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HEADER HYDROLASE 08-OCT-21 7VMD
TITLE CRYSTAL STRUCTURE OF A HYDROLASES PLE628 FROM MARINE MICROBIAL
TITLE 2 CONSORTIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE PLE628;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SEQUENCE HAS BEEN DEPOSITED TO GENBANK WITH ACCESSION
COMPND 6 NUMBER OK558824.
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: PET-32A
KEYWDS 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 7VMD 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. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_4158
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 26572
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1329
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 25.9700 - 3.5000 1.00 2981 157 0.1437 0.1575
REMARK 3 2 3.5000 - 2.7800 1.00 2845 150 0.1432 0.1735
REMARK 3 3 2.7800 - 2.4300 1.00 2811 148 0.1527 0.1673
REMARK 3 4 2.4300 - 2.2100 1.00 2814 149 0.1454 0.2099
REMARK 3 5 2.2100 - 2.0500 1.00 2788 146 0.1482 0.1770
REMARK 3 6 2.0500 - 1.9300 1.00 2799 147 0.1556 0.2098
REMARK 3 7 1.9300 - 1.8300 1.00 2767 146 0.1709 0.2086
REMARK 3 8 1.8300 - 1.7500 1.00 2755 145 0.1955 0.2356
REMARK 3 9 1.7500 - 1.6900 0.97 2683 141 0.2133 0.2757
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) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.72
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 7VMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-21.
REMARK 100 THE DEPOSITION ID IS D_1300024960.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17B1
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 : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26625
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.600
REMARK 200 R MERGE (I) : 0.12400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 3.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.62000
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 (%): 33.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 0.2M CALCIUM ACELATE,
REMARK 280 0.1M SODIUM CACODYLATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
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 21.86650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.70450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.27000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.70450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.86650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.27000
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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9640 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 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 GLU A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 4
REMARK 465 THR A 5
REMARK 465 LEU A 6
REMARK 465 GLU A 7
REMARK 465 GLY A 8
REMARK 465 SER A 9
REMARK 465 GLU A 10
REMARK 465 PHE A 11
REMARK 465 ALA A 12
REMARK 465 GLY A 13
REMARK 465 GLY A 14
REMARK 465 GLY A 15
REMARK 465 GLY A 16
REMARK 465 ASP A 17
REMARK 465 GLY A 18
REMARK 465 GLY A 19
REMARK 465 ASP A 20
REMARK 465 GLY A 21
REMARK 465 GLY A 22
REMARK 465 CYS A 23
REMARK 465 THR A 24
REMARK 465 SER A 25
REMARK 465 ASP A 26
REMARK 465 CYS A 27
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 83 -167.65 -77.63
REMARK 500 SER A 87 32.63 -87.42
REMARK 500 SER A 91 -157.23 -131.40
REMARK 500 ASP A 116 -85.92 -151.44
REMARK 500 SER A 158 -122.20 68.71
REMARK 500 HIS A 212 -89.22 -129.71
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 763 DISTANCE = 6.38 ANGSTROMS
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 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 202 OE1
REMARK 620 2 ASN A 232 OD1 73.5
REMARK 620 3 ASN A 233 OD1 87.9 82.1
REMARK 620 4 HOH A 453 O 152.1 78.6 86.8
REMARK 620 5 HOH A 501 O 84.2 85.9 167.1 95.5
REMARK 620 6 HOH A 630 O 79.6 148.5 80.7 126.3 107.7
REMARK 620 7 HOH A 713 O 143.6 137.3 111.6 62.8 80.5 74.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 302 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 288 O
REMARK 620 2 PRO A 290 O 75.9
REMARK 620 3 HOH A 424 O 123.4 91.2
REMARK 620 4 HOH A 429 O 114.2 160.9 95.7
REMARK 620 5 HOH A 456 O 148.1 75.9 71.8 89.3
REMARK 620 6 HOH A 482 O 83.0 93.0 153.4 73.1 83.8
REMARK 620 7 HOH A 623 O 71.1 127.6 75.2 71.5 139.8 121.2
REMARK 620 N 1 2 3 4 5 6
DBREF 7VMD A 1 293 PDB 7VMD 7VMD 1 293
SEQRES 1 A 293 MET GLU LEU GLY THR LEU GLU GLY SER GLU PHE ALA GLY
SEQRES 2 A 293 GLY GLY GLY ASP GLY GLY ASP GLY GLY CYS THR SER ASP
SEQRES 3 A 293 CYS GLY PHE GLN ARG GLY PRO ASP PRO THR VAL SER PHE
SEQRES 4 A 293 LEU GLU ALA SER SER GLY PRO TYR SER VAL ARG THR ASP
SEQRES 5 A 293 ASN VAL SER SER LEU VAL GLY GLY PHE GLY GLY GLY THR
SEQRES 6 A 293 VAL HIS TYR PRO THR GLY THR THR GLY THR MET ALA ALA
SEQRES 7 A 293 VAL VAL VAL ILE PRO GLY PHE VAL SER ALA GLU SER SER
SEQRES 8 A 293 ILE GLU TRP TRP GLY PRO LYS LEU ALA SER TYR GLY PHE
SEQRES 9 A 293 VAL VAL MET THR ILE ASP THR ASN SER GLY PHE ASP GLN
SEQRES 10 A 293 PRO PRO SER ARG ALA THR GLN ILE ASN ASN ALA LEU ASP
SEQRES 11 A 293 TYR LEU LEU GLU GLU ASN ASP SER SER SER SER PRO TYR
SEQRES 12 A 293 SER GLY MET ILE ASP PRO ASN ARG LEU GLY VAL ILE GLY
SEQRES 13 A 293 TRP SER MET GLY GLY GLY GLY THR LEU ARG VAL ALA ALA
SEQRES 14 A 293 GLU GLY ARG ILE GLN ALA ALA ILE PRO LEU ALA PRO TRP
SEQRES 15 A 293 ASP THR SER SER LEU ARG PHE ARG ASN ILE GLU THR PRO
SEQRES 16 A 293 THR LEU ILE PHE ALA CYS GLU SER ASP VAL ILE ALA PRO
SEQRES 17 A 293 VAL GLY SER HIS ALA ASP PRO PHE TYR GLU ALA ILE PRO
SEQRES 18 A 293 ASP SER THR ASP LYS ALA PHE PHE GLU LEU ASN ASN GLY
SEQRES 19 A 293 SER HIS TYR CYS GLY ASN GLY GLY ASN SER TYR ASN ASN
SEQRES 20 A 293 GLU LEU GLY ARG LEU GLY VAL SER TRP MET LYS LEU HIS
SEQRES 21 A 293 LEU ASP GLN ASP GLN ARG TYR ASN GLN PHE LEU CYS GLY
SEQRES 22 A 293 PRO ASP HIS GLU ASP GLU TYR ARG ILE SER GLU TYR ARG
SEQRES 23 A 293 GLY THR CYS PRO TYR LEU GLU
HET CA A 301 1
HET CA A 302 1
HETNAM CA CALCIUM ION
FORMUL 2 CA 2(CA 2+)
FORMUL 4 HOH *363(H2 O)
HELIX 1 AA1 THR A 36 ALA A 42 1 7
HELIX 2 AA2 TRP A 94 SER A 101 1 8
HELIX 3 AA3 GLN A 117 ASP A 137 1 21
HELIX 4 AA4 SER A 158 GLY A 171 1 14
HELIX 5 AA5 SER A 186 ARG A 190 5 5
HELIX 6 AA6 PRO A 208 SER A 211 5 4
HELIX 7 AA7 HIS A 212 ILE A 220 1 9
HELIX 8 AA8 TYR A 237 GLY A 241 5 5
HELIX 9 AA9 TYR A 245 ASP A 262 1 18
HELIX 10 AB1 ASP A 264 ARG A 266 5 3
HELIX 11 AB2 TYR A 267 CYS A 272 1 6
HELIX 12 AB3 ASP A 275 GLU A 279 5 5
SHEET 1 AA1 6 VAL A 49 VAL A 54 0
SHEET 2 AA1 6 GLY A 64 PRO A 69 -1 O GLY A 64 N VAL A 54
SHEET 3 AA1 6 VAL A 105 ILE A 109 -1 O VAL A 106 N HIS A 67
SHEET 4 AA1 6 MET A 76 ILE A 82 1 N VAL A 81 O MET A 107
SHEET 5 AA1 6 ILE A 147 TRP A 157 1 O ILE A 155 N VAL A 80
SHEET 6 AA1 6 ALA A 175 LEU A 179 1 O LEU A 179 N GLY A 156
SHEET 1 AA2 3 THR A 196 CYS A 201 0
SHEET 2 AA2 3 LYS A 226 LEU A 231 1 O LEU A 231 N ALA A 200
SHEET 3 AA2 3 ILE A 282 GLY A 287 -1 O ARG A 286 N PHE A 228
SSBOND 1 CYS A 201 CYS A 238 1555 1555 2.02
SSBOND 2 CYS A 272 CYS A 289 1555 1555 2.02
LINK OE1 GLU A 202 CA CA A 301 1555 1555 2.43
LINK OD1 ASN A 232 CA CA A 301 1555 1555 2.29
LINK OD1 ASN A 233 CA CA A 301 1555 1555 2.24
LINK O THR A 288 CA CA A 302 1555 1555 2.21
LINK O PRO A 290 CA CA A 302 1555 1555 2.46
LINK CA CA A 301 O HOH A 453 1555 1455 2.43
LINK CA CA A 301 O HOH A 501 1555 1555 2.40
LINK CA CA A 301 O HOH A 630 1555 1555 2.22
LINK CA CA A 301 O HOH A 713 1555 1455 2.41
LINK CA CA A 302 O HOH A 424 1555 1555 2.33
LINK CA CA A 302 O HOH A 429 1555 1555 2.50
LINK CA CA A 302 O HOH A 456 1555 1555 2.29
LINK CA CA A 302 O HOH A 482 1555 1555 2.23
LINK CA CA A 302 O HOH A 623 1555 1555 2.68
CISPEP 1 CYS A 289 PRO A 290 0 -0.33
CRYST1 43.733 64.540 81.409 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 0.022866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015494 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012284 0.00000
TER 2027 GLU A 293
MASTER 299 0 2 12 9 0 0 6 2391 1 20 23
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