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HEADER HYDROLASE 26-AUG-14 3WYD
TITLE C-TERMINAL ESTERASE DOMAIN OF LC-EST1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LC-EST1C;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED ORGANISM;
SOURCE 3 ORGANISM_TAXID: 155900;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28B
KEYWDS LEAF-BRANCH COMPOST; METAGENOME, ALPHA/BETA HYDROLASE FOLD, ESTERASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.OKANO,X.HONG,C.ANGKAWIDJAJA,S.KANAYA
REVDAT 1 12-NOV-14 3WYD 0
JRNL AUTH H.OKANO,X.HONG,E.KANAYA,C.ANGKAWIDJAJA,S.KANAYA
JRNL TITL STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF A
JRNL TITL 2 METAGENOME-DERIVED ESTERASE WITH A LONG N-TERMINAL EXTENSION
JRNL REF PROTEIN SCI. 2014
JRNL REFN ESSN 1469-896X
JRNL PMID 25348365
JRNL DOI 10.1002/PRO.2591
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 56727
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3030
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) : 1.53
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4164
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.82
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 233
REMARK 3 BIN FREE R VALUE : 0.2940
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 451
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
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): 0.085
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.087
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.281
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3073 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4162 ; 1.439 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 380 ; 6.535 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;31.669 ;22.867
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 479 ;13.999 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;20.109 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 432 ; 0.116 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2393 ; 0.017 ; 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): 1901 ; 1.649 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3053 ; 2.563 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1172 ; 3.798 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1109 ; 5.707 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER 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 : 1.40
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3WYD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-AUG-14.
REMARK 100 THE RCSB ID CODE IS RCSB096947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-MAY-14; 18-JUL-14
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL44XU; BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9; 0.978769, 0.979101, 0.994813
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE CRYSTAL;
REMARK 200 ROTATED-INCLINED DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE; RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60179
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 78.140
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.18100
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; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM CHLORIDE, 0.1M BIS-TRIS,
REMARK 280 25% PEG3,350, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 22.93050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 78.13750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 27.72300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 78.13750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.93050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 27.72300
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 283
REMARK 465 GLY A 284
REMARK 465 SER A 285
REMARK 465 SER A 286
REMARK 465 HIS A 287
REMARK 465 HIS A 288
REMARK 465 HIS A 289
REMARK 465 HIS A 290
REMARK 465 HIS A 291
REMARK 465 HIS A 292
REMARK 465 SER A 293
REMARK 465 SER A 294
REMARK 465 GLY A 295
REMARK 465 LEU A 296
REMARK 465 VAL A 297
REMARK 465 PRO A 298
REMARK 465 ARG A 299
REMARK 465 GLY A 300
REMARK 465 SER A 301
REMARK 465 HIS A 302
REMARK 465 MET A 303
REMARK 465 ARG A 361
REMARK 465 GLN A 362
REMARK 465 PRO A 363
REMARK 465 ALA A 364
REMARK 465 SER A 365
REMARK 465 MET A 366
REMARK 465 ALA A 503
REMARK 465 ALA A 504
REMARK 465 LYS A 505
REMARK 465 ALA A 506
REMARK 465 ALA A 507
REMARK 465 THR A 508
REMARK 465 ASN A 509
REMARK 465 LYS A 510
REMARK 465 MET B 283
REMARK 465 GLY B 284
REMARK 465 SER B 285
REMARK 465 SER B 286
REMARK 465 HIS B 287
REMARK 465 HIS B 288
REMARK 465 HIS B 289
REMARK 465 HIS B 290
REMARK 465 HIS B 291
REMARK 465 HIS B 292
REMARK 465 SER B 293
REMARK 465 SER B 294
REMARK 465 GLY B 295
REMARK 465 LEU B 296
REMARK 465 VAL B 297
REMARK 465 PRO B 298
REMARK 465 ARG B 299
REMARK 465 GLY B 300
REMARK 465 SER B 301
REMARK 465 HIS B 302
REMARK 465 MET B 303
REMARK 465 ARG B 361
REMARK 465 GLN B 362
REMARK 465 PRO B 363
REMARK 465 ALA B 364
REMARK 465 SER B 365
REMARK 465 MET B 366
REMARK 465 ARG B 501
REMARK 465 PRO B 502
REMARK 465 ALA B 503
REMARK 465 ALA B 504
REMARK 465 LYS B 505
REMARK 465 ALA B 506
REMARK 465 ALA B 507
REMARK 465 THR B 508
REMARK 465 ASN B 509
REMARK 465 LYS B 510
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 338 -157.88 -113.19
REMARK 500 TYR A 339 71.34 51.64
REMARK 500 SER A 399 -118.17 68.14
REMARK 500 SER B 338 -167.12 -116.92
REMARK 500 SER B 399 -114.83 67.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THIS PROTEIN WAS NOT AVAILABLE AT THE UNIPROT
REMARK 999 KNOWLEDGEBASE DATABASE (UNIPROTKB) AT THE TIME OF DEPOSITION.
REMARK 999 AUTHORS STATE THAT THE GENEBANK ACCESSION NUMBER IS KM406409 FOR
REMARK 999 THE SEQUENCE.
DBREF 3WYD A 283 510 PDB 3WYD 3WYD 283 510
DBREF 3WYD B 283 510 PDB 3WYD 3WYD 283 510
SEQRES 1 A 228 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 228 LEU VAL PRO ARG GLY SER HIS MET PRO TYR ARG LEU TYR
SEQRES 3 A 228 VAL PRO THR THR TYR ASP GLY THR LYS ALA PHE PRO LEU
SEQRES 4 A 228 VAL ILE ALA LEU HIS GLY MET GLY GLY ASP GLU ASN SER
SEQRES 5 A 228 TYR PHE ASP SER TYR GLN ARG GLY ALA PHE MET ILE GLU
SEQRES 6 A 228 ALA GLU ASN ARG GLY TYR ILE VAL ALA CYS PRO LYS GLY
SEQRES 7 A 228 ARG GLN PRO ALA SER MET TYR VAL GLY PRO ALA GLU ARG
SEQRES 8 A 228 ASP VAL MET ASP VAL ILE ALA GLU VAL ARG ARG ASP TYR
SEQRES 9 A 228 LYS ILE ASP PRO ASP ARG ILE TYR MET THR GLY HIS SER
SEQRES 10 A 228 MET GLY GLY TYR GLY THR TRP SER ILE ALA MET ASN HIS
SEQRES 11 A 228 PRO ASP VAL PHE ALA ALA LEU ALA PRO VAL ALA GLY GLY
SEQRES 12 A 228 GLY ASN PRO LEU GLY MET ALA ASN ILE ALA HIS ILE PRO
SEQRES 13 A 228 GLN LEU VAL VAL HIS GLY ASP ASN ASP LYS THR VAL PRO
SEQRES 14 A 228 VAL GLU ARG SER ARG VAL MET VAL GLU ALA ALA LYS LYS
SEQRES 15 A 228 HIS GLY THR GLU ILE LYS TYR ILE GLU ILE PRO GLY GLY
SEQRES 16 A 228 ASP HIS VAL SER VAL ALA ALA ARG THR PHE LYS ASP VAL
SEQRES 17 A 228 PHE ASP TRP PHE ASP SER HIS LYS ARG LYS ARG PRO ALA
SEQRES 18 A 228 ALA LYS ALA ALA THR ASN LYS
SEQRES 1 B 228 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 228 LEU VAL PRO ARG GLY SER HIS MET PRO TYR ARG LEU TYR
SEQRES 3 B 228 VAL PRO THR THR TYR ASP GLY THR LYS ALA PHE PRO LEU
SEQRES 4 B 228 VAL ILE ALA LEU HIS GLY MET GLY GLY ASP GLU ASN SER
SEQRES 5 B 228 TYR PHE ASP SER TYR GLN ARG GLY ALA PHE MET ILE GLU
SEQRES 6 B 228 ALA GLU ASN ARG GLY TYR ILE VAL ALA CYS PRO LYS GLY
SEQRES 7 B 228 ARG GLN PRO ALA SER MET TYR VAL GLY PRO ALA GLU ARG
SEQRES 8 B 228 ASP VAL MET ASP VAL ILE ALA GLU VAL ARG ARG ASP TYR
SEQRES 9 B 228 LYS ILE ASP PRO ASP ARG ILE TYR MET THR GLY HIS SER
SEQRES 10 B 228 MET GLY GLY TYR GLY THR TRP SER ILE ALA MET ASN HIS
SEQRES 11 B 228 PRO ASP VAL PHE ALA ALA LEU ALA PRO VAL ALA GLY GLY
SEQRES 12 B 228 GLY ASN PRO LEU GLY MET ALA ASN ILE ALA HIS ILE PRO
SEQRES 13 B 228 GLN LEU VAL VAL HIS GLY ASP ASN ASP LYS THR VAL PRO
SEQRES 14 B 228 VAL GLU ARG SER ARG VAL MET VAL GLU ALA ALA LYS LYS
SEQRES 15 B 228 HIS GLY THR GLU ILE LYS TYR ILE GLU ILE PRO GLY GLY
SEQRES 16 B 228 ASP HIS VAL SER VAL ALA ALA ARG THR PHE LYS ASP VAL
SEQRES 17 B 228 PHE ASP TRP PHE ASP SER HIS LYS ARG LYS ARG PRO ALA
SEQRES 18 B 228 ALA LYS ALA ALA THR ASN LYS
FORMUL 3 HOH *451(H2 O)
HELIX 1 1 ASN A 333 SER A 338 1 6
HELIX 2 2 SER A 338 GLY A 352 1 15
HELIX 3 3 GLY A 369 TYR A 386 1 18
HELIX 4 4 SER A 399 HIS A 412 1 14
HELIX 5 5 ASN A 427 ALA A 435 5 9
HELIX 6 6 VAL A 452 LYS A 464 1 13
HELIX 7 7 SER A 481 THR A 486 1 6
HELIX 8 8 THR A 486 SER A 496 1 11
HELIX 9 9 ASN B 333 SER B 338 1 6
HELIX 10 10 SER B 338 GLY B 352 1 15
HELIX 11 11 GLY B 369 TYR B 386 1 18
HELIX 12 12 SER B 399 HIS B 412 1 14
HELIX 13 13 ASN B 427 ALA B 435 5 9
HELIX 14 14 VAL B 452 HIS B 465 1 14
HELIX 15 15 SER B 481 THR B 486 1 6
HELIX 16 16 THR B 486 SER B 496 1 11
SHEET 1 A 5 TYR A 305 TYR A 308 0
SHEET 2 A 5 ILE A 354 PRO A 358 -1 O CYS A 357 N ARG A 306
SHEET 3 A 5 PHE A 319 LEU A 325 1 N VAL A 322 O ALA A 356
SHEET 4 A 5 ILE A 388 HIS A 398 1 O TYR A 394 N LEU A 321
SHEET 5 A 5 ALA A 418 VAL A 422 1 O VAL A 422 N GLY A 397
SHEET 1 B 2 GLN A 439 GLY A 444 0
SHEET 2 B 2 ILE A 469 ILE A 474 1 O ILE A 472 N VAL A 441
SHEET 1 C 5 TYR B 305 TYR B 308 0
SHEET 2 C 5 ILE B 354 PRO B 358 -1 O CYS B 357 N ARG B 306
SHEET 3 C 5 PHE B 319 LEU B 325 1 N VAL B 322 O ALA B 356
SHEET 4 C 5 ILE B 388 HIS B 398 1 O TYR B 394 N LEU B 321
SHEET 5 C 5 ALA B 418 VAL B 422 1 O VAL B 422 N GLY B 397
SHEET 1 D 2 GLN B 439 GLY B 444 0
SHEET 2 D 2 ILE B 469 ILE B 474 1 O ILE B 472 N VAL B 441
CRYST1 45.861 55.446 156.275 90.00 90.00 90.00 P 21 21 21 8
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 0.021805 0.000000 0.000000 0.00000
SCALE2 0.000000 0.018036 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006399 0.00000
TER 1506 PRO A 502
TER 2994 LYS B 500
MASTER 347 0 0 16 14 0 0 6 3443 2 0 36
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