| 7vpa-pdb | HEADER HYDROLASE 15-OCT-21 7VPA
TITLE CRYSTAL STRUCTURE OF PLE629 FROM MARINE MICROBIAL CONSORTIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE PLE629;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: THE SEQUENCE HAS BEEN DEPOSITED TO GENBAND WITH
COMPND 6 ACCESSION NUMBER OK558825.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCLASSIFIED MARINOBACTER;
SOURCE 3 ORGANISM_TAXID: 83889;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS PLASTIC DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.WU,Y.P.ZHAO,Z.S.LI,M.C.INGRID,P.LARA,J.GAO,X.HAN,Q.LI,O.BASAK,
AUTHOR 2 W.D.LIU,R.WEI
REVDAT 1 24-AUG-22 7VPA 0
JRNL AUTH I.E.MEYER CIFUENTES,P.WU,Y.ZHAO,W.LIU,M.NEUMANN-SCHAAL,
JRNL AUTH 2 L.PFAFF,J.BARYS,Z.LI,J.GAO,X.HAN,U.T.BORNSCHEUER,R.WEI,
JRNL AUTH 3 B.OZTURK
JRNL TITL MOLECULAR AND BIOCHEMICAL DIFFERENCES OF THE TANDEM AND
JRNL TITL 2 COLD-ADAPTED PET HYDROLASES PLE628 AND PLE629, ISOLATED FROM
JRNL TITL 3 A MARINE MICROBIAL CONSORTIUM.
JRNL REF FRONT BIOENG BIOTECHNOL V. 10 30140 2022
JRNL REFN ISSN 2296-4185
JRNL PMID 35935485
JRNL DOI 10.3389/FBIOE.2022.930140
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.040
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 22745
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 1136
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 28.6600 - 4.7000 0.95 2591 135 0.1589 0.2410
REMARK 3 2 4.6900 - 3.7300 0.95 2597 142 0.1670 0.2411
REMARK 3 3 3.7300 - 3.2600 0.99 2702 151 0.1898 0.2437
REMARK 3 4 3.2600 - 2.9600 1.00 2728 146 0.2441 0.2967
REMARK 3 5 2.9600 - 2.7500 1.00 2756 140 0.1965 0.3008
REMARK 3 6 2.7500 - 2.5900 1.00 2754 146 0.2343 0.3175
REMARK 3 7 2.5900 - 2.4600 1.00 2752 138 0.2655 0.3068
REMARK 3 8 2.4600 - 2.3500 0.99 2729 138 0.2941 0.3561
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.370
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.89
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 7VPA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1300025109.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL18U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22794
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.22500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.50
REMARK 200 R MERGE FOR SHELL (I) : 0.67900
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: 6SBN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M AMMONIUM ACETATE,
REMARK 280 0.1M TRI-SODIUM CITRATE DIHYDRATE, PH 5.6, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 60.49133
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 30.24567
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1
REMARK 465 GLY A 2
REMARK 465 GLY A 3
REMARK 465 GLY A 4
REMARK 465 GLY A 5
REMARK 465 SER A 6
REMARK 465 GLY A 7
REMARK 465 GLY A 8
REMARK 465 GLY A 9
REMARK 465 ASN A 10
REMARK 465 ASN A 11
REMARK 465 GLY A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 GLY A 16
REMARK 465 GLU A 291
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLY B 3
REMARK 465 GLY B 4
REMARK 465 GLY B 5
REMARK 465 SER B 6
REMARK 465 GLY B 7
REMARK 465 GLY B 8
REMARK 465 GLY B 9
REMARK 465 ASN B 10
REMARK 465 ASN B 11
REMARK 465 GLY B 12
REMARK 465 GLY B 13
REMARK 465 GLY B 14
REMARK 465 GLY B 15
REMARK 465 GLY B 16
REMARK 465 CYS B 17
REMARK 465 GLU B 18
REMARK 465 ALA B 19
REMARK 465 GLU B 291
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 152 -117.66 61.01
REMARK 500 ASN A 197 46.84 -101.14
REMARK 500 HIS A 206 -91.08 -130.60
REMARK 500 LYS A 261 40.68 37.14
REMARK 500 PHE B 79 -138.56 63.50
REMARK 500 SER B 152 -117.50 57.14
REMARK 500 ASN B 197 39.65 -91.63
REMARK 500 HIS B 206 -87.56 -134.33
REMARK 500 GLU B 282 136.01 -170.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF 7VPA A 1 291 PDB 7VPA 7VPA 1 291
DBREF 7VPA B 1 291 PDB 7VPA 7VPA 1 291
SEQRES 1 A 291 MET GLY GLY GLY GLY SER GLY GLY GLY ASN ASN GLY GLY
SEQRES 2 A 291 GLY GLY GLY CYS GLU ALA ASP CYS GLY TYR GLU ARG GLY
SEQRES 3 A 291 PRO ASP PRO SER VAL SER LEU LEU GLU ALA SER THR GLY
SEQRES 4 A 291 PRO PHE SER VAL ARG THR SER ASN VAL SER SER SER VAL
SEQRES 5 A 291 ARG GLY PHE GLY GLY GLY THR ILE HIS TYR PRO THR ASN
SEQRES 6 A 291 THR THR GLY THR MET ALA ALA ILE VAL VAL ILE PRO GLY
SEQRES 7 A 291 PHE VAL SER PRO GLU SER SER ILE ALA TRP TRP GLY PRO
SEQRES 8 A 291 LYS LEU ALA SER HIS GLY PHE VAL VAL MET THR ILE GLY
SEQRES 9 A 291 THR ASN SER GLY PHE ASP GLN PRO ALA SER ARG ALA SER
SEQRES 10 A 291 GLN LEU ASN ASN ALA LEU ASP TYR LEU ILE GLU GLN ASN
SEQRES 11 A 291 GLY SER SER ARG SER PRO ILE ASN GLY MET ILE ASP THR
SEQRES 12 A 291 ASP ARG LEU GLY VAL MET GLY TRP SER MET GLY GLY GLY
SEQRES 13 A 291 GLY THR LEU ARG VAL ALA THR GLU GLY ARG VAL SER ALA
SEQRES 14 A 291 ALA ILE PRO LEU ALA PRO TRP ASP SER SER SER SER GLN
SEQRES 15 A 291 PHE ARG SER ILE ASP THR PRO THR LEU ILE PHE ALA CYS
SEQRES 16 A 291 GLU ASN ASP SER THR ALA PRO VAL ARG SER HIS ALA ASP
SEQRES 17 A 291 PRO PHE TYR ASP ALA ILE PRO ASP SER THR ALA LYS ALA
SEQRES 18 A 291 PHE VAL GLU LEU ASP GLY GLY GLY HIS THR CYS ALA ASN
SEQRES 19 A 291 GLY SER SER GLY PHE GLY GLY SER TYR ASN ASP VAL LEU
SEQRES 20 A 291 SER ARG LEU GLY VAL SER TRP MET LYS LEU HIS LEU ASP
SEQRES 21 A 291 LYS ASP GLN ARG TYR ASN GLN PHE VAL CYS GLY PRO ASN
SEQRES 22 A 291 HIS GLU SER ASP ARG SER ILE SER GLU TYR ARG GLY THR
SEQRES 23 A 291 CYS PRO TYR LEU GLU
SEQRES 1 B 291 MET GLY GLY GLY GLY SER GLY GLY GLY ASN ASN GLY GLY
SEQRES 2 B 291 GLY GLY GLY CYS GLU ALA ASP CYS GLY TYR GLU ARG GLY
SEQRES 3 B 291 PRO ASP PRO SER VAL SER LEU LEU GLU ALA SER THR GLY
SEQRES 4 B 291 PRO PHE SER VAL ARG THR SER ASN VAL SER SER SER VAL
SEQRES 5 B 291 ARG GLY PHE GLY GLY GLY THR ILE HIS TYR PRO THR ASN
SEQRES 6 B 291 THR THR GLY THR MET ALA ALA ILE VAL VAL ILE PRO GLY
SEQRES 7 B 291 PHE VAL SER PRO GLU SER SER ILE ALA TRP TRP GLY PRO
SEQRES 8 B 291 LYS LEU ALA SER HIS GLY PHE VAL VAL MET THR ILE GLY
SEQRES 9 B 291 THR ASN SER GLY PHE ASP GLN PRO ALA SER ARG ALA SER
SEQRES 10 B 291 GLN LEU ASN ASN ALA LEU ASP TYR LEU ILE GLU GLN ASN
SEQRES 11 B 291 GLY SER SER ARG SER PRO ILE ASN GLY MET ILE ASP THR
SEQRES 12 B 291 ASP ARG LEU GLY VAL MET GLY TRP SER MET GLY GLY GLY
SEQRES 13 B 291 GLY THR LEU ARG VAL ALA THR GLU GLY ARG VAL SER ALA
SEQRES 14 B 291 ALA ILE PRO LEU ALA PRO TRP ASP SER SER SER SER GLN
SEQRES 15 B 291 PHE ARG SER ILE ASP THR PRO THR LEU ILE PHE ALA CYS
SEQRES 16 B 291 GLU ASN ASP SER THR ALA PRO VAL ARG SER HIS ALA ASP
SEQRES 17 B 291 PRO PHE TYR ASP ALA ILE PRO ASP SER THR ALA LYS ALA
SEQRES 18 B 291 PHE VAL GLU LEU ASP GLY GLY GLY HIS THR CYS ALA ASN
SEQRES 19 B 291 GLY SER SER GLY PHE GLY GLY SER TYR ASN ASP VAL LEU
SEQRES 20 B 291 SER ARG LEU GLY VAL SER TRP MET LYS LEU HIS LEU ASP
SEQRES 21 B 291 LYS ASP GLN ARG TYR ASN GLN PHE VAL CYS GLY PRO ASN
SEQRES 22 B 291 HIS GLU SER ASP ARG SER ILE SER GLU TYR ARG GLY THR
SEQRES 23 B 291 CYS PRO TYR LEU GLU
FORMUL 3 HOH *167(H2 O)
HELIX 1 AA1 SER A 30 ALA A 36 1 7
HELIX 2 AA2 PRO A 82 ALA A 87 5 6
HELIX 3 AA3 TRP A 88 SER A 95 1 8
HELIX 4 AA4 GLN A 111 GLY A 131 1 21
HELIX 5 AA5 SER A 152 ALA A 162 1 11
HELIX 6 AA6 SER A 180 ILE A 186 5 7
HELIX 7 AA7 PRO A 202 SER A 205 5 4
HELIX 8 AA8 HIS A 206 ILE A 214 1 9
HELIX 9 AA9 TYR A 243 ASP A 260 1 18
HELIX 10 AB1 ASP A 262 VAL A 269 5 8
HELIX 11 AB2 ASN A 273 ASP A 277 5 5
HELIX 12 AB3 SER B 30 ALA B 36 1 7
HELIX 13 AB4 PRO B 82 ALA B 87 5 6
HELIX 14 AB5 TRP B 88 SER B 95 1 8
HELIX 15 AB6 GLN B 111 ASN B 130 1 20
HELIX 16 AB7 SER B 152 ALA B 162 1 11
HELIX 17 AB8 SER B 180 ILE B 186 5 7
HELIX 18 AB9 PRO B 202 SER B 205 5 4
HELIX 19 AC1 HIS B 206 ILE B 214 1 9
HELIX 20 AC2 TYR B 243 LEU B 259 1 17
HELIX 21 AC3 ASP B 262 VAL B 269 5 8
HELIX 22 AC4 ASN B 273 ASP B 277 5 5
SHEET 1 AA1 6 VAL A 43 VAL A 48 0
SHEET 2 AA1 6 GLY A 58 PRO A 63 -1 O ILE A 60 N SER A 46
SHEET 3 AA1 6 VAL A 99 ILE A 103 -1 O VAL A 100 N HIS A 61
SHEET 4 AA1 6 MET A 70 ILE A 76 1 N ILE A 73 O MET A 101
SHEET 5 AA1 6 ILE A 141 TRP A 151 1 O GLY A 147 N ALA A 72
SHEET 6 AA1 6 ALA A 169 LEU A 173 1 O LEU A 173 N GLY A 150
SHEET 1 AA2 3 THR A 190 CYS A 195 0
SHEET 2 AA2 3 LYS A 220 LEU A 225 1 O ALA A 221 N ILE A 192
SHEET 3 AA2 3 ILE A 280 GLY A 285 -1 O ARG A 284 N PHE A 222
SHEET 1 AA3 6 VAL B 43 VAL B 48 0
SHEET 2 AA3 6 GLY B 58 PRO B 63 -1 O ILE B 60 N SER B 46
SHEET 3 AA3 6 VAL B 99 ILE B 103 -1 O VAL B 100 N HIS B 61
SHEET 4 AA3 6 MET B 70 ILE B 76 1 N ILE B 73 O MET B 101
SHEET 5 AA3 6 ILE B 141 TRP B 151 1 O GLY B 147 N ALA B 72
SHEET 6 AA3 6 ALA B 169 LEU B 173 1 O LEU B 173 N GLY B 150
SHEET 1 AA4 3 THR B 190 CYS B 195 0
SHEET 2 AA4 3 LYS B 220 LEU B 225 1 O ALA B 221 N ILE B 192
SHEET 3 AA4 3 ILE B 280 GLY B 285 -1 O ARG B 284 N PHE B 222
SSBOND 1 CYS A 17 CYS A 21 1555 1555 2.01
SSBOND 2 CYS A 195 CYS A 232 1555 1555 2.04
SSBOND 3 CYS A 270 CYS A 287 1555 1555 2.05
SSBOND 4 CYS B 195 CYS B 232 1555 1555 2.04
SSBOND 5 CYS B 270 CYS B 287 1555 1555 2.04
CISPEP 1 CYS A 287 PRO A 288 0 14.28
CISPEP 2 CYS B 287 PRO B 288 0 10.95
CRYST1 73.927 73.927 90.737 90.00 90.00 120.00 P 32 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 0.013527 0.007810 0.000000 0.00000
SCALE2 0.000000 0.015619 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011021 0.00000
TER 2038 LEU A 290
TER 4056 LEU B 290
MASTER 268 0 0 22 18 0 0 6 4221 2 10 46
END
|
|---|
