HEADER OXIDOREDUCTASE 24-JAN-07 2ONN
TITLE ARG475GLN MUTANT OF HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE, APO
TITLE 2 FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALDEHYDE DEHYDROGENASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: ALDH CLASS 2, ALDHI, ALDH-E2;
COMPND 5 EC: 1.2.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ALDH2, ALDM;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT-7-7
KEYWDS OXIDOREDUCTASE, ALDH, NAD, ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR H.N.LARSON,T.D.HURLEY
REVDAT 7 30-AUG-23 2ONN 1 REMARK
REVDAT 6 20-OCT-21 2ONN 1 SEQADV
REVDAT 5 18-OCT-17 2ONN 1 REMARK
REVDAT 4 12-NOV-14 2ONN 1 KEYWDS
REVDAT 3 24-FEB-09 2ONN 1 VERSN
REVDAT 2 29-MAY-07 2ONN 1 JRNL
REVDAT 1 06-MAR-07 2ONN 0
JRNL AUTH H.N.LARSON,J.ZHOU,Z.CHEN,J.S.STAMLER,H.WEINER,T.D.HURLEY
JRNL TITL STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF COENZYME BINDING
JRNL TITL 2 TO THE INACTIVE ASIAN VARIANT OF MITOCHONDRIAL ALDEHYDE
JRNL TITL 3 DEHYDROGENASE: ROLES OF RESIDUES 475 AND 487.
JRNL REF J.BIOL.CHEM. V. 282 12940 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17327228
JRNL DOI 10.1074/JBC.M607959200
REMARK 2
REMARK 2 RESOLUTION. 2.75 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) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 4648163.510
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 95183
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) : 0.226
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4795
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.92
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.70
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 13463
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 740
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 30368
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 737
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.76000
REMARK 3 B22 (A**2) : 1.97000
REMARK 3 B33 (A**2) : -12.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.34
REMARK 3 ESD FROM SIGMAA (A) : 0.44
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) : 0.42
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.49
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.160
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) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.090 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.680 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.630 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.27
REMARK 3 BSOL : 10.00
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.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : &_1_PARAMETER_INFILE_4
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ONN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-NOV-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
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
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IIC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95356
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 99.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.29800
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR
REMARK 200 STARTING MODEL: PDB ENTRY 1O05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM ACES (N-[2-ACETAMIDO]-2
REMARK 280 -AMINOETHANE SUFONIC ACID), 10MM MGCL2, 100 MM GUANIDINE HCL, 16%
REMARK 280 W/V PEG 6000, 4 MM DTT, PH 6.6, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 70.39000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.61500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.43000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.61500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 70.39000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.43000
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
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 300 REMARK: THE BIOLOGICAL UNIT IS A TETRAMER. THERE ARE 3 BIOLOGICAL
REMARK 300 UNTILS IN THE ASSYMMETRIC UNIT. THE BIOLOGICAL UNIT 1 CONSISTS OF
REMARK 300 CHAIN(S) A, B, C, D. THE BIOLOGICAL UNIT 2 CONSISTS OF CHAIN(S) E,
REMARK 300 F, G, H.
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: 20340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
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 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: 20420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, 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 SER A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 THR A 5
REMARK 465 GLN A 6
REMARK 465 SER B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 ALA B 4
REMARK 465 THR B 5
REMARK 465 GLN B 6
REMARK 465 SER C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 ALA C 4
REMARK 465 THR C 5
REMARK 465 GLN C 6
REMARK 465 SER D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 3
REMARK 465 ALA D 4
REMARK 465 THR D 5
REMARK 465 GLN D 6
REMARK 465 SER E 1
REMARK 465 ALA E 2
REMARK 465 ALA E 3
REMARK 465 ALA E 4
REMARK 465 THR E 5
REMARK 465 GLN E 6
REMARK 465 SER F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 3
REMARK 465 ALA F 4
REMARK 465 THR F 5
REMARK 465 GLN F 6
REMARK 465 SER G 1
REMARK 465 ALA G 2
REMARK 465 ALA G 3
REMARK 465 ALA G 4
REMARK 465 THR G 5
REMARK 465 GLN G 6
REMARK 465 SER H 1
REMARK 465 ALA H 2
REMARK 465 ALA H 3
REMARK 465 ALA H 4
REMARK 465 THR H 5
REMARK 465 GLN H 6
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU C 476 CD GLU C 476 OE1 -0.189
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLU C 476 OE1 - CD - OE2 ANGL. DEV. = -18.8 DEGREES
REMARK 500 GLU C 476 CG - CD - OE1 ANGL. DEV. = 18.9 DEGREES
REMARK 500 ARG H 34 NE - CZ - NH2 ANGL. DEV. = -3.2 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 ASN A 20 24.20 -147.41
REMARK 500 ARG A 34 11.96 57.80
REMARK 500 ASP A 98 32.73 -96.59
REMARK 500 PRO A 167 -169.68 -71.51
REMARK 500 THR A 227 -77.70 -93.43
REMARK 500 SER A 260 -70.19 -93.37
REMARK 500 ASN A 261 23.62 -148.08
REMARK 500 TYR A 379 51.59 -117.29
REMARK 500 LYS A 397 -33.10 -130.47
REMARK 500 LYS A 469 -124.08 51.22
REMARK 500 LEU A 477 153.16 71.29
REMARK 500 GLN B 13 -6.77 -56.17
REMARK 500 ASN B 20 26.04 -146.36
REMARK 500 ARG B 34 15.94 58.83
REMARK 500 CYS B 49 175.00 178.33
REMARK 500 VAL B 120 -80.34 -103.63
REMARK 500 THR B 227 -78.66 -89.27
REMARK 500 SER B 260 -70.16 -97.13
REMARK 500 ASN B 261 19.26 -144.86
REMARK 500 TYR B 379 55.88 -110.18
REMARK 500 LYS B 397 -36.65 -132.99
REMARK 500 LYS B 411 -69.79 -108.34
REMARK 500 LYS B 469 -121.40 52.09
REMARK 500 LEU B 477 158.78 70.07
REMARK 500 GLN C 13 -9.16 -53.48
REMARK 500 ASN C 20 28.95 -149.97
REMARK 500 ARG C 34 -0.69 71.99
REMARK 500 CYS C 49 -178.92 -174.96
REMARK 500 ASP C 98 32.23 -98.00
REMARK 500 VAL C 120 -77.60 -104.60
REMARK 500 THR C 227 -80.47 -99.11
REMARK 500 SER C 260 -69.07 -95.64
REMARK 500 ASN C 261 21.84 -148.08
REMARK 500 TYR C 379 60.07 -116.34
REMARK 500 LYS C 469 -122.75 56.75
REMARK 500 LEU C 477 157.55 68.71
REMARK 500 GLN D 13 -4.11 -57.69
REMARK 500 ASN D 20 27.80 -149.10
REMARK 500 ASP D 98 30.10 -95.11
REMARK 500 VAL D 120 -72.51 -108.44
REMARK 500 THR D 227 -77.89 -90.91
REMARK 500 SER D 260 -69.40 -95.52
REMARK 500 ASN D 261 19.48 -147.12
REMARK 500 ALA D 375 149.12 -170.20
REMARK 500 TYR D 379 52.36 -117.31
REMARK 500 LYS D 469 -122.80 51.48
REMARK 500 LEU D 477 156.47 67.03
REMARK 500 GLN D 497 116.45 -161.12
REMARK 500 GLN E 13 -4.92 -59.01
REMARK 500 ASN E 20 25.38 -147.96
REMARK 500
REMARK 500 THIS ENTRY HAS 90 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ONN A 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN B 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN C 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN D 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN E 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN F 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN G 1 500 UNP P05091 ALDH2_HUMAN 18 517
DBREF 2ONN H 1 500 UNP P05091 ALDH2_HUMAN 18 517
SEQADV 2ONN GLN A 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN B 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN C 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN D 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN E 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN F 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN G 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQADV 2ONN GLN H 475 UNP P05091 ARG 492 ENGINEERED MUTATION
SEQRES 1 A 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 A 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 A 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 A 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 A 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 A 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 A 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 A 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 A 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 A 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 A 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 A 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 A 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 A 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 A 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 A 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 A 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 A 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 A 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 A 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 A 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 A 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 A 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 A 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 A 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 A 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 A 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 A 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 A 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 A 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 A 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 A 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 A 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 A 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 A 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 A 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 A 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 A 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 A 500 VAL PRO GLN LYS ASN SER
SEQRES 1 B 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 B 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 B 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 B 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 B 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 B 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 B 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 B 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 B 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 B 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 B 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 B 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 B 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 B 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 B 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 B 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 B 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 B 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 B 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 B 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 B 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 B 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 B 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 B 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 B 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 B 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 B 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 B 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 B 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 B 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 B 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 B 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 B 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 B 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 B 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 B 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 B 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 B 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 B 500 VAL PRO GLN LYS ASN SER
SEQRES 1 C 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 C 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 C 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 C 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 C 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 C 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 C 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 C 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 C 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 C 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 C 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 C 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 C 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 C 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 C 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 C 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 C 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 C 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 C 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 C 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 C 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 C 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 C 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 C 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 C 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 C 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 C 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 C 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 C 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 C 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 C 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 C 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 C 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 C 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 C 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 C 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 C 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 C 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 C 500 VAL PRO GLN LYS ASN SER
SEQRES 1 D 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 D 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 D 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 D 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 D 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 D 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 D 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 D 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 D 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 D 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 D 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 D 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 D 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 D 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 D 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 D 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 D 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 D 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 D 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 D 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 D 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 D 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 D 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 D 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 D 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 D 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 D 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 D 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 D 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 D 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 D 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 D 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 D 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 D 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 D 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 D 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 D 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 D 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 D 500 VAL PRO GLN LYS ASN SER
SEQRES 1 E 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 E 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 E 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 E 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 E 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 E 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 E 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 E 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 E 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 E 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 E 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 E 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 E 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 E 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 E 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 E 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 E 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 E 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 E 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 E 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 E 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 E 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 E 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 E 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 E 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 E 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 E 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 E 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 E 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 E 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 E 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 E 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 E 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 E 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 E 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 E 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 E 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 E 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 E 500 VAL PRO GLN LYS ASN SER
SEQRES 1 F 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 F 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 F 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 F 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 F 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 F 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 F 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 F 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 F 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 F 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 F 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 F 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 F 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 F 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 F 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 F 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 F 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 F 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 F 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 F 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 F 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 F 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 F 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 F 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 F 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 F 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 F 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 F 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 F 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 F 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 F 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 F 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 F 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 F 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 F 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 F 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 F 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 F 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 F 500 VAL PRO GLN LYS ASN SER
SEQRES 1 G 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 G 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 G 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 G 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 G 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 G 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 G 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 G 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 G 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 G 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 G 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 G 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 G 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 G 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 G 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 G 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 G 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 G 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 G 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 G 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 G 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 G 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 G 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 G 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 G 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 G 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 G 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 G 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 G 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 G 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 G 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 G 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 G 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 G 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 G 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 G 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 G 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 G 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 G 500 VAL PRO GLN LYS ASN SER
SEQRES 1 H 500 SER ALA ALA ALA THR GLN ALA VAL PRO ALA PRO ASN GLN
SEQRES 2 H 500 GLN PRO GLU VAL PHE CYS ASN GLN ILE PHE ILE ASN ASN
SEQRES 3 H 500 GLU TRP HIS ASP ALA VAL SER ARG LYS THR PHE PRO THR
SEQRES 4 H 500 VAL ASN PRO SER THR GLY GLU VAL ILE CYS GLN VAL ALA
SEQRES 5 H 500 GLU GLY ASP LYS GLU ASP VAL ASP LYS ALA VAL LYS ALA
SEQRES 6 H 500 ALA ARG ALA ALA PHE GLN LEU GLY SER PRO TRP ARG ARG
SEQRES 7 H 500 MET ASP ALA SER HIS ARG GLY ARG LEU LEU ASN ARG LEU
SEQRES 8 H 500 ALA ASP LEU ILE GLU ARG ASP ARG THR TYR LEU ALA ALA
SEQRES 9 H 500 LEU GLU THR LEU ASP ASN GLY LYS PRO TYR VAL ILE SER
SEQRES 10 H 500 TYR LEU VAL ASP LEU ASP MET VAL LEU LYS CYS LEU ARG
SEQRES 11 H 500 TYR TYR ALA GLY TRP ALA ASP LYS TYR HIS GLY LYS THR
SEQRES 12 H 500 ILE PRO ILE ASP GLY ASP PHE PHE SER TYR THR ARG HIS
SEQRES 13 H 500 GLU PRO VAL GLY VAL CYS GLY GLN ILE ILE PRO TRP ASN
SEQRES 14 H 500 PHE PRO LEU LEU MET GLN ALA TRP LYS LEU GLY PRO ALA
SEQRES 15 H 500 LEU ALA THR GLY ASN VAL VAL VAL MET LYS VAL ALA GLU
SEQRES 16 H 500 GLN THR PRO LEU THR ALA LEU TYR VAL ALA ASN LEU ILE
SEQRES 17 H 500 LYS GLU ALA GLY PHE PRO PRO GLY VAL VAL ASN ILE VAL
SEQRES 18 H 500 PRO GLY PHE GLY PRO THR ALA GLY ALA ALA ILE ALA SER
SEQRES 19 H 500 HIS GLU ASP VAL ASP LYS VAL ALA PHE THR GLY SER THR
SEQRES 20 H 500 GLU ILE GLY ARG VAL ILE GLN VAL ALA ALA GLY SER SER
SEQRES 21 H 500 ASN LEU LYS ARG VAL THR LEU GLU LEU GLY GLY LYS SER
SEQRES 22 H 500 PRO ASN ILE ILE MET SER ASP ALA ASP MET ASP TRP ALA
SEQRES 23 H 500 VAL GLU GLN ALA HIS PHE ALA LEU PHE PHE ASN GLN GLY
SEQRES 24 H 500 GLN CYS CYS CYS ALA GLY SER ARG THR PHE VAL GLN GLU
SEQRES 25 H 500 ASP ILE TYR ASP GLU PHE VAL GLU ARG SER VAL ALA ARG
SEQRES 26 H 500 ALA LYS SER ARG VAL VAL GLY ASN PRO PHE ASP SER LYS
SEQRES 27 H 500 THR GLU GLN GLY PRO GLN VAL ASP GLU THR GLN PHE LYS
SEQRES 28 H 500 LYS ILE LEU GLY TYR ILE ASN THR GLY LYS GLN GLU GLY
SEQRES 29 H 500 ALA LYS LEU LEU CYS GLY GLY GLY ILE ALA ALA ASP ARG
SEQRES 30 H 500 GLY TYR PHE ILE GLN PRO THR VAL PHE GLY ASP VAL GLN
SEQRES 31 H 500 ASP GLY MET THR ILE ALA LYS GLU GLU ILE PHE GLY PRO
SEQRES 32 H 500 VAL MET GLN ILE LEU LYS PHE LYS THR ILE GLU GLU VAL
SEQRES 33 H 500 VAL GLY ARG ALA ASN ASN SER THR TYR GLY LEU ALA ALA
SEQRES 34 H 500 ALA VAL PHE THR LYS ASP LEU ASP LYS ALA ASN TYR LEU
SEQRES 35 H 500 SER GLN ALA LEU GLN ALA GLY THR VAL TRP VAL ASN CYS
SEQRES 36 H 500 TYR ASP VAL PHE GLY ALA GLN SER PRO PHE GLY GLY TYR
SEQRES 37 H 500 LYS MET SER GLY SER GLY GLN GLU LEU GLY GLU TYR GLY
SEQRES 38 H 500 LEU GLN ALA TYR THR GLU VAL LYS THR VAL THR VAL LYS
SEQRES 39 H 500 VAL PRO GLN LYS ASN SER
FORMUL 9 HOH *737(H2 O)
HELIX 1 1 ASP A 55 PHE A 70 1 16
HELIX 2 2 SER A 74 MET A 79 1 6
HELIX 3 3 ASP A 80 ASP A 98 1 19
HELIX 4 4 ASP A 98 GLY A 111 1 14
HELIX 5 5 PRO A 113 VAL A 120 1 8
HELIX 6 6 VAL A 120 ALA A 136 1 17
HELIX 7 7 PHE A 170 THR A 185 1 16
HELIX 8 8 PRO A 198 GLY A 212 1 15
HELIX 9 9 THR A 227 HIS A 235 1 9
HELIX 10 10 SER A 246 SER A 259 1 14
HELIX 11 11 ASP A 282 PHE A 296 1 15
HELIX 12 12 ASN A 297 GLN A 300 5 4
HELIX 13 13 GLU A 312 ARG A 329 1 18
HELIX 14 14 ASP A 346 GLU A 363 1 18
HELIX 15 15 MET A 393 LYS A 397 5 5
HELIX 16 16 THR A 412 ASN A 421 1 10
HELIX 17 17 ASP A 435 LEU A 446 1 12
HELIX 18 18 TYR A 468 MET A 470 5 3
HELIX 19 19 GLU A 479 TYR A 485 1 7
HELIX 20 20 ASP B 55 PHE B 70 1 16
HELIX 21 21 SER B 74 MET B 79 1 6
HELIX 22 22 ASP B 80 ASP B 98 1 19
HELIX 23 23 ASP B 98 GLY B 111 1 14
HELIX 24 24 PRO B 113 VAL B 120 1 8
HELIX 25 25 VAL B 120 ALA B 136 1 17
HELIX 26 26 PHE B 170 THR B 185 1 16
HELIX 27 27 PRO B 198 GLY B 212 1 15
HELIX 28 28 THR B 227 HIS B 235 1 9
HELIX 29 29 SER B 246 SER B 259 1 14
HELIX 30 30 ASP B 282 PHE B 296 1 15
HELIX 31 31 ASN B 297 GLN B 300 5 4
HELIX 32 32 GLU B 312 ARG B 329 1 18
HELIX 33 33 ASP B 346 GLU B 363 1 18
HELIX 34 34 MET B 393 LYS B 397 5 5
HELIX 35 35 THR B 412 ASN B 422 1 11
HELIX 36 36 ASP B 435 LEU B 446 1 12
HELIX 37 37 GLU B 479 ALA B 484 1 6
HELIX 38 38 ASP C 55 PHE C 70 1 16
HELIX 39 39 SER C 74 MET C 79 1 6
HELIX 40 40 ASP C 80 ASP C 98 1 19
HELIX 41 41 ASP C 98 GLY C 111 1 14
HELIX 42 42 PRO C 113 VAL C 120 1 8
HELIX 43 43 VAL C 120 GLY C 134 1 15
HELIX 44 44 PHE C 170 THR C 185 1 16
HELIX 45 45 PRO C 198 GLY C 212 1 15
HELIX 46 46 THR C 227 HIS C 235 1 9
HELIX 47 47 GLU C 248 SER C 259 1 12
HELIX 48 48 ASP C 282 PHE C 296 1 15
HELIX 49 49 ASN C 297 GLN C 300 5 4
HELIX 50 50 GLU C 312 ARG C 329 1 18
HELIX 51 51 ASP C 346 GLU C 363 1 18
HELIX 52 52 MET C 393 LYS C 397 5 5
HELIX 53 53 THR C 412 ASN C 422 1 11
HELIX 54 54 ASP C 435 LEU C 446 1 12
HELIX 55 55 TYR C 468 GLY C 472 5 5
HELIX 56 56 GLU C 479 ALA C 484 1 6
HELIX 57 57 ASP D 55 PHE D 70 1 16
HELIX 58 58 SER D 74 MET D 79 1 6
HELIX 59 59 ASP D 80 ASP D 98 1 19
HELIX 60 60 ASP D 98 GLY D 111 1 14
HELIX 61 61 PRO D 113 VAL D 120 1 8
HELIX 62 62 VAL D 120 GLY D 134 1 15
HELIX 63 63 PHE D 170 THR D 185 1 16
HELIX 64 64 PRO D 198 GLY D 212 1 15
HELIX 65 65 THR D 227 HIS D 235 1 9
HELIX 66 66 SER D 246 SER D 259 1 14
HELIX 67 67 ASP D 282 PHE D 296 1 15
HELIX 68 68 ASN D 297 GLN D 300 5 4
HELIX 69 69 GLU D 312 ARG D 329 1 18
HELIX 70 70 ASP D 346 GLU D 363 1 18
HELIX 71 71 MET D 393 LYS D 397 5 5
HELIX 72 72 THR D 412 ASN D 421 1 10
HELIX 73 73 ASP D 435 LEU D 446 1 12
HELIX 74 74 TYR D 468 GLY D 472 5 5
HELIX 75 75 TYR D 480 TYR D 485 1 6
HELIX 76 76 ASP E 55 PHE E 70 1 16
HELIX 77 77 SER E 74 MET E 79 1 6
HELIX 78 78 ASP E 80 ASP E 98 1 19
HELIX 79 79 ASP E 98 GLY E 111 1 14
HELIX 80 80 PRO E 113 VAL E 120 1 8
HELIX 81 81 VAL E 120 GLY E 134 1 15
HELIX 82 82 PHE E 170 THR E 185 1 16
HELIX 83 83 PRO E 198 GLY E 212 1 15
HELIX 84 84 THR E 227 HIS E 235 1 9
HELIX 85 85 SER E 246 SER E 259 1 14
HELIX 86 86 ASP E 282 PHE E 296 1 15
HELIX 87 87 ASN E 297 GLN E 300 5 4
HELIX 88 88 GLU E 312 ARG E 329 1 18
HELIX 89 89 ASP E 346 GLU E 363 1 18
HELIX 90 90 MET E 393 LYS E 397 5 5
HELIX 91 91 THR E 412 ASN E 421 1 10
HELIX 92 92 ASP E 435 LEU E 446 1 12
HELIX 93 93 TYR E 468 GLY E 472 5 5
HELIX 94 94 TYR E 480 TYR E 485 1 6
HELIX 95 95 ASP F 55 PHE F 70 1 16
HELIX 96 96 SER F 74 MET F 79 1 6
HELIX 97 97 ASP F 80 ASP F 98 1 19
HELIX 98 98 ASP F 98 GLY F 111 1 14
HELIX 99 99 PRO F 113 VAL F 120 1 8
HELIX 100 100 VAL F 120 ALA F 136 1 17
HELIX 101 101 PHE F 170 THR F 185 1 16
HELIX 102 102 PRO F 198 GLY F 212 1 15
HELIX 103 103 THR F 227 HIS F 235 1 9
HELIX 104 104 SER F 246 SER F 259 1 14
HELIX 105 105 ASP F 282 PHE F 296 1 15
HELIX 106 106 ASN F 297 GLN F 300 5 4
HELIX 107 107 GLU F 312 ARG F 329 1 18
HELIX 108 108 ASP F 346 GLU F 363 1 18
HELIX 109 109 THR F 412 ASN F 421 1 10
HELIX 110 110 ASP F 435 LEU F 446 1 12
HELIX 111 111 TYR F 468 MET F 470 5 3
HELIX 112 112 GLY F 478 GLN F 483 5 6
HELIX 113 113 ASP G 55 PHE G 70 1 16
HELIX 114 114 SER G 74 MET G 79 1 6
HELIX 115 115 ASP G 80 ASP G 98 1 19
HELIX 116 116 ASP G 98 GLY G 111 1 14
HELIX 117 117 PRO G 113 VAL G 120 1 8
HELIX 118 118 VAL G 120 ALA G 136 1 17
HELIX 119 119 PHE G 170 THR G 185 1 16
HELIX 120 120 PRO G 198 GLY G 212 1 15
HELIX 121 121 THR G 227 HIS G 235 1 9
HELIX 122 122 SER G 246 SER G 259 1 14
HELIX 123 123 ASP G 282 PHE G 296 1 15
HELIX 124 124 ASN G 297 GLN G 300 5 4
HELIX 125 125 GLU G 312 ARG G 329 1 18
HELIX 126 126 ASP G 346 GLU G 363 1 18
HELIX 127 127 MET G 393 LYS G 397 5 5
HELIX 128 128 THR G 412 ASN G 421 1 10
HELIX 129 129 ASP G 435 LEU G 446 1 12
HELIX 130 130 TYR G 468 GLY G 472 5 5
HELIX 131 131 GLU G 479 ALA G 484 1 6
HELIX 132 132 ASP H 55 PHE H 70 1 16
HELIX 133 133 SER H 74 MET H 79 1 6
HELIX 134 134 ASP H 80 ASP H 98 1 19
HELIX 135 135 ASP H 98 GLY H 111 1 14
HELIX 136 136 PRO H 113 VAL H 120 1 8
HELIX 137 137 VAL H 120 ALA H 136 1 17
HELIX 138 138 PHE H 170 THR H 185 1 16
HELIX 139 139 PRO H 198 GLY H 212 1 15
HELIX 140 140 THR H 227 HIS H 235 1 9
HELIX 141 141 SER H 246 SER H 259 1 14
HELIX 142 142 ASP H 282 PHE H 296 1 15
HELIX 143 143 ASN H 297 GLN H 300 5 4
HELIX 144 144 GLU H 312 ARG H 329 1 18
HELIX 145 145 ASP H 346 GLU H 363 1 18
HELIX 146 146 MET H 393 LYS H 397 5 5
HELIX 147 147 THR H 412 ASN H 421 1 10
HELIX 148 148 ASP H 435 LEU H 446 1 12
HELIX 149 149 TYR H 468 GLY H 472 5 5
HELIX 150 150 TYR H 480 TYR H 485 1 6
SHEET 1 A 2 ILE A 22 ILE A 24 0
SHEET 2 A 2 GLU A 27 HIS A 29 -1 O HIS A 29 N ILE A 22
SHEET 1 B 2 THR A 36 VAL A 40 0
SHEET 2 B 2 VAL A 47 ALA A 52 -1 O ILE A 48 N THR A 39
SHEET 1 C20 LYS B 366 CYS B 369 0
SHEET 2 C20 THR B 384 GLY B 387 -1 O VAL B 385 N LEU B 368
SHEET 3 C20 VAL B 404 PHE B 410 1 O MET B 405 N PHE B 386
SHEET 4 C20 ARG B 307 GLN B 311 1 N VAL B 310 O LEU B 408
SHEET 5 C20 PRO B 274 ILE B 277 1 N ILE B 277 O PHE B 309
SHEET 6 C20 ALA B 428 PHE B 432 1 O ALA B 430 N ILE B 276
SHEET 7 C20 THR B 450 VAL B 453 1 O TRP B 452 N VAL B 431
SHEET 8 C20 THR A 486 LYS A 494 1 N THR A 490 O VAL B 451
SHEET 9 C20 PHE A 150 PRO A 158 -1 N GLU A 157 O GLU A 487
SHEET 10 C20 GLY A 141 ILE A 144 -1 N ILE A 144 O SER A 152
SHEET 11 C20 GLY D 141 ILE D 144 -1 O THR D 143 N GLY A 141
SHEET 12 C20 PHE D 150 PRO D 158 -1 O SER D 152 N ILE D 144
SHEET 13 C20 THR D 486 LYS D 494 -1 O GLU D 487 N GLU D 157
SHEET 14 C20 THR C 450 VAL C 453 1 N VAL C 451 O THR D 490
SHEET 15 C20 ALA C 428 PHE C 432 1 N ALA C 429 O TRP C 452
SHEET 16 C20 PRO C 274 ILE C 277 1 N ILE C 276 O PHE C 432
SHEET 17 C20 ARG C 307 GLN C 311 1 O ARG C 307 N ASN C 275
SHEET 18 C20 VAL C 404 PHE C 410 1 O GLN C 406 N THR C 308
SHEET 19 C20 THR C 384 GLY C 387 1 N PHE C 386 O MET C 405
SHEET 20 C20 LYS C 366 CYS C 369 -1 N LEU C 368 O VAL C 385
SHEET 1 D 6 VAL A 218 ILE A 220 0
SHEET 2 D 6 VAL A 188 LYS A 192 1 N MET A 191 O ASN A 219
SHEET 3 D 6 VAL A 161 ILE A 165 1 N GLN A 164 O LYS A 192
SHEET 4 D 6 LYS A 240 THR A 244 1 O LYS A 240 N GLY A 163
SHEET 5 D 6 ARG A 264 GLU A 268 1 O ARG A 264 N VAL A 241
SHEET 6 D 6 GLY A 472 SER A 473 -1 O SER A 473 N LEU A 267
SHEET 1 E20 LYS A 366 CYS A 369 0
SHEET 2 E20 THR A 384 GLY A 387 -1 O VAL A 385 N LEU A 368
SHEET 3 E20 VAL A 404 PHE A 410 1 O MET A 405 N THR A 384
SHEET 4 E20 ARG A 307 GLN A 311 1 N VAL A 310 O LEU A 408
SHEET 5 E20 PRO A 274 ILE A 277 1 N ILE A 277 O PHE A 309
SHEET 6 E20 ALA A 428 PHE A 432 1 O ALA A 430 N ILE A 276
SHEET 7 E20 THR A 450 VAL A 453 1 O TRP A 452 N VAL A 431
SHEET 8 E20 THR B 486 LYS B 494 1 O THR B 490 N VAL A 451
SHEET 9 E20 PHE B 150 PRO B 158 -1 N GLU B 157 O GLU B 487
SHEET 10 E20 GLY B 141 ILE B 144 -1 N ILE B 144 O SER B 152
SHEET 11 E20 GLY C 141 ILE C 144 -1 O GLY C 141 N THR B 143
SHEET 12 E20 PHE C 150 PRO C 158 -1 O SER C 152 N ILE C 144
SHEET 13 E20 THR C 486 LYS C 494 -1 O GLU C 487 N GLU C 157
SHEET 14 E20 THR D 450 VAL D 453 1 O VAL D 453 N THR C 492
SHEET 15 E20 ALA D 428 PHE D 432 1 N VAL D 431 O TRP D 452
SHEET 16 E20 PRO D 274 ILE D 277 1 N ILE D 276 O ALA D 430
SHEET 17 E20 ARG D 307 GLN D 311 1 O PHE D 309 N ILE D 277
SHEET 18 E20 VAL D 404 PHE D 410 1 O LEU D 408 N VAL D 310
SHEET 19 E20 THR D 384 GLY D 387 1 N PHE D 386 O MET D 405
SHEET 20 E20 LYS D 366 CYS D 369 -1 N LYS D 366 O GLY D 387
SHEET 1 F 2 PHE A 465 GLY A 466 0
SHEET 2 F 2 GLN A 475 GLU A 476 -1 O GLU A 476 N PHE A 465
SHEET 1 G 2 ILE B 22 ILE B 24 0
SHEET 2 G 2 GLU B 27 HIS B 29 -1 O GLU B 27 N ILE B 24
SHEET 1 H 2 THR B 36 VAL B 40 0
SHEET 2 H 2 VAL B 47 ALA B 52 -1 O ILE B 48 N THR B 39
SHEET 1 I 5 VAL B 218 ILE B 220 0
SHEET 2 I 5 VAL B 188 LYS B 192 1 N MET B 191 O ASN B 219
SHEET 3 I 5 VAL B 161 ILE B 165 1 N CYS B 162 O VAL B 188
SHEET 4 I 5 LYS B 240 THR B 244 1 O LYS B 240 N GLY B 163
SHEET 5 I 5 ARG B 264 GLU B 268 1 O ARG B 264 N VAL B 241
SHEET 1 J 2 PHE B 465 GLY B 466 0
SHEET 2 J 2 GLN B 475 GLU B 476 -1 O GLU B 476 N PHE B 465
SHEET 1 K 2 ILE C 22 ILE C 24 0
SHEET 2 K 2 GLU C 27 HIS C 29 -1 O HIS C 29 N ILE C 22
SHEET 1 L 2 THR C 36 VAL C 40 0
SHEET 2 L 2 VAL C 47 ALA C 52 -1 O ILE C 48 N THR C 39
SHEET 1 M 5 VAL C 218 ILE C 220 0
SHEET 2 M 5 VAL C 188 LYS C 192 1 N MET C 191 O ASN C 219
SHEET 3 M 5 VAL C 161 ILE C 165 1 N CYS C 162 O VAL C 188
SHEET 4 M 5 LYS C 240 THR C 244 1 O LYS C 240 N GLY C 163
SHEET 5 M 5 ARG C 264 GLU C 268 1 O ARG C 264 N VAL C 241
SHEET 1 N 2 ILE D 22 ILE D 24 0
SHEET 2 N 2 GLU D 27 HIS D 29 -1 O HIS D 29 N ILE D 22
SHEET 1 O 2 THR D 36 VAL D 40 0
SHEET 2 O 2 VAL D 47 ALA D 52 -1 O ILE D 48 N THR D 39
SHEET 1 P 5 VAL D 218 ILE D 220 0
SHEET 2 P 5 VAL D 188 LYS D 192 1 N MET D 191 O ASN D 219
SHEET 3 P 5 VAL D 161 ILE D 165 1 N GLN D 164 O LYS D 192
SHEET 4 P 5 LYS D 240 THR D 244 1 O LYS D 240 N GLY D 163
SHEET 5 P 5 ARG D 264 GLU D 268 1 O ARG D 264 N VAL D 241
SHEET 1 Q 2 PHE D 465 GLY D 466 0
SHEET 2 Q 2 GLN D 475 GLU D 476 -1 O GLU D 476 N PHE D 465
SHEET 1 R 2 ILE E 22 ILE E 24 0
SHEET 2 R 2 GLU E 27 HIS E 29 -1 O HIS E 29 N ILE E 22
SHEET 1 S 2 THR E 36 VAL E 40 0
SHEET 2 S 2 VAL E 47 ALA E 52 -1 O ILE E 48 N THR E 39
SHEET 1 T20 LYS F 366 CYS F 369 0
SHEET 2 T20 THR F 384 GLY F 387 -1 O VAL F 385 N LEU F 368
SHEET 3 T20 VAL F 404 PHE F 410 1 O MET F 405 N PHE F 386
SHEET 4 T20 ARG F 307 GLN F 311 1 N THR F 308 O GLN F 406
SHEET 5 T20 PRO F 274 ILE F 277 1 N ASN F 275 O ARG F 307
SHEET 6 T20 ALA F 428 PHE F 432 1 O ALA F 430 N ILE F 276
SHEET 7 T20 THR F 450 VAL F 453 1 O TRP F 452 N VAL F 431
SHEET 8 T20 THR E 486 LYS E 494 1 N THR E 490 O VAL F 451
SHEET 9 T20 PHE E 150 PRO E 158 -1 N GLU E 157 O GLU E 487
SHEET 10 T20 GLY E 141 ILE E 144 -1 N ILE E 144 O SER E 152
SHEET 11 T20 GLY H 141 ILE H 144 -1 O GLY H 141 N THR E 143
SHEET 12 T20 PHE H 150 PRO H 158 -1 O THR H 154 N LYS H 142
SHEET 13 T20 THR H 486 LYS H 494 -1 O GLU H 487 N GLU H 157
SHEET 14 T20 THR G 450 VAL G 453 1 N VAL G 451 O THR H 490
SHEET 15 T20 ALA G 428 PHE G 432 1 N VAL G 431 O TRP G 452
SHEET 16 T20 PRO G 274 ILE G 277 1 N ILE G 276 O PHE G 432
SHEET 17 T20 ARG G 307 GLN G 311 1 O PHE G 309 N ILE G 277
SHEET 18 T20 VAL G 404 PHE G 410 1 O LEU G 408 N VAL G 310
SHEET 19 T20 THR G 384 GLY G 387 1 N PHE G 386 O MET G 405
SHEET 20 T20 LYS G 366 CYS G 369 -1 N LEU G 368 O VAL G 385
SHEET 1 U 5 VAL E 218 ILE E 220 0
SHEET 2 U 5 VAL E 188 LYS E 192 1 N MET E 191 O ASN E 219
SHEET 3 U 5 VAL E 161 ILE E 165 1 N GLN E 164 O LYS E 192
SHEET 4 U 5 LYS E 240 THR E 244 1 O LYS E 240 N GLY E 163
SHEET 5 U 5 ARG E 264 GLU E 268 1 O ARG E 264 N VAL E 241
SHEET 1 V20 LYS E 366 CYS E 369 0
SHEET 2 V20 THR E 384 GLY E 387 -1 O GLY E 387 N LYS E 366
SHEET 3 V20 VAL E 404 PHE E 410 1 O MET E 405 N PHE E 386
SHEET 4 V20 ARG E 307 GLN E 311 1 N VAL E 310 O LEU E 408
SHEET 5 V20 PRO E 274 ILE E 277 1 N ASN E 275 O ARG E 307
SHEET 6 V20 ALA E 428 PHE E 432 1 O PHE E 432 N ILE E 276
SHEET 7 V20 THR E 450 VAL E 453 1 O TRP E 452 N ALA E 429
SHEET 8 V20 THR F 486 LYS F 494 1 O THR F 490 N VAL E 451
SHEET 9 V20 PHE F 150 PRO F 158 -1 N GLU F 157 O GLU F 487
SHEET 10 V20 GLY F 141 ILE F 144 -1 N ILE F 144 O SER F 152
SHEET 11 V20 GLY G 141 ILE G 144 -1 O THR G 143 N GLY F 141
SHEET 12 V20 PHE G 150 PRO G 158 -1 O SER G 152 N ILE G 144
SHEET 13 V20 THR G 486 LYS G 494 -1 O GLU G 487 N GLU G 157
SHEET 14 V20 THR H 450 VAL H 453 1 O VAL H 451 N THR G 490
SHEET 15 V20 ALA H 428 PHE H 432 1 N VAL H 431 O TRP H 452
SHEET 16 V20 PRO H 274 ILE H 277 1 N ILE H 276 O ALA H 430
SHEET 17 V20 ARG H 307 GLN H 311 1 O PHE H 309 N ILE H 277
SHEET 18 V20 VAL H 404 PHE H 410 1 O LEU H 408 N VAL H 310
SHEET 19 V20 THR H 384 GLY H 387 1 N PHE H 386 O MET H 405
SHEET 20 V20 LYS H 366 CYS H 369 -1 N LEU H 368 O VAL H 385
SHEET 1 W 2 PHE E 465 GLY E 466 0
SHEET 2 W 2 GLN E 475 GLU E 476 -1 O GLU E 476 N PHE E 465
SHEET 1 X 2 ILE F 22 ILE F 24 0
SHEET 2 X 2 GLU F 27 HIS F 29 -1 O HIS F 29 N ILE F 22
SHEET 1 Y 2 THR F 36 VAL F 40 0
SHEET 2 Y 2 VAL F 47 ALA F 52 -1 O ILE F 48 N THR F 39
SHEET 1 Z 6 VAL F 218 ILE F 220 0
SHEET 2 Z 6 VAL F 188 LYS F 192 1 N MET F 191 O ASN F 219
SHEET 3 Z 6 VAL F 161 ILE F 165 1 N GLN F 164 O LYS F 192
SHEET 4 Z 6 LYS F 240 THR F 244 1 O LYS F 240 N GLY F 163
SHEET 5 Z 6 ARG F 264 GLU F 268 1 O ARG F 264 N VAL F 241
SHEET 6 Z 6 GLY F 472 SER F 473 -1 O SER F 473 N LEU F 267
SHEET 1 AA 2 ILE G 22 ILE G 24 0
SHEET 2 AA 2 GLU G 27 HIS G 29 -1 O HIS G 29 N ILE G 22
SHEET 1 AB 2 THR G 36 VAL G 40 0
SHEET 2 AB 2 VAL G 47 ALA G 52 -1 O ILE G 48 N THR G 39
SHEET 1 AC 5 VAL G 218 ILE G 220 0
SHEET 2 AC 5 VAL G 188 LYS G 192 1 N MET G 191 O ASN G 219
SHEET 3 AC 5 VAL G 161 ILE G 165 1 N CYS G 162 O VAL G 188
SHEET 4 AC 5 LYS G 240 THR G 244 1 O LYS G 240 N GLY G 163
SHEET 5 AC 5 ARG G 264 GLU G 268 1 O ARG G 264 N VAL G 241
SHEET 1 AD 2 PHE G 465 GLY G 466 0
SHEET 2 AD 2 GLN G 475 GLU G 476 -1 O GLU G 476 N PHE G 465
SHEET 1 AE 2 ILE H 22 ILE H 24 0
SHEET 2 AE 2 GLU H 27 HIS H 29 -1 O HIS H 29 N ILE H 22
SHEET 1 AF 2 THR H 36 VAL H 40 0
SHEET 2 AF 2 VAL H 47 ALA H 52 -1 O ILE H 48 N THR H 39
SHEET 1 AG 5 VAL H 218 ILE H 220 0
SHEET 2 AG 5 VAL H 188 LYS H 192 1 N MET H 191 O ASN H 219
SHEET 3 AG 5 VAL H 161 ILE H 165 1 N CYS H 162 O VAL H 188
SHEET 4 AG 5 LYS H 240 THR H 244 1 O LYS H 240 N GLY H 163
SHEET 5 AG 5 ARG H 264 GLU H 268 1 O ARG H 264 N VAL H 241
SHEET 1 AH 2 PHE H 465 GLY H 466 0
SHEET 2 AH 2 GLN H 475 GLU H 476 -1 O GLU H 476 N PHE H 465
CRYST1 140.780 150.860 177.230 90.00 90.00 90.00 P 21 21 21 32
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 0.007103 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005642 0.00000
(ATOM LINES ARE NOT SHOWN.)
END