REMARK 500 ASP B 248 34.00 -166.11
REMARK 500 LYS B 249 55.36 36.48
REMARK 500 ASN C 57 130.57 -35.37
REMARK 500 VAL C 72 -36.58 -177.83
REMARK 500 ASN C 73 -154.35 -89.86
REMARK 500 GLU C 74 -77.01 -70.22
REMARK 500 THR C 87 40.17 -81.84
REMARK 500 ASN C 88 57.93 167.78
REMARK 500 PRO C 89 10.07 -57.90
REMARK 500 ASP C 93 -76.42 -43.69
REMARK 500 LYS C 102 2.13 -64.39
REMARK 500 ARG C 103 2.11 -52.37
REMARK 500 GLU C 126 131.40 -18.79
REMARK 500 PHE C 130 -70.68 -69.15
REMARK 500 ILE C 134 -39.92 -32.14
REMARK 500 LEU C 160 -17.57 -46.80
REMARK 500 PRO C 164 152.53 -49.66
REMARK 500 VAL C 168 -9.04 -52.94
REMARK 500 LYS C 208 -74.89 -55.96
REMARK 500 THR C 247 -80.26 -87.02
REMARK 500 ASP C 248 76.89 -118.08
REMARK 500 LYS C 249 66.42 -7.55
REMARK 500 LYS C 293 -38.05 -38.69
REMARK 500 ASN C 301 -154.55 -73.83
REMARK 500 TYR C 302 -71.44 60.13
REMARK 500 ASN D 88 58.25 145.39
REMARK 500 PRO D 89 -14.95 -44.26
REMARK 500 ASP D 93 -71.68 -42.18
REMARK 500 ARG D 103 -15.20 -43.31
REMARK 500 ILE D 117 -18.35 -48.52
REMARK 500 THR D 146 -30.84 -135.42
REMARK 500 VAL D 162 15.59 -152.81
REMARK 500 TYR D 165 -33.99 -38.51
REMARK 500 LYS D 249 59.19 26.01
REMARK 500 ASN D 301 -107.28 -78.60
REMARK 500 PHE E 92 -88.55 -55.47
REMARK 500 ASP E 93 -60.00 -19.70
REMARK 500 GLU E 100 -53.93 -29.70
REMARK 500 ASN E 124 17.49 41.03
REMARK 500 LYS E 221 -8.66 -59.22
REMARK 500 ASN E 225 30.79 76.05
REMARK 500 LYS E 249 78.63 -5.90
REMARK 500 SER F 24 84.30 -51.70
REMARK 500 ARG F 40 114.99 174.66
REMARK 500 LEU F 81 -4.76 -56.38
REMARK 500 THR F 87 45.70 -81.15
REMARK 500 ASN F 88 65.42 169.35
REMARK 500 PRO F 89 9.08 -53.39
REMARK 500 PHE F 92 -86.22 -76.00
REMARK 500 ASP F 93 -64.82 -10.89
REMARK 500 LYS F 102 31.39 -95.05
REMARK 500 ALA F 120 -77.72 -64.18
REMARK 500 HIS F 122 -71.46 -66.22
REMARK 500 VAL F 127 64.18 -151.89
REMARK 500 THR F 133 -11.00 -146.36
REMARK 500 LYS F 249 36.85 38.31
REMARK 500 ASN F 301 40.87 91.99
REMARK 500 TYR F 302 11.05 -170.22
REMARK 500 VAL F 303 -13.97 -143.18
REMARK 500 LYS G 3 52.62 -106.00
REMARK 500 SER G 24 73.51 -62.45
REMARK 500 VAL G 72 -84.80 -121.36
REMARK 500 ASN G 88 70.74 -155.21
REMARK 500 PRO G 89 5.36 -55.27
REMARK 500 PHE G 92 -76.43 -64.97
REMARK 500 ASP G 93 -45.14 -24.45
REMARK 500 LYS G 94 -75.87 -61.91
REMARK 500 PHE G 96 -9.02 -52.35
REMARK 500 LYS G 102 71.80 -104.37
REMARK 500 ASN G 124 2.84 55.68
REMARK 500 ILE G 125 98.83 -59.33
REMARK 500 VAL G 127 74.78 -155.85
REMARK 500 PRO G 128 14.20 -61.20
REMARK 500 THR G 135 24.13 -64.33
REMARK 500 SER G 136 -34.25 -146.64
REMARK 500 TYR G 142 -54.88 -120.97
REMARK 500 ASP G 143 102.60 -45.93
REMARK 500 LYS G 144 -6.89 125.67
REMARK 500 LEU G 163 139.57 -179.64
REMARK 500 TYR G 165 -36.56 -38.56
REMARK 500 ASN G 225 -2.59 77.09
REMARK 500 LYS G 249 45.65 38.07
REMARK 500 ASN G 301 -79.76 -30.01
REMARK 500 ILE H 4 -179.19 55.51
REMARK 500 ASN H 16 43.49 72.01
REMARK 500 GLN H 19 -38.83 -37.69
REMARK 500 SER H 24 107.68 -47.75
REMARK 500 VAL H 72 -165.05 48.38
REMARK 500 ASN H 73 -158.64 -63.80
REMARK 500 ASN H 88 73.36 -159.39
REMARK 500 PRO H 89 -6.07 -52.87
REMARK 500 PHE H 92 -88.37 -69.48
REMARK 500 ASP H 93 -37.45 -29.45
REMARK 500 GLN H 97 -8.19 -53.06
REMARK 500 ASN H 124 20.14 47.19
REMARK 500 PHE H 130 -76.13 -55.07
REMARK 500 ASN H 131 -6.96 -47.74
REMARK 500 LYS H 144 52.70 -104.70
REMARK 500 THR H 146 -31.61 -140.34
REMARK 500 LYS H 249 59.36 34.43
REMARK 500 LYS H 288 62.39 60.92
REMARK 500 ASN H 301 82.63 -65.66
REMARK 500 LYS I 3 52.31 -119.91
REMARK 500 ASP I 38 32.78 75.77
REMARK 500 ARG I 40 93.48 176.17
REMARK 500 ASN I 57 138.55 -39.23
REMARK 500 ASN I 73 -170.99 -175.66
REMARK 500 THR I 75 -67.53 -92.25
REMARK 500 PRO I 89 7.29 -55.96
REMARK 500 LEU I 91 -14.73 -46.12
REMARK 500 GLU I 100 -54.68 -29.78
REMARK 500 LYS I 102 39.90 -73.61
REMARK 500 THR I 129 -5.84 -58.94
REMARK 500 PHE I 130 -88.78 -84.60
REMARK 500 ASN I 131 -34.94 -33.17
REMARK 500 LYS I 132 -70.50 -62.39
REMARK 500 THR I 133 -101.81 -59.29
REMARK 500 ILE I 134 -75.94 31.77
REMARK 500 PHE I 182 50.65 -111.18
REMARK 500 ARG I 205 39.37 72.89
REMARK 500 LYS I 249 74.89 -1.58
REMARK 500 LYS I 288 70.59 49.87
REMARK 500 ASN I 301 0.70 -60.71
REMARK 500 LEU J 15 0.52 -69.25
REMARK 500 ASN J 16 79.80 60.60
REMARK 500 SER J 24 40.95 -62.25
REMARK 500 LYS J 29 -81.14 -2.09
REMARK 500 GLU J 36 5.54 -63.26
REMARK 500 SER J 39 44.56 -109.80
REMARK 500 ARG J 40 142.15 174.17
REMARK 500 PRO J 89 9.50 -57.25
REMARK 500 PHE J 92 -70.65 -77.12
REMARK 500 LYS J 94 -70.34 -47.55
REMARK 500 VAL J 127 48.45 -154.75
REMARK 500 ARG J 205 26.11 47.44
REMARK 500 ASN J 225 -9.07 92.92
REMARK 500 LYS J 249 33.80 38.29
REMARK 500 GLU J 300 27.92 -74.59
REMARK 500 SER K 24 91.53 -50.12
REMARK 500 SER K 39 -72.98 -107.20
REMARK 500 PRO K 41 150.03 -47.48
REMARK 500 ASN K 57 129.39 -36.52
REMARK 500 ILE K 85 -4.16 -56.71
REMARK 500 ASN K 88 71.19 -119.50
REMARK 500 PHE K 92 -99.26 -52.61
REMARK 500 ASP K 93 -43.42 -17.41
REMARK 500 ASN K 124 52.53 26.83
REMARK 500 VAL K 127 60.00 -149.59
REMARK 500 PHE K 130 -70.18 -61.90
REMARK 500 VAL K 162 21.15 -140.32
REMARK 500 ASN K 225 1.54 83.18
REMARK 500 LYS K 249 60.40 30.82
REMARK 500 LYS L 3 49.85 -93.34
REMARK 500 ASP L 38 39.08 71.14
REMARK 500 ASN L 73 -160.43 -172.00
REMARK 500 PRO L 89 3.32 -62.28
REMARK 500 PHE L 92 -84.81 -58.64
REMARK 500 ILE L 99 -63.73 -94.26
REMARK 500 VAL L 162 37.24 -141.36
REMARK 500 GLU L 167 0.58 -69.54
REMARK 500 LYS L 249 57.60 2.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH F 318 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH F 324 DISTANCE = 7.48 ANGSTROMS
REMARK 525 HOH F 329 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH F 337 DISTANCE = 8.67 ANGSTROMS
REMARK 525 HOH F 339 DISTANCE = 7.92 ANGSTROMS
REMARK 525 HOH F 354 DISTANCE = 5.09 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2AW6 RELATED DB: PDB
REMARK 900 RELATED ID: 2AWI RELATED DB: PDB
REMARK 900 RELATED ID: 2AXV RELATED DB: PDB
REMARK 900 RELATED ID: 2AXZ RELATED DB: PDB
DBREF 2AXU A 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU B 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU C 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU D 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU E 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU F 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU G 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU H 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU I 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU J 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU K 1 317 UNP Q04114 Q04114_ENTFA 1 317
DBREF 2AXU L 1 317 UNP Q04114 Q04114_ENTFA 1 317
SEQADV 2AXU MSE A 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE A 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE A 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE A 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE A 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE B 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE B 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE B 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE B 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE B 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE C 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE C 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE C 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE C 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE C 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE D 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE D 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE D 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE D 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE D 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE E 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE E 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE E 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE E 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE E 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE F 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE F 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE F 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE F 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE F 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE G 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE G 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE G 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE G 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE G 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE H 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE H 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE H 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE H 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE H 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE I 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE I 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE I 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE I 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE I 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE J 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE J 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE J 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE J 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE J 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE K 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE K 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE K 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE K 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE K 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQADV 2AXU MSE L 1 UNP Q04114 MET 1 MODIFIED RESIDUE
SEQADV 2AXU MSE L 27 UNP Q04114 MET 27 MODIFIED RESIDUE
SEQADV 2AXU MSE L 67 UNP Q04114 MET 67 MODIFIED RESIDUE
SEQADV 2AXU MSE L 175 UNP Q04114 MET 175 MODIFIED RESIDUE
SEQADV 2AXU MSE L 203 UNP Q04114 MET 203 MODIFIED RESIDUE
SEQRES 1 A 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 A 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 A 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 A 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 A 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 A 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 A 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 A 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 A 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 A 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 A 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 A 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 A 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 A 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 A 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 A 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 A 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 A 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 A 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 A 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 A 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 A 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 A 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 A 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 A 317 ILE LYS GLU GLN SER
SEQRES 1 B 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 B 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 B 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 B 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 B 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 B 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 B 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 B 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 B 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 B 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 B 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 B 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 B 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 B 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 B 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 B 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 B 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 B 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 B 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 B 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 B 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 B 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 B 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 B 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 B 317 ILE LYS GLU GLN SER
SEQRES 1 C 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 C 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 C 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 C 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 C 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 C 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 C 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 C 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 C 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 C 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 C 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 C 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 C 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 C 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 C 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 C 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 C 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 C 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 C 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 C 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 C 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 C 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 C 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 C 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 C 317 ILE LYS GLU GLN SER
SEQRES 1 D 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 D 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 D 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 D 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 D 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 D 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 D 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 D 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 D 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 D 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 D 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 D 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 D 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 D 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 D 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 D 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 D 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 D 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 D 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 D 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 D 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 D 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 D 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 D 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 D 317 ILE LYS GLU GLN SER
SEQRES 1 E 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 E 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 E 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 E 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 E 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 E 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 E 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 E 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 E 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 E 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 E 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 E 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 E 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 E 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 E 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 E 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 E 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 E 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 E 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 E 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 E 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 E 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 E 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 E 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 E 317 ILE LYS GLU GLN SER
SEQRES 1 F 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 F 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 F 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 F 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 F 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 F 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 F 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 F 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 F 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 F 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 F 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 F 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 F 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 F 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 F 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 F 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 F 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 F 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 F 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 F 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 F 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 F 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 F 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 F 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 F 317 ILE LYS GLU GLN SER
SEQRES 1 G 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 G 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 G 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 G 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 G 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 G 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 G 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 G 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 G 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 G 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 G 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 G 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 G 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 G 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 G 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 G 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 G 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 G 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 G 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 G 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 G 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 G 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 G 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 G 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 G 317 ILE LYS GLU GLN SER
SEQRES 1 H 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 H 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 H 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 H 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 H 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 H 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 H 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 H 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 H 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 H 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 H 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 H 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 H 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 H 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 H 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 H 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 H 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 H 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 H 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 H 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 H 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 H 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 H 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 H 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 H 317 ILE LYS GLU GLN SER
SEQRES 1 I 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 I 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 I 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 I 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 I 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 I 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 I 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 I 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 I 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 I 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 I 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 I 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 I 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 I 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 I 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 I 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 I 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 I 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 I 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 I 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 I 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 I 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 I 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 I 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 I 317 ILE LYS GLU GLN SER
SEQRES 1 J 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 J 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 J 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 J 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 J 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 J 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 J 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 J 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 J 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 J 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 J 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 J 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 J 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 J 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 J 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 J 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 J 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 J 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 J 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 J 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 J 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 J 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 J 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 J 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 J 317 ILE LYS GLU GLN SER
SEQRES 1 K 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 K 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 K 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 K 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 K 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 K 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 K 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 K 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 K 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 K 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 K 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 K 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 K 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 K 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 K 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 K 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 K 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 K 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 K 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 K 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 K 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 K 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 K 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 K 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 K 317 ILE LYS GLU GLN SER
SEQRES 1 L 317 MSE PHE LYS ILE GLY SER VAL LEU LYS GLN ILE ARG GLN
SEQRES 2 L 317 GLU LEU ASN TYR HIS GLN ILE ASP LEU TYR SER GLY ILE
SEQRES 3 L 317 MSE SER LYS SER VAL TYR ILE LYS VAL GLU ALA ASP SER
SEQRES 4 L 317 ARG PRO ILE SER VAL GLU GLU LEU SER LYS PHE SER GLU
SEQRES 5 L 317 ARG LEU GLY VAL ASN PHE PHE GLU ILE LEU ASN ARG ALA
SEQRES 6 L 317 GLY MSE ASN THR LYS SER VAL ASN GLU THR GLY LYS GLU
SEQRES 7 L 317 LYS LEU LEU ILE SER LYS ILE PHE THR ASN PRO ASP LEU
SEQRES 8 L 317 PHE ASP LYS ASN PHE GLN ARG ILE GLU PRO LYS ARG LEU
SEQRES 9 L 317 THR SER LEU GLN TYR PHE SER ILE TYR LEU GLY TYR ILE
SEQRES 10 L 317 SER ILE ALA HIS HIS TYR ASN ILE GLU VAL PRO THR PHE
SEQRES 11 L 317 ASN LYS THR ILE THR SER ASP LEU LYS HIS LEU TYR ASP
SEQRES 12 L 317 LYS ARG THR THR PHE PHE GLY ILE ASP TYR GLU ILE VAL
SEQRES 13 L 317 SER ASN LEU LEU ASN VAL LEU PRO TYR GLU GLU VAL SER
SEQRES 14 L 317 SER ILE ILE LYS PRO MSE TYR PRO ILE VAL ASP SER PHE
SEQRES 15 L 317 GLY LYS ASP TYR ASP LEU THR ILE GLN THR VAL LEU LYS
SEQRES 16 L 317 ASN ALA LEU THR ILE SER ILE MSE ASN ARG ASN LEU LYS
SEQRES 17 L 317 GLU ALA GLN TYR TYR ILE ASN GLN PHE GLU HIS LEU LYS
SEQRES 18 L 317 THR ILE LYS ASN ILE SER ILE ASN GLY TYR TYR ASP LEU
SEQRES 19 L 317 GLU ILE ASN TYR LEU LYS GLN ILE TYR GLN PHE LEU THR
SEQRES 20 L 317 ASP LYS ASN ILE ASP SER TYR LEU ASN ALA VAL ASN ILE
SEQRES 21 L 317 ILE ASN ILE PHE LYS ILE ILE GLY LYS GLU ASP ILE HIS
SEQRES 22 L 317 ARG SER LEU VAL GLU GLU LEU THR LYS ILE SER ALA LYS
SEQRES 23 L 317 GLU LYS PHE THR PRO PRO LYS GLU VAL THR MET TYR TYR
SEQRES 24 L 317 GLU ASN TYR VAL ALA ILE GLU ASN ASN PRO ILE PRO GLU
SEQRES 25 L 317 ILE LYS GLU GLN SER
MODRES 2AXU MSE A 1 MET SELENOMETHIONINE
MODRES 2AXU MSE A 27 MET SELENOMETHIONINE
MODRES 2AXU MSE A 67 MET SELENOMETHIONINE
MODRES 2AXU MSE A 175 MET SELENOMETHIONINE
MODRES 2AXU MSE A 203 MET SELENOMETHIONINE
MODRES 2AXU MSE B 27 MET SELENOMETHIONINE
MODRES 2AXU MSE B 67 MET SELENOMETHIONINE
MODRES 2AXU MSE B 175 MET SELENOMETHIONINE
MODRES 2AXU MSE B 203 MET SELENOMETHIONINE
MODRES 2AXU MSE C 27 MET SELENOMETHIONINE
MODRES 2AXU MSE C 67 MET SELENOMETHIONINE
MODRES 2AXU MSE C 175 MET SELENOMETHIONINE
MODRES 2AXU MSE C 203 MET SELENOMETHIONINE
MODRES 2AXU MSE D 27 MET SELENOMETHIONINE
MODRES 2AXU MSE D 67 MET SELENOMETHIONINE
MODRES 2AXU MSE D 175 MET SELENOMETHIONINE
MODRES 2AXU MSE D 203 MET SELENOMETHIONINE
MODRES 2AXU MSE E 27 MET SELENOMETHIONINE
MODRES 2AXU MSE E 67 MET SELENOMETHIONINE
MODRES 2AXU MSE E 175 MET SELENOMETHIONINE
MODRES 2AXU MSE E 203 MET SELENOMETHIONINE
MODRES 2AXU MSE F 27 MET SELENOMETHIONINE
MODRES 2AXU MSE F 67 MET SELENOMETHIONINE
MODRES 2AXU MSE F 175 MET SELENOMETHIONINE
MODRES 2AXU MSE F 203 MET SELENOMETHIONINE
MODRES 2AXU MSE G 27 MET SELENOMETHIONINE
MODRES 2AXU MSE G 67 MET SELENOMETHIONINE
MODRES 2AXU MSE G 175 MET SELENOMETHIONINE
MODRES 2AXU MSE G 203 MET SELENOMETHIONINE
MODRES 2AXU MSE H 27 MET SELENOMETHIONINE
MODRES 2AXU MSE H 67 MET SELENOMETHIONINE
MODRES 2AXU MSE H 175 MET SELENOMETHIONINE
MODRES 2AXU MSE H 203 MET SELENOMETHIONINE
MODRES 2AXU MSE I 27 MET SELENOMETHIONINE
MODRES 2AXU MSE I 67 MET SELENOMETHIONINE
MODRES 2AXU MSE I 175 MET SELENOMETHIONINE
MODRES 2AXU MSE I 203 MET SELENOMETHIONINE
MODRES 2AXU MSE J 27 MET SELENOMETHIONINE
MODRES 2AXU MSE J 67 MET SELENOMETHIONINE
MODRES 2AXU MSE J 175 MET SELENOMETHIONINE
MODRES 2AXU MSE J 203 MET SELENOMETHIONINE
MODRES 2AXU MSE K 27 MET SELENOMETHIONINE
MODRES 2AXU MSE K 67 MET SELENOMETHIONINE
MODRES 2AXU MSE K 175 MET SELENOMETHIONINE
MODRES 2AXU MSE K 203 MET SELENOMETHIONINE
MODRES 2AXU MSE L 27 MET SELENOMETHIONINE
MODRES 2AXU MSE L 67 MET SELENOMETHIONINE
MODRES 2AXU MSE L 175 MET SELENOMETHIONINE
MODRES 2AXU MSE L 203 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 27 8
HET MSE A 67 8
HET MSE A 175 8
HET MSE A 203 8
HET MSE B 27 8
HET MSE B 67 8
HET MSE B 175 8
HET MSE B 203 8
HET MSE C 27 8
HET MSE C 67 8
HET MSE C 175 8
HET MSE C 203 8
HET MSE D 27 8
HET MSE D 67 8
HET MSE D 175 8
HET MSE D 203 8
HET MSE E 27 8
HET MSE E 67 8
HET MSE E 175 8
HET MSE E 203 8
HET MSE F 27 8
HET MSE F 67 8
HET MSE F 175 8
HET MSE F 203 8
HET MSE G 27 8
HET MSE G 67 8
HET MSE G 175 8
HET MSE G 203 8
HET MSE H 27 8
HET MSE H 67 8
HET MSE H 175 8
HET MSE H 203 8
HET MSE I 27 8
HET MSE I 67 8
HET MSE I 175 8
HET MSE I 203 8
HET MSE J 27 8
HET MSE J 67 8
HET MSE J 175 8
HET MSE J 203 8
HET MSE K 27 8
HET MSE K 67 8
HET MSE K 175 8
HET MSE K 203 8
HET MSE L 27 8
HET MSE L 67 8
HET MSE L 175 8
HET MSE L 203 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 49(C5 H11 N O2 SE)
FORMUL 13 HOH *384(H2 O)
HELIX 1 1 LYS A 3 LEU A 15 1 13
HELIX 2 2 HIS A 18 SER A 24 1 7
HELIX 3 3 SER A 28 ALA A 37 1 10
HELIX 4 4 SER A 43 GLY A 55 1 13
HELIX 5 5 ASN A 57 GLY A 66 1 10
HELIX 6 6 ASN A 73 ASN A 88 1 16
HELIX 7 7 LEU A 91 GLU A 100 1 10
HELIX 8 8 PRO A 101 ARG A 103 5 3
HELIX 9 9 SER A 106 TYR A 123 1 18
HELIX 10 10 VAL A 127 ASP A 143 1 17
HELIX 11 11 PHE A 149 VAL A 162 1 14
HELIX 12 12 PRO A 164 LYS A 173 1 10
HELIX 13 13 PRO A 174 TYR A 176 5 3
HELIX 14 14 GLY A 183 ASN A 204 1 22
HELIX 15 15 ASN A 206 LYS A 221 1 16
HELIX 16 16 ASN A 229 LYS A 249 1 21
HELIX 17 17 ASN A 250 ILE A 267 1 18
HELIX 18 18 LYS A 269 GLU A 287 1 19
HELIX 19 19 PRO A 292 ALA A 304 1 13
HELIX 20 20 LYS B 3 LEU B 15 1 13
HELIX 21 21 GLN B 19 SER B 24 1 6
HELIX 22 22 SER B 28 ALA B 37 1 10
HELIX 23 23 SER B 43 GLY B 55 1 13
HELIX 24 24 ASN B 57 ALA B 65 1 9
HELIX 25 25 ASN B 73 THR B 87 1 15
HELIX 26 26 ASN B 88 ASP B 90 5 3
HELIX 27 27 LEU B 91 GLU B 100 1 10
HELIX 28 28 PRO B 101 ARG B 103 5 3
HELIX 29 29 SER B 106 TYR B 123 1 18
HELIX 30 30 VAL B 127 ASP B 143 1 17
HELIX 31 31 PHE B 149 LEU B 163 1 15
HELIX 32 32 PRO B 164 GLU B 167 5 4
HELIX 33 33 VAL B 168 LYS B 173 1 6
HELIX 34 34 PRO B 174 TYR B 176 5 3
HELIX 35 35 GLY B 183 ASN B 204 1 22
HELIX 36 36 ASN B 206 THR B 222 1 17
HELIX 37 37 ASN B 229 LYS B 249 1 21
HELIX 38 38 ASN B 250 ILE B 267 1 18
HELIX 39 39 LYS B 269 GLU B 287 1 19
HELIX 40 40 PRO B 292 ASN B 301 1 10
HELIX 41 41 LYS C 3 LEU C 15 1 13
HELIX 42 42 HIS C 18 SER C 24 1 7
HELIX 43 43 SER C 28 GLU C 36 1 9
HELIX 44 44 SER C 43 GLY C 55 1 13
HELIX 45 45 ASN C 57 GLY C 66 1 10
HELIX 46 46 ASN C 73 ILE C 85 1 13
HELIX 47 47 LEU C 91 ARG C 103 1 13
HELIX 48 48 SER C 106 TYR C 123 1 18
HELIX 49 49 VAL C 127 ASP C 143 1 17
HELIX 50 50 PHE C 149 ASN C 161 1 13
HELIX 51 51 PRO C 164 LYS C 173 1 10
HELIX 52 52 PRO C 174 TYR C 176 5 3
HELIX 53 53 GLY C 183 ASN C 204 1 22
HELIX 54 54 ASN C 206 LYS C 221 1 16
HELIX 55 55 ASN C 229 LYS C 249 1 21
HELIX 56 56 ASN C 250 ILE C 267 1 18
HELIX 57 57 LYS C 269 GLU C 287 1 19
HELIX 58 58 PRO C 292 ASN C 301 1 10
HELIX 59 59 LYS D 3 LEU D 15 1 13
HELIX 60 60 HIS D 18 SER D 24 1 7
HELIX 61 61 SER D 28 ASP D 38 1 11
HELIX 62 62 SER D 43 GLY D 55 1 13
HELIX 63 63 ASN D 57 ARG D 64 1 8
HELIX 64 64 ASN D 73 THR D 87 1 15
HELIX 65 65 ASN D 88 ASP D 90 5 3
HELIX 66 66 LEU D 91 GLU D 100 1 10
HELIX 67 67 PRO D 101 ARG D 103 5 3
HELIX 68 68 SER D 106 TYR D 123 1 18
HELIX 69 69 PRO D 128 ASP D 143 1 16
HELIX 70 70 PHE D 149 LEU D 160 1 12
HELIX 71 71 PRO D 164 LYS D 173 1 10
HELIX 72 72 PRO D 174 TYR D 176 5 3
HELIX 73 73 GLY D 183 ARG D 205 1 23
HELIX 74 74 ASN D 206 LYS D 221 1 16
HELIX 75 75 ASN D 229 LYS D 249 1 21
HELIX 76 76 ASN D 250 ILE D 267 1 18
HELIX 77 77 LYS D 269 LYS D 286 1 18
HELIX 78 78 GLU D 294 ASN D 301 1 8
HELIX 79 79 LYS E 3 LEU E 15 1 13
HELIX 80 80 HIS E 18 SER E 24 1 7
HELIX 81 81 SER E 28 GLU E 36 1 9
HELIX 82 82 SER E 43 GLY E 55 1 13
HELIX 83 83 ASN E 57 ALA E 65 1 9
HELIX 84 84 ASN E 73 ASN E 88 1 16
HELIX 85 85 LEU E 91 GLU E 100 1 10
HELIX 86 86 PRO E 101 ARG E 103 5 3
HELIX 87 87 SER E 106 TYR E 123 1 18
HELIX 88 88 VAL E 127 ASP E 143 1 17
HELIX 89 89 PHE E 149 LEU E 163 1 15
HELIX 90 90 PRO E 164 GLU E 167 5 4
HELIX 91 91 VAL E 168 LYS E 173 1 6
HELIX 92 92 PRO E 174 TYR E 176 5 3
HELIX 93 93 GLY E 183 ASN E 204 1 22
HELIX 94 94 ASN E 206 LYS E 221 1 16
HELIX 95 95 ASN E 229 LYS E 249 1 21
HELIX 96 96 ASN E 250 ILE E 267 1 18
HELIX 97 97 LYS E 269 GLU E 287 1 19
HELIX 98 98 PRO E 292 VAL E 303 1 12
HELIX 99 99 LYS F 3 LEU F 15 1 13
HELIX 100 100 HIS F 18 SER F 24 1 7
HELIX 101 101 SER F 28 ALA F 37 1 10
HELIX 102 102 SER F 43 GLY F 55 1 13
HELIX 103 103 ASN F 57 ARG F 64 1 8
HELIX 104 104 ASN F 73 THR F 87 1 15
HELIX 105 105 PHE F 92 GLU F 100 1 9
HELIX 106 106 PRO F 101 ARG F 103 5 3
HELIX 107 107 SER F 106 ASN F 124 1 19
HELIX 108 108 VAL F 127 LYS F 132 1 6
HELIX 109 109 THR F 133 ASP F 143 1 11
HELIX 110 110 PHE F 149 LEU F 163 1 15
HELIX 111 111 PRO F 164 LYS F 173 1 10
HELIX 112 112 PRO F 174 TYR F 176 5 3
HELIX 113 113 GLY F 183 ASN F 204 1 22
HELIX 114 114 ASN F 206 LYS F 221 1 16
HELIX 115 115 ASN F 229 LYS F 249 1 21
HELIX 116 116 ASN F 250 ILE F 267 1 18
HELIX 117 117 LYS F 269 LYS F 288 1 20
HELIX 118 118 PRO F 292 GLU F 300 1 9
HELIX 119 119 LYS G 3 ASN G 16 1 14
HELIX 120 120 HIS G 18 TYR G 23 1 6
HELIX 121 121 SER G 28 ALA G 37 1 10
HELIX 122 122 SER G 43 GLY G 55 1 13
HELIX 123 123 ASN G 57 ARG G 64 1 8
HELIX 124 124 ASN G 73 LYS G 79 1 7
HELIX 125 125 ILE G 82 THR G 87 1 6
HELIX 126 126 LEU G 91 GLU G 100 1 10
HELIX 127 127 SER G 106 TYR G 123 1 18
HELIX 128 128 THR G 133 TYR G 142 1 10
HELIX 129 129 PHE G 149 VAL G 162 1 14
HELIX 130 130 PRO G 164 LYS G 173 1 10
HELIX 131 131 PRO G 174 TYR G 176 5 3
HELIX 132 132 GLY G 183 ARG G 205 1 23
HELIX 133 133 ASN G 206 LYS G 221 1 16
HELIX 134 134 ASN G 229 LYS G 249 1 21
HELIX 135 135 ASN G 250 ILE G 267 1 18
HELIX 136 136 LYS G 269 GLU G 287 1 19
HELIX 137 137 PRO G 292 ILE G 305 1 14
HELIX 138 138 GLY H 5 ASN H 16 1 12
HELIX 139 139 GLN H 19 SER H 24 1 6
HELIX 140 140 SER H 28 ALA H 37 1 10
HELIX 141 141 SER H 43 GLY H 55 1 13
HELIX 142 142 ASN H 57 ALA H 65 1 9
HELIX 143 143 ASN H 73 THR H 87 1 15
HELIX 144 144 ASN H 88 ASP H 90 5 3
HELIX 145 145 LEU H 91 GLU H 100 1 10
HELIX 146 146 PRO H 101 ARG H 103 5 3
HELIX 147 147 SER H 106 TYR H 123 1 18
HELIX 148 148 THR H 129 TYR H 142 1 14
HELIX 149 149 PHE H 149 LEU H 163 1 15
HELIX 150 150 TYR H 165 LYS H 173 1 9
HELIX 151 151 PRO H 174 TYR H 176 5 3
HELIX 152 152 PHE H 182 ARG H 205 1 24
HELIX 153 153 ASN H 206 LYS H 221 1 16
HELIX 154 154 ASN H 229 LYS H 249 1 21
HELIX 155 155 ASN H 250 ILE H 267 1 18
HELIX 156 156 LYS H 269 GLU H 287 1 19
HELIX 157 157 GLU H 294 ASN H 301 1 8
HELIX 158 158 LYS I 3 LEU I 15 1 13
HELIX 159 159 HIS I 18 SER I 24 1 7
HELIX 160 160 SER I 28 ASP I 38 1 11
HELIX 161 161 SER I 43 GLY I 55 1 13
HELIX 162 162 ASN I 57 GLY I 66 1 10
HELIX 163 163 THR I 75 LEU I 80 1 6
HELIX 164 164 SER I 83 ASN I 88 1 6
HELIX 165 165 ASP I 90 GLU I 100 1 11
HELIX 166 166 PRO I 101 LEU I 104 5 4
HELIX 167 167 SER I 106 ASN I 124 1 19
HELIX 168 168 PRO I 128 THR I 133 1 6
HELIX 169 169 ILE I 134 ASP I 143 1 10
HELIX 170 170 PHE I 149 LEU I 163 1 15
HELIX 171 171 PRO I 164 GLU I 167 5 4
HELIX 172 172 VAL I 168 LYS I 173 1 6
HELIX 173 173 PRO I 174 TYR I 176 5 3
HELIX 174 174 GLY I 183 ARG I 205 1 23
HELIX 175 175 ASN I 206 LYS I 221 1 16
HELIX 176 176 ASN I 229 LYS I 249 1 21
HELIX 177 177 ASN I 250 ILE I 267 1 18
HELIX 178 178 LYS I 269 GLU I 287 1 19
HELIX 179 179 PRO I 292 ASN I 301 1 10
HELIX 180 180 ILE J 4 LEU J 15 1 12
HELIX 181 181 HIS J 18 TYR J 23 1 6
HELIX 182 182 SER J 28 GLU J 36 1 9
HELIX 183 183 SER J 43 GLY J 55 1 13
HELIX 184 184 ASN J 57 GLY J 66 1 10
HELIX 185 185 ASN J 73 ASN J 88 1 16
HELIX 186 186 ASP J 90 GLU J 100 1 11
HELIX 187 187 PRO J 101 ARG J 103 5 3
HELIX 188 188 SER J 106 TYR J 123 1 18
HELIX 189 189 VAL J 127 ASP J 143 1 17
HELIX 190 190 PHE J 149 LEU J 160 1 12
HELIX 191 191 PRO J 164 LYS J 173 1 10
HELIX 192 192 PRO J 174 TYR J 176 5 3
HELIX 193 193 PHE J 182 ASN J 204 1 23
HELIX 194 194 ASN J 206 LYS J 221 1 16
HELIX 195 195 ASN J 229 LYS J 249 1 21
HELIX 196 196 ASN J 250 ILE J 267 1 18
HELIX 197 197 LYS J 269 GLU J 287 1 19
HELIX 198 198 GLU J 294 TYR J 298 5 5
HELIX 199 199 ILE K 4 LEU K 15 1 12
HELIX 200 200 HIS K 18 SER K 24 1 7
HELIX 201 201 SER K 28 GLU K 36 1 9
HELIX 202 202 SER K 43 GLY K 55 1 13
HELIX 203 203 ASN K 57 ALA K 65 1 9
HELIX 204 204 ASN K 73 ILE K 85 1 13
HELIX 205 205 PHE K 86 THR K 87 5 2
HELIX 206 206 ASN K 88 ASP K 90 5 3
HELIX 207 207 LEU K 91 ARG K 103 1 13
HELIX 208 208 SER K 106 TYR K 123 1 18
HELIX 209 209 VAL K 127 ASP K 143 1 17
HELIX 210 210 PHE K 149 LEU K 160 1 12
HELIX 211 211 PRO K 164 LYS K 173 1 10
HELIX 212 212 PRO K 174 TYR K 176 5 3
HELIX 213 213 LYS K 184 ASN K 204 1 21
HELIX 214 214 ASN K 206 LYS K 221 1 16
HELIX 215 215 ASN K 229 LYS K 249 1 21
HELIX 216 216 ASN K 250 ILE K 267 1 18
HELIX 217 217 LYS K 269 GLU K 287 1 19
HELIX 218 218 PRO K 292 ASN K 301 1 10
HELIX 219 219 LYS L 3 LEU L 15 1 13
HELIX 220 220 HIS L 18 TYR L 23 1 6
HELIX 221 221 SER L 28 ALA L 37 1 10
HELIX 222 222 SER L 43 GLY L 55 1 13
HELIX 223 223 ASN L 57 ALA L 65 1 9
HELIX 224 224 ASN L 73 ASN L 88 1 16
HELIX 225 225 LEU L 91 GLU L 100 1 10
HELIX 226 226 PRO L 101 ARG L 103 5 3
HELIX 227 227 SER L 106 ASN L 124 1 19
HELIX 228 228 VAL L 127 TYR L 142 1 16
HELIX 229 229 PHE L 149 VAL L 162 1 14
HELIX 230 230 TYR L 165 LYS L 173 1 9
HELIX 231 231 PRO L 174 TYR L 176 5 3
HELIX 232 232 GLY L 183 ARG L 205 1 23
HELIX 233 233 ASN L 206 LYS L 221 1 16
HELIX 234 234 ASN L 229 LYS L 249 1 21
HELIX 235 235 ASN L 250 ILE L 267 1 18
HELIX 236 236 LYS L 269 GLU L 287 1 19
HELIX 237 237 PRO L 292 GLU L 300 1 9
LINK C MSE A 1 N PHE A 2 1555 1555 1.33
LINK C ILE A 26 N MSE A 27 1555 1555 1.33
LINK C MSE A 27 N SER A 28 1555 1555 1.33
LINK C GLY A 66 N MSE A 67 1555 1555 1.33
LINK C MSE A 67 N ASN A 68 1555 1555 1.33
LINK C PRO A 174 N MSE A 175 1555 1555 1.33
LINK C MSE A 175 N TYR A 176 1555 1555 1.33
LINK C ILE A 202 N MSE A 203 1555 1555 1.33
LINK C MSE A 203 N ASN A 204 1555 1555 1.33
LINK C ILE B 26 N MSE B 27 1555 1555 1.33
LINK C MSE B 27 N SER B 28 1555 1555 1.33
LINK C GLY B 66 N MSE B 67 1555 1555 1.33
LINK C MSE B 67 N ASN B 68 1555 1555 1.33
LINK C PRO B 174 N MSE B 175 1555 1555 1.33
LINK C MSE B 175 N TYR B 176 1555 1555 1.33
LINK C ILE B 202 N MSE B 203 1555 1555 1.33
LINK C MSE B 203 N ASN B 204 1555 1555 1.33
LINK C ILE C 26 N MSE C 27 1555 1555 1.33
LINK C MSE C 27 N SER C 28 1555 1555 1.33
LINK C GLY C 66 N MSE C 67 1555 1555 1.33
LINK C MSE C 67 N ASN C 68 1555 1555 1.33
LINK C PRO C 174 N MSE C 175 1555 1555 1.33
LINK C MSE C 175 N TYR C 176 1555 1555 1.33
LINK C ILE C 202 N MSE C 203 1555 1555 1.33
LINK C MSE C 203 N ASN C 204 1555 1555 1.33
LINK C ILE D 26 N MSE D 27 1555 1555 1.33
LINK C MSE D 27 N SER D 28 1555 1555 1.33
LINK C GLY D 66 N MSE D 67 1555 1555 1.33
LINK C MSE D 67 N ASN D 68 1555 1555 1.33
LINK C PRO D 174 N MSE D 175 1555 1555 1.33
LINK C MSE D 175 N TYR D 176 1555 1555 1.33
LINK C ILE D 202 N MSE D 203 1555 1555 1.33
LINK C MSE D 203 N ASN D 204 1555 1555 1.33
LINK C ILE E 26 N MSE E 27 1555 1555 1.33
LINK C MSE E 27 N SER E 28 1555 1555 1.33
LINK C GLY E 66 N MSE E 67 1555 1555 1.33
LINK C MSE E 67 N ASN E 68 1555 1555 1.33
LINK C PRO E 174 N MSE E 175 1555 1555 1.33
LINK C MSE E 175 N TYR E 176 1555 1555 1.33
LINK C ILE E 202 N MSE E 203 1555 1555 1.33
LINK C MSE E 203 N ASN E 204 1555 1555 1.33
LINK C ILE F 26 N MSE F 27 1555 1555 1.33
LINK C MSE F 27 N SER F 28 1555 1555 1.33
LINK C GLY F 66 N MSE F 67 1555 1555 1.33
LINK C MSE F 67 N ASN F 68 1555 1555 1.33
LINK C PRO F 174 N MSE F 175 1555 1555 1.33
LINK C MSE F 175 N TYR F 176 1555 1555 1.33
LINK C ILE F 202 N MSE F 203 1555 1555 1.33
LINK C MSE F 203 N ASN F 204 1555 1555 1.33
LINK C ILE G 26 N MSE G 27 1555 1555 1.33
LINK C MSE G 27 N SER G 28 1555 1555 1.33
LINK C GLY G 66 N MSE G 67 1555 1555 1.33
LINK C MSE G 67 N ASN G 68 1555 1555 1.33
LINK C PRO G 174 N MSE G 175 1555 1555 1.33
LINK C MSE G 175 N TYR G 176 1555 1555 1.33
LINK C ILE G 202 N MSE G 203 1555 1555 1.33
LINK C MSE G 203 N ASN G 204 1555 1555 1.33
LINK C ILE H 26 N MSE H 27 1555 1555 1.33
LINK C MSE H 27 N SER H 28 1555 1555 1.33
LINK C GLY H 66 N MSE H 67 1555 1555 1.33
LINK C MSE H 67 N ASN H 68 1555 1555 1.33
LINK C PRO H 174 N MSE H 175 1555 1555 1.33
LINK C MSE H 175 N TYR H 176 1555 1555 1.33
LINK C ILE H 202 N MSE H 203 1555 1555 1.33
LINK C MSE H 203 N ASN H 204 1555 1555 1.33
LINK C ILE I 26 N MSE I 27 1555 1555 1.33
LINK C MSE I 27 N SER I 28 1555 1555 1.33
LINK C GLY I 66 N MSE I 67 1555 1555 1.33
LINK C MSE I 67 N ASN I 68 1555 1555 1.33
LINK C PRO I 174 N MSE I 175 1555 1555 1.33
LINK C MSE I 175 N TYR I 176 1555 1555 1.33
LINK C ILE I 202 N MSE I 203 1555 1555 1.33
LINK C MSE I 203 N ASN I 204 1555 1555 1.33
LINK C ILE J 26 N MSE J 27 1555 1555 1.33
LINK C MSE J 27 N SER J 28 1555 1555 1.33
LINK C GLY J 66 N MSE J 67 1555 1555 1.33
LINK C MSE J 67 N ASN J 68 1555 1555 1.33
LINK C PRO J 174 N MSE J 175 1555 1555 1.33
LINK C MSE J 175 N TYR J 176 1555 1555 1.33
LINK C ILE J 202 N MSE J 203 1555 1555 1.33
LINK C MSE J 203 N ASN J 204 1555 1555 1.33
LINK C ILE K 26 N MSE K 27 1555 1555 1.33
LINK C MSE K 27 N SER K 28 1555 1555 1.33
LINK C GLY K 66 N MSE K 67 1555 1555 1.33
LINK C MSE K 67 N ASN K 68 1555 1555 1.33
LINK C PRO K 174 N MSE K 175 1555 1555 1.33
LINK C MSE K 175 N TYR K 176 1555 1555 1.33
LINK C ILE K 202 N MSE K 203 1555 1555 1.33
LINK C MSE K 203 N ASN K 204 1555 1555 1.33
LINK C ILE L 26 N MSE L 27 1555 1555 1.33
LINK C MSE L 27 N SER L 28 1555 1555 1.33
LINK C GLY L 66 N MSE L 67 1555 1555 1.33
LINK C MSE L 67 N ASN L 68 1555 1555 1.33
LINK C PRO L 174 N MSE L 175 1555 1555 1.33
LINK C MSE L 175 N TYR L 176 1555 1555 1.33
LINK C ILE L 202 N MSE L 203 1555 1555 1.33
LINK C MSE L 203 N ASN L 204 1555 1555 1.33
CISPEP 1 TYR A 176 PRO A 177 0 0.15
CISPEP 2 TYR B 176 PRO B 177 0 -2.61
CISPEP 3 TYR C 176 PRO C 177 0 0.01
CISPEP 4 TYR D 176 PRO D 177 0 0.04
CISPEP 5 TYR E 176 PRO E 177 0 0.06
CISPEP 6 TYR F 176 PRO F 177 0 -1.79
CISPEP 7 TYR G 176 PRO G 177 0 0.06
CISPEP 8 TYR H 176 PRO H 177 0 0.03
CISPEP 9 TYR I 176 PRO I 177 0 0.35
CISPEP 10 TYR J 176 PRO J 177 0 -0.10
CISPEP 11 TYR K 176 PRO K 177 0 -0.87
CISPEP 12 TYR L 176 PRO L 177 0 -0.42
CRYST1 92.654 134.718 195.930 90.00 100.30 90.00 P 1 21 1 24
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 0.010793 0.000000 0.001961 0.00000
SCALE2 0.000000 0.007423 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005187 0.00000
HETATM 1 N MSE A 1 57.395 -12.433 39.781 1.00 99.63 N
HETATM 2 CA MSE A 1 57.507 -12.714 41.242 1.00101.77 C
HETATM 3 C MSE A 1 56.234 -12.325 41.977 1.00102.47 C
HETATM 4 O MSE A 1 55.468 -13.186 42.412 1.00101.07 O
HETATM 5 CB MSE A 1 58.678 -11.943 41.852 1.00192.72 C
HETATM 6 CG MSE A 1 60.044 -12.342 41.340 1.00192.72 C
HETATM 7 SE MSE A 1 61.440 -11.473 42.347 1.00176.94 SE
HETATM 8 CE MSE A 1 61.746 -12.840 43.674 1.00176.94 C
(ATOM LINES ARE NOT SHOWN.)
END
