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HEADER HYDROLASE 27-APR-13 3WA6
TITLE CRYSTAL STRUCTURE OF TANNASE FROM LACTOBACILLUS PLANTARUM IN THE
TITLE 2 ORTHORHOMBIC CRYSTAL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANNASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.20;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LACTOBACILLUS PLANTARUM;
SOURCE 3 ORGANISM_TAXID: 1590;
SOURCE 4 STRAIN: SN35N;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21A(+)
KEYWDS ALPHA/BETA-HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.MATOBA,N.TANAKA,M.SUGIYAMA
REVDAT 1 24-JUL-13 3WA6 0
JRNL AUTH Y.MATOBA,N.TANAKA,M.NODA,F.HIGASHIKAWA,T.KUMAGAI,M.SUGIYAMA
JRNL TITL CRYSTALLOGRAPHIC AND MUTATIONAL ANALYSES OF TANNASE FROM
JRNL TITL 2 LACTOBACILLUS PLANTARUM
JRNL REF PROTEINS 2013
JRNL REFN ESSN 1097-0134
JRNL PMID 23836494
JRNL DOI 10.1002/PROT.24355
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3617886.270
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 39790
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) : 0.178
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2023
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.005
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6007
REMARK 3 BIN R VALUE (WORKING SET) : 0.2450
REMARK 3 BIN FREE R VALUE : 0.2800
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 303
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.016
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3560
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 331
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.35000
REMARK 3 B22 (A**2) : 3.92000
REMARK 3 B33 (A**2) : -2.57000
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) : 0.18
REMARK 3 ESD FROM SIGMAA (A) : 0.16
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) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.21
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.79
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) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.660 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.890 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.710 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 62.48
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 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3WA6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-MAY-13.
REMARK 100 THE RCSB ID CODE IS RCSB096079.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-NOV-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL26B2
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 : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41361
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.43500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.66
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM ACETATE, AMMONIUM
REMARK 280 SULFATE, PH 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 100.00500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.00500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 27.93500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 39.12000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 27.93500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 39.12000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 100.00500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 27.93500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 39.12000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 100.00500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 27.93500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 39.12000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 100.00500
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 863 LIES ON A SPECIAL POSITION.
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 SER A 2
REMARK 465 ASN A 3
REMARK 465 LEU A 470
REMARK 465 GLU A 471
REMARK 465 HIS A 472
REMARK 465 HIS A 473
REMARK 465 HIS A 474
REMARK 465 HIS A 475
REMARK 465 HIS A 476
REMARK 465 HIS A 477
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 163 -121.98 60.85
REMARK 500 CYS A 204 58.79 30.75
REMARK 500 THR A 236 -141.35 -93.27
REMARK 500 THR A 340 151.84 84.00
REMARK 500 ALA A 344 -158.66 -81.15
REMARK 500 HIS A 451 99.63 -69.27
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 SO4 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 502
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN DOES NOT CURRENTLY
REMARK 999 EXIST.
DBREF 3WA6 A 1 477 PDB 3WA6 3WA6 1 477
SEQRES 1 A 477 MET SER ASN ARG LEU ILE PHE ASP ALA ASP TRP LEU VAL
SEQRES 2 A 477 PRO GLU GLN VAL GLN VAL ALA GLY GLN ALA ILE GLN TYR
SEQRES 3 A 477 TYR ALA ALA ARG ASN ILE GLN TYR VAL GLN HIS PRO VAL
SEQRES 4 A 477 ALA ALA ILE GLN VAL LEU ASN VAL PHE VAL PRO ALA ALA
SEQRES 5 A 477 TYR LEU HIS GLY SER SER VAL ASN GLY TYR GLN ARG ALA
SEQRES 6 A 477 THR ALA PRO ILE LEU MET PRO ASN THR VAL GLY GLY TYR
SEQRES 7 A 477 LEU PRO GLY PRO ALA ASP ASP PRO GLN ARG VAL THR TRP
SEQRES 8 A 477 PRO THR ASN ALA GLY THR ILE GLN GLN ALA LEU LYS ARG
SEQRES 9 A 477 GLY TYR VAL VAL VAL ALA ALA GLY ILE ARG GLY ARG THR
SEQRES 10 A 477 THR VAL ASP LYS SER GLY GLN ARG VAL GLY GLN ALA PRO
SEQRES 11 A 477 ALA PHE ILE VAL ASP MET LYS ALA ALA ILE ARG TYR VAL
SEQRES 12 A 477 LYS TYR ASN GLN GLY ARG LEU PRO GLY ASP THR ASN ARG
SEQRES 13 A 477 ILE ILE THR ASN GLY THR SER ALA GLY GLY ALA THR SER
SEQRES 14 A 477 ALA LEU ALA GLY ALA SER GLY ASN SER ALA TYR PHE GLU
SEQRES 15 A 477 PRO ALA LEU THR ALA LEU GLY ALA ALA PRO ALA THR ASP
SEQRES 16 A 477 ASP ILE PHE ALA VAL SER ALA TYR CYS PRO ILE HIS ASN
SEQRES 17 A 477 LEU GLU HIS ALA ASP MET ALA TYR GLU TRP GLN PHE ASN
SEQRES 18 A 477 GLY ILE ASN ASP TRP HIS ARG TYR GLN PRO VAL ALA GLY
SEQRES 19 A 477 THR THR LYS ASN GLY ARG PRO LYS PHE GLU PRO VAL SER
SEQRES 20 A 477 GLY GLN LEU THR VAL GLU GLU GLN ALA LEU SER LEU ALA
SEQRES 21 A 477 LEU LYS ALA GLN PHE SER THR TYR LEU ASN GLN LEU GLN
SEQRES 22 A 477 LEU THR ALA SER ASP GLY THR HIS LEU THR LEU ASN GLU
SEQRES 23 A 477 ALA GLY MET GLY SER PHE ARG ASP VAL VAL ARG GLN LEU
SEQRES 24 A 477 LEU ILE SER SER ALA GLN THR ALA PHE ASP GLN GLY THR
SEQRES 25 A 477 ASP ILE HIS LYS TYR ALA GLY PHE VAL VAL THR GLY ASN
SEQRES 26 A 477 GLN VAL THR ASP LEU ASP LEU SER ALA TYR LEU LYS SER
SEQRES 27 A 477 LEU THR ARG MET LYS ALA VAL PRO ALA PHE ASP GLN LEU
SEQRES 28 A 477 ASP LEU THR SER PRO GLU ASN ASN LEU PHE GLY ASP ALA
SEQRES 29 A 477 THR ALA LYS ALA LYS HIS PHE THR ALA LEU ALA GLN THR
SEQRES 30 A 477 ARG SER THR VAL THR ALA GLN LEU ALA ASP ALA GLU LEU
SEQRES 31 A 477 ILE GLN ALA ILE ASN PRO LEU SER TYR LEU THR THR THR
SEQRES 32 A 477 SER SER GLN VAL ALA LYS HIS TRP ARG ILE ARG HIS GLY
SEQRES 33 A 477 ALA ALA ASP ARG ASP THR SER PHE ALA ILE PRO ILE ILE
SEQRES 34 A 477 LEU ALA ILE MET LEU GLU ASN HIS GLY TYR GLY ILE ASP
SEQRES 35 A 477 PHE ALA LEU PRO TRP ASP ILE PRO HIS SER GLY ASP TYR
SEQRES 36 A 477 ASP LEU GLY ASP LEU PHE SER TRP ILE ASP GLY LEU CYS
SEQRES 37 A 477 GLN LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 501 5
HET SO4 A 502 5
HETNAM SO4 SULFATE ION
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 HOH *331(H2 O)
HELIX 1 1 ASP A 8 LEU A 12 5 5
HELIX 2 2 ALA A 52 HIS A 55 5 4
HELIX 3 3 ASN A 94 GLY A 105 1 12
HELIX 4 4 PRO A 130 ASN A 146 1 17
HELIX 5 5 SER A 163 SER A 175 1 13
HELIX 6 6 SER A 178 TYR A 180 5 3
HELIX 7 7 PHE A 181 GLY A 189 1 9
HELIX 8 8 ASN A 208 ASN A 221 1 14
HELIX 9 9 LYS A 237 GLY A 239 5 3
HELIX 10 10 THR A 251 LEU A 272 1 22
HELIX 11 11 GLY A 290 GLN A 310 1 21
HELIX 12 12 ASP A 331 THR A 340 1 10
HELIX 13 13 SER A 355 PHE A 361 1 7
HELIX 14 14 THR A 372 ARG A 378 1 7
HELIX 15 15 ASP A 387 ILE A 394 1 8
HELIX 16 16 ASN A 395 LEU A 400 5 6
HELIX 17 17 PHE A 424 HIS A 437 1 14
HELIX 18 18 ASP A 456 GLN A 469 1 14
SHEET 1 A 9 VAL A 13 VAL A 19 0
SHEET 2 A 9 GLN A 22 GLN A 33 -1 O GLN A 22 N VAL A 19
SHEET 3 A 9 VAL A 44 PRO A 50 -1 O VAL A 47 N ALA A 29
SHEET 4 A 9 VAL A 107 ALA A 111 -1 O VAL A 108 N PHE A 48
SHEET 5 A 9 ILE A 69 PRO A 72 1 N LEU A 70 O VAL A 107
SHEET 6 A 9 ILE A 157 ASN A 160 1 O ILE A 158 N MET A 71
SHEET 7 A 9 ALA A 199 TYR A 203 1 O SER A 201 N THR A 159
SHEET 8 A 9 HIS A 410 ARG A 414 1 O HIS A 410 N VAL A 200
SHEET 9 A 9 GLY A 440 ALA A 444 1 O ASP A 442 N ILE A 413
SHEET 1 B 2 ASP A 225 THR A 235 0
SHEET 2 B 2 PRO A 241 GLN A 249 -1 O VAL A 246 N ARG A 228
SHEET 1 C 2 PHE A 320 THR A 323 0
SHEET 2 C 2 GLN A 326 LEU A 330 -1 O GLN A 326 N THR A 323
CISPEP 1 TRP A 91 PRO A 92 0 -0.04
CISPEP 2 ALA A 129 PRO A 130 0 0.32
CISPEP 3 VAL A 345 PRO A 346 0 -0.43
SITE 1 AC1 9 MET A 289 ARG A 293 ARG A 297 LEU A 330
SITE 2 AC1 9 ASP A 331 LEU A 332 SER A 333 HOH A 781
SITE 3 AC1 9 HOH A 920
SITE 1 AC2 7 GLY A 76 GLY A 77 SER A 163 HIS A 451
SITE 2 AC2 7 HOH A 701 HOH A 766 HOH A 805
CRYST1 55.870 78.240 200.010 90.00 90.00 90.00 C 2 2 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 0.017899 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012781 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005000 0.00000
TER 3572 GLN A 469
MASTER 306 0 2 18 13 0 5 6 3901 1 10 37
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