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HEADER HYDROLASE 20-SEP-12 4H7D
TITLE CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE LINB T81A MUTANT FROM
TITLE 2 SPHINGOBIUM SP. MI1205
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOBIUM;
SOURCE 3 ORGANISM_TAXID: 407020;
SOURCE 4 STRAIN: MI1205;
SOURCE 5 GENE: LINB, DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.OKAI,J.OHTSUKA,L.F.IMAI,T.MASE,R.MORIUCHI,M.TSUDA,K.NAGATA,
AUTHOR 2 Y.NAGATA,M.TANOKURA
REVDAT 1 05-JUN-13 4H7D 0
JRNL AUTH M.OKAI,J.OHTSUKA,L.F.IMAI,T.MASE,R.MORIUCHI,M.TSUDA,
JRNL AUTH 2 K.NAGATA,Y.NAGATA,M.TANOKURA
JRNL TITL CRYSTAL STRUCTURE AND SITE-DIRECTED MUTAGENESIS ANALYSES OF
JRNL TITL 2 HALOALKANE DEHALOGENASE LINB FROM SPHINGOBIUM SP. STRAIN
JRNL TITL 3 MI1205.
JRNL REF J.BACTERIOL. V. 195 2642 2013
JRNL REFN ISSN 0021-9193
JRNL PMID 23564170
JRNL DOI 10.1128/JB.02020-12
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 18916
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 : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1013
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1156
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.1860
REMARK 3 BIN FREE R VALUE SET COUNT : 65
REMARK 3 BIN FREE R VALUE : 0.1930
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 15
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.46000
REMARK 3 B22 (A**2) : -0.40000
REMARK 3 B33 (A**2) : 1.86000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.186
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.080
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2404 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3266 ; 1.310 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 293 ; 5.427 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;31.055 ;22.773
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 375 ;13.500 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;13.821 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 343 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1890 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 4H7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-12.
REMARK 100 THE RCSB ID CODE IS RCSB075111.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19954
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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: NULL
REMARK 200 STARTING MODEL: 4H77
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 278K
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 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 25.22000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.02850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.22000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.02850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 MET A 1
REMARK 465 ALA A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
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 PRO A 39 43.83 -98.73
REMARK 500 THR A 40 -158.98 -101.77
REMARK 500 ASP A 108 -131.63 61.14
REMARK 500 ARG A 155 34.21 -85.34
REMARK 500 HIS A 247 -74.73 -157.48
REMARK 500 ALA A 271 -97.99 -106.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 526 O
REMARK 620 2 PRO A 175 O 85.6
REMARK 620 3 ILE A 178 O 84.8 87.3
REMARK 620 4 HOH A 521 O 163.5 92.5 78.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H77 RELATED DB: PDB
REMARK 900 RELATED ID: 4H7E RELATED DB: PDB
REMARK 900 RELATED ID: 4H7F RELATED DB: PDB
REMARK 900 RELATED ID: 4H7H RELATED DB: PDB
REMARK 900 RELATED ID: 4H7I RELATED DB: PDB
REMARK 900 RELATED ID: 4H7J RELATED DB: PDB
REMARK 900 RELATED ID: 4H7K RELATED DB: PDB
DBREF 4H7D A 1 296 UNP A4PEU6 A4PEU6_9SPHN 1 296
SEQADV 4H7D ALA A 81 UNP A4PEU6 THR 81 ENGINEERED MUTATION
SEQADV 4H7D HIS A 297 UNP A4PEU6 EXPRESSION TAG
SEQADV 4H7D HIS A 298 UNP A4PEU6 EXPRESSION TAG
SEQADV 4H7D HIS A 299 UNP A4PEU6 EXPRESSION TAG
SEQADV 4H7D HIS A 300 UNP A4PEU6 EXPRESSION TAG
SEQADV 4H7D HIS A 301 UNP A4PEU6 EXPRESSION TAG
SEQADV 4H7D HIS A 302 UNP A4PEU6 EXPRESSION TAG
SEQRES 1 A 302 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 302 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 302 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 302 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 302 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 302 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 302 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 302 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 302 VAL VAL HIS ASP TRP GLY SER VAL LEU GLY PHE ASP TRP
SEQRES 10 A 302 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 302 MET GLU ALA VAL THR MET PRO LEU GLU TRP ALA ASP PHE
SEQRES 12 A 302 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 302 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 302 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 302 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 302 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 302 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 302 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 302 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY HIS
SEQRES 20 A 302 LEU THR THR GLY ARG ILE ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 302 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE
SEQRES 22 A 302 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 302 ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
HET GOL A 401 6
HET GOL A 402 6
HET CA A 403 1
HET CL A 404 1
HET CL A 405 1
HETNAM GOL GLYCEROL
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 CA CA 2+
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *154(H2 O)
HELIX 1 1 SER A 41 ARG A 46 5 6
HELIX 2 2 ILE A 48 ALA A 53 5 6
HELIX 3 3 ALA A 81 LEU A 96 1 16
HELIX 4 4 ASP A 108 HIS A 121 1 14
HELIX 5 5 GLU A 139 PHE A 143 5 5
HELIX 6 6 ASP A 147 ARG A 155 1 9
HELIX 7 7 ALA A 158 LEU A 164 1 7
HELIX 8 8 ASN A 167 GLN A 172 1 6
HELIX 9 9 GLN A 172 LEU A 177 1 6
HELIX 10 10 SER A 183 GLU A 192 1 10
HELIX 11 11 PRO A 193 LEU A 195 5 3
HELIX 12 12 GLY A 198 ALA A 200 5 3
HELIX 13 13 ARG A 201 ILE A 211 1 11
HELIX 14 14 PRO A 217 SER A 232 1 16
HELIX 15 15 THR A 250 ARG A 258 1 9
HELIX 16 16 PHE A 273 ASP A 277 5 5
HELIX 17 17 SER A 278 ARG A 294 1 17
SHEET 1 A 8 LYS A 12 ILE A 16 0
SHEET 2 A 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 A 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 A 8 PRO A 31 GLN A 35 1 N PHE A 34 O ILE A 59
SHEET 5 A 8 VAL A 102 HIS A 107 1 O VAL A 103 N LEU A 33
SHEET 6 A 8 VAL A 125 MET A 131 1 O ALA A 129 N LEU A 104
SHEET 7 A 8 LYS A 238 PRO A 245 1 O ILE A 241 N TYR A 130
SHEET 8 A 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
LINK CA CA A 403 O HOH A 526 1555 1555 2.29
LINK O PRO A 175 CA CA A 403 1555 1555 2.31
LINK O ILE A 178 CA CA A 403 1555 1555 2.32
LINK CA CA A 403 O HOH A 521 1555 1555 2.34
CISPEP 1 ASN A 38 PRO A 39 0 -11.12
CISPEP 2 ASP A 73 PRO A 74 0 -0.96
CISPEP 3 THR A 216 PRO A 217 0 -2.48
CISPEP 4 GLU A 244 PRO A 245 0 -0.40
SITE 1 AC1 4 GLU A 139 ALA A 214 GLY A 215 HOH A 645
SITE 1 AC2 5 GLU A 123 THR A 264 PHE A 289 ARG A 292
SITE 2 AC2 5 HOH A 560
SITE 1 AC3 6 ASP A 166 PRO A 175 ILE A 178 HOH A 521
SITE 2 AC3 6 HOH A 526 HOH A 568
SITE 1 AC4 4 ASN A 38 TRP A 109 PHE A 169 PRO A 208
SITE 1 AC5 3 HOH A 517 HOH A 580 HOH A 624
CRYST1 50.440 72.057 73.544 90.00 90.00 90.00 P 21 21 2 4
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 0.019826 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013878 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013597 0.00000
TER 2331 PRO A 295
MASTER 311 0 5 17 8 0 7 6 2499 1 17 24
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