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HEADER HYDROLASE 28-JUL-08 3DYI
TITLE SNAPSHOTS OF ESTERASE D FROM LACTOBACILLUS RHAMNOSUS:
TITLE 2 INSIGHTS INTO A ROTATION DRIVEN CATALYTIC MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE D;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS RHAMNOSUS;
SOURCE 3 ORGANISM_TAXID: 486408;
SOURCE 4 STRAIN: HN001;
SOURCE 5 GENE: ESTD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PPROEXHT C
KEYWDS ALPHA BETA HYDROLASE, MECHANISM, CATALYTIC TRIAD, ROTATION,
KEYWDS 2 ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.BENNETT,M.-L.DELABRE,R.HOLLAND,G.E.NORRIS
REVDAT 1 28-JUL-09 3DYI 0
JRNL AUTH M.D.BENNETT,M.-L.DELABRE,R.HOLLAND,G.E.NORRIS
JRNL TITL SNAPSHOTS OF ESTERASE D FROM LACTOBACILLUS
JRNL TITL 2 RHAMNOSUS: INSIGHTS INTO A ROTATION DRIVEN
JRNL TITL 3 CATALYTIC MECHANISM
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 24097
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 + TEST SET) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1241
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1564
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2080
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1837
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : 0.33000
REMARK 3 B33 (A**2) : -0.49000
REMARK 3 B12 (A**2) : 0.16000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.119
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.108
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.066
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.970
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1886 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2571 ; 1.030 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 239 ; 5.199 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 85 ;33.822 ;24.471
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 278 ;11.560 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;15.923 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 284 ; 0.070 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1465 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 919 ; 0.191 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1308 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 149 ; 0.085 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.091 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1218 ; 0.405 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1901 ; 0.688 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 761 ; 1.131 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 670 ; 1.741 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3DYI COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUL-08.
REMARK 100 THE RCSB ID CODE IS RCSB048648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-06
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.0
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 MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : OSMIC BLUE
REMARK 200 OPTICS : OSMIC BLUE
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3DKR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, NA ACETATE, PH 6.0,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 116.12000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.06000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.06000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 116.12000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -6
REMARK 465 ALA A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ILE A -2
REMARK 465 ARG A -1
REMARK 465 ASN A 0
REMARK 465 SER A 1
REMARK 465 ILE A 2
REMARK 465 GLU A 243
REMARK 465 GLY A 244
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 124 CD CE NZ
REMARK 470 LYS A 133 CD CE NZ
REMARK 470 ARG A 140 NE CZ NH1 NH2
REMARK 470 LYS A 144 CG CD CE NZ
REMARK 470 LYS A 177 CE NZ
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 THR A 14 -78.21 -122.62
REMARK 500 THR A 25 -5.47 72.43
REMARK 500 SER A 94 -112.58 50.44
REMARK 500 ILE A 120 -59.59 71.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 245
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DKR RELATED DB: PDB
REMARK 900 ESTD ACETATE COMPLEX
REMARK 900 RELATED ID: 3DLT RELATED DB: PDB
REMARK 900 ESTD BUTYRATE COMPLEX
REMARK 900 RELATED ID: 3DYV RELATED DB: PDB
DBREF 3DYI A 2 244 UNP B2CZF3 B2CZF3_LACRH 2 244
SEQADV 3DYI GLY A -6 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI ALA A -5 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI MET A -4 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI GLY A -3 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI ILE A -2 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI ARG A -1 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI ASN A 0 UNP B2CZF3 EXPRESSION TAG
SEQADV 3DYI SER A 1 UNP B2CZF3 EXPRESSION TAG
SEQRES 1 A 251 GLY ALA MET GLY ILE ARG ASN SER ILE PHE ARG LYS PRO
SEQRES 2 A 251 GLN PRO PHE GLU TYR GLU GLY THR ASP THR GLY VAL VAL
SEQRES 3 A 251 LEU LEU HIS ALA TYR THR GLY SER PRO ASN ASP MET ASN
SEQRES 4 A 251 PHE MET ALA ARG ALA LEU GLN ARG SER GLY TYR GLY VAL
SEQRES 5 A 251 TYR VAL PRO LEU PHE SER GLY HIS GLY THR VAL GLU PRO
SEQRES 6 A 251 LEU ASP ILE LEU THR LYS GLY ASN PRO ASP ILE TRP TRP
SEQRES 7 A 251 ALA GLU SER SER ALA ALA VAL ALA HIS MET THR ALA LYS
SEQRES 8 A 251 TYR ALA LYS VAL PHE VAL PHE GLY LEU SER LEU GLY GLY
SEQRES 9 A 251 ILE PHE ALA MET LYS ALA LEU GLU THR LEU PRO GLY ILE
SEQRES 10 A 251 THR ALA GLY GLY VAL PHE SER SER PRO ILE LEU PRO GLY
SEQRES 11 A 251 LYS HIS HIS LEU VAL PRO GLY PHE LEU LYS TYR ALA GLU
SEQRES 12 A 251 TYR MET ASN ARG LEU ALA GLY LYS SER ASP GLU SER THR
SEQRES 13 A 251 GLN ILE LEU ALA TYR LEU PRO GLY GLN LEU ALA ALA ILE
SEQRES 14 A 251 ASP GLN PHE ALA THR THR VAL ALA ALA ASP LEU ASN LEU
SEQRES 15 A 251 VAL LYS GLN PRO THR PHE ILE GLY GLN ALA GLY GLN ASP
SEQRES 16 A 251 GLU LEU VAL ASP GLY ARG LEU ALA TYR GLN LEU ARG ASP
SEQRES 17 A 251 ALA LEU ILE ASN ALA ALA ARG VAL ASP PHE HIS TRP TYR
SEQRES 18 A 251 ASP ASP ALA LYS HIS VAL ILE THR VAL ASN SER ALA HIS
SEQRES 19 A 251 HIS ALA LEU GLU GLU ASP VAL ILE ALA PHE MET GLN GLN
SEQRES 20 A 251 GLU ASN GLU GLY
HET CL A 245 1
HETNAM CL CHLORIDE ION
FORMUL 2 CL CL 1-
FORMUL 3 HOH *242(H2 O)
HELIX 1 1 SER A 27 ASP A 30 5 4
HELIX 2 2 MET A 31 SER A 41 1 11
HELIX 3 3 PRO A 58 GLY A 65 1 8
HELIX 4 4 ASN A 66 ALA A 83 1 18
HELIX 5 5 SER A 94 LEU A 107 1 14
HELIX 6 6 HIS A 126 GLY A 143 1 18
HELIX 7 7 GLU A 147 ALA A 153 1 7
HELIX 8 8 TYR A 154 ASP A 172 1 19
HELIX 9 9 LEU A 173 VAL A 176 5 4
HELIX 10 10 ARG A 194 LEU A 203 1 10
HELIX 11 11 ALA A 226 GLU A 241 1 16
SHEET 1 A 7 PHE A 9 TYR A 11 0
SHEET 2 A 7 GLY A 44 VAL A 47 -1 O VAL A 45 N TYR A 11
SHEET 3 A 7 THR A 16 LEU A 21 1 N THR A 16 O GLY A 44
SHEET 4 A 7 LYS A 87 LEU A 93 1 O LYS A 87 N GLY A 17
SHEET 5 A 7 ALA A 112 PHE A 116 1 O PHE A 116 N GLY A 92
SHEET 6 A 7 THR A 180 ALA A 185 1 O PHE A 181 N GLY A 113
SHEET 7 A 7 VAL A 209 TYR A 214 1 O HIS A 212 N ILE A 182
SITE 1 AC1 4 TYR A 24 SER A 94 LEU A 95 HOH A 344
CRYST1 47.442 47.442 174.180 90.00 90.00 120.00 P 32 2 1 6
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 0.021079 0.012170 0.000000 0.00000
SCALE2 0.000000 0.024339 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005741 0.00000
TER 1838 ASN A 242
MASTER 301 0 1 11 7 0 1 6 2080 1 0 20
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