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HEADER HYDROLASE 13-AUG-07 2QXT
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE BACILLUS SUBTILIS LIPASE
TITLE 2 CRYSTALLIZED AT PH 4.5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
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,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.RAJAKUMARA,R.SANKARANARAYANAN
REVDAT 1 18-DEC-07 2QXT 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. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2543611.470
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 21661
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) : 0.208
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 : 1093
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1888
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 94
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.036
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2702
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.26000
REMARK 3 B22 (A**2) : 2.26000
REMARK 3 B33 (A**2) : -4.52000
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) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.20
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) : 0.23
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) : 24.40
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) : 1.720 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.980 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.770 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 43.11
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 2QXT 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 RCSB044179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.50
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 : 21687
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
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 (%) : 97.7
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45700
REMARK 200 FOR SHELL : 2.300
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 (%): 39.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG 4000, 50MM SODIUM CITRATE
REMARK 280 PH 4.5, 50MM AMMONIUM SULFATE, VAPOR DIFFUSION, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
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 1/2-Y,1/2+X,3/4+Z
REMARK 290 4555 1/2+Y,1/2-X,1/4+Z
REMARK 290 5555 1/2-X,1/2+Y,3/4-Z
REMARK 290 6555 1/2+X,1/2-Y,1/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.00800
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 37.46800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 37.46800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 84.01200
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 37.46800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 37.46800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 28.00400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 37.46800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 37.46800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 84.01200
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 37.46800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 37.46800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 28.00400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.00800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 990 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: B
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 -74.93600
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 112.01600
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NE2 GLN B 178 NE2 GLN B 178 8775 1.52
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 SER A 77 -121.39 49.17
REMARK 500 LEU A 90 -148.36 -103.32
REMARK 500 ALA A 97 -67.43 -107.65
REMARK 500 ALA A 105 47.53 -90.26
REMARK 500 GLN A 121 116.48 -163.82
REMARK 500 SER B 77 -123.67 50.45
REMARK 500 LEU B 90 -147.94 -106.24
REMARK 500 ALA B 105 49.81 -92.53
REMARK 500 GLN B 121 116.85 -163.38
REMARK 500 ASN B 179 96.33 -163.71
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 B 276 DISTANCE = 6.72 ANGSTROMS
REMARK 525 HOH B 279 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B 316 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH B 317 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH B 319 DISTANCE = 5.62 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QXU RELATED DB: PDB
REMARK 900 THE SAME PROTEIN CRYSTALLIZED AT PH 5.0
DBREF 2QXT A 3 181 UNP P37957 LIP_BACSU 34 212
DBREF 2QXT B 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
FORMUL 3 HOH *280(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 ASN A 89 1 12
HELIX 6 6 ALA A 105 THR A 109 5 5
HELIX 7 7 MET A 137 ARG A 142 1 6
HELIX 8 8 ILE A 157 TYR A 161 5 5
HELIX 9 9 SER A 162 ASN A 174 1 13
HELIX 10 10 ALA B 15 ASN B 18 5 4
HELIX 11 11 PHE B 19 SER B 28 1 10
HELIX 12 12 SER B 32 ASP B 34 5 3
HELIX 13 13 THR B 47 GLY B 67 1 21
HELIX 14 14 MET B 78 ASN B 89 1 12
HELIX 15 15 ASP B 91 ASN B 94 5 4
HELIX 16 16 ALA B 105 THR B 109 5 5
HELIX 17 17 MET B 137 ARG B 142 1 6
HELIX 18 18 ILE B 157 TYR B 161 5 5
HELIX 19 19 SER B 162 ASN B 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 ILE A 128 N THR A 101
SHEET 6 A 6 ARG A 147 ILE A 151 1 O ILE A 151 N TYR A 129
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 ASN B 98 N ILE B 73
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
CRYST1 74.936 74.936 112.016 90.00 90.00 90.00 P 43 21 2 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013345 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013345 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008927 0.00000
TER 1352 ASN A 181
TER 2704 ASN B 181
MASTER 317 0 0 19 12 0 0 6 2982 2 0 28
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