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HEADER LYASE/TRANSFERASE 15-SEP-10 3OUR
TITLE CRYSTAL STRUCTURE OF COMPLEX BETWEEN EIIA AND A NOVEL PYRUVATE
TITLE 2 DECARBOXYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UPF0255 PROTEIN VV1_0328;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 SYNONYM: FERMENTATION/RESPIRATION SWITCH PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHOSPHOTRANSFERASE SYSTEM IIA COMPONENT;
COMPND 8 CHAIN: B, D, F, H;
COMPND 9 SYNONYM: EIIA;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 3 ORGANISM_TAXID: 216895;
SOURCE 4 STRAIN: CMCP6;
SOURCE 5 GENE: VV1_0328;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PQE;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: VIBRIO VULNIFICUS;
SOURCE 13 ORGANISM_TAXID: 216895;
SOURCE 14 STRAIN: CMCP6;
SOURCE 15 GENE: VV1_0212;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PQE
KEYWDS EXHIBIT NO HYDROLASE ACTIVITY1, LYASE-TRANSFERASE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.-S.JEONG,Y.J.AN,S.-S.CHA
REVDAT 1 01-JUN-11 3OUR 0
JRNL AUTH K.-J.LEE,C.-S.JEONG,Y.J.AN,H.-J.LEE,S.-J.PARK,Y.-J.SEOK,
JRNL AUTH 2 P.KIM,J.-H.LEE,K.-H.LEE,S.-S.CHA
JRNL TITL FRSA FUNCTIONS AS A COFACTOR-INDEPENDENT DECARBOXYLASE TO
JRNL TITL 2 CONTROL METABOLIC FLUX
JRNL REF NAT.CHEM.BIOL. 2011
JRNL REFN ESSN 1552-4469
JRNL DOI 10.1038/NCHEMBIO.589
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.37
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.100
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 44259.560
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 90.5
REMARK 3 NUMBER OF REFLECTIONS : 108181
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5459
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 14187
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE : 0.3120
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 757
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.011
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16723
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 927
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.04000
REMARK 3 B22 (A**2) : 3.22000
REMARK 3 B33 (A**2) : -0.18000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.32
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.35
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.80
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.32
REMARK 3 BSOL : 43.33
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : ION.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : ION.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3OUR COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-OCT-10.
REMARK 100 THE RCSB ID CODE IS RCSB061598.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 119307
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: 3MVE, 1O2F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG MME 550, 0.1M MES PH 6.5,
REMARK 280 0.01M ZN-ACETATE, MICROBATCH, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 161.43300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.03350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 161.43300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.03350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 ARG A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 ALA A -7
REMARK 465 CYS A -6
REMARK 465 GLU A -5
REMARK 465 LEU A -4
REMARK 465 GLY A -3
REMARK 465 THR A -2
REMARK 465 PRO A -1
REMARK 465 ASN A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ASN A 8
REMARK 465 LEU A 9
REMARK 465 SER A 10
REMARK 465 GLU A 11
REMARK 465 THR A 12
REMARK 465 LEU A 13
REMARK 465 PHE A 14
REMARK 465 VAL A 15
REMARK 465 LYS A 16
REMARK 465 HIS A 17
REMARK 465 LYS A 18
REMARK 465 GLN A 19
REMARK 465 ALA A 20
REMARK 465 ARG A 415
REMARK 465 MET B -13
REMARK 465 ARG B -12
REMARK 465 GLY B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 GLY B -3
REMARK 465 SER B -2
REMARK 465 ASP B -1
REMARK 465 THR B 0
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 LEU B 3
REMARK 465 PHE B 4
REMARK 465 ASP B 5
REMARK 465 LYS B 6
REMARK 465 LEU B 7
REMARK 465 LYS B 8
REMARK 465 LYS B 9
REMARK 465 LEU B 10
REMARK 465 VAL B 11
REMARK 465 SER B 12
REMARK 465 ASP B 13
REMARK 465 ASP B 14
REMARK 465 SER B 15
REMARK 465 ALA B 16
REMARK 465 SER B 17
REMARK 465 ALA B 18
REMARK 465 GLY B 19
REMARK 465 MET C -19
REMARK 465 ARG C -18
REMARK 465 GLY C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 GLY C -9
REMARK 465 SER C -8
REMARK 465 ALA C -7
REMARK 465 CYS C -6
REMARK 465 GLU C -5
REMARK 465 LEU C -4
REMARK 465 GLY C -3
REMARK 465 THR C -2
REMARK 465 PRO C -1
REMARK 465 ASN C 0
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
REMARK 465 GLU C 4
REMARK 465 VAL C 5
REMARK 465 SER C 6
REMARK 465 LYS C 7
REMARK 465 ASN C 8
REMARK 465 LEU C 9
REMARK 465 SER C 10
REMARK 465 GLU C 11
REMARK 465 THR C 12
REMARK 465 LEU C 13
REMARK 465 PHE C 14
REMARK 465 VAL C 15
REMARK 465 LYS C 16
REMARK 465 HIS C 17
REMARK 465 LYS C 18
REMARK 465 ASN C 44
REMARK 465 LEU C 414
REMARK 465 ARG C 415
REMARK 465 MET D -13
REMARK 465 ARG D -12
REMARK 465 GLY D -11
REMARK 465 SER D -10
REMARK 465 HIS D -9
REMARK 465 HIS D -8
REMARK 465 HIS D -7
REMARK 465 HIS D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 GLY D -3
REMARK 465 SER D -2
REMARK 465 ASP D -1
REMARK 465 THR D 0
REMARK 465 MET D 1
REMARK 465 GLY D 2
REMARK 465 LEU D 3
REMARK 465 PHE D 4
REMARK 465 ASP D 5
REMARK 465 LYS D 6
REMARK 465 LEU D 7
REMARK 465 LYS D 8
REMARK 465 LYS D 9
REMARK 465 LEU D 10
REMARK 465 VAL D 11
REMARK 465 SER D 12
REMARK 465 ASP D 13
REMARK 465 ASP D 14
REMARK 465 SER D 15
REMARK 465 ALA D 16
REMARK 465 SER D 17
REMARK 465 ALA D 18
REMARK 465 GLY D 19
REMARK 465 MET E -19
REMARK 465 ARG E -18
REMARK 465 GLY E -17
REMARK 465 SER E -16
REMARK 465 HIS E -15
REMARK 465 HIS E -14
REMARK 465 HIS E -13
REMARK 465 HIS E -12
REMARK 465 HIS E -11
REMARK 465 HIS E -10
REMARK 465 GLY E -9
REMARK 465 SER E -8
REMARK 465 ALA E -7
REMARK 465 CYS E -6
REMARK 465 GLU E -5
REMARK 465 LEU E -4
REMARK 465 GLY E -3
REMARK 465 THR E -2
REMARK 465 PRO E -1
REMARK 465 ASN E 0
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 GLU E 3
REMARK 465 GLU E 4
REMARK 465 VAL E 5
REMARK 465 SER E 6
REMARK 465 LYS E 7
REMARK 465 ASN E 8
REMARK 465 LEU E 9
REMARK 465 SER E 10
REMARK 465 GLU E 11
REMARK 465 THR E 12
REMARK 465 LEU E 13
REMARK 465 PHE E 14
REMARK 465 VAL E 15
REMARK 465 LYS E 16
REMARK 465 HIS E 17
REMARK 465 LYS E 18
REMARK 465 ARG E 415
REMARK 465 MET F -13
REMARK 465 ARG F -12
REMARK 465 GLY F -11
REMARK 465 SER F -10
REMARK 465 HIS F -9
REMARK 465 HIS F -8
REMARK 465 HIS F -7
REMARK 465 HIS F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 GLY F -3
REMARK 465 SER F -2
REMARK 465 ASP F -1
REMARK 465 THR F 0
REMARK 465 MET F 1
REMARK 465 GLY F 2
REMARK 465 LEU F 3
REMARK 465 PHE F 4
REMARK 465 ASP F 5
REMARK 465 LYS F 6
REMARK 465 LEU F 7
REMARK 465 LYS F 8
REMARK 465 LYS F 9
REMARK 465 LEU F 10
REMARK 465 VAL F 11
REMARK 465 SER F 12
REMARK 465 ASP F 13
REMARK 465 ASP F 14
REMARK 465 SER F 15
REMARK 465 ALA F 16
REMARK 465 SER F 17
REMARK 465 ALA F 18
REMARK 465 GLY F 19
REMARK 465 MET G -19
REMARK 465 ARG G -18
REMARK 465 GLY G -17
REMARK 465 SER G -16
REMARK 465 HIS G -15
REMARK 465 HIS G -14
REMARK 465 HIS G -13
REMARK 465 HIS G -12
REMARK 465 HIS G -11
REMARK 465 HIS G -10
REMARK 465 GLY G -9
REMARK 465 SER G -8
REMARK 465 ALA G -7
REMARK 465 CYS G -6
REMARK 465 GLU G -5
REMARK 465 LEU G -4
REMARK 465 GLY G -3
REMARK 465 THR G -2
REMARK 465 PRO G -1
REMARK 465 ASN G 0
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 GLU G 3
REMARK 465 GLU G 4
REMARK 465 VAL G 5
REMARK 465 SER G 6
REMARK 465 LYS G 7
REMARK 465 ASN G 8
REMARK 465 LEU G 9
REMARK 465 SER G 10
REMARK 465 GLU G 11
REMARK 465 THR G 12
REMARK 465 LEU G 13
REMARK 465 PHE G 14
REMARK 465 VAL G 15
REMARK 465 LYS G 16
REMARK 465 HIS G 17
REMARK 465 LYS G 18
REMARK 465 GLN G 19
REMARK 465 MET H -13
REMARK 465 ARG H -12
REMARK 465 GLY H -11
REMARK 465 SER H -10
REMARK 465 HIS H -9
REMARK 465 HIS H -8
REMARK 465 HIS H -7
REMARK 465 HIS H -6
REMARK 465 HIS H -5
REMARK 465 HIS H -4
REMARK 465 GLY H -3
REMARK 465 SER H -2
REMARK 465 ASP H -1
REMARK 465 THR H 0
REMARK 465 MET H 1
REMARK 465 GLY H 2
REMARK 465 LEU H 3
REMARK 465 PHE H 4
REMARK 465 ASP H 5
REMARK 465 LYS H 6
REMARK 465 LEU H 7
REMARK 465 LYS H 8
REMARK 465 LYS H 9
REMARK 465 LEU H 10
REMARK 465 VAL H 11
REMARK 465 SER H 12
REMARK 465 ASP H 13
REMARK 465 ASP H 14
REMARK 465 SER H 15
REMARK 465 ALA H 16
REMARK 465 SER H 17
REMARK 465 ALA H 18
REMARK 465 GLY H 19
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLN A 28 CG CD OE1 NE2
REMARK 470 GLN A 34 CG CD OE1 NE2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 ILE A 40 CG1 CG2 CD1
REMARK 470 GLU A 42 CG CD OE1 OE2
REMARK 470 LYS A 43 CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 LYS A 141 CG CD CE NZ
REMARK 470 LYS A 165 CG CD CE NZ
REMARK 470 LYS A 177 CG CD CE NZ
REMARK 470 LYS A 191 CG CD CE NZ
REMARK 470 LYS A 219 CG CD CE NZ
REMARK 470 LYS A 237 CG CD CE NZ
REMARK 470 GLN A 307 CG CD OE1 NE2
REMARK 470 GLN A 310 CG CD OE1 NE2
REMARK 470 GLN A 311 CG CD OE1 NE2
REMARK 470 LYS A 344 CG CD CE NZ
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 GLU A 364 CG CD OE1 OE2
REMARK 470 GLN A 375 CG CD OE1 NE2
REMARK 470 LYS A 385 CG CD CE NZ
REMARK 470 LYS A 387 CG CD CE NZ
REMARK 470 LYS A 392 CG CD CE NZ
REMARK 470 GLN A 396 CG CD OE1 NE2
REMARK 470 GLU A 399 CG CD OE1 OE2
REMARK 470 GLN A 400 CG CD OE1 NE2
REMARK 470 SER A 401 OG
REMARK 470 LEU A 404 CG CD1 CD2
REMARK 470 LYS A 407 CG CD CE NZ
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 GLN C 19 CG CD OE1 NE2
REMARK 470 LYS C 21 CG CD CE NZ
REMARK 470 GLU C 42 CG CD OE1 OE2
REMARK 470 LYS C 43 CG CD CE NZ
REMARK 470 GLU C 119 CG CD OE1 OE2
REMARK 470 LYS C 177 CG CD CE NZ
REMARK 470 LYS C 219 CG CD CE NZ
REMARK 470 LYS C 237 CG CD CE NZ
REMARK 470 GLN C 307 CG CD OE1 NE2
REMARK 470 LYS C 326 CG CD CE NZ
REMARK 470 VAL C 328 CG1 CG2
REMARK 470 LYS C 355 CG CD CE NZ
REMARK 470 LYS C 387 CG CD CE NZ
REMARK 470 LYS C 392 CG CD CE NZ
REMARK 470 LYS C 407 CG CD CE NZ
REMARK 470 GLU D 130 CG CD OE1 OE2
REMARK 470 GLU D 149 CG CD OE1 OE2
REMARK 470 GLN E 19 CG CD OE1 NE2
REMARK 470 GLU E 39 CG CD OE1 OE2
REMARK 470 GLU E 42 CG CD OE1 OE2
REMARK 470 LYS E 43 CG CD CE NZ
REMARK 470 ASN E 44 CG OD1
REMARK 470 GLU E 108 CG CD OE1 OE2
REMARK 470 ARG E 112 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 141 CG CD CE NZ
REMARK 470 LYS E 165 CG CD CE NZ
REMARK 470 LYS E 177 CG CD CE NZ
REMARK 470 LYS E 179 CG CD CE NZ
REMARK 470 LYS E 219 CG CD CE NZ
REMARK 470 PRO E 259 CG CD
REMARK 470 TYR E 260 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS E 290 CG CD CE NZ
REMARK 470 GLN E 307 CG CD OE1 NE2
REMARK 470 SER E 350 OG
REMARK 470 LYS E 355 CG CD CE NZ
REMARK 470 LYS E 385 CG CD CE NZ
REMARK 470 LYS E 387 CG CD CE NZ
REMARK 470 LYS E 392 CG CD CE NZ
REMARK 470 GLN E 396 CG CD OE1 NE2
REMARK 470 TYR E 398 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN E 400 CG CD OE1 NE2
REMARK 470 ASP E 403 CG OD1 OD2
REMARK 470 LYS E 407 CG CD CE NZ
REMARK 470 GLU F 30 CG CD OE1 OE2
REMARK 470 LYS G 21 CG CD CE NZ
REMARK 470 LYS G 43 CG CD CE NZ
REMARK 470 GLU G 115 CG CD OE1 OE2
REMARK 470 LYS G 141 CG CD CE NZ
REMARK 470 GLN G 148 CG CD OE1 NE2
REMARK 470 LYS G 177 CG CD CE NZ
REMARK 470 LYS G 219 CG CD CE NZ
REMARK 470 LYS G 237 CG CD CE NZ
REMARK 470 GLU G 242 CG CD OE1 OE2
REMARK 470 GLN G 337 CG CD OE1 NE2
REMARK 470 LYS G 385 CG CD CE NZ
REMARK 470 LYS G 392 CG CD CE NZ
REMARK 470 LYS G 407 CG CD CE NZ
REMARK 470 ARG G 415 CG CD NE CZ NH1 NH2
REMARK 470 LYS H 148 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LEU D 27 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 LEU H 88 CA - CB - CG ANGL. DEV. = 15.4 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 23 -61.19 -23.33
REMARK 500 GLU A 42 2.78 -60.12
REMARK 500 PHE A 46 124.12 52.17
REMARK 500 ARG A 53 55.79 -119.69
REMARK 500 LEU A 87 -7.53 -59.13
REMARK 500 THR A 89 40.78 -104.20
REMARK 500 GLU A 115 47.49 -144.19
REMARK 500 THR A 117 -164.97 -64.16
REMARK 500 PHE A 175 142.72 -171.69
REMARK 500 GLU A 176 59.26 31.80
REMARK 500 THR A 189 45.09 -105.00
REMARK 500 ASP A 190 -82.45 -84.78
REMARK 500 ALA A 200 -154.91 -98.36
REMARK 500 HIS A 216 -40.98 -145.48
REMARK 500 SER A 231 -4.50 89.60
REMARK 500 HIS A 263 0.85 -59.83
REMARK 500 ARG A 272 -137.97 48.38
REMARK 500 GLU A 285 40.22 -140.25
REMARK 500 ILE A 299 -70.47 -69.06
REMARK 500 HIS A 300 -57.26 -125.43
REMARK 500 ASP A 301 -72.78 -31.05
REMARK 500 SER A 305 78.31 -174.71
REMARK 500 MET A 312 163.18 -38.30
REMARK 500 MET A 338 -23.95 -38.46
REMARK 500 PHE A 348 -35.23 -36.28
REMARK 500 SER A 350 -66.77 167.14
REMARK 500 SER A 351 -71.39 -109.51
REMARK 500 PHE A 380 30.76 -68.80
REMARK 500 LYS A 392 106.30 -47.55
REMARK 500 THR A 393 71.47 49.45
REMARK 500 TYR A 398 -60.42 -171.17
REMARK 500 ASN B 58 15.39 -146.69
REMARK 500 ASN B 143 60.25 -112.25
REMARK 500 GLU B 161 -63.65 -125.04
REMARK 500 ASP C 38 1.41 -65.46
REMARK 500 SER C 47 -159.68 -153.36
REMARK 500 ARG C 53 54.20 -112.48
REMARK 500 SER C 95 139.48 -37.82
REMARK 500 ASN C 118 -54.79 -23.27
REMARK 500 GLU C 176 75.90 37.02
REMARK 500 ASN C 188 -161.36 -175.27
REMARK 500 LYS C 191 166.43 175.03
REMARK 500 HIS C 216 -55.27 -135.23
REMARK 500 THR C 241 -158.30 -63.44
REMARK 500 ASP C 243 57.94 -105.52
REMARK 500 HIS C 263 5.04 -66.49
REMARK 500 ARG C 272 -134.57 48.95
REMARK 500 HIS C 300 -61.29 -149.73
REMARK 500 LYS C 326 -174.27 -49.15
REMARK 500 SER C 327 -115.83 -114.81
REMARK 500
REMARK 500 THIS ENTRY HAS 96 RAMACHANDRAN OUTLIERS.
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 A 421 DISTANCE = 5.54 ANGSTROMS
REMARK 525 HOH A 445 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A 446 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 535 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 564 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH A 927 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 930 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH B 394 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH B 667 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH B 669 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH B 923 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH C 416 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH C 469 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH C 471 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH C 502 DISTANCE = 5.06 ANGSTROMS
REMARK 525 HOH C 504 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH C 522 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH C 528 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH C 531 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH C 532 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH C 534 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH C 535 DISTANCE = 5.80 ANGSTROMS
REMARK 525 HOH C 539 DISTANCE = 6.69 ANGSTROMS
REMARK 525 HOH C 544 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH C 550 DISTANCE = 6.81 ANGSTROMS
REMARK 525 HOH C 626 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH C 634 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH C 828 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH C 864 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH D 566 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH D 727 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH E 440 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH E 443 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH E 582 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH E 587 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH E 591 DISTANCE = 5.36 ANGSTROMS
REMARK 525 HOH E 601 DISTANCE = 5.76 ANGSTROMS
REMARK 525 HOH E 618 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH E 826 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH E 837 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH G 449 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH G 461 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH G 462 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH G 466 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH G 469 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH G 483 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH G 484 DISTANCE = 5.81 ANGSTROMS
REMARK 525 HOH G 519 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH G 520 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH G 526 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH G 674 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH G 693 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH H 486 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH H 504 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH H 515 DISTANCE = 5.48 ANGSTROMS
DBREF 3OUR A 1 415 UNP Q8DF91 Y328_VIBVU 1 415
DBREF 3OUR B 1 169 UNP Q8DFJ9 Q8DFJ9_VIBVU 1 169
DBREF 3OUR C 1 415 UNP Q8DF91 Y328_VIBVU 1 415
DBREF 3OUR D 1 169 UNP Q8DFJ9 Q8DFJ9_VIBVU 1 169
DBREF 3OUR E 1 415 UNP Q8DF91 Y328_VIBVU 1 415
DBREF 3OUR F 1 169 UNP Q8DFJ9 Q8DFJ9_VIBVU 1 169
DBREF 3OUR G 1 415 UNP Q8DF91 Y328_VIBVU 1 415
DBREF 3OUR H 1 169 UNP Q8DFJ9 Q8DFJ9_VIBVU 1 169
SEQADV 3OUR MET A -19 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ARG A -18 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY A -17 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER A -16 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -15 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -14 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -13 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -12 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -11 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS A -10 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY A -9 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER A -8 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ALA A -7 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR CYS A -6 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLU A -5 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR LEU A -4 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY A -3 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR THR A -2 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR PRO A -1 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ASN A 0 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR MET B -13 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ARG B -12 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY B -11 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER B -10 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -9 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -8 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -7 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -6 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -5 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS B -4 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY B -3 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER B -2 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ASP B -1 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR THR B 0 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR MET C -19 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ARG C -18 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY C -17 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER C -16 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -15 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -14 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -13 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -12 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -11 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS C -10 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY C -9 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER C -8 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ALA C -7 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR CYS C -6 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLU C -5 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR LEU C -4 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY C -3 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR THR C -2 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR PRO C -1 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ASN C 0 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR MET D -13 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ARG D -12 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY D -11 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER D -10 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -9 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -8 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -7 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -6 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -5 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS D -4 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY D -3 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER D -2 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ASP D -1 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR THR D 0 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR MET E -19 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ARG E -18 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY E -17 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER E -16 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -15 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -14 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -13 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -12 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -11 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS E -10 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY E -9 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER E -8 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ALA E -7 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR CYS E -6 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLU E -5 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR LEU E -4 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY E -3 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR THR E -2 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR PRO E -1 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ASN E 0 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR MET F -13 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ARG F -12 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY F -11 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER F -10 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -9 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -8 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -7 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -6 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -5 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS F -4 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY F -3 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER F -2 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ASP F -1 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR THR F 0 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR MET G -19 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ARG G -18 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY G -17 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER G -16 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -15 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -14 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -13 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -12 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -11 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR HIS G -10 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY G -9 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR SER G -8 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ALA G -7 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR CYS G -6 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLU G -5 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR LEU G -4 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR GLY G -3 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR THR G -2 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR PRO G -1 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR ASN G 0 UNP Q8DF91 EXPRESSION TAG
SEQADV 3OUR MET H -13 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ARG H -12 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY H -11 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER H -10 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -9 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -8 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -7 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -6 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -5 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR HIS H -4 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR GLY H -3 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR SER H -2 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR ASP H -1 UNP Q8DFJ9 EXPRESSION TAG
SEQADV 3OUR THR H 0 UNP Q8DFJ9 EXPRESSION TAG
SEQRES 1 A 435 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 A 435 CYS GLU LEU GLY THR PRO ASN MET SER GLU GLU VAL SER
SEQRES 3 A 435 LYS ASN LEU SER GLU THR LEU PHE VAL LYS HIS LYS GLN
SEQRES 4 A 435 ALA LYS GLU THR SER ALA LEU THR GLN TYR MET PRO THR
SEQRES 5 A 435 SER GLN SER LEU LEU ASP GLU ILE LYS GLU LYS ASN GLY
SEQRES 6 A 435 PHE SER TRP TYR ARG ASN LEU ARG ARG LEU GLN TRP VAL
SEQRES 7 A 435 TRP GLN GLY VAL ASP PRO ILE GLU GLN GLU GLN VAL LEU
SEQRES 8 A 435 ALA ARG ILE ALA SER SER LYS HIS SER ARG THR ASP GLU
SEQRES 9 A 435 GLN TRP LEU ASP THR VAL MET GLY TYR HIS SER GLY ASN
SEQRES 10 A 435 TRP ALA TYR GLU TRP THR ARG LEU GLY MET GLU HIS GLN
SEQRES 11 A 435 LYS ARG ALA GLY GLU MET THR ASN GLU ALA ALA SER GLU
SEQRES 12 A 435 ALA LEU PHE SER ALA SER LEU CYS TYR SER ILE ALA GLY
SEQRES 13 A 435 TYR PRO HIS LEU LYS SER ASP ASN LEU ALA ILE GLN ALA
SEQRES 14 A 435 GLN VAL LEU ALA ASN SER ALA TYR LEU GLU ALA ALA LYS
SEQRES 15 A 435 LYS SER LYS TYR ILE ILE LYS GLN LEU GLU ILE PRO PHE
SEQRES 16 A 435 GLU LYS GLY LYS ILE THR ALA HIS LEU HIS LEU THR ASN
SEQRES 17 A 435 THR ASP LYS PRO HIS PRO VAL VAL ILE VAL SER ALA GLY
SEQRES 18 A 435 LEU ASP SER LEU GLN THR ASP MET TRP ARG LEU PHE ARG
SEQRES 19 A 435 ASP HIS LEU ALA LYS HIS ASP ILE ALA MET LEU THR VAL
SEQRES 20 A 435 ASP MET PRO SER VAL GLY TYR SER SER LYS TYR PRO LEU
SEQRES 21 A 435 THR GLU ASP TYR SER ARG LEU HIS GLN ALA VAL LEU ASN
SEQRES 22 A 435 GLU LEU PHE SER ILE PRO TYR VAL ASP HIS HIS ARG VAL
SEQRES 23 A 435 GLY LEU ILE GLY PHE ARG PHE GLY GLY ASN ALA MET VAL
SEQRES 24 A 435 ARG LEU SER PHE LEU GLU GLN GLU LYS ILE LYS ALA CYS
SEQRES 25 A 435 VAL ILE LEU GLY ALA PRO ILE HIS ASP ILE PHE ALA SER
SEQRES 26 A 435 PRO GLN LYS LEU GLN GLN MET PRO LYS MET TYR LEU ASP
SEQRES 27 A 435 VAL LEU ALA SER ARG LEU GLY LYS SER VAL VAL ASP ILE
SEQRES 28 A 435 TYR SER LEU SER GLY GLN MET ALA ALA TRP SER LEU LYS
SEQRES 29 A 435 VAL GLN GLY PHE LEU SER SER ARG LYS THR LYS VAL PRO
SEQRES 30 A 435 ILE LEU ALA MET SER LEU GLU GLY ASP PRO VAL SER PRO
SEQRES 31 A 435 TYR SER ASP ASN GLN MET VAL ALA PHE PHE SER THR TYR
SEQRES 32 A 435 GLY LYS ALA LYS LYS ILE SER SER LYS THR ILE THR GLN
SEQRES 33 A 435 GLY TYR GLU GLN SER LEU ASP LEU ALA ILE LYS TRP LEU
SEQRES 34 A 435 GLU ASP GLU LEU LEU ARG
SEQRES 1 B 183 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 B 183 THR MET GLY LEU PHE ASP LYS LEU LYS LYS LEU VAL SER
SEQRES 3 B 183 ASP ASP SER ALA SER ALA GLY ALA ILE GLU ILE ILE ALA
SEQRES 4 B 183 PRO LEU SER GLY GLU ILE VAL ASN ILE GLU ASP VAL PRO
SEQRES 5 B 183 ASP VAL VAL PHE ALA GLU LYS ILE VAL GLY ASP GLY ILE
SEQRES 6 B 183 ALA ILE LYS PRO THR GLY ASN LYS MET VAL ALA PRO VAL
SEQRES 7 B 183 ASN GLY THR ILE GLY LYS ILE PHE GLU THR ASN HIS ALA
SEQRES 8 B 183 PHE SER ILE GLU SER ASP ASP GLY VAL GLU LEU PHE VAL
SEQRES 9 B 183 HIS PHE GLY ILE ASP THR VAL GLU LEU LYS GLY GLU GLY
SEQRES 10 B 183 PHE THR ARG ILE ALA GLU GLU GLY GLN THR VAL LYS ALA
SEQRES 11 B 183 GLY ASP THR VAL ILE GLU PHE ASP LEU ALA LEU LEU GLU
SEQRES 12 B 183 GLU LYS ALA LYS SER THR LEU THR PRO VAL VAL ILE SER
SEQRES 13 B 183 ASN MET ASP GLU ILE LYS GLU LEU ASN LYS LEU SER GLY
SEQRES 14 B 183 SER VAL VAL VAL GLY GLU THR PRO VAL LEU ARG VAL THR
SEQRES 15 B 183 LYS
SEQRES 1 C 435 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 C 435 CYS GLU LEU GLY THR PRO ASN MET SER GLU GLU VAL SER
SEQRES 3 C 435 LYS ASN LEU SER GLU THR LEU PHE VAL LYS HIS LYS GLN
SEQRES 4 C 435 ALA LYS GLU THR SER ALA LEU THR GLN TYR MET PRO THR
SEQRES 5 C 435 SER GLN SER LEU LEU ASP GLU ILE LYS GLU LYS ASN GLY
SEQRES 6 C 435 PHE SER TRP TYR ARG ASN LEU ARG ARG LEU GLN TRP VAL
SEQRES 7 C 435 TRP GLN GLY VAL ASP PRO ILE GLU GLN GLU GLN VAL LEU
SEQRES 8 C 435 ALA ARG ILE ALA SER SER LYS HIS SER ARG THR ASP GLU
SEQRES 9 C 435 GLN TRP LEU ASP THR VAL MET GLY TYR HIS SER GLY ASN
SEQRES 10 C 435 TRP ALA TYR GLU TRP THR ARG LEU GLY MET GLU HIS GLN
SEQRES 11 C 435 LYS ARG ALA GLY GLU MET THR ASN GLU ALA ALA SER GLU
SEQRES 12 C 435 ALA LEU PHE SER ALA SER LEU CYS TYR SER ILE ALA GLY
SEQRES 13 C 435 TYR PRO HIS LEU LYS SER ASP ASN LEU ALA ILE GLN ALA
SEQRES 14 C 435 GLN VAL LEU ALA ASN SER ALA TYR LEU GLU ALA ALA LYS
SEQRES 15 C 435 LYS SER LYS TYR ILE ILE LYS GLN LEU GLU ILE PRO PHE
SEQRES 16 C 435 GLU LYS GLY LYS ILE THR ALA HIS LEU HIS LEU THR ASN
SEQRES 17 C 435 THR ASP LYS PRO HIS PRO VAL VAL ILE VAL SER ALA GLY
SEQRES 18 C 435 LEU ASP SER LEU GLN THR ASP MET TRP ARG LEU PHE ARG
SEQRES 19 C 435 ASP HIS LEU ALA LYS HIS ASP ILE ALA MET LEU THR VAL
SEQRES 20 C 435 ASP MET PRO SER VAL GLY TYR SER SER LYS TYR PRO LEU
SEQRES 21 C 435 THR GLU ASP TYR SER ARG LEU HIS GLN ALA VAL LEU ASN
SEQRES 22 C 435 GLU LEU PHE SER ILE PRO TYR VAL ASP HIS HIS ARG VAL
SEQRES 23 C 435 GLY LEU ILE GLY PHE ARG PHE GLY GLY ASN ALA MET VAL
SEQRES 24 C 435 ARG LEU SER PHE LEU GLU GLN GLU LYS ILE LYS ALA CYS
SEQRES 25 C 435 VAL ILE LEU GLY ALA PRO ILE HIS ASP ILE PHE ALA SER
SEQRES 26 C 435 PRO GLN LYS LEU GLN GLN MET PRO LYS MET TYR LEU ASP
SEQRES 27 C 435 VAL LEU ALA SER ARG LEU GLY LYS SER VAL VAL ASP ILE
SEQRES 28 C 435 TYR SER LEU SER GLY GLN MET ALA ALA TRP SER LEU LYS
SEQRES 29 C 435 VAL GLN GLY PHE LEU SER SER ARG LYS THR LYS VAL PRO
SEQRES 30 C 435 ILE LEU ALA MET SER LEU GLU GLY ASP PRO VAL SER PRO
SEQRES 31 C 435 TYR SER ASP ASN GLN MET VAL ALA PHE PHE SER THR TYR
SEQRES 32 C 435 GLY LYS ALA LYS LYS ILE SER SER LYS THR ILE THR GLN
SEQRES 33 C 435 GLY TYR GLU GLN SER LEU ASP LEU ALA ILE LYS TRP LEU
SEQRES 34 C 435 GLU ASP GLU LEU LEU ARG
SEQRES 1 D 183 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 D 183 THR MET GLY LEU PHE ASP LYS LEU LYS LYS LEU VAL SER
SEQRES 3 D 183 ASP ASP SER ALA SER ALA GLY ALA ILE GLU ILE ILE ALA
SEQRES 4 D 183 PRO LEU SER GLY GLU ILE VAL ASN ILE GLU ASP VAL PRO
SEQRES 5 D 183 ASP VAL VAL PHE ALA GLU LYS ILE VAL GLY ASP GLY ILE
SEQRES 6 D 183 ALA ILE LYS PRO THR GLY ASN LYS MET VAL ALA PRO VAL
SEQRES 7 D 183 ASN GLY THR ILE GLY LYS ILE PHE GLU THR ASN HIS ALA
SEQRES 8 D 183 PHE SER ILE GLU SER ASP ASP GLY VAL GLU LEU PHE VAL
SEQRES 9 D 183 HIS PHE GLY ILE ASP THR VAL GLU LEU LYS GLY GLU GLY
SEQRES 10 D 183 PHE THR ARG ILE ALA GLU GLU GLY GLN THR VAL LYS ALA
SEQRES 11 D 183 GLY ASP THR VAL ILE GLU PHE ASP LEU ALA LEU LEU GLU
SEQRES 12 D 183 GLU LYS ALA LYS SER THR LEU THR PRO VAL VAL ILE SER
SEQRES 13 D 183 ASN MET ASP GLU ILE LYS GLU LEU ASN LYS LEU SER GLY
SEQRES 14 D 183 SER VAL VAL VAL GLY GLU THR PRO VAL LEU ARG VAL THR
SEQRES 15 D 183 LYS
SEQRES 1 E 435 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 E 435 CYS GLU LEU GLY THR PRO ASN MET SER GLU GLU VAL SER
SEQRES 3 E 435 LYS ASN LEU SER GLU THR LEU PHE VAL LYS HIS LYS GLN
SEQRES 4 E 435 ALA LYS GLU THR SER ALA LEU THR GLN TYR MET PRO THR
SEQRES 5 E 435 SER GLN SER LEU LEU ASP GLU ILE LYS GLU LYS ASN GLY
SEQRES 6 E 435 PHE SER TRP TYR ARG ASN LEU ARG ARG LEU GLN TRP VAL
SEQRES 7 E 435 TRP GLN GLY VAL ASP PRO ILE GLU GLN GLU GLN VAL LEU
SEQRES 8 E 435 ALA ARG ILE ALA SER SER LYS HIS SER ARG THR ASP GLU
SEQRES 9 E 435 GLN TRP LEU ASP THR VAL MET GLY TYR HIS SER GLY ASN
SEQRES 10 E 435 TRP ALA TYR GLU TRP THR ARG LEU GLY MET GLU HIS GLN
SEQRES 11 E 435 LYS ARG ALA GLY GLU MET THR ASN GLU ALA ALA SER GLU
SEQRES 12 E 435 ALA LEU PHE SER ALA SER LEU CYS TYR SER ILE ALA GLY
SEQRES 13 E 435 TYR PRO HIS LEU LYS SER ASP ASN LEU ALA ILE GLN ALA
SEQRES 14 E 435 GLN VAL LEU ALA ASN SER ALA TYR LEU GLU ALA ALA LYS
SEQRES 15 E 435 LYS SER LYS TYR ILE ILE LYS GLN LEU GLU ILE PRO PHE
SEQRES 16 E 435 GLU LYS GLY LYS ILE THR ALA HIS LEU HIS LEU THR ASN
SEQRES 17 E 435 THR ASP LYS PRO HIS PRO VAL VAL ILE VAL SER ALA GLY
SEQRES 18 E 435 LEU ASP SER LEU GLN THR ASP MET TRP ARG LEU PHE ARG
SEQRES 19 E 435 ASP HIS LEU ALA LYS HIS ASP ILE ALA MET LEU THR VAL
SEQRES 20 E 435 ASP MET PRO SER VAL GLY TYR SER SER LYS TYR PRO LEU
SEQRES 21 E 435 THR GLU ASP TYR SER ARG LEU HIS GLN ALA VAL LEU ASN
SEQRES 22 E 435 GLU LEU PHE SER ILE PRO TYR VAL ASP HIS HIS ARG VAL
SEQRES 23 E 435 GLY LEU ILE GLY PHE ARG PHE GLY GLY ASN ALA MET VAL
SEQRES 24 E 435 ARG LEU SER PHE LEU GLU GLN GLU LYS ILE LYS ALA CYS
SEQRES 25 E 435 VAL ILE LEU GLY ALA PRO ILE HIS ASP ILE PHE ALA SER
SEQRES 26 E 435 PRO GLN LYS LEU GLN GLN MET PRO LYS MET TYR LEU ASP
SEQRES 27 E 435 VAL LEU ALA SER ARG LEU GLY LYS SER VAL VAL ASP ILE
SEQRES 28 E 435 TYR SER LEU SER GLY GLN MET ALA ALA TRP SER LEU LYS
SEQRES 29 E 435 VAL GLN GLY PHE LEU SER SER ARG LYS THR LYS VAL PRO
SEQRES 30 E 435 ILE LEU ALA MET SER LEU GLU GLY ASP PRO VAL SER PRO
SEQRES 31 E 435 TYR SER ASP ASN GLN MET VAL ALA PHE PHE SER THR TYR
SEQRES 32 E 435 GLY LYS ALA LYS LYS ILE SER SER LYS THR ILE THR GLN
SEQRES 33 E 435 GLY TYR GLU GLN SER LEU ASP LEU ALA ILE LYS TRP LEU
SEQRES 34 E 435 GLU ASP GLU LEU LEU ARG
SEQRES 1 F 183 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 F 183 THR MET GLY LEU PHE ASP LYS LEU LYS LYS LEU VAL SER
SEQRES 3 F 183 ASP ASP SER ALA SER ALA GLY ALA ILE GLU ILE ILE ALA
SEQRES 4 F 183 PRO LEU SER GLY GLU ILE VAL ASN ILE GLU ASP VAL PRO
SEQRES 5 F 183 ASP VAL VAL PHE ALA GLU LYS ILE VAL GLY ASP GLY ILE
SEQRES 6 F 183 ALA ILE LYS PRO THR GLY ASN LYS MET VAL ALA PRO VAL
SEQRES 7 F 183 ASN GLY THR ILE GLY LYS ILE PHE GLU THR ASN HIS ALA
SEQRES 8 F 183 PHE SER ILE GLU SER ASP ASP GLY VAL GLU LEU PHE VAL
SEQRES 9 F 183 HIS PHE GLY ILE ASP THR VAL GLU LEU LYS GLY GLU GLY
SEQRES 10 F 183 PHE THR ARG ILE ALA GLU GLU GLY GLN THR VAL LYS ALA
SEQRES 11 F 183 GLY ASP THR VAL ILE GLU PHE ASP LEU ALA LEU LEU GLU
SEQRES 12 F 183 GLU LYS ALA LYS SER THR LEU THR PRO VAL VAL ILE SER
SEQRES 13 F 183 ASN MET ASP GLU ILE LYS GLU LEU ASN LYS LEU SER GLY
SEQRES 14 F 183 SER VAL VAL VAL GLY GLU THR PRO VAL LEU ARG VAL THR
SEQRES 15 F 183 LYS
SEQRES 1 G 435 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ALA
SEQRES 2 G 435 CYS GLU LEU GLY THR PRO ASN MET SER GLU GLU VAL SER
SEQRES 3 G 435 LYS ASN LEU SER GLU THR LEU PHE VAL LYS HIS LYS GLN
SEQRES 4 G 435 ALA LYS GLU THR SER ALA LEU THR GLN TYR MET PRO THR
SEQRES 5 G 435 SER GLN SER LEU LEU ASP GLU ILE LYS GLU LYS ASN GLY
SEQRES 6 G 435 PHE SER TRP TYR ARG ASN LEU ARG ARG LEU GLN TRP VAL
SEQRES 7 G 435 TRP GLN GLY VAL ASP PRO ILE GLU GLN GLU GLN VAL LEU
SEQRES 8 G 435 ALA ARG ILE ALA SER SER LYS HIS SER ARG THR ASP GLU
SEQRES 9 G 435 GLN TRP LEU ASP THR VAL MET GLY TYR HIS SER GLY ASN
SEQRES 10 G 435 TRP ALA TYR GLU TRP THR ARG LEU GLY MET GLU HIS GLN
SEQRES 11 G 435 LYS ARG ALA GLY GLU MET THR ASN GLU ALA ALA SER GLU
SEQRES 12 G 435 ALA LEU PHE SER ALA SER LEU CYS TYR SER ILE ALA GLY
SEQRES 13 G 435 TYR PRO HIS LEU LYS SER ASP ASN LEU ALA ILE GLN ALA
SEQRES 14 G 435 GLN VAL LEU ALA ASN SER ALA TYR LEU GLU ALA ALA LYS
SEQRES 15 G 435 LYS SER LYS TYR ILE ILE LYS GLN LEU GLU ILE PRO PHE
SEQRES 16 G 435 GLU LYS GLY LYS ILE THR ALA HIS LEU HIS LEU THR ASN
SEQRES 17 G 435 THR ASP LYS PRO HIS PRO VAL VAL ILE VAL SER ALA GLY
SEQRES 18 G 435 LEU ASP SER LEU GLN THR ASP MET TRP ARG LEU PHE ARG
SEQRES 19 G 435 ASP HIS LEU ALA LYS HIS ASP ILE ALA MET LEU THR VAL
SEQRES 20 G 435 ASP MET PRO SER VAL GLY TYR SER SER LYS TYR PRO LEU
SEQRES 21 G 435 THR GLU ASP TYR SER ARG LEU HIS GLN ALA VAL LEU ASN
SEQRES 22 G 435 GLU LEU PHE SER ILE PRO TYR VAL ASP HIS HIS ARG VAL
SEQRES 23 G 435 GLY LEU ILE GLY PHE ARG PHE GLY GLY ASN ALA MET VAL
SEQRES 24 G 435 ARG LEU SER PHE LEU GLU GLN GLU LYS ILE LYS ALA CYS
SEQRES 25 G 435 VAL ILE LEU GLY ALA PRO ILE HIS ASP ILE PHE ALA SER
SEQRES 26 G 435 PRO GLN LYS LEU GLN GLN MET PRO LYS MET TYR LEU ASP
SEQRES 27 G 435 VAL LEU ALA SER ARG LEU GLY LYS SER VAL VAL ASP ILE
SEQRES 28 G 435 TYR SER LEU SER GLY GLN MET ALA ALA TRP SER LEU LYS
SEQRES 29 G 435 VAL GLN GLY PHE LEU SER SER ARG LYS THR LYS VAL PRO
SEQRES 30 G 435 ILE LEU ALA MET SER LEU GLU GLY ASP PRO VAL SER PRO
SEQRES 31 G 435 TYR SER ASP ASN GLN MET VAL ALA PHE PHE SER THR TYR
SEQRES 32 G 435 GLY LYS ALA LYS LYS ILE SER SER LYS THR ILE THR GLN
SEQRES 33 G 435 GLY TYR GLU GLN SER LEU ASP LEU ALA ILE LYS TRP LEU
SEQRES 34 G 435 GLU ASP GLU LEU LEU ARG
SEQRES 1 H 183 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 H 183 THR MET GLY LEU PHE ASP LYS LEU LYS LYS LEU VAL SER
SEQRES 3 H 183 ASP ASP SER ALA SER ALA GLY ALA ILE GLU ILE ILE ALA
SEQRES 4 H 183 PRO LEU SER GLY GLU ILE VAL ASN ILE GLU ASP VAL PRO
SEQRES 5 H 183 ASP VAL VAL PHE ALA GLU LYS ILE VAL GLY ASP GLY ILE
SEQRES 6 H 183 ALA ILE LYS PRO THR GLY ASN LYS MET VAL ALA PRO VAL
SEQRES 7 H 183 ASN GLY THR ILE GLY LYS ILE PHE GLU THR ASN HIS ALA
SEQRES 8 H 183 PHE SER ILE GLU SER ASP ASP GLY VAL GLU LEU PHE VAL
SEQRES 9 H 183 HIS PHE GLY ILE ASP THR VAL GLU LEU LYS GLY GLU GLY
SEQRES 10 H 183 PHE THR ARG ILE ALA GLU GLU GLY GLN THR VAL LYS ALA
SEQRES 11 H 183 GLY ASP THR VAL ILE GLU PHE ASP LEU ALA LEU LEU GLU
SEQRES 12 H 183 GLU LYS ALA LYS SER THR LEU THR PRO VAL VAL ILE SER
SEQRES 13 H 183 ASN MET ASP GLU ILE LYS GLU LEU ASN LYS LEU SER GLY
SEQRES 14 H 183 SER VAL VAL VAL GLY GLU THR PRO VAL LEU ARG VAL THR
SEQRES 15 H 183 LYS
FORMUL 9 HOH *927(H2 O)
HELIX 1 1 GLU A 22 LEU A 26 5 5
HELIX 2 2 MET A 30 GLY A 45 1 16
HELIX 3 3 ARG A 53 GLN A 60 1 8
HELIX 4 4 ASP A 63 SER A 77 1 15
HELIX 5 5 ASN A 97 ARG A 112 1 16
HELIX 6 6 ALA A 113 MET A 116 5 4
HELIX 7 7 THR A 117 TYR A 137 1 21
HELIX 8 8 ASP A 143 LYS A 163 1 21
HELIX 9 9 LEU A 205 ASP A 208 5 4
HELIX 10 10 MET A 209 ASP A 215 1 7
HELIX 11 11 LEU A 217 ASP A 221 5 5
HELIX 12 12 VAL A 232 SER A 236 5 5
HELIX 13 13 SER A 245 LEU A 255 1 11
HELIX 14 14 PHE A 256 ILE A 258 5 3
HELIX 15 15 ARG A 272 GLU A 285 1 14
HELIX 16 16 GLN A 286 ILE A 289 5 4
HELIX 17 17 HIS A 300 ALA A 304 5 5
HELIX 18 18 SER A 305 GLN A 310 1 6
HELIX 19 19 PRO A 313 LEU A 324 1 12
HELIX 20 20 ASP A 330 MET A 338 1 9
HELIX 21 21 ALA A 339 SER A 342 5 4
HELIX 22 22 SER A 372 PHE A 380 1 9
HELIX 23 23 THR A 395 LEU A 413 1 19
HELIX 24 24 GLU B 35 VAL B 37 5 3
HELIX 25 25 ASP B 39 GLU B 44 1 6
HELIX 26 26 ASP B 95 LYS B 100 5 6
HELIX 27 27 ASP B 124 ALA B 132 1 9
HELIX 28 28 ASN B 143 ILE B 147 5 5
HELIX 29 29 GLU C 22 LEU C 26 5 5
HELIX 30 30 MET C 30 LYS C 41 1 12
HELIX 31 31 ARG C 53 GLY C 61 1 9
HELIX 32 32 ASP C 63 SER C 77 1 15
HELIX 33 33 TRP C 86 VAL C 90 5 5
HELIX 34 34 ASN C 97 GLY C 114 1 18
HELIX 35 35 THR C 117 TYR C 137 1 21
HELIX 36 36 ASP C 143 SER C 164 1 22
HELIX 37 37 LEU C 205 ASP C 208 5 4
HELIX 38 38 MET C 209 HIS C 216 1 8
HELIX 39 39 VAL C 232 SER C 236 5 5
HELIX 40 40 SER C 245 ASN C 253 1 9
HELIX 41 41 GLU C 254 ILE C 258 5 5
HELIX 42 42 ARG C 272 GLU C 285 1 14
HELIX 43 43 HIS C 300 ALA C 304 5 5
HELIX 44 44 SER C 305 MET C 312 1 8
HELIX 45 45 PRO C 313 GLY C 325 1 13
HELIX 46 46 ASP C 330 GLN C 337 1 8
HELIX 47 47 MET C 338 SER C 342 5 5
HELIX 48 48 PRO C 370 PHE C 380 1 11
HELIX 49 49 THR C 393 LEU C 413 1 21
HELIX 50 50 GLU D 35 VAL D 37 5 3
HELIX 51 51 ASP D 39 GLU D 44 1 6
HELIX 52 52 ASP D 95 LYS D 100 5 6
HELIX 53 53 ASP D 124 ALA D 132 1 9
HELIX 54 54 ASN D 143 ILE D 147 5 5
HELIX 55 55 GLU E 22 LEU E 26 5 5
HELIX 56 56 MET E 30 GLY E 45 1 16
HELIX 57 57 ARG E 53 GLN E 60 1 8
HELIX 58 58 ASP E 63 SER E 77 1 15
HELIX 59 59 ASN E 97 GLY E 114 1 18
HELIX 60 60 THR E 117 TYR E 137 1 21
HELIX 61 61 ASP E 143 SER E 164 1 22
HELIX 62 62 LEU E 205 ASP E 208 5 4
HELIX 63 63 MET E 209 ASP E 215 1 7
HELIX 64 64 HIS E 216 ASP E 221 5 6
HELIX 65 65 VAL E 232 SER E 236 5 5
HELIX 66 66 SER E 245 ASN E 253 1 9
HELIX 67 67 GLU E 254 ILE E 258 5 5
HELIX 68 68 ARG E 272 GLU E 285 1 14
HELIX 69 69 ASP E 301 ALA E 304 5 4
HELIX 70 70 SER E 305 GLN E 310 1 6
HELIX 71 71 PRO E 313 GLY E 325 1 13
HELIX 72 72 ASP E 330 MET E 338 1 9
HELIX 73 73 ALA E 339 SER E 342 5 4
HELIX 74 74 PRO E 370 PHE E 380 1 11
HELIX 75 75 THR E 393 LEU E 413 1 21
HELIX 76 76 GLU F 35 VAL F 37 5 3
HELIX 77 77 ASP F 39 GLU F 44 1 6
HELIX 78 78 ASP F 95 LYS F 100 5 6
HELIX 79 79 ASP F 124 ALA F 132 1 9
HELIX 80 80 ASN F 143 ILE F 147 5 5
HELIX 81 81 GLU G 22 LEU G 26 5 5
HELIX 82 82 MET G 30 GLY G 45 1 16
HELIX 83 83 ARG G 53 GLY G 61 1 9
HELIX 84 84 ASP G 63 SER G 77 1 15
HELIX 85 85 ASN G 97 GLY G 114 1 18
HELIX 86 86 THR G 117 TYR G 137 1 21
HELIX 87 87 ASP G 143 SER G 164 1 22
HELIX 88 88 LEU G 205 ASP G 208 5 4
HELIX 89 89 MET G 209 HIS G 216 1 8
HELIX 90 90 LEU G 217 ASP G 221 5 5
HELIX 91 91 VAL G 232 SER G 236 5 5
HELIX 92 92 SER G 245 ASN G 253 1 9
HELIX 93 93 GLU G 254 ILE G 258 5 5
HELIX 94 94 ARG G 272 GLU G 285 1 14
HELIX 95 95 SER G 305 GLN G 310 1 6
HELIX 96 96 PRO G 313 GLY G 325 1 13
HELIX 97 97 ASP G 330 ALA G 339 1 10
HELIX 98 98 ALA G 340 SER G 342 5 3
HELIX 99 99 PRO G 370 PHE G 380 1 11
HELIX 100 100 THR G 393 LEU G 414 1 22
HELIX 101 101 GLU H 35 VAL H 37 5 3
HELIX 102 102 ASP H 39 GLU H 44 1 6
HELIX 103 103 ASP H 95 LYS H 100 5 6
HELIX 104 104 ASP H 124 ALA H 132 1 9
HELIX 105 105 ASN H 143 ILE H 147 5 5
SHEET 1 A 7 ILE A 167 PRO A 174 0
SHEET 2 A 7 LYS A 179 LEU A 186 -1 O LEU A 186 N ILE A 167
SHEET 3 A 7 ALA A 223 VAL A 227 -1 O MET A 224 N HIS A 185
SHEET 4 A 7 HIS A 193 SER A 199 1 N VAL A 196 O LEU A 225
SHEET 5 A 7 VAL A 261 PHE A 271 1 O GLY A 267 N VAL A 195
SHEET 6 A 7 ALA A 291 LEU A 295 1 O VAL A 293 N LEU A 268
SHEET 7 A 7 ILE A 358 MET A 361 1 O LEU A 359 N CYS A 292
SHEET 1 B 3 ILE B 21 ILE B 24 0
SHEET 2 B 3 PRO B 163 THR B 168 -1 O VAL B 164 N ILE B 23
SHEET 3 B 3 GLU B 149 LYS B 152 -1 N ASN B 151 O ARG B 166
SHEET 1 C 8 THR B 113 VAL B 114 0
SHEET 2 C 8 GLY B 66 ILE B 71 -1 N GLY B 66 O VAL B 114
SHEET 3 C 8 ALA B 77 SER B 82 -1 O GLU B 81 N THR B 67
SHEET 4 C 8 GLU B 87 HIS B 91 -1 O LEU B 88 N ILE B 80
SHEET 5 C 8 THR B 137 ILE B 141 -1 O PRO B 138 N HIS B 91
SHEET 6 C 8 ASP B 49 PRO B 55 -1 N ASP B 49 O ILE B 141
SHEET 7 C 8 GLY B 29 ASN B 33 -1 N GLU B 30 O LYS B 54
SHEET 8 C 8 SER B 156 VAL B 157 -1 O VAL B 157 N GLY B 29
SHEET 1 D 3 LYS B 59 VAL B 61 0
SHEET 2 D 3 THR B 119 PHE B 123 -1 O ILE B 121 N MET B 60
SHEET 3 D 3 PHE B 104 ARG B 106 -1 N THR B 105 O GLU B 122
SHEET 1 E 8 ILE C 167 PRO C 174 0
SHEET 2 E 8 LYS C 179 LEU C 186 -1 O ALA C 182 N LEU C 171
SHEET 3 E 8 ALA C 223 VAL C 227 -1 O THR C 226 N HIS C 183
SHEET 4 E 8 HIS C 193 SER C 199 1 N VAL C 198 O LEU C 225
SHEET 5 E 8 VAL C 261 PHE C 271 1 O GLY C 267 N VAL C 195
SHEET 6 E 8 ALA C 291 LEU C 295 1 O VAL C 293 N LEU C 268
SHEET 7 E 8 ILE C 358 LEU C 363 1 O LEU C 359 N CYS C 292
SHEET 8 E 8 LYS C 385 ILE C 389 1 O LYS C 385 N ALA C 360
SHEET 1 F 3 ILE D 21 ILE D 24 0
SHEET 2 F 3 PRO D 163 THR D 168 -1 O LEU D 165 N ILE D 23
SHEET 3 F 3 GLU D 149 LYS D 152 -1 N ASN D 151 O ARG D 166
SHEET 1 G 8 THR D 113 VAL D 114 0
SHEET 2 G 8 GLY D 66 ILE D 71 -1 N GLY D 66 O VAL D 114
SHEET 3 G 8 ALA D 77 SER D 82 -1 O SER D 79 N LYS D 70
SHEET 4 G 8 GLU D 87 HIS D 91 -1 O LEU D 88 N ILE D 80
SHEET 5 G 8 THR D 137 ILE D 141 -1 O VAL D 140 N PHE D 89
SHEET 6 G 8 ASP D 49 PRO D 55 -1 N ILE D 51 O VAL D 139
SHEET 7 G 8 GLY D 29 ASN D 33 -1 N VAL D 32 O ALA D 52
SHEET 8 G 8 SER D 156 VAL D 157 -1 O VAL D 157 N GLY D 29
SHEET 1 H 3 LYS D 59 VAL D 61 0
SHEET 2 H 3 THR D 119 PHE D 123 -1 O ILE D 121 N MET D 60
SHEET 3 H 3 PHE D 104 ARG D 106 -1 N THR D 105 O GLU D 122
SHEET 1 I 2 GLN E 28 TYR E 29 0
SHEET 2 I 2 VAL E 328 VAL E 329 1 O VAL E 329 N GLN E 28
SHEET 1 J 8 ILE E 167 PHE E 175 0
SHEET 2 J 8 GLY E 178 LEU E 186 -1 O ILE E 180 N ILE E 173
SHEET 3 J 8 ALA E 223 VAL E 227 -1 O MET E 224 N HIS E 185
SHEET 4 J 8 HIS E 193 SER E 199 1 N VAL E 198 O LEU E 225
SHEET 5 J 8 VAL E 261 PHE E 271 1 O GLY E 267 N VAL E 195
SHEET 6 J 8 ALA E 291 LEU E 295 1 O LEU E 295 N GLY E 270
SHEET 7 J 8 ILE E 358 LEU E 363 1 O LEU E 359 N CYS E 292
SHEET 8 J 8 LYS E 385 ILE E 389 1 O LYS E 385 N ALA E 360
SHEET 1 K 3 ILE F 21 ILE F 24 0
SHEET 2 K 3 PRO F 163 THR F 168 -1 O VAL F 167 N ILE F 21
SHEET 3 K 3 GLU F 149 LYS F 152 -1 N ASN F 151 O ARG F 166
SHEET 1 L 8 THR F 113 VAL F 114 0
SHEET 2 L 8 GLY F 66 ILE F 71 -1 N GLY F 66 O VAL F 114
SHEET 3 L 8 ALA F 77 SER F 82 -1 O SER F 79 N GLY F 69
SHEET 4 L 8 GLU F 87 HIS F 91 -1 O LEU F 88 N ILE F 80
SHEET 5 L 8 THR F 137 ILE F 141 -1 O VAL F 140 N PHE F 89
SHEET 6 L 8 ASP F 49 PRO F 55 -1 N ILE F 51 O VAL F 139
SHEET 7 L 8 GLY F 29 ASN F 33 -1 N VAL F 32 O ALA F 52
SHEET 8 L 8 SER F 156 VAL F 157 -1 O VAL F 157 N GLY F 29
SHEET 1 M 3 LYS F 59 VAL F 61 0
SHEET 2 M 3 THR F 119 PHE F 123 -1 O ILE F 121 N MET F 60
SHEET 3 M 3 PHE F 104 ARG F 106 -1 N THR F 105 O GLU F 122
SHEET 1 N 2 GLN G 28 TYR G 29 0
SHEET 2 N 2 VAL G 328 VAL G 329 1 O VAL G 329 N GLN G 28
SHEET 1 O 8 ILE G 167 PHE G 175 0
SHEET 2 O 8 GLY G 178 LEU G 186 -1 O LEU G 186 N ILE G 167
SHEET 3 O 8 ALA G 223 VAL G 227 -1 O MET G 224 N HIS G 185
SHEET 4 O 8 HIS G 193 SER G 199 1 N VAL G 196 O LEU G 225
SHEET 5 O 8 VAL G 261 PHE G 271 1 O GLY G 267 N VAL G 195
SHEET 6 O 8 ALA G 291 LEU G 295 1 O VAL G 293 N LEU G 268
SHEET 7 O 8 ILE G 358 LEU G 363 1 O LEU G 359 N CYS G 292
SHEET 8 O 8 LYS G 385 ILE G 389 1 O ILE G 389 N SER G 362
SHEET 1 P 3 ILE H 21 ILE H 24 0
SHEET 2 P 3 PRO H 163 THR H 168 -1 O LEU H 165 N ILE H 23
SHEET 3 P 3 GLU H 149 LYS H 152 -1 N ASN H 151 O ARG H 166
SHEET 1 Q 8 THR H 113 VAL H 114 0
SHEET 2 Q 8 GLY H 66 ILE H 71 -1 N GLY H 66 O VAL H 114
SHEET 3 Q 8 ALA H 77 SER H 82 -1 O SER H 79 N GLY H 69
SHEET 4 Q 8 GLU H 87 HIS H 91 -1 O LEU H 88 N ILE H 80
SHEET 5 Q 8 THR H 137 ILE H 141 -1 O VAL H 140 N PHE H 89
SHEET 6 Q 8 ASP H 49 PRO H 55 -1 N ILE H 51 O VAL H 139
SHEET 7 Q 8 GLY H 29 ASN H 33 -1 N VAL H 32 O ALA H 52
SHEET 8 Q 8 SER H 156 VAL H 157 -1 O VAL H 157 N GLY H 29
SHEET 1 R 3 LYS H 59 VAL H 61 0
SHEET 2 R 3 THR H 119 PHE H 123 -1 O VAL H 120 N MET H 60
SHEET 3 R 3 PHE H 104 ARG H 106 -1 N THR H 105 O GLU H 122
CISPEP 1 TYR A 137 PRO A 138 0 0.28
CISPEP 2 TYR C 137 PRO C 138 0 0.13
CISPEP 3 TYR E 137 PRO E 138 0 0.40
CISPEP 4 TYR G 137 PRO G 138 0 0.28
CRYST1 322.866 62.067 126.362 90.00 110.80 90.00 C 1 2 1 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.003097 0.000000 0.001177 0.00000
SCALE2 0.000000 0.016112 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008466 0.00000
TER 3019 LEU A 414
TER 4141 LYS B 169
TER 7221 LEU C 413
TER 8339 LYS D 169
TER 11388 LEU E 414
TER 12510 LYS F 169
TER 15609 ARG G 415
TER 16731 LYS H 169
MASTER 807 0 0 105 91 0 0 617650 8 0 196
END |