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HEADER HYDROLASE 08-MAY-08 3D2C
TITLE STRUCTURE OF 4D3, A THERMOSTABLE MUTANT OF BACILLUS
TITLE 2 SUBTILIS LIPASE OBTAINED THROUGH DIRECTED EVOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 GENE: LIPA, LIP, BSU02700;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET21B
KEYWDS LIPASE, ALPHA/BETA HYDROLASE, STABILITY, DIRECTED EVOLUTION,
KEYWDS 2 HYDROLASE, LIPID DEGRADATION, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SANKARANARAYANAN,M.Z.KAMAL
REVDAT 1 03-JUN-08 3D2C 0
JRNL AUTH S.AHMAD,M.Z.KAMAL,R.SANKARANARAYANAN,N.M.RAO
JRNL TITL THERMOSTABLE BACILLUS SUBTILIS LIPASES: IN VITRO
JRNL TITL 2 EVOLUTION AND STRUCTURAL INSIGHT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.18 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) : 2.18
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 133186
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) : 0.202
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 6662
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 : 16380
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 1130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00600
REMARK 3 B22 (A**2) : -2.08500
REMARK 3 B33 (A**2) : 1.07900
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) : 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) : 0.005 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.210 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 53.06
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3D2C COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB047503.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
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 : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133252
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.180
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.18
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.48900
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M SUCCINIC ACID, 0.1M HEPES, 1%(W/
REMARK 280 V) POLYETHELENE GLYCOL MONOMETHYL ETHER 2000, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 -X,Y,1/2-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 1/2+X,1/2+Y,Z
REMARK 290 6555 1/2-X,1/2-Y,1/2+Z
REMARK 290 7555 1/2-X,1/2+Y,1/2-Z
REMARK 290 8555 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 98.95100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 98.95100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 66.14250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 99.02100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 66.14250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 99.02100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 98.95100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 66.14250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 99.02100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 98.95100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 66.14250
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 99.02100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G
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: 8
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 9
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I
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: 10
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 11
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K
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: 12
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 13
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 24MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33680 ANGSTROM**2
REMARK 350 TOTAL SURFACE AREA FOR THE COMPLEX: 144270 ANGSTROM**2
REMARK 350 GAIN IN SOLVENT FREE ENERGY: -268 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -98.95100
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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 ALA C 1
REMARK 465 GLU C 2
REMARK 465 ALA D 1
REMARK 465 GLU D 2
REMARK 465 ALA E 1
REMARK 465 GLU E 2
REMARK 465 ALA F 1
REMARK 465 GLU F 2
REMARK 465 ALA G 1
REMARK 465 GLU G 2
REMARK 465 ALA H 1
REMARK 465 GLU H 2
REMARK 465 ALA I 1
REMARK 465 GLU I 2
REMARK 465 ALA J 1
REMARK 465 GLU J 2
REMARK 465 ALA K 1
REMARK 465 GLU K 2
REMARK 465 ALA L 1
REMARK 465 GLU L 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 44 3.06 -69.77
REMARK 500 SER A 77 -119.34 46.48
REMARK 500 LEU A 90 -149.92 -112.43
REMARK 500 ALA A 97 -63.00 -106.02
REMARK 500 ASN A 179 62.84 -175.13
REMARK 500 THR A 180 28.87 -69.74
REMARK 500 SER B 77 -118.83 43.97
REMARK 500 LEU B 90 -147.25 -137.96
REMARK 500 ARG B 107 5.28 -65.59
REMARK 500 ASN B 179 85.69 -165.77
REMARK 500 THR B 180 37.78 -87.06
REMARK 500 SER C 77 -120.61 50.60
REMARK 500 LEU C 90 -139.09 -116.91
REMARK 500 ASN C 179 88.90 -162.63
REMARK 500 THR C 180 35.92 -93.32
REMARK 500 SER D 77 -123.27 52.28
REMARK 500 LEU D 90 -148.31 -110.78
REMARK 500 ASN D 179 88.57 -155.75
REMARK 500 THR D 180 39.38 -85.89
REMARK 500 SER E 77 -120.76 52.01
REMARK 500 LEU E 90 -150.25 -94.92
REMARK 500 ALA E 105 57.82 -92.22
REMARK 500 ASN E 179 87.16 -153.32
REMARK 500 SER F 77 -121.18 48.24
REMARK 500 LEU F 90 -149.38 -115.24
REMARK 500 ALA F 105 53.09 -96.77
REMARK 500 ASN F 179 104.68 -178.16
REMARK 500 SER G 77 -121.36 47.72
REMARK 500 LEU G 90 -139.17 -101.22
REMARK 500 ALA G 105 48.12 -88.74
REMARK 500 THR G 109 -55.13 -128.24
REMARK 500 ASN G 179 73.85 -168.13
REMARK 500 THR G 180 28.83 -76.79
REMARK 500 SER H 77 -117.67 52.59
REMARK 500 LEU H 90 -149.54 -99.79
REMARK 500 ASN H 179 89.02 -161.33
REMARK 500 SER I 77 -117.94 50.53
REMARK 500 LEU I 90 -133.98 -98.15
REMARK 500 ALA I 105 49.79 -93.80
REMARK 500 THR I 109 -52.14 -125.29
REMARK 500 GLN I 121 125.19 -172.25
REMARK 500 ASN I 179 88.58 -160.65
REMARK 500 SER J 77 -119.91 44.51
REMARK 500 LEU J 90 -145.24 -113.98
REMARK 500 ALA J 97 -63.08 -103.44
REMARK 500 ALA J 105 51.32 -90.48
REMARK 500 ARG J 107 0.47 -66.03
REMARK 500 GLN J 178 148.80 175.56
REMARK 500 ASN J 179 81.38 -156.24
REMARK 500 SER K 77 -119.74 44.61
REMARK 500 LEU K 90 -145.70 -92.30
REMARK 500 ALA K 105 52.09 -92.00
REMARK 500 ASN K 179 95.96 -172.92
REMARK 500 SER L 77 -122.51 49.44
REMARK 500 LEU L 90 -141.33 -106.26
REMARK 500 ASN L 179 87.30 -166.79
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 L 274 DISTANCE = 7.46 ANGSTROMS
REMARK 525 HOH L 277 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH A 219 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH B 222 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH G 227 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH K 283 DISTANCE = 5.27 ANGSTROMS
REMARK 525 HOH A 244 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH K 291 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH F 252 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH L 344 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A 253 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH B 256 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH I 260 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH H 262 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH K 310 DISTANCE = 5.17 ANGSTROMS
REMARK 525 HOH G 266 DISTANCE = 5.57 ANGSTROMS
REMARK 525 HOH D 269 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH J 329 DISTANCE = 5.40 ANGSTROMS
REMARK 525 HOH G 275 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH L 373 DISTANCE = 5.82 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T2N RELATED DB: PDB
REMARK 900 RELATED ID: 1T4M RELATED DB: PDB
REMARK 900 RELATED ID: 3D2A RELATED DB: PDB
REMARK 900 RELATED ID: 3D2B RELATED DB: PDB
DBREF 3D2C A 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C B 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C C 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C D 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C E 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C F 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C G 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C H 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C I 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C J 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C K 1 181 UNP P37957 LIP_BACSU 32 212
DBREF 3D2C L 1 181 UNP P37957 LIP_BACSU 32 212
SEQADV 3D2C SER A 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER A 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU A 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR A 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP A 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO A 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP A 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET A 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR A 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER B 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER B 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU B 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR B 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP B 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO B 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP B 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET B 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR B 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER C 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER C 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU C 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR C 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP C 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO C 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP C 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET C 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR C 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER D 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER D 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU D 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR D 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP D 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO D 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP D 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET D 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR D 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER E 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER E 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU E 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR E 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP E 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO E 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP E 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET E 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR E 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER F 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER F 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU F 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR F 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP F 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO F 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP F 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET F 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR F 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER G 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER G 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU G 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR G 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP G 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO G 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP G 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET G 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR G 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER H 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER H 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU H 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR H 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP H 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO H 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP H 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET H 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR H 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER I 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER I 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU I 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR I 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP I 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO I 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP I 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET I 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR I 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER J 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER J 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU J 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR J 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP J 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO J 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP J 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET J 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR J 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER K 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER K 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU K 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR K 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP K 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO K 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP K 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET K 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR K 166 UNP P37957 ASN 197 ENGINEERED
SEQADV 3D2C SER L 15 UNP P37957 ALA 46 ENGINEERED
SEQADV 3D2C SER L 17 UNP P37957 PHE 48 ENGINEERED
SEQADV 3D2C GLU L 20 UNP P37957 ALA 51 ENGINEERED
SEQADV 3D2C TYR L 89 UNP P37957 ASN 120 ENGINEERED
SEQADV 3D2C ASP L 111 UNP P37957 GLY 142 ENGINEERED
SEQADV 3D2C PRO L 114 UNP P37957 LEU 145 ENGINEERED
SEQADV 3D2C ASP L 132 UNP P37957 ALA 163 ENGINEERED
SEQADV 3D2C MET L 157 UNP P37957 ILE 188 ENGINEERED
SEQADV 3D2C TYR L 166 UNP P37957 ASN 197 ENGINEERED
SEQRES 1 A 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 A 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 A 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 A 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 A 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 A 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 A 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 A 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 A 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 A 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 A 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 A 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 A 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 A 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 B 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 B 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 B 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 B 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 B 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 B 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 B 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 B 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 B 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 B 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 B 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 B 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 B 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 C 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 C 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 C 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 C 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 C 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 C 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 C 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 C 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 C 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 C 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 C 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 C 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 C 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 C 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 D 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 D 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 D 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 D 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 D 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 D 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 D 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 D 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 D 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 D 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 D 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 D 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 D 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 D 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 E 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 E 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 E 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 E 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 E 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 E 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 E 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 E 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 E 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 E 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 E 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 E 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 E 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 E 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 F 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 F 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 F 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 F 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 F 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 F 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 F 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 F 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 F 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 F 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 F 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 F 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 F 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 F 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 G 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 G 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 G 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 G 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 G 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 G 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 G 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 G 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 G 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 G 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 G 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 G 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 G 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 G 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 H 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 H 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 H 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 H 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 H 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 H 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 H 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 H 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 H 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 H 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 H 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 H 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 H 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 H 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 I 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 I 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 I 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 I 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 I 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 I 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 I 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 I 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 I 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 I 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 I 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 I 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 I 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 I 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 J 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 J 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 J 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 J 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 J 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 J 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 J 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 J 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 J 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 J 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 J 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 J 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 J 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 J 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 K 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 K 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 K 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 K 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 K 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 K 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 K 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 K 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 K 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 K 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 K 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 K 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 K 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 K 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 L 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 L 181 GLY SER SER SER ASN PHE GLU GLY ILE LYS SER TYR LEU
SEQRES 3 L 181 VAL SER GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL
SEQRES 4 L 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 L 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 L 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 L 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS TYR LEU ASP
SEQRES 8 L 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 L 181 ALA ASN ARG LEU THR THR ASP LYS ALA PRO PRO GLY THR
SEQRES 10 L 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 L 181 SER ASP ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU
SEQRES 12 L 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 L 181 MET GLY LEU LEU TYR SER SER GLN VAL TYR SER LEU ILE
SEQRES 14 L 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
FORMUL 13 HOH *1130(H2 O)
HELIX 1 1 SER A 15 ASN A 18 5 4
HELIX 2 2 PHE A 19 GLN A 29 1 11
HELIX 3 3 SER A 32 ASP A 34 5 3
HELIX 4 4 THR A 47 GLY A 67 1 21
HELIX 5 5 MET A 78 LEU A 90 1 13
HELIX 6 6 ASP A 91 ASN A 94 5 4
HELIX 7 7 ALA A 105 THR A 109 5 5
HELIX 8 8 MET A 137 ARG A 142 1 6
HELIX 9 9 HIS A 156 TYR A 161 5 6
HELIX 10 10 SER A 162 ASN A 174 1 13
HELIX 11 11 SER B 15 ASN B 18 5 4
HELIX 12 12 PHE B 19 GLN B 29 1 11
HELIX 13 13 SER B 32 ASP B 34 5 3
HELIX 14 14 THR B 47 GLY B 67 1 21
HELIX 15 15 MET B 78 LEU B 90 1 13
HELIX 16 16 ASP B 91 ASN B 94 5 4
HELIX 17 17 ALA B 105 THR B 109 5 5
HELIX 18 18 MET B 137 ARG B 142 1 6
HELIX 19 19 MET B 157 TYR B 161 5 5
HELIX 20 20 SER B 162 ASN B 174 1 13
HELIX 21 21 SER C 15 ASN C 18 5 4
HELIX 22 22 PHE C 19 GLN C 29 1 11
HELIX 23 23 SER C 32 ASP C 34 5 3
HELIX 24 24 THR C 47 GLY C 67 1 21
HELIX 25 25 MET C 78 LEU C 90 1 13
HELIX 26 26 ASP C 91 ASN C 94 5 4
HELIX 27 27 ALA C 105 THR C 109 5 5
HELIX 28 28 MET C 137 ARG C 142 1 6
HELIX 29 29 MET C 157 TYR C 161 5 5
HELIX 30 30 SER C 162 ASN C 174 1 13
HELIX 31 31 SER D 15 ASN D 18 5 4
HELIX 32 32 PHE D 19 GLN D 29 1 11
HELIX 33 33 SER D 32 ASP D 34 5 3
HELIX 34 34 THR D 47 GLY D 67 1 21
HELIX 35 35 MET D 78 LEU D 90 1 13
HELIX 36 36 ASP D 91 ASN D 94 5 4
HELIX 37 37 ALA D 105 THR D 109 5 5
HELIX 38 38 MET D 137 ARG D 142 1 6
HELIX 39 39 MET D 157 TYR D 161 5 5
HELIX 40 40 SER D 162 ASN D 174 1 13
HELIX 41 41 SER E 15 ASN E 18 5 4
HELIX 42 42 PHE E 19 GLN E 29 1 11
HELIX 43 43 SER E 32 ASP E 34 5 3
HELIX 44 44 THR E 47 GLY E 67 1 21
HELIX 45 45 MET E 78 TYR E 89 1 12
HELIX 46 46 LEU E 90 ASN E 94 5 5
HELIX 47 47 ALA E 105 THR E 109 5 5
HELIX 48 48 MET E 137 ARG E 142 1 6
HELIX 49 49 MET E 157 TYR E 161 5 5
HELIX 50 50 SER E 162 ASN E 174 1 13
HELIX 51 51 SER F 15 ASN F 18 5 4
HELIX 52 52 PHE F 19 GLN F 29 1 11
HELIX 53 53 SER F 32 ASP F 34 5 3
HELIX 54 54 THR F 47 GLY F 67 1 21
HELIX 55 55 MET F 78 LEU F 90 1 13
HELIX 56 56 ALA F 105 THR F 109 5 5
HELIX 57 57 MET F 137 ARG F 142 1 6
HELIX 58 58 HIS F 156 TYR F 161 5 6
HELIX 59 59 SER F 162 ASN F 174 1 13
HELIX 60 60 SER G 15 ASN G 18 5 4
HELIX 61 61 PHE G 19 GLN G 29 1 11
HELIX 62 62 SER G 32 ASP G 34 5 3
HELIX 63 63 THR G 47 GLY G 67 1 21
HELIX 64 64 MET G 78 LEU G 90 1 13
HELIX 65 65 ALA G 105 THR G 109 5 5
HELIX 66 66 MET G 137 ARG G 142 1 6
HELIX 67 67 HIS G 156 TYR G 161 5 6
HELIX 68 68 SER G 162 ASN G 174 1 13
HELIX 69 69 SER H 15 ASN H 18 5 4
HELIX 70 70 PHE H 19 GLN H 29 1 11
HELIX 71 71 SER H 32 ASP H 34 5 3
HELIX 72 72 THR H 47 GLY H 67 1 21
HELIX 73 73 MET H 78 LEU H 90 1 13
HELIX 74 74 ASP H 91 ASN H 94 5 4
HELIX 75 75 ALA H 105 THR H 109 5 5
HELIX 76 76 MET H 137 ARG H 142 1 6
HELIX 77 77 MET H 157 TYR H 161 5 5
HELIX 78 78 SER H 162 ASN H 174 1 13
HELIX 79 79 SER I 15 ASN I 18 5 4
HELIX 80 80 PHE I 19 GLN I 29 1 11
HELIX 81 81 SER I 32 ASP I 34 5 3
HELIX 82 82 THR I 47 GLY I 67 1 21
HELIX 83 83 MET I 78 LEU I 90 1 13
HELIX 84 84 ASP I 91 ASN I 94 5 4
HELIX 85 85 ALA I 105 THR I 109 5 5
HELIX 86 86 MET I 137 ARG I 142 1 6
HELIX 87 87 HIS I 156 TYR I 161 5 6
HELIX 88 88 SER I 162 ASN I 174 1 13
HELIX 89 89 SER J 15 ASN J 18 5 4
HELIX 90 90 PHE J 19 GLN J 29 1 11
HELIX 91 91 SER J 32 ASP J 34 5 3
HELIX 92 92 THR J 47 GLY J 67 1 21
HELIX 93 93 MET J 78 LEU J 90 1 13
HELIX 94 94 ASP J 91 ASN J 94 5 4
HELIX 95 95 ALA J 105 THR J 109 5 5
HELIX 96 96 MET J 137 ARG J 142 1 6
HELIX 97 97 MET J 157 TYR J 161 5 5
HELIX 98 98 SER J 162 ASN J 174 1 13
HELIX 99 99 SER K 15 ASN K 18 5 4
HELIX 100 100 PHE K 19 GLN K 29 1 11
HELIX 101 101 SER K 32 ASP K 34 5 3
HELIX 102 102 THR K 47 GLY K 67 1 21
HELIX 103 103 MET K 78 TYR K 89 1 12
HELIX 104 104 ASP K 91 ASN K 94 5 4
HELIX 105 105 ALA K 105 THR K 109 5 5
HELIX 106 106 MET K 137 ARG K 142 1 6
HELIX 107 107 HIS K 156 TYR K 161 5 6
HELIX 108 108 SER K 162 ASN K 174 1 13
HELIX 109 109 SER L 15 ASN L 18 5 4
HELIX 110 110 PHE L 19 GLN L 29 1 11
HELIX 111 111 SER L 32 ASP L 34 5 3
HELIX 112 112 THR L 47 GLY L 67 1 21
HELIX 113 113 MET L 78 LEU L 90 1 13
HELIX 114 114 ASP L 91 ASN L 94 5 4
HELIX 115 115 ALA L 105 THR L 109 5 5
HELIX 116 116 MET L 137 ARG L 142 1 6
HELIX 117 117 HIS L 156 TYR L 161 5 6
HELIX 118 118 SER L 162 ASN L 174 1 13
SHEET 1 A 6 LEU A 36 ALA A 38 0
SHEET 2 A 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 A 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 A 6 VAL A 96 LEU A 102 1 O VAL A 100 N ILE A 73
SHEET 5 A 6 LEU A 124 SER A 130 1 O ILE A 128 N THR A 101
SHEET 6 A 6 ARG A 147 ILE A 151 1 O ARG A 147 N SER A 127
SHEET 1 B 6 LEU B 36 ALA B 38 0
SHEET 2 B 6 VAL B 6 VAL B 9 1 N VAL B 6 O TYR B 37
SHEET 3 B 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 B 6 VAL B 96 LEU B 102 1 O LEU B 102 N ALA B 75
SHEET 5 B 6 LEU B 124 SER B 130 1 O ILE B 128 N THR B 101
SHEET 6 B 6 ARG B 147 ILE B 151 1 O ARG B 147 N SER B 127
SHEET 1 C 6 LEU C 36 ALA C 38 0
SHEET 2 C 6 VAL C 6 VAL C 9 1 N VAL C 6 O TYR C 37
SHEET 3 C 6 VAL C 71 HIS C 76 1 O ASP C 72 N VAL C 7
SHEET 4 C 6 VAL C 96 LEU C 102 1 O VAL C 100 N ALA C 75
SHEET 5 C 6 LEU C 124 SER C 130 1 O ILE C 128 N THR C 101
SHEET 6 C 6 ARG C 147 ILE C 151 1 O VAL C 149 N SER C 127
SHEET 1 D 6 LEU D 36 ALA D 38 0
SHEET 2 D 6 VAL D 6 VAL D 9 1 N VAL D 6 O TYR D 37
SHEET 3 D 6 VAL D 71 HIS D 76 1 O HIS D 76 N VAL D 9
SHEET 4 D 6 VAL D 96 LEU D 102 1 O ASN D 98 N ILE D 73
SHEET 5 D 6 LEU D 124 SER D 130 1 O ILE D 128 N THR D 101
SHEET 6 D 6 ARG D 147 ILE D 151 1 O VAL D 149 N SER D 127
SHEET 1 E 6 LEU E 36 ALA E 38 0
SHEET 2 E 6 VAL E 6 VAL E 9 1 N VAL E 6 O TYR E 37
SHEET 3 E 6 VAL E 71 HIS E 76 1 O HIS E 76 N VAL E 9
SHEET 4 E 6 VAL E 96 LEU E 102 1 O LEU E 102 N ALA E 75
SHEET 5 E 6 LEU E 124 SER E 130 1 O ILE E 128 N THR E 101
SHEET 6 E 6 ARG E 147 ILE E 151 1 O VAL E 149 N SER E 127
SHEET 1 F 6 LEU F 36 ALA F 38 0
SHEET 2 F 6 VAL F 6 VAL F 9 1 N VAL F 6 O TYR F 37
SHEET 3 F 6 VAL F 71 HIS F 76 1 O HIS F 76 N VAL F 9
SHEET 4 F 6 VAL F 96 LEU F 102 1 O LEU F 102 N ALA F 75
SHEET 5 F 6 LEU F 124 SER F 130 1 O LEU F 124 N VAL F 99
SHEET 6 F 6 ARG F 147 ILE F 151 1 O VAL F 149 N SER F 127
SHEET 1 G 6 LEU G 36 ALA G 38 0
SHEET 2 G 6 VAL G 6 VAL G 9 1 N VAL G 6 O TYR G 37
SHEET 3 G 6 VAL G 71 HIS G 76 1 O ASP G 72 N VAL G 7
SHEET 4 G 6 VAL G 96 LEU G 102 1 O LEU G 102 N ALA G 75
SHEET 5 G 6 LEU G 124 SER G 130 1 O ILE G 128 N THR G 101
SHEET 6 G 6 ARG G 147 ILE G 151 1 O VAL G 149 N SER G 127
SHEET 1 H 6 LEU H 36 ALA H 38 0
SHEET 2 H 6 VAL H 6 VAL H 9 1 N VAL H 6 O TYR H 37
SHEET 3 H 6 VAL H 71 HIS H 76 1 O HIS H 76 N VAL H 9
SHEET 4 H 6 VAL H 96 LEU H 102 1 O VAL H 100 N ALA H 75
SHEET 5 H 6 LEU H 124 SER H 130 1 O LEU H 124 N ALA H 97
SHEET 6 H 6 ARG H 147 ILE H 151 1 O VAL H 149 N SER H 127
SHEET 1 I 6 LEU I 36 ALA I 38 0
SHEET 2 I 6 VAL I 6 VAL I 9 1 N VAL I 6 O TYR I 37
SHEET 3 I 6 VAL I 71 HIS I 76 1 O ASP I 72 N VAL I 7
SHEET 4 I 6 VAL I 96 LEU I 102 1 O LEU I 102 N ALA I 75
SHEET 5 I 6 LEU I 124 SER I 130 1 O ILE I 128 N THR I 101
SHEET 6 I 6 ARG I 147 ILE I 151 1 O VAL I 149 N SER I 127
SHEET 1 J 6 LEU J 36 ALA J 38 0
SHEET 2 J 6 VAL J 6 VAL J 9 1 N VAL J 6 O TYR J 37
SHEET 3 J 6 VAL J 71 HIS J 76 1 O HIS J 76 N VAL J 9
SHEET 4 J 6 VAL J 96 LEU J 102 1 O LEU J 102 N ALA J 75
SHEET 5 J 6 LEU J 124 SER J 130 1 O ILE J 128 N THR J 101
SHEET 6 J 6 ARG J 147 ILE J 151 1 O VAL J 149 N SER J 127
SHEET 1 K 6 LEU K 36 ALA K 38 0
SHEET 2 K 6 VAL K 6 VAL K 9 1 N VAL K 6 O TYR K 37
SHEET 3 K 6 VAL K 71 HIS K 76 1 O ASP K 72 N VAL K 7
SHEET 4 K 6 VAL K 96 LEU K 102 1 O ASN K 98 N ILE K 73
SHEET 5 K 6 LEU K 124 SER K 130 1 O LEU K 124 N VAL K 99
SHEET 6 K 6 ARG K 147 ILE K 151 1 O VAL K 149 N SER K 127
SHEET 1 L 6 LEU L 36 ALA L 38 0
SHEET 2 L 6 VAL L 6 VAL L 9 1 N VAL L 6 O TYR L 37
SHEET 3 L 6 VAL L 71 HIS L 76 1 O ASP L 72 N VAL L 7
SHEET 4 L 6 VAL L 96 LEU L 102 1 O LEU L 102 N ALA L 75
SHEET 5 L 6 LEU L 124 SER L 130 1 O ILE L 128 N THR L 101
SHEET 6 L 6 ARG L 147 ILE L 151 1 O VAL L 149 N SER L 127
CRYST1 132.285 198.042 197.902 90.00 90.00 90.00 C 2 2 21 96
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 0.007559 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005049 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005053 0.00000
TER 1366 ASN A 181
TER 2732 ASN B 181
TER 4098 ASN C 181
TER 5464 ASN D 181
TER 6830 ASN E 181
TER 8196 ASN F 181
TER 9562 ASN G 181
TER 10928 ASN H 181
TER 12294 ASN I 181
TER 13660 ASN J 181
TER 15026 ASN K 181
TER 16392 ASN L 181
MASTER 465 0 0 118 72 0 0 617510 12 0 168
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