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HEADER HYDROLASE 21-SEP-17 5YFE
TITLE ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF THE POLY (ETHYLENE
TITLE 2 TEREPHTHALATE) HYDROLASE PETASE FROM I. SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETASE;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
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_PLASMID: PET-21(B)
KEYWDS PET DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.BAO,L.H.HE,B.LIU
REVDAT 1 26-SEP-18 5YFE 0
JRNL AUTH R.BAO,L.H.HE
JRNL TITL ENZYMATIC AND STRUCTURAL CHARACTERIZATION OF THE POLY
JRNL TITL 2 (ETHYLENE TEREPHTHALATE) HYDROLASE PETASE FROM I. SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.88
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.410
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 47650
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.200
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 37.8927 - 3.3494 1.00 3474 153 0.1820 0.1796
REMARK 3 2 3.3494 - 2.6587 1.00 3329 145 0.2317 0.2497
REMARK 3 3 2.6587 - 2.3227 1.00 3291 144 0.2303 0.2449
REMARK 3 4 2.3227 - 2.1103 1.00 3267 143 0.2336 0.2562
REMARK 3 5 2.1103 - 1.9591 1.00 3256 143 0.2333 0.2603
REMARK 3 6 1.9591 - 1.8436 1.00 3271 143 0.2288 0.2465
REMARK 3 7 1.8436 - 1.7513 1.00 3233 142 0.2296 0.1989
REMARK 3 8 1.7513 - 1.6750 1.00 3227 141 0.2244 0.2501
REMARK 3 9 1.6750 - 1.6105 1.00 3223 142 0.2268 0.2445
REMARK 3 10 1.6105 - 1.5550 1.00 3216 140 0.2294 0.2489
REMARK 3 11 1.5550 - 1.5063 1.00 3256 143 0.2311 0.2377
REMARK 3 12 1.5063 - 1.4633 1.00 3191 140 0.2355 0.2438
REMARK 3 13 1.4633 - 1.4248 1.00 3207 141 0.2450 0.2892
REMARK 3 14 1.4248 - 1.3900 1.00 3209 140 0.2626 0.2712
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.024 2042
REMARK 3 ANGLE : 2.016 2778
REMARK 3 CHIRALITY : 0.114 302
REMARK 3 PLANARITY : 0.012 367
REMARK 3 DIHEDRAL : 13.155 718
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 7.2139 57.8608 6.7276
REMARK 3 T TENSOR
REMARK 3 T11: 0.0543 T22: 0.0422
REMARK 3 T33: 0.0550 T12: 0.0046
REMARK 3 T13: 0.0051 T23: -0.0035
REMARK 3 L TENSOR
REMARK 3 L11: 0.3364 L22: 0.4652
REMARK 3 L33: 0.9192 L12: 0.1202
REMARK 3 L13: -0.1306 L23: -0.0994
REMARK 3 S TENSOR
REMARK 3 S11: -0.0269 S12: -0.0137 S13: -0.0403
REMARK 3 S21: -0.0010 S22: 0.0070 S23: -0.0507
REMARK 3 S31: 0.1824 S32: 0.0056 S33: 0.0047
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5YFE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1300005116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47656
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 37.880
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: PHASER
REMARK 200 STARTING MODEL: 5LUI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25%PEG 4000, SODIUM ACETATE PH 4.6,
REMARK 280 0.2M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 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 25.47250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.30550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.32200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.30550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.47250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.32200
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 TOTAL BURIED SURFACE AREA: 170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 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 HIS A 269
REMARK 465 HIS A 270
REMARK 465 HIS A 271
REMARK 465 HIS A 272
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 PRO A 45 C PRO A 45 O -0.121
REMARK 500 TYR A 61 CG TYR A 61 CD1 -0.084
REMARK 500 SER A 110 CB SER A 110 OG -0.079
REMARK 500 SER A 115 CB SER A 115 OG -0.099
REMARK 500 TYR A 120 CG TYR A 120 CD1 -0.097
REMARK 500 SER A 181 CB SER A 181 OG -0.093
REMARK 500 GLU A 205 CD GLU A 205 OE1 -0.091
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 97 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 97 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 106 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 ARG A 106 NE - CZ - NH1 ANGL. DEV. = 7.8 DEGREES
REMARK 500 ARG A 106 NE - CZ - NH2 ANGL. DEV. = -5.1 DEGREES
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 ARG A 33 70.83 51.28
REMARK 500 THR A 62 -8.75 78.20
REMARK 500 SER A 134 -117.24 60.71
REMARK 500 SER A 188 -70.39 -130.87
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 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 304
DBREF1 5YFE A 1 264 UNP PETH_IDESA
DBREF2 5YFE A A0A0K8P6T7 27 290
SEQADV 5YFE ASN A 46 UNP A0A0K8P6T THR 72 ENGINEERED MUTATION
SEQADV 5YFE ALA A 198 UNP A0A0K8P6T ARG 224 ENGINEERED MUTATION
SEQADV 5YFE ASN A 261 UNP A0A0K8P6T ALA 287 ENGINEERED MUTATION
SEQADV 5YFE LEU A 265 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE GLU A 266 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 267 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 268 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 269 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 270 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 271 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5YFE HIS A 272 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 272 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 2 A 272 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 3 A 272 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 4 A 272 GLY THR VAL TYR TYR PRO ASN ASN ALA GLY GLY THR VAL
SEQRES 5 A 272 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 6 A 272 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 7 A 272 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 8 A 272 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 9 A 272 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 10 A 272 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 11 A 272 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 12 A 272 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 13 A 272 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 14 A 272 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 15 A 272 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 16 A 272 MET SER ALA ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 17 A 272 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 18 A 272 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 19 A 272 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 20 A 272 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 21 A 272 ASN ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 301 5
HET SO4 A 302 5
HET GOL A 303 14
HET GOL A 304 13
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 SO4 2(O4 S 2-)
FORMUL 4 GOL 2(C3 H8 O3)
FORMUL 6 HOH *69(H2 O)
HELIX 1 AA1 THR A 13 ALA A 19 1 7
HELIX 2 AA2 ARG A 64 LYS A 69 5 6
HELIX 3 AA3 TRP A 70 SER A 77 1 8
HELIX 4 AA4 GLN A 93 GLY A 113 1 21
HELIX 5 AA5 SER A 134 ASN A 147 1 14
HELIX 6 AA6 SER A 188 MET A 196 1 9
HELIX 7 AA7 ASN A 220 ASP A 237 1 18
HELIX 8 AA8 ASP A 239 ARG A 241 5 3
HELIX 9 AA9 TYR A 242 GLU A 248 1 7
SHEET 1 AA1 6 VAL A 26 VAL A 31 0
SHEET 2 AA1 6 ALA A 39 PRO A 45 -1 O VAL A 42 N PHE A 29
SHEET 3 AA1 6 VAL A 81 ASP A 86 -1 O VAL A 82 N TYR A 43
SHEET 4 AA1 6 VAL A 52 VAL A 58 1 N ILE A 57 O ILE A 83
SHEET 5 AA1 6 VAL A 123 GLY A 132 1 O ASP A 124 N VAL A 52
SHEET 6 AA1 6 ALA A 152 ALA A 153 1 O ALA A 152 N VAL A 130
SHEET 1 AA2 3 THR A 172 CYS A 177 0
SHEET 2 AA2 3 LYS A 201 ILE A 206 1 O ILE A 206 N ALA A 176
SHEET 3 AA2 3 VAL A 255 ASN A 261 -1 O ARG A 259 N PHE A 203
SSBOND 1 CYS A 177 CYS A 213 1555 1555 2.04
SSBOND 2 CYS A 247 CYS A 263 1555 1555 2.08
SITE 1 AC1 4 GLN A 93 PRO A 94 SER A 95 HOH A 412
SITE 1 AC2 3 TYR A 193 ASN A 261 HOH A 435
SITE 1 AC3 9 ASN A 164 PHE A 165 SER A 166 SER A 167
SITE 2 AC3 9 SER A 264 LEU A 265 GLU A 266 HIS A 267
SITE 3 AC3 9 GOL A 304
SITE 1 AC4 7 PHE A 235 ASN A 262 CYS A 263 SER A 264
SITE 2 AC4 7 GOL A 303 HOH A 403 HOH A 429
CRYST1 50.945 56.644 80.611 90.00 90.00 90.00 P 21 21 21 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 0.019629 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017654 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012405 0.00000
TER 3866 HIS A 268
MASTER 318 0 4 9 9 0 7 6 2065 1 41 21
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