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HEADER HYDROLASE 26-JUL-99 1C2O
TITLE ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYLCHOLINESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: A4 FORM;
COMPND 5 EC: 3.1.1.7
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ELECTROPHORUS ELECTRICUS;
SOURCE 3 ORGANISM_COMMON: ELECTRIC EEL;
SOURCE 4 OTHER_DETAILS: ELECTRIC ORGAN
KEYWDS SERINE HYDROLASE, ALPHA/BETA HYDROLASE, TETRAMER
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.BOURNE,P.MARCHOT
REVDAT 1 19-JAN-00 1C2O 0
JRNL AUTH Y.BOURNE,J.GRASSI,P.E.BOUGIS,P.MARCHOT
JRNL TITL CONFORMATIONAL FLEXIBILITY OF THE
JRNL TITL 2 ACETYLCHOLINESTERASE TETRAMER SUGGESTED BY X-RAY
JRNL TITL 3 CRYSTALLOGRAPHY
JRNL REF J.BIOL.CHEM. V. 274 30370 1999
JRNL REFN ASTM JBCHA3 US ISSN 0021-9258
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 66.0
REMARK 3 NUMBER OF REFLECTIONS : 24590
REMARK 3
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.375
REMARK 3 FREE R VALUE : 0.385
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 : 16688
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
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
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 1C2O COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-1999.
REMARK 100 THE RCSB ID CODE IS RCSB009404.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-1996
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24590
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.200
REMARK 200 RESOLUTION RANGE LOW (A) : 12.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 66.0
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.18000
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) : 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 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): NULL
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M AMMONIUM SULFATE
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 1/2+X,1/2+Y,Z
REMARK 290 4555 1/2-X,1/2+Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 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 105.58000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 105.58000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 64.87500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ASP A 491 CG OD1 OD2
REMARK 470 ARG A 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 494 CG OD1 OD2
REMARK 470 SER A 495 OG
REMARK 470 LYS A 496 CG CD CE NZ
REMARK 470 SER A 497 OG
REMARK 470 ASP B 491 CG OD1 OD2
REMARK 470 ARG B 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 494 CG OD1 OD2
REMARK 470 SER B 495 OG
REMARK 470 LYS B 496 CG CD CE NZ
REMARK 470 SER B 497 OG
REMARK 470 ASP C 491 CG OD1 OD2
REMARK 470 ARG C 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 494 CG OD1 OD2
REMARK 470 SER C 495 OG
REMARK 470 LYS C 496 CG CD CE NZ
REMARK 470 SER C 497 OG
REMARK 470 ASP D 491 CG OD1 OD2
REMARK 470 ARG D 493 CG CD NE CZ NH1 NH2
REMARK 470 ASP D 494 CG OD1 OD2
REMARK 470 SER D 495 OG
REMARK 470 LYS D 496 CG CD CE NZ
REMARK 470 SER D 497 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OD1 ASP A 306 CB PRO B 259 1.98
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE2 TYR C 105 NH2 ARG C 21 2655 0.66
REMARK 500 O PRO A 88 CG GLU A 91 2554 1.08
REMARK 500 CZ TYR C 105 NH2 ARG C 21 2655 1.12
REMARK 500 CD GLU A 91 O PRO A 88 2554 1.17
REMARK 500 NZ LYS C 23 OH TYR C 105 2655 1.21
REMARK 500 O PRO A 88 OE1 GLU A 91 2554 1.53
REMARK 500 NH1 ARG C 21 NH1 ARG C 21 2655 1.61
REMARK 500 CZ ARG C 21 CE2 TYR C 105 2655 1.72
REMARK 500 NH1 ARG C 21 CD ARG C 21 2655 1.78
REMARK 500 O ASN A 87 OE1 GLU A 91 2554 1.82
REMARK 500 C PRO A 88 OE1 GLU A 91 2554 1.85
REMARK 500 NH2 ARG C 21 CD2 TYR C 105 2655 1.93
REMARK 500 CE LYS C 23 OH TYR C 105 2655 1.94
REMARK 500 NH2 ARG C 21 OH TYR C 105 2655 1.95
REMARK 500 C ASN A 87 OE1 GLU A 91 2554 2.02
REMARK 500 NH1 ARG C 21 CZ ARG C 21 2655 2.15
REMARK 500 C PRO A 88 CG GLU A 91 2554 2.19
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 THR A 543 CA - C - O ANGL. DEV. = 15.9 DEGREES
REMARK 500 THR B 543 CA - C - O ANGL. DEV. = 15.9 DEGREES
REMARK 500 THR C 543 CA - C - O ANGL. DEV. = 15.9 DEGREES
REMARK 500 THR D 543 CA - C - O ANGL. DEV. = 15.8 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 LEU A 76 43.27 -74.73
REMARK 500 SER A 203 27.43 -121.02
REMARK 500 LEU B 76 43.28 -74.82
REMARK 500 SER B 203 27.33 -121.01
REMARK 500 LEU C 76 43.16 -74.76
REMARK 500 SER C 203 27.43 -121.03
REMARK 500 LEU D 76 43.31 -74.86
REMARK 500 SER D 203 27.48 -121.13
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEA RELATED DB: PDB
REMARK 900 RELATED ID: 1C2B RELATED DB: PDB
REMARK 900 RELATED ID: 1MAA RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE LISTED IN THE SEQRES RECORD IS OF
REMARK 999 MOUSE ACETYLCHOLINESTERASE, (CORRESPONDING TO
REMARK 999 THE STRUCTURE) NOT OF ELECTROPHORUS ELECTRICUS.
REMARK 999 AT THE RESOLUTION OF THE EXPERIMENTAL DATA (4.2A)
REMARK 999 NO SEQUENCE DISCREPANCIES CAN BE SEEN.
DBREF 1C2O A 5 543 SWS P21836 ACES_MOUSE 36 574
DBREF 1C2O B 5 543 SWS P21836 ACES_MOUSE 36 574
DBREF 1C2O C 5 543 SWS P21836 ACES_MOUSE 36 574
DBREF 1C2O D 5 543 SWS P21836 ACES_MOUSE 36 574
SEQRES 1 A 539 ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN LEU
SEQRES 2 A 539 ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL SER
SEQRES 3 A 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY
SEQRES 4 A 539 SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO TRP
SEQRES 5 A 539 SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL CYS
SEQRES 6 A 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 A 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 A 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 A 539 ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 A 539 GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR ASP
SEQRES 11 A 539 GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU VAL
SEQRES 12 A 539 SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU ALA
SEQRES 13 A 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 A 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 A 539 ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR LEU
SEQRES 16 A 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 A 539 ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG ALA
SEQRES 18 A 539 VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA THR
SEQRES 19 A 539 VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU LEU
SEQRES 20 A 539 ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY GLY
SEQRES 21 A 539 ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG PRO
SEQRES 22 A 539 ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 A 539 GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 A 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 A 539 ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL GLY
SEQRES 26 A 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 A 539 VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 A 539 ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL PRO
SEQRES 29 A 539 GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 A 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS LEU
SEQRES 31 A 539 ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 A 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 A 539 GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS ARG
SEQRES 34 A 539 ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 A 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO LEU
SEQRES 36 A 539 ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE PHE
SEQRES 37 A 539 ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA ARG
SEQRES 38 A 539 THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER PRO
SEQRES 39 A 539 GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR VAL
SEQRES 40 A 539 SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 A 539 ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 A 539 LYS LEU LEU SER ALA THR
SEQRES 1 B 539 ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN LEU
SEQRES 2 B 539 ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL SER
SEQRES 3 B 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY
SEQRES 4 B 539 SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO TRP
SEQRES 5 B 539 SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL CYS
SEQRES 6 B 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 B 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 B 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 B 539 ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 B 539 GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR ASP
SEQRES 11 B 539 GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU VAL
SEQRES 12 B 539 SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU ALA
SEQRES 13 B 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 B 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 B 539 ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR LEU
SEQRES 16 B 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 B 539 ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG ALA
SEQRES 18 B 539 VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA THR
SEQRES 19 B 539 VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU LEU
SEQRES 20 B 539 ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY GLY
SEQRES 21 B 539 ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG PRO
SEQRES 22 B 539 ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 B 539 GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 B 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 B 539 ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL GLY
SEQRES 26 B 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 B 539 VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 B 539 ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL PRO
SEQRES 29 B 539 GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 B 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS LEU
SEQRES 31 B 539 ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 B 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 B 539 GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS ARG
SEQRES 34 B 539 ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 B 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO LEU
SEQRES 36 B 539 ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE PHE
SEQRES 37 B 539 ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA ARG
SEQRES 38 B 539 THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER PRO
SEQRES 39 B 539 GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR VAL
SEQRES 40 B 539 SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 B 539 ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 B 539 LYS LEU LEU SER ALA THR
SEQRES 1 C 539 ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN LEU
SEQRES 2 C 539 ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL SER
SEQRES 3 C 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY
SEQRES 4 C 539 SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO TRP
SEQRES 5 C 539 SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL CYS
SEQRES 6 C 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 C 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 C 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 C 539 ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 C 539 GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR ASP
SEQRES 11 C 539 GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU VAL
SEQRES 12 C 539 SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU ALA
SEQRES 13 C 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 C 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 C 539 ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR LEU
SEQRES 16 C 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 C 539 ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG ALA
SEQRES 18 C 539 VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA THR
SEQRES 19 C 539 VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU LEU
SEQRES 20 C 539 ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY GLY
SEQRES 21 C 539 ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG PRO
SEQRES 22 C 539 ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 C 539 GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 C 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 C 539 ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL GLY
SEQRES 26 C 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 C 539 VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 C 539 ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL PRO
SEQRES 29 C 539 GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 C 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS LEU
SEQRES 31 C 539 ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 C 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 C 539 GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS ARG
SEQRES 34 C 539 ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 C 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO LEU
SEQRES 36 C 539 ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE PHE
SEQRES 37 C 539 ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA ARG
SEQRES 38 C 539 THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER PRO
SEQRES 39 C 539 GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR VAL
SEQRES 40 C 539 SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 C 539 ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 C 539 LYS LEU LEU SER ALA THR
SEQRES 1 D 539 ASP PRO GLN LEU LEU VAL ARG VAL ARG GLY GLY GLN LEU
SEQRES 2 D 539 ARG GLY ILE ARG LEU LYS ALA PRO GLY GLY PRO VAL SER
SEQRES 3 D 539 ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY
SEQRES 4 D 539 SER ARG ARG PHE MET PRO PRO GLU PRO LYS ARG PRO TRP
SEQRES 5 D 539 SER GLY VAL LEU ASP ALA THR THR PHE GLN ASN VAL CYS
SEQRES 6 D 539 TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU GLY
SEQRES 7 D 539 THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU ASP
SEQRES 8 D 539 CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG PRO
SEQRES 9 D 539 ALA SER PRO THR PRO VAL LEU ILE TRP ILE TYR GLY GLY
SEQRES 10 D 539 GLY PHE TYR SER GLY ALA ALA SER LEU ASP VAL TYR ASP
SEQRES 11 D 539 GLY ARG PHE LEU ALA GLN VAL GLU GLY ALA VAL LEU VAL
SEQRES 12 D 539 SER MET ASN TYR ARG VAL GLY THR PHE GLY PHE LEU ALA
SEQRES 13 D 539 LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY LEU
SEQRES 14 D 539 LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU ASN
SEQRES 15 D 539 ILE ALA ALA PHE GLY GLY ASP PRO MET SER VAL THR LEU
SEQRES 16 D 539 PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET HIS
SEQRES 17 D 539 ILE LEU SER LEU PRO SER ARG SER LEU PHE HIS ARG ALA
SEQRES 18 D 539 VAL LEU GLN SER GLY THR PRO ASN GLY PRO TRP ALA THR
SEQRES 19 D 539 VAL SER ALA GLY GLU ALA ARG ARG ARG ALA THR LEU LEU
SEQRES 20 D 539 ALA ARG LEU VAL GLY CYS PRO PRO GLY GLY ALA GLY GLY
SEQRES 21 D 539 ASN ASP THR GLU LEU ILE ALA CYS LEU ARG THR ARG PRO
SEQRES 22 D 539 ALA GLN ASP LEU VAL ASP HIS GLU TRP HIS VAL LEU PRO
SEQRES 23 D 539 GLN GLU SER ILE PHE ARG PHE SER PHE VAL PRO VAL VAL
SEQRES 24 D 539 ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU ILE
SEQRES 25 D 539 ASN THR GLY ASP PHE GLN ASP LEU GLN VAL LEU VAL GLY
SEQRES 26 D 539 VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR GLY
SEQRES 27 D 539 VAL PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE SER
SEQRES 28 D 539 ARG ALA GLN PHE LEU ALA GLY VAL ARG ILE GLY VAL PRO
SEQRES 29 D 539 GLN ALA SER ASP LEU ALA ALA GLU ALA VAL VAL LEU HIS
SEQRES 30 D 539 TYR THR ASP TRP LEU HIS PRO GLU ASP PRO THR HIS LEU
SEQRES 31 D 539 ARG ASP ALA MET SER ALA VAL VAL GLY ASP HIS ASN VAL
SEQRES 32 D 539 VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA ALA
SEQRES 33 D 539 GLN GLY ALA ARG VAL TYR ALA TYR ILE PHE GLU HIS ARG
SEQRES 34 D 539 ALA SER THR LEU THR TRP PRO LEU TRP MET GLY VAL PRO
SEQRES 35 D 539 HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY LEU PRO LEU
SEQRES 36 D 539 ASP PRO SER LEU ASN TYR THR THR GLU GLU ARG ILE PHE
SEQRES 37 D 539 ALA GLN ARG LEU MET LYS TYR TRP THR ASN PHE ALA ARG
SEQRES 38 D 539 THR GLY ASP PRO ASN ASP PRO ARG ASP SER LYS SER PRO
SEQRES 39 D 539 GLN TRP PRO PRO TYR THR THR ALA ALA GLN GLN TYR VAL
SEQRES 40 D 539 SER LEU ASN LEU LYS PRO LEU GLU VAL ARG ARG GLY LEU
SEQRES 41 D 539 ARG ALA GLN THR CYS ALA PHE TRP ASN ARG PHE LEU PRO
SEQRES 42 D 539 LYS LEU LEU SER ALA THR
HELIX 1 1 VAL A 42 ARG A 46 5 5
HELIX 2 2 PHE A 80 MET A 85 1 6
HELIX 3 3 LEU A 130 ASP A 134 5 5
HELIX 4 4 GLY A 135 VAL A 141 1 7
HELIX 5 5 VAL A 153 LEU A 159 1 7
HELIX 6 6 ASN A 170 ILE A 187 1 18
HELIX 7 7 ALA A 188 PHE A 190 5 3
HELIX 8 8 SER A 203 SER A 215 1 13
HELIX 9 9 SER A 218 PHE A 222 5 5
HELIX 10 10 SER A 240 VAL A 255 1 16
HELIX 11 11 ASN A 265 ARG A 274 1 10
HELIX 12 12 PRO A 277 GLU A 285 1 9
HELIX 13 13 TRP A 286 VAL A 288 5 3
HELIX 14 14 THR A 311 GLY A 319 1 9
HELIX 15 15 GLY A 335 TYR A 341 1 7
HELIX 16 16 SER A 355 VAL A 367 1 13
HELIX 17 17 SER A 371 THR A 383 1 13
HELIX 18 18 ASP A 390 VAL A 407 1 18
HELIX 19 19 VAL A 407 GLN A 421 1 15
HELIX 20 20 PRO A 440 GLY A 444 5 5
HELIX 21 21 GLU A 450 GLY A 456 1 7
HELIX 22 22 LEU A 457 ASP A 460 5 4
HELIX 23 23 THR A 466 THR A 486 1 21
HELIX 24 24 ARG A 525 ARG A 534 1 10
HELIX 25 25 ARG A 534 SER A 541 1 8
HELIX 26 26 VAL B 42 ARG B 46 5 5
HELIX 27 27 PHE B 80 MET B 85 1 6
HELIX 28 28 LEU B 130 ASP B 134 5 5
HELIX 29 29 GLY B 135 VAL B 141 1 7
HELIX 30 30 VAL B 153 LEU B 159 1 7
HELIX 31 31 ASN B 170 ILE B 187 1 18
HELIX 32 32 ALA B 188 PHE B 190 5 3
HELIX 33 33 SER B 203 SER B 215 1 13
HELIX 34 34 SER B 218 PHE B 222 5 5
HELIX 35 35 SER B 240 VAL B 255 1 16
HELIX 36 36 ASN B 265 ARG B 274 1 10
HELIX 37 37 PRO B 277 GLU B 285 1 9
HELIX 38 38 TRP B 286 VAL B 288 5 3
HELIX 39 39 THR B 311 GLY B 319 1 9
HELIX 40 40 GLY B 335 TYR B 341 1 7
HELIX 41 41 SER B 355 VAL B 367 1 13
HELIX 42 42 SER B 371 THR B 383 1 13
HELIX 43 43 ASP B 390 VAL B 407 1 18
HELIX 44 44 VAL B 407 GLN B 421 1 15
HELIX 45 45 PRO B 440 GLY B 444 5 5
HELIX 46 46 GLU B 450 GLY B 456 1 7
HELIX 47 47 LEU B 457 ASP B 460 5 4
HELIX 48 48 THR B 466 THR B 486 1 21
HELIX 49 49 ARG B 525 ARG B 534 1 10
HELIX 50 50 ARG B 534 SER B 541 1 8
HELIX 51 51 VAL C 42 ARG C 46 5 5
HELIX 52 52 PHE C 80 MET C 85 1 6
HELIX 53 53 LEU C 130 ASP C 134 5 5
HELIX 54 54 GLY C 135 VAL C 141 1 7
HELIX 55 55 VAL C 153 LEU C 159 1 7
HELIX 56 56 ASN C 170 ILE C 187 1 18
HELIX 57 57 ALA C 188 PHE C 190 5 3
HELIX 58 58 SER C 203 SER C 215 1 13
HELIX 59 59 SER C 218 PHE C 222 5 5
HELIX 60 60 SER C 240 VAL C 255 1 16
HELIX 61 61 ASN C 265 ARG C 274 1 10
HELIX 62 62 PRO C 277 GLU C 285 1 9
HELIX 63 63 TRP C 286 VAL C 288 5 3
HELIX 64 64 THR C 311 GLY C 319 1 9
HELIX 65 65 GLY C 335 TYR C 341 1 7
HELIX 66 66 SER C 355 VAL C 367 1 13
HELIX 67 67 SER C 371 THR C 383 1 13
HELIX 68 68 ASP C 390 VAL C 407 1 18
HELIX 69 69 VAL C 407 GLN C 421 1 15
HELIX 70 70 PRO C 440 GLY C 444 5 5
HELIX 71 71 GLU C 450 GLY C 456 1 7
HELIX 72 72 LEU C 457 ASP C 460 5 4
HELIX 73 73 THR C 466 THR C 486 1 21
HELIX 74 74 ARG C 525 ARG C 534 1 10
HELIX 75 75 ARG C 534 SER C 541 1 8
HELIX 76 76 VAL D 42 ARG D 46 5 5
HELIX 77 77 PHE D 80 MET D 85 1 6
HELIX 78 78 LEU D 130 ASP D 134 5 5
HELIX 79 79 GLY D 135 VAL D 141 1 7
HELIX 80 80 VAL D 153 LEU D 159 1 7
HELIX 81 81 ASN D 170 ILE D 187 1 18
HELIX 82 82 ALA D 188 PHE D 190 5 3
HELIX 83 83 SER D 203 SER D 215 1 13
HELIX 84 84 SER D 218 PHE D 222 5 5
HELIX 85 85 SER D 240 VAL D 255 1 16
HELIX 86 86 ASN D 265 ARG D 274 1 10
HELIX 87 87 PRO D 277 GLU D 285 1 9
HELIX 88 88 TRP D 286 VAL D 288 5 3
HELIX 89 89 THR D 311 GLY D 319 1 9
HELIX 90 90 GLY D 335 TYR D 341 1 7
HELIX 91 91 SER D 355 VAL D 367 1 13
HELIX 92 92 SER D 371 THR D 383 1 13
HELIX 93 93 ASP D 390 VAL D 407 1 18
HELIX 94 94 VAL D 407 GLN D 421 1 15
HELIX 95 95 PRO D 440 GLY D 444 5 5
HELIX 96 96 GLU D 450 GLY D 456 1 7
HELIX 97 97 LEU D 457 ASP D 460 5 4
HELIX 98 98 THR D 466 THR D 486 1 21
HELIX 99 99 ARG D 525 ARG D 534 1 10
HELIX 100 100 ARG D 534 SER D 541 1 8
SHEET 1 A 3 LEU A 9 VAL A 12 0
SHEET 2 A 3 GLY A 15 ARG A 18 -1 O GLY A 15 N VAL A 12
SHEET 3 A 3 VAL A 59 ASP A 61 1 N LEU A 60 O GLN A 16
SHEET 1 B 2 ALA A 38 GLU A 39 0
SHEET 2 B 2 GLU A 51 PRO A 52 -1 O GLU A 51 N GLU A 39
SHEET 1 C 9 ILE A 20 ALA A 24 0
SHEET 2 C 9 GLY A 27 ALA A 31 -1 N GLY A 27 O ALA A 24
SHEET 3 C 9 TYR A 98 PRO A 104 -1 O THR A 103 N SER A 30
SHEET 4 C 9 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 5 C 9 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 6 C 9 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 7 C 9 ARG A 224 GLN A 228 1 N ARG A 224 O VAL A 197
SHEET 8 C 9 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 9 C 9 ARG A 424 TYR A 426 1 O ARG A 424 N VAL A 326
SHEET 1 D10 ILE A 35 PRO A 36 0
SHEET 2 D10 TYR A 98 PRO A 104 -1 O LEU A 99 N ILE A 35
SHEET 3 D10 VAL A 145 MET A 149 -1 O LEU A 146 N TRP A 102
SHEET 4 D10 THR A 112 ILE A 118 1 O PRO A 113 N VAL A 145
SHEET 5 D10 GLY A 192 GLU A 202 1 N ASP A 193 O THR A 112
SHEET 6 D10 ARG A 224 GLN A 228 1 N ARG A 224 O VAL A 197
SHEET 7 D10 GLN A 325 VAL A 331 1 O GLN A 325 N ALA A 225
SHEET 8 D10 TYR A 428 PHE A 430 1 O TYR A 428 N VAL A 330
SHEET 9 D10 GLN A 509 LEU A 513 1 O VAL A 511 N ILE A 429
SHEET 10 D10 ARG A 521 ARG A 522 -1 N ARG A 521 O TYR A 510
SHEET 1 E 3 LEU B 9 VAL B 12 0
SHEET 2 E 3 GLY B 15 ARG B 18 -1 O GLY B 15 N VAL B 12
SHEET 3 E 3 VAL B 59 ASP B 61 1 N LEU B 60 O GLN B 16
SHEET 1 F 2 ALA B 38 GLU B 39 0
SHEET 2 F 2 GLU B 51 PRO B 52 -1 O GLU B 51 N GLU B 39
SHEET 1 G 9 ILE B 20 ALA B 24 0
SHEET 2 G 9 GLY B 27 ALA B 31 -1 N GLY B 27 O ALA B 24
SHEET 3 G 9 TYR B 98 PRO B 104 -1 O THR B 103 N SER B 30
SHEET 4 G 9 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 5 G 9 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 6 G 9 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 7 G 9 ARG B 224 GLN B 228 1 N ARG B 224 O VAL B 197
SHEET 8 G 9 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 9 G 9 ARG B 424 TYR B 426 1 O ARG B 424 N VAL B 326
SHEET 1 H10 ILE B 35 PRO B 36 0
SHEET 2 H10 TYR B 98 PRO B 104 -1 O LEU B 99 N ILE B 35
SHEET 3 H10 VAL B 145 MET B 149 -1 O LEU B 146 N TRP B 102
SHEET 4 H10 THR B 112 ILE B 118 1 O PRO B 113 N VAL B 145
SHEET 5 H10 GLY B 192 GLU B 202 1 N ASP B 193 O THR B 112
SHEET 6 H10 ARG B 224 GLN B 228 1 N ARG B 224 O VAL B 197
SHEET 7 H10 GLN B 325 VAL B 331 1 O GLN B 325 N ALA B 225
SHEET 8 H10 TYR B 428 PHE B 430 1 O TYR B 428 N VAL B 330
SHEET 9 H10 GLN B 509 LEU B 513 1 O VAL B 511 N ILE B 429
SHEET 10 H10 ARG B 521 ARG B 522 -1 N ARG B 521 O TYR B 510
SHEET 1 I 3 LEU C 9 VAL C 12 0
SHEET 2 I 3 GLY C 15 ARG C 18 -1 O GLY C 15 N VAL C 12
SHEET 3 I 3 VAL C 59 ASP C 61 1 N LEU C 60 O GLN C 16
SHEET 1 J 2 ALA C 38 GLU C 39 0
SHEET 2 J 2 GLU C 51 PRO C 52 -1 O GLU C 51 N GLU C 39
SHEET 1 K 9 ILE C 20 ALA C 24 0
SHEET 2 K 9 GLY C 27 ALA C 31 -1 N GLY C 27 O ALA C 24
SHEET 3 K 9 TYR C 98 PRO C 104 -1 O THR C 103 N SER C 30
SHEET 4 K 9 VAL C 145 MET C 149 -1 O LEU C 146 N TRP C 102
SHEET 5 K 9 THR C 112 ILE C 118 1 O PRO C 113 N VAL C 145
SHEET 6 K 9 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 7 K 9 ARG C 224 GLN C 228 1 N ARG C 224 O VAL C 197
SHEET 8 K 9 GLN C 325 VAL C 331 1 O GLN C 325 N ALA C 225
SHEET 9 K 9 ARG C 424 TYR C 426 1 O ARG C 424 N VAL C 326
SHEET 1 L10 ILE C 35 PRO C 36 0
SHEET 2 L10 TYR C 98 PRO C 104 -1 O LEU C 99 N ILE C 35
SHEET 3 L10 VAL C 145 MET C 149 -1 O LEU C 146 N TRP C 102
SHEET 4 L10 THR C 112 ILE C 118 1 O PRO C 113 N VAL C 145
SHEET 5 L10 GLY C 192 GLU C 202 1 N ASP C 193 O THR C 112
SHEET 6 L10 ARG C 224 GLN C 228 1 N ARG C 224 O VAL C 197
SHEET 7 L10 GLN C 325 VAL C 331 1 O GLN C 325 N ALA C 225
SHEET 8 L10 TYR C 428 PHE C 430 1 O TYR C 428 N VAL C 330
SHEET 9 L10 GLN C 509 LEU C 513 1 O VAL C 511 N ILE C 429
SHEET 10 L10 ARG C 521 ARG C 522 -1 N ARG C 521 O TYR C 510
SHEET 1 M 3 LEU D 9 VAL D 12 0
SHEET 2 M 3 GLY D 15 ARG D 18 -1 O GLY D 15 N VAL D 12
SHEET 3 M 3 VAL D 59 ASP D 61 1 N LEU D 60 O GLN D 16
SHEET 1 N 2 ALA D 38 GLU D 39 0
SHEET 2 N 2 GLU D 51 PRO D 52 -1 O GLU D 51 N GLU D 39
SHEET 1 O 9 ILE D 20 ALA D 24 0
SHEET 2 O 9 GLY D 27 ALA D 31 -1 N GLY D 27 O ALA D 24
SHEET 3 O 9 TYR D 98 PRO D 104 -1 O THR D 103 N SER D 30
SHEET 4 O 9 VAL D 145 MET D 149 -1 O LEU D 146 N TRP D 102
SHEET 5 O 9 THR D 112 ILE D 118 1 O PRO D 113 N VAL D 145
SHEET 6 O 9 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 7 O 9 ARG D 224 GLN D 228 1 N ARG D 224 O VAL D 197
SHEET 8 O 9 GLN D 325 VAL D 331 1 O GLN D 325 N ALA D 225
SHEET 9 O 9 ARG D 424 TYR D 426 1 O ARG D 424 N VAL D 326
SHEET 1 P10 ILE D 35 PRO D 36 0
SHEET 2 P10 TYR D 98 PRO D 104 -1 O LEU D 99 N ILE D 35
SHEET 3 P10 VAL D 145 MET D 149 -1 O LEU D 146 N TRP D 102
SHEET 4 P10 THR D 112 ILE D 118 1 O PRO D 113 N VAL D 145
SHEET 5 P10 GLY D 192 GLU D 202 1 N ASP D 193 O THR D 112
SHEET 6 P10 ARG D 224 GLN D 228 1 N ARG D 224 O VAL D 197
SHEET 7 P10 GLN D 325 VAL D 331 1 O GLN D 325 N ALA D 225
SHEET 8 P10 TYR D 428 PHE D 430 1 O TYR D 428 N VAL D 330
SHEET 9 P10 GLN D 509 LEU D 513 1 O VAL D 511 N ILE D 429
SHEET 10 P10 ARG D 521 ARG D 522 -1 N ARG D 521 O TYR D 510
SSBOND 1 CYS A 69 CYS A 96
SSBOND 2 CYS A 257 CYS A 272
SSBOND 3 CYS A 409 CYS A 529
SSBOND 4 CYS B 69 CYS B 96
SSBOND 5 CYS B 257 CYS B 272
SSBOND 6 CYS B 409 CYS B 529
SSBOND 7 CYS C 69 CYS C 96
SSBOND 8 CYS C 257 CYS C 272
SSBOND 9 CYS C 409 CYS C 529
SSBOND 10 CYS D 69 CYS D 96
SSBOND 11 CYS D 257 CYS D 272
SSBOND 12 CYS D 409 CYS D 529
CISPEP 1 TYR A 105 PRO A 106 0 5.67
CISPEP 2 CYS A 257 PRO A 258 0 -9.87
CISPEP 3 TYR B 105 PRO B 106 0 5.84
CISPEP 4 CYS B 257 PRO B 258 0 -9.89
CISPEP 5 TYR C 105 PRO C 106 0 5.74
CISPEP 6 CYS C 257 PRO C 258 0 -9.84
CISPEP 7 TYR D 105 PRO D 106 0 5.67
CISPEP 8 CYS D 257 PRO D 258 0 -9.94
CRYST1 211.160 129.750 195.420 90.00 103.20 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 0.004736 0.000000 0.001111 0.00000
SCALE2 0.000000 0.007707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005256 0.00000 |