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HEADER HYDROLASE 19-NOV-21 7W1K
TITLE CRYSTAL STRUCTURE OF CARBOXYLESTERASE FROM THERMOBIFIDA FUSCA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOBIFIDA FUSCA;
SOURCE 3 ORGANISM_COMMON: THERMOMONOSPORA FUSCA;
SOURCE 4 ORGANISM_TAXID: 2021;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS PLASTIC DEGRADATION, HYDROLASE, CATALYSIS
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,H.GERLIS,Z.LI,J.GAO,R.WEI,W.LIU
REVDAT 1 23-NOV-22 7W1K 0
JRNL AUTH X.HAN,H.GERLIS,Z.LI,J.GAO,R.WEI,W.LIU
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE MUTANT FROM
JRNL TITL 2 THERMOBIFIDA FUSCA WITH C8X AND C9C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.19.2_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) : 1.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 103747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.184
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5188
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 24.8900 - 3.0000 1.00 10035 528 0.1493 0.1664
REMARK 3 2 3.0000 - 2.3800 0.99 9907 522 0.1691 0.1875
REMARK 3 3 2.3800 - 2.0800 1.00 10005 527 0.1623 0.1832
REMARK 3 4 2.0800 - 1.8900 0.99 9837 518 0.1701 0.1808
REMARK 3 5 1.8900 - 1.7600 1.00 9913 521 0.1725 0.1812
REMARK 3 6 1.7600 - 1.6500 1.00 9928 523 0.1810 0.1915
REMARK 3 7 1.6500 - 1.5700 1.00 9881 520 0.1812 0.2013
REMARK 3 8 1.5700 - 1.5000 0.98 9805 516 0.1857 0.2161
REMARK 3 9 1.5000 - 1.4400 0.99 9858 519 0.2013 0.2202
REMARK 3 10 1.4400 - 1.3900 0.94 9390 494 0.2228 0.2475
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.850
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.37
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 7W1K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-NOV-21.
REMARK 100 THE DEPOSITION ID IS D_1300025799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-21
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL10U2
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 : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 103778
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.390
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.56300
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: 2OGT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% W/V POLY(ACRYLIC ACID SODIUM SALT)
REMARK 280 5100 0.02 M MGCL2 0.1 M HEPES PH 7.5, 10% GLYCEROL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 56.48050
REMARK 290 SMTRY3 2 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 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 LEU A 497
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 THR A 7 -152.29 -106.00
REMARK 500 ASN A 18 62.64 64.87
REMARK 500 ALA A 58 151.51 -46.03
REMARK 500 ASP A 92 118.52 -167.61
REMARK 500 SER A 185 -122.72 55.71
REMARK 500 ALA A 213 -147.17 -134.15
REMARK 500 ALA A 416 -7.73 81.81
REMARK 500 ASP A 483 66.51 29.59
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 A1224 DISTANCE = 5.83 ANGSTROMS
REMARK 525 HOH A1225 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH A1226 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A1227 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH A1228 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A1229 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH A1230 DISTANCE = 6.98 ANGSTROMS
DBREF 7W1K A 1 497 UNP P86325 EST1_THEFU 1 497
SEQRES 1 A 497 MET GLU ILE VAL ILE ARG THR GLY SER GLY ASP VAL ARG
SEQRES 2 A 497 GLY SER LYS GLU ASN GLY ILE ALA VAL PHE ARG GLY ILE
SEQRES 3 A 497 PRO TYR ALA GLU PRO PRO VAL GLY ALA HIS ARG PHE THR
SEQRES 4 A 497 ALA PRO ARG PRO PRO ARG PRO TRP ASP GLY VAL ARG ASP
SEQRES 5 A 497 ALA THR GLU PHE SER ALA THR ALA PRO ARG PRO PRO TYR
SEQRES 6 A 497 PRO GLU ALA ILE GLY ALA LEU LEU ILE GLU ARG PHE ILE
SEQRES 7 A 497 PRO GLY ASP ASP TYR LEU THR LEU ASN VAL TRP THR PRO
SEQRES 8 A 497 ASP PRO ASN ALA VAL GLY LEU PRO VAL MET VAL TRP ILE
SEQRES 9 A 497 HIS GLY GLY ALA PHE THR ASN GLY SER GLY SER GLU PRO
SEQRES 10 A 497 VAL TYR ASP GLY ALA ALA PHE ALA ARG ASP GLY VAL VAL
SEQRES 11 A 497 PHE VAL SER PHE ASN TYR ARG LEU GLY ILE ILE GLY PHE
SEQRES 12 A 497 ALA ASP LEU PRO ASP ALA PRO SER ASN ARG GLY LEU LEU
SEQRES 13 A 497 ASP GLN ILE ALA ALA LEU GLU TRP VAL ARG ASP ASN ILE
SEQRES 14 A 497 ALA ARG PHE GLY GLY ASP PRO GLY ASN VAL THR VAL PHE
SEQRES 15 A 497 GLY GLU SER ALA GLY ALA MET SER VAL CYS THR LEU MET
SEQRES 16 A 497 ALA THR PRO ARG ALA ARG GLY LEU PHE ARG ARG ALA ILE
SEQRES 17 A 497 LEU GLN SER GLY ALA GLY ASN MET ALA VAL ALA ALA GLU
SEQRES 18 A 497 ASP ALA THR THR ILE ALA ALA VAL ILE ALA HIS ARG LEU
SEQRES 19 A 497 GLY VAL GLU PRO THR ALA ALA ALA LEU ALA HIS VAL PRO
SEQRES 20 A 497 VAL ALA GLN LEU LEU ASP VAL GLN GLN GLN VAL ALA GLN
SEQRES 21 A 497 GLU ILE GLN GLY ALA PRO ASP PRO ALA VAL TRP GLY GLU
SEQRES 22 A 497 ARG ILE ALA GLY GLY SER VAL LEU LEU PRO PHE ALA PRO
SEQRES 23 A 497 VAL ILE ASP GLY GLU LEU LEU SER GLN ARG PRO ALA GLU
SEQRES 24 A 497 ALA ILE ALA GLY GLY ALA GLY HIS ASP VAL ASP LEU LEU
SEQRES 25 A 497 PHE GLY THR THR THR ASP GLU TYR ARG LEU PHE LEU ALA
SEQRES 26 A 497 PRO THR GLY LEU LEU PRO PHE ILE THR SER ASP TYR VAL
SEQRES 27 A 497 THR ALA HIS LEU ALA LYS SER GLY LEU ASP ALA ASP ALA
SEQRES 28 A 497 ALA LYS ALA TYR THR ALA GLU GLY ARG GLY GLU GLU PRO
SEQRES 29 A 497 GLY ASP ILE LEU ALA SER ILE ILE THR ASP GLN VAL PHE
SEQRES 30 A 497 ARG ILE PRO ALA LEU ARG ILE ALA GLU SER ARG VAL ASP
SEQRES 31 A 497 ALA PRO ALA ARG THR PHE GLY TYR GLU PHE ALA TRP ARG
SEQRES 32 A 497 THR PRO GLN LEU ASP GLY ILE LEU GLY ALA CYS HIS ALA
SEQRES 33 A 497 VAL GLU LEU PRO PHE VAL PHE ARG THR LEU ASP ARG ALA
SEQRES 34 A 497 ALA SER LEU VAL GLY THR ASN PRO PRO GLU GLU LEU ALA
SEQRES 35 A 497 GLU THR VAL HIS ASN ALA TRP VAL ARG PHE ALA THR SER
SEQRES 36 A 497 GLY ASP PRO GLY TRP PRO ALA TRP ASN PRO GLU THR ARG
SEQRES 37 A 497 SER VAL MET ARG PHE ASP HIS PRO VAL SER GLU MET VAL
SEQRES 38 A 497 THR ASP PRO TYR PRO ALA THR ARG ALA LEU TRP ASP GLY
SEQRES 39 A 497 VAL PRO LEU
FORMUL 2 HOH *730(H2 O)
HELIX 1 AA1 VAL A 33 PHE A 38 5 6
HELIX 2 AA2 PRO A 66 LEU A 73 1 8
HELIX 3 AA3 GLU A 116 ASP A 120 5 5
HELIX 4 AA4 GLY A 121 ASP A 127 1 7
HELIX 5 AA5 LEU A 138 ALA A 144 1 7
HELIX 6 AA6 ASN A 152 ILE A 169 1 18
HELIX 7 AA7 ALA A 170 PHE A 172 5 3
HELIX 8 AA8 SER A 185 ALA A 196 1 12
HELIX 9 AA9 THR A 197 ARG A 201 5 5
HELIX 10 AB1 ALA A 220 GLY A 235 1 16
HELIX 11 AB2 THR A 239 ALA A 244 1 6
HELIX 12 AB3 PRO A 247 GLY A 264 1 18
HELIX 13 AB4 ASP A 267 GLY A 277 1 11
HELIX 14 AB5 ARG A 296 GLY A 303 1 8
HELIX 15 AB6 TYR A 320 ALA A 325 1 6
HELIX 16 AB7 LEU A 329 ILE A 333 5 5
HELIX 17 AB8 THR A 334 SER A 345 1 12
HELIX 18 AB9 ASP A 350 GLU A 358 1 9
HELIX 19 AC1 GLU A 363 PHE A 377 1 15
HELIX 20 AC2 PHE A 377 ARG A 388 1 12
HELIX 21 AC3 PRO A 405 ILE A 410 5 6
HELIX 22 AC4 GLU A 418 ARG A 424 1 7
HELIX 23 AC5 THR A 425 ARG A 428 5 4
HELIX 24 AC6 ALA A 429 GLY A 434 1 6
HELIX 25 AC7 PRO A 438 GLY A 456 1 19
HELIX 26 AC8 TYR A 485 LEU A 491 1 7
SHEET 1 AA1 3 GLU A 2 ARG A 6 0
SHEET 2 AA1 3 ASP A 11 LYS A 16 -1 O GLY A 14 N ILE A 3
SHEET 3 AA1 3 VAL A 50 ASP A 52 1 O ARG A 51 N ASP A 11
SHEET 1 AA212 GLU A 2 ARG A 6 0
SHEET 2 AA212 ASP A 11 LYS A 16 -1 O GLY A 14 N ILE A 3
SHEET 3 AA212 ALA A 21 PRO A 27 -1 O VAL A 22 N SER A 15
SHEET 4 AA212 THR A 85 THR A 90 -1 O THR A 90 N ALA A 21
SHEET 5 AA212 VAL A 130 PHE A 134 -1 O SER A 133 N ASN A 87
SHEET 6 AA212 LEU A 98 ILE A 104 1 N TRP A 103 O VAL A 132
SHEET 7 AA212 GLY A 174 GLU A 184 1 O THR A 180 N VAL A 100
SHEET 8 AA212 ARG A 206 GLN A 210 1 O GLN A 210 N GLY A 183
SHEET 9 AA212 ASP A 310 THR A 316 1 O LEU A 312 N LEU A 209
SHEET 10 AA212 THR A 395 PHE A 400 1 O PHE A 400 N THR A 315
SHEET 11 AA212 SER A 469 PHE A 473 1 O MET A 471 N GLU A 399
SHEET 12 AA212 GLU A 479 THR A 482 -1 O GLU A 479 N ARG A 472
SHEET 1 AA3 2 VAL A 218 ALA A 219 0
SHEET 2 AA3 2 VAL A 287 ILE A 288 1 O ILE A 288 N VAL A 218
CISPEP 1 HIS A 475 PRO A 476 0 10.03
CRYST1 45.277 112.961 54.780 90.00 106.04 90.00 P 1 21 1 2
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 0.022086 0.000000 0.006349 0.00000
SCALE2 0.000000 0.008853 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018994 0.00000
TER 3736 PRO A 496
MASTER 241 0 0 26 17 0 0 6 4465 1 0 39
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