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HEADER HYDROLASE 13-AUG-07 2QXU
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS SUBTILIS LIPASE
TITLE 2 CRYSTALLIZED AT PH 5.0
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 SYNONYM: TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 GENE: LIPA;
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: PET-21B
KEYWDS ALPHA/BETA HYDROLASE FOLD, LIPID DEGRADATION, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR E.RAJAKUMARA,R.SANKARANARAYANAN
REVDAT 1 18-DEC-07 2QXU 0
JRNL AUTH E.RAJAKUMARA,P.ACHARYA,S.AHMAD,R.SANKARANARYANAN,
JRNL AUTH 2 N.M.RAO
JRNL TITL STRUCTURAL BASIS FOR THE REMARKABLE STABILITY OF
JRNL TITL 2 BACILLUS SUBTILIS LIPASE (LIP A) AT LOW PH
JRNL REF BIOCHIM.BIOPHYS.ACTA 2007
JRNL REFN ASTM BBACAQ NE ISSN 0006-3002
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 238428.730
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 96547
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) : 0.211
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4872
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 : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9342
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 488
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10808
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 840
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.88000
REMARK 3 B22 (A**2) : -2.47000
REMARK 3 B33 (A**2) : 1.59000
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) : 0.22
REMARK 3 ESD FROM SIGMAA (A) : 0.08
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) : 0.27
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.67
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) : 1.180 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.620 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.060 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.870 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 39.85
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 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QXU COMPLIES WITH FORMAT V. 3.1, 1-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.
REMARK 100 THE RCSB ID CODE IS RCSB044180.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-OCT-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.00
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 : RIGAKU RUH3R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRROR SYSTEM
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96606
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.9
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09500
REMARK 200 FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.23000
REMARK 200 FOR SHELL : 3.900
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: PDB ENTRY 1I6W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 6000, 100MM SODIUM ACETATE
REMARK 280 PH 5.0, 15MM AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 1/2-X,1/2+Y,-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 109.30400
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.46700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 109.30400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.46700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND 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: MONOMER
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: MONOMER
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: MONOMER
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: MONOMER
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: MONOMER
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: MONOMER
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: MONOMER
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: MONOMER
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 960 ANGSTROM**2
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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -109.30400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -55.46700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.98800
REMARK 350
REMARK 350 BIOMOLECULE: 10
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 1080 ANGSTROM**2
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -109.30400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 55.46700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.98800
REMARK 350
REMARK 350 BIOMOLECULE: 11
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 960 ANGSTROM**2
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 APPLY THE FOLLOWING TO CHAINS: F
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 327.91200
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -55.46700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 103.97600
REMARK 350
REMARK 350 BIOMOLECULE: 12
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 1060 ANGSTROM**2
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 BIOMT1 2 -1.000000 0.000000 0.000000 437.21600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 110.93400
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 13
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 1110 ANGSTROM**2
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 BIOMT1 2 -1.000000 0.000000 0.000000 437.21600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 221.86800
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 SER A 77 -121.91 48.40
REMARK 500 LEU A 90 -145.03 -110.03
REMARK 500 ALA A 105 47.80 -90.44
REMARK 500 ARG A 107 1.96 -68.52
REMARK 500 THR A 109 -51.20 -120.92
REMARK 500 GLN A 121 108.59 -169.71
REMARK 500 ASN A 179 99.87 -161.51
REMARK 500 SER B 77 -123.43 49.85
REMARK 500 LEU B 90 -141.94 -109.02
REMARK 500 ALA B 97 -67.03 -108.80
REMARK 500 ALA B 105 52.38 -91.45
REMARK 500 GLN B 121 116.70 -166.44
REMARK 500 TYR B 161 50.69 -140.39
REMARK 500 SER C 77 -118.24 49.57
REMARK 500 LEU C 90 -149.54 -103.20
REMARK 500 ALA C 97 -71.08 -103.63
REMARK 500 ARG C 107 7.08 -64.71
REMARK 500 ASN C 179 104.88 -174.46
REMARK 500 SER D 77 -131.47 52.99
REMARK 500 LEU D 90 -143.89 -100.38
REMARK 500 ALA D 97 -62.29 -100.71
REMARK 500 ASN D 179 99.12 -162.60
REMARK 500 SER E 77 -124.93 50.48
REMARK 500 LEU E 90 -134.55 -104.32
REMARK 500 ALA E 97 -67.64 -103.30
REMARK 500 SER F 77 -125.26 47.89
REMARK 500 LEU F 90 -145.29 -101.67
REMARK 500 ALA F 97 -70.53 -105.99
REMARK 500 ARG F 107 1.86 -68.35
REMARK 500 ASN F 179 107.48 -169.57
REMARK 500 SER G 77 -123.48 48.30
REMARK 500 LEU G 90 -144.59 -105.33
REMARK 500 ALA G 97 -68.02 -102.67
REMARK 500 ALA G 105 52.59 -92.47
REMARK 500 GLN G 121 111.00 -167.80
REMARK 500 ASN G 179 99.45 -165.59
REMARK 500 SER H 77 -121.89 41.84
REMARK 500 LEU H 90 -137.65 -103.76
REMARK 500 ALA H 97 -72.21 -107.55
REMARK 500 GLN H 121 107.43 -172.93
REMARK 500 ASN H 179 102.64 -162.35
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 C 251 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH G 257 DISTANCE = 5.00 ANGSTROMS
REMARK 525 HOH C 265 DISTANCE = 6.92 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QXT RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED AT PH 4.5
DBREF 2QXU A 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU B 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU C 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU D 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU E 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU F 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU G 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXU H 3 181 UNP P37957 LIP_BACSU 34 212
SEQRES 1 A 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 A 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 A 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 A 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 A 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 A 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 A 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 A 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 A 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 A 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 A 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 A 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 A 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 A 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 B 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 B 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 B 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 B 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 B 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 B 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 B 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 B 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 B 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 B 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 B 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 B 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 B 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 C 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 C 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 C 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 C 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 C 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 C 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 C 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 C 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 C 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 C 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 C 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 C 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 C 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 C 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 D 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 D 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 D 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 D 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 D 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 D 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 D 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 D 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 D 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 D 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 D 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 D 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 D 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 D 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 E 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 E 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 E 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 E 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 E 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 E 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 E 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 E 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 E 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 E 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 E 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 E 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 E 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 E 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 F 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 F 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 F 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 F 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 F 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 F 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 F 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 F 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 F 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 F 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 F 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 F 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 F 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 F 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 G 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 G 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 G 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 G 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 G 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 G 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 G 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 G 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 G 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 G 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 G 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 G 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 G 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 G 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 H 179 HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY GLY ALA
SEQRES 2 H 179 SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU VAL SER
SEQRES 3 H 179 GLN GLY TRP SER ARG ASP LYS LEU TYR ALA VAL ASP PHE
SEQRES 4 H 179 TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY PRO VAL
SEQRES 5 H 179 LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU THR GLY
SEQRES 6 H 179 ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET GLY GLY
SEQRES 7 H 179 ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP GLY GLY
SEQRES 8 H 179 ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY ALA ASN
SEQRES 9 H 179 ARG LEU THR THR GLY LYS ALA LEU PRO GLY THR ASP PRO
SEQRES 10 H 179 ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER SER ALA
SEQRES 11 H 179 ASP MET ILE VAL MET ASN TYR LEU SER ARG LEU ASP GLY
SEQRES 12 H 179 ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS ILE GLY
SEQRES 13 H 179 LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE LYS GLU
SEQRES 14 H 179 GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
FORMUL 9 HOH *840(H2 O)
HELIX 1 1 ALA 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 ALA 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 HIS B 156 TYR B 161 5 6
HELIX 20 20 SER B 162 ASN B 174 1 13
HELIX 21 21 ALA 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 ILE C 157 TYR C 161 5 5
HELIX 30 30 SER C 162 ASN C 174 1 13
HELIX 31 31 ALA 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 ASN D 89 1 12
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 SER D 141 5 5
HELIX 39 39 ILE D 157 TYR D 161 5 5
HELIX 40 40 SER D 162 ASN D 174 1 13
HELIX 41 41 ALA 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 LEU E 90 1 13
HELIX 46 46 ASP E 91 ASN E 94 5 4
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 ILE E 157 TYR E 161 5 5
HELIX 50 50 SER E 162 ASN E 174 1 13
HELIX 51 51 ALA 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 ASP F 91 ASN F 94 5 4
HELIX 57 57 ALA F 105 THR F 109 5 5
HELIX 58 58 MET F 137 SER F 141 5 5
HELIX 59 59 ILE F 157 TYR F 161 5 5
HELIX 60 60 SER F 162 ASN F 174 1 13
HELIX 61 61 ALA G 15 ASN G 18 5 4
HELIX 62 62 PHE G 19 GLN G 29 1 11
HELIX 63 63 SER G 32 ASP G 34 5 3
HELIX 64 64 THR G 47 GLY G 67 1 21
HELIX 65 65 MET G 78 LEU G 90 1 13
HELIX 66 66 ASP G 91 ASN G 94 5 4
HELIX 67 67 ALA G 105 THR G 109 5 5
HELIX 68 68 MET G 137 ARG G 142 1 6
HELIX 69 69 HIS G 156 TYR G 161 5 6
HELIX 70 70 SER G 162 ASN G 174 1 13
HELIX 71 71 ALA H 15 ASN H 18 5 4
HELIX 72 72 PHE H 19 GLN H 29 1 11
HELIX 73 73 SER H 32 ASP H 34 5 3
HELIX 74 74 THR H 47 GLY H 67 1 21
HELIX 75 75 MET H 78 LEU H 90 1 13
HELIX 76 76 ASP H 91 ASN H 94 5 4
HELIX 77 77 ALA H 105 THR H 109 5 5
HELIX 78 78 MET H 137 ARG H 142 1 6
HELIX 79 79 ILE H 157 TYR H 161 5 5
HELIX 80 80 SER H 162 ASN H 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 LEU A 102 N ALA A 75
SHEET 5 A 6 LEU A 124 SER A 130 1 O LEU A 124 N VAL A 99
SHEET 6 A 6 ARG A 147 ILE A 151 1 O VAL A 149 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 LEU B 124 N VAL B 99
SHEET 6 B 6 ARG B 147 ILE B 151 1 O VAL B 149 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 LEU C 102 N ALA C 75
SHEET 5 C 6 LEU C 124 SER C 130 1 O LEU C 124 N VAL C 99
SHEET 6 C 6 ARG C 147 ILE C 151 1 O ARG C 147 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 LEU D 102 N ALA D 75
SHEET 5 D 6 LEU D 124 SER D 130 1 O LEU D 124 N VAL D 99
SHEET 6 D 6 ARG D 147 ILE D 151 1 O ILE D 151 N TYR D 129
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 ASP E 72 N VAL E 7
SHEET 4 E 6 VAL E 96 LEU E 102 1 O ASN E 98 N ILE E 73
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 ILE F 128 N THR F 101
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 ASN G 98 N ILE G 73
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 ASP H 72 N VAL H 7
SHEET 4 H 6 VAL H 96 LEU H 102 1 O LEU H 102 N ALA H 75
SHEET 5 H 6 LEU H 124 SER H 130 1 O LEU H 124 N VAL H 99
SHEET 6 H 6 ARG H 147 ILE H 151 1 O VAL H 149 N SER H 127
CRYST1 218.608 110.934 51.988 90.00 90.00 90.00 P 21 21 2 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 0.004574 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009014 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019235 0.00000
TER 1352 ASN A 181
TER 2704 ASN B 181
TER 4056 ASN C 181
TER 5408 ASN D 181
TER 6760 ASN E 181
TER 8112 ASN F 181
TER 9464 ASN G 181
TER 10816 ASN H 181
MASTER 403 0 0 80 48 0 0 611648 8 0 112
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